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permease protein of polyamine ABC transporter
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polyamine ABC transporter
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polyamine transport system
polyamine-binding protein of polyamine ABC transporter
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polyamine-transporting ATPase
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putrescine export system ATP-binding protein
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
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putrescine export system permease protein
SapC
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
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spermidine/putrescine ABC transporter permease
spermidine/putrescine ABC transporter permease I
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Spermidine/putrescine ABC transporter permease protein
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spermidine/putrescine import ATP-binding protein
spermidine/putrescine-binding periplasmic protein
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polyamine transport system
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polyamine transport system
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PotA
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potABCD
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potADB
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PotB
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PotD
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putrescine export system permease protein
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
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putrescine export system permease protein
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
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putrescine exporter
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
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putrescine exporter
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
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SapA
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
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SapA
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
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SapB
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
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SapB
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
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SapBCDF
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
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SapBCDF
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
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spermidine/putrescine ABC transporter permease
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spermidine/putrescine ABC transporter permease
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spermidine/putrescine import ATP-binding protein
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spermidine/putrescine import ATP-binding protein
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spermidine/putrescine import ATP-binding protein
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spermidine/putrescine import ATP-binding protein
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spermidine/putrescine import ATP-binding protein
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-
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ATP + H2O + polyamine-[polyamine-binding protein][side 1]
ADP + phosphate + polyamine[side 2] + [polyamine-binding protein][side 1]
ATP + H2O + putrescine-[polyamine-binding protein][side 1]
ADP + phosphate + putrescine[side 2] + [polyamine-binding protein][side 1]
ATP + H2O + putrescine/out
ADP + phosphate + putrescine/in
ATP + H2O + spermidine-[polyamine-binding protein][side 1]
ADP + phosphate + spermidine[side 2] + [polyamine-binding protein][side 1]
ATP + H2O + spermidine/out
ADP + phosphate + spermidine/in
ATP + H2O + spermine-[polyamine-binding protein][side 1]
ADP + phosphate + spermine[side 2] + [polyamine-binding protein][side 1]
putrescine/out + ATP + H2O
putrescine/in + ADP + phosphate
spermidine/out + ADP + H2O
spermidine/in + ?
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the nucleotide specificity of PotA from the spermidine-preferential system in the order of decreasing activity: ATP, GTP = ADP, CTP = UTP
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-
?
spermidine/out + ATP + H2O
spermidine/in + ADP + phosphate
spermidine/out + CTP + H2O
spermidine/in + CDP + phosphate
-
the nucleotide specificity of PotA from the spermidine-preferential system in the order of decreasing activity: ATP, GTP = ADP, CTP = UTP
-
?
spermidine/out + GTP + H2O
spermidine/in + GDP + phosphate
-
the nucleotide specificity of PotA from the spermidine-preferential system in the order of decreasing activity: ATP, GTP = ADP, CTP = UTP
-
?
spermidine/out + UTP + H2O
spermidine/in + UDP + phosphate
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the nucleotide specificity of PotA from the spermidine-preferential system in the order of decreasing activity: ATP, GTP = ADP, CTP = UTP
-
?
spermine/out + ATP + H2O
spermine/in + ADP + phosphate
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two polyamine-uptake systems: one is a putrescine-specific system and the other is a spermidine-preferential system
-
?
additional information
?
-
ATP + H2O + polyamine-[polyamine-binding protein][side 1]
ADP + phosphate + polyamine[side 2] + [polyamine-binding protein][side 1]
-
-
-
?
ATP + H2O + polyamine-[polyamine-binding protein][side 1]
ADP + phosphate + polyamine[side 2] + [polyamine-binding protein][side 1]
-
-
-
?
ATP + H2O + polyamine-[polyamine-binding protein][side 1]
ADP + phosphate + polyamine[side 2] + [polyamine-binding protein][side 1]
-
-
-
?
ATP + H2O + polyamine-[polyamine-binding protein][side 1]
ADP + phosphate + polyamine[side 2] + [polyamine-binding protein][side 1]
-
-
-
?
ATP + H2O + polyamine-[polyamine-binding protein][side 1]
ADP + phosphate + polyamine[side 2] + [polyamine-binding protein][side 1]
-
-
-
?
ATP + H2O + putrescine-[polyamine-binding protein][side 1]
ADP + phosphate + putrescine[side 2] + [polyamine-binding protein][side 1]
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
-
-
-
?
ATP + H2O + putrescine-[polyamine-binding protein][side 1]
ADP + phosphate + putrescine[side 2] + [polyamine-binding protein][side 1]
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
-
-
-
?
ATP + H2O + putrescine-[polyamine-binding protein][side 1]
ADP + phosphate + putrescine[side 2] + [polyamine-binding protein][side 1]
-
-
-
?
ATP + H2O + putrescine-[polyamine-binding protein][side 1]
ADP + phosphate + putrescine[side 2] + [polyamine-binding protein][side 1]
-
-
-
?
ATP + H2O + putrescine-[polyamine-binding protein][side 1]
ADP + phosphate + putrescine[side 2] + [polyamine-binding protein][side 1]
-
-
-
?
ATP + H2O + putrescine/out
ADP + phosphate + putrescine/in
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putrescine-ornithine antiporter, encoded by the gene potE
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r
ATP + H2O + putrescine/out
ADP + phosphate + putrescine/in
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the putrescine-specific system, encoded by the genes potABCD, is specific for this polyamine
-
-
?
ATP + H2O + spermidine-[polyamine-binding protein][side 1]
ADP + phosphate + spermidine[side 2] + [polyamine-binding protein][side 1]
-
-
-
?
ATP + H2O + spermidine-[polyamine-binding protein][side 1]
ADP + phosphate + spermidine[side 2] + [polyamine-binding protein][side 1]
-
-
-
?
ATP + H2O + spermidine-[polyamine-binding protein][side 1]
ADP + phosphate + spermidine[side 2] + [polyamine-binding protein][side 1]
-
-
-
?
ATP + H2O + spermidine-[polyamine-binding protein][side 1]
ADP + phosphate + spermidine[side 2] + [polyamine-binding protein][side 1]
-
-
-
?
ATP + H2O + spermidine-[polyamine-binding protein][side 1]
ADP + phosphate + spermidine[side 2] + [polyamine-binding protein][side 1]
-
-
-
?
ATP + H2O + spermidine/out
ADP + phosphate + spermidine/in
-
the spermidine-preferential system, encoded by the genes potFGHI, can transport both spermidine and putrescine
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-
?
ATP + H2O + spermidine/out
ADP + phosphate + spermidine/in
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the spermidine-preferential system, encoded by the genes potFGHI, can trasport both spermidine and putrescine
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-
?
ATP + H2O + spermine-[polyamine-binding protein][side 1]
ADP + phosphate + spermine[side 2] + [polyamine-binding protein][side 1]
-
-
-
?
ATP + H2O + spermine-[polyamine-binding protein][side 1]
ADP + phosphate + spermine[side 2] + [polyamine-binding protein][side 1]
-
-
-
?
putrescine/out + ATP + H2O
putrescine/in + ADP + phosphate
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two polyamine-uptake systems: one is a putrescine-specific system and the other is a spermidine-preferential system
-
?
putrescine/out + ATP + H2O
putrescine/in + ADP + phosphate
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higher affinity for spermidine than for putrescine
-
?
spermidine/out + ATP + H2O
spermidine/in + ADP + phosphate
-
-
-
-
?
spermidine/out + ATP + H2O
spermidine/in + ADP + phosphate
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two polyamine-uptake systems: one is a putrescine-specific system and the other is a spermidine-preferential system.The nucleotide specificity of PotA from the spermidine-preferential system in the order of decreasing activity: ATP, GTP = ADP, CTP = UTP
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-
?
additional information
?
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mechanism of polyamine binding by PotD
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-
?
additional information
?
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PotA protein and PotD protein are absolutely necessary for spermidine uptake in conjugation with the two channel forming proteins PotB and PotC
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-
?
additional information
?
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the following amino acids of the PotD protein are involved in binding of spermidine: Trp34, Thr35, Glu36, Tyr37, Ser83, Tyr85, Asp168, Glu171, Trp229
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-
?
additional information
?
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the following amino acids of the PotD protein are involved in binding of spermidine: Trp34, Thr35, Glu36, Tyr37, Ser83, Tyr85, Asp168, Glu171, Trp229
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-
?
additional information
?
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the following amino acids of the PotD protein are involved in binding of spermidine: Trp34, Thr35, Glu36, Tyr37, Ser83, Tyr85, Asp168, Glu171, Trp229
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-
?
additional information
?
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the following amino acids of the PotD protein are involved in binding of spermidine: Trp34, Thr35, Glu36, Tyr37, Ser83, Tyr85, Asp168, Glu171, Trp229
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-
?
additional information
?
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Trp255, Asp257, Tyr293 and Gln327
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-
?
additional information
?
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PotA protein is involved in the energy-coupling step
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-
?
additional information
?
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Pot D is the primary receptor of the polyamine transport system, which regulates the polyamine content in E. coli
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?
additional information
?
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PotD binding assays and ATPase activity assays of PotA are performed. A preference for extracellular polyamines in Streptococcus suis is identified as spermidine, spermine, putrescine in descending order, the uptake is competitive among the three
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-
?
additional information
?
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PotD binding assays and ATPase activity assays of PotA are performed. A preference for extracellular polyamines in Streptococcus suis is identified as spermidine, spermine, putrescine in descending order, the uptake is competitive among the three
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-
?
additional information
?
-
PotD binding assays and ATPase activity assays of PotA are performed. A preference for extracellular polyamines in Streptococcus suis is identified as spermidine, spermine, putrescine in descending order, the uptake is competitive among the three
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-
?
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Carcinogenesis
Involvement of the polyamine transport system in cellular uptake of the radioprotectants WR-1065 and WR-33278.
Carcinoma, Hepatocellular
Antitumor effects and preliminary systemic toxicity of ANISpm in vivo and in vitro.
Hypertension
ATP13A3 is a major component of the enigmatic mammalian polyamine transport system.
Infections
Functional characterization of murB-potABCD operon for polyamine uptake and peptidoglycan synthesis in Streptococcus suis.
Infections
Polyamine transport in human promyelocytic leukemia cells and polymorphonuclear leukocytes.
Leukemia
Aliphatic chain length specificity of the polyamine transport system in ascites L1210 leukemia cells.
Melanoma
Harnessing the polyamine transport system to treat BRAF inhibitor-resistant melanoma.
Melanoma
Tailoring of silica-based nanoporous pod by spermidine multi-activity.
Melanoma, Experimental
Paraquat is not accumulated in B16 tumor cells by the polyamine transport system.
Meningitis, Bacterial
Computational approaches to identify common subunit vaccine candidates against bacterial meningitis.
Neoplasms
(99m)Tc-HYNIC-spermine for imaging polyamine transport system-positive tumours: preclinical evaluation.
Neoplasms
(Z)-1,4-diamino-2-butene as a vector of boron, fluorine, or iodine for cancer therapy and imaging: synthesis and biological evaluation.
Neoplasms
A fluorescent biomarker of the polyamine transport system to select patients with AML for F14512 treatment.
Neoplasms
A Novel Polyamine-Targeted Therapy for BRAF Mutant Melanoma Tumors.
Neoplasms
A putrescine-anthracence conjugate: a paradigm for selective drug delivery.
Neoplasms
Activity of the polyamine-vectorized anti-cancer drug F14512 against pediatric glioma and neuroblastoma cell lines.
Neoplasms
Analysis of the in vitro and in vivo effects of photodynamic therapy on prostate cancer by using new photosensitizers, protoporphyrin IX-polyamine derivatives.
Neoplasms
Ant 4,4, a polyamine-anthracene conjugate, induces cell death and recovery in human promyelogenous leukemia cells (HL-60).
Neoplasms
Clickable polyamine derivatives as chemical probes for the polyamine transport system.
Neoplasms
Development of Polyamine Transport Ligands with Improved Metabolic Stability and Selectivity against Specific Human Cancers.
Neoplasms
Evaluation of Polyamine Transport Inhibitors in a Drosophila Epithelial Model Suggests the Existence of Multiple Transport Systems.
Neoplasms
F14512, a polyamine-vectorized anti-cancer drug, currently in clinical trials exhibits a marked preclinical anti-leukemic activity.
Neoplasms
F14512, a potent antitumor agent targeting topoisomerase II vectored into cancer cells via the polyamine transport system.
Neoplasms
Interactions between the Etoposide Derivative F14512 and Human Type II Topoisomerases: Implications for the C4 Spermine Moiety in Promoting Enzyme-Mediated DNA Cleavage.
Neoplasms
N-Benzylpolyamines as vectors of boron and fluorine for cancer therapy and imaging: synthesis and biological evaluation.
Neoplasms
Paraquat is not accumulated in B16 tumor cells by the polyamine transport system.
Neoplasms
Phase I dose-escalation study of F14512, a polyamine-vectorized topoisomerase II inhibitor, in patients with platinum-refractory or resistant ovarian cancer.
Neoplasms
Polyamine transport system-targeted nanometric micelles assembled from epipodophyllotoxin-amphiphiles.
Neoplasms
Polyamine-blocking therapy reverses immunosuppression in the tumor microenvironment.
Neoplasms
Polyamine-containing etoposide derivatives as poisons of human type II topoisomerases: Differential effects on topoisomerase II? and II?.
Neoplasms
Polyamines and Cancer.
Neoplasms
Polyaminoquinoline iron chelators for vectorization of antiproliferative agents: design, synthesis, and validation.
Neoplasms
Preclinical activity of F14512, designed to target tumors expressing an active polyamine transport system.
Neoplasms
Quilamine HQ1-44, an iron chelator vectorized toward tumor cells by the polyamine transport system, inhibits HCT116 tumor growth without adverse effect.
Neoplasms
Regulation by survivin of cancer cell death induced by F14512, a polyamine-containing inhibitor of DNA topoisomerase II.
Neoplasms
Synthesis and biological evaluation of chalcone-polyamine conjugates as novel vectorized agents in colorectal and prostate cancer chemotherapy.
Neoplasms
Synthesis and biological properties of Quilamines II, new iron chelators with antiproliferative activities.
Neoplasms
Tailoring of silica-based nanoporous pod by spermidine multi-activity.
Neoplasms
Targeting the Polyamine Transport System with Benzazepine- and Azepine-Polyamine Conjugates ().
Neoplasms
The antitumor drug F14512 enhances cisplatin and ionizing radiation effects in head and neck squamous carcinoma cell lines.
Neoplasms
The polyamine analog PG11047 potentiates the antitumor activity of cisplatin and bevacizumab in preclinical models of lung and prostate cancer.
Neoplasms
The potential of a novel polyamine transport inhibitor in cancer chemotherapy.
Neuroblastoma
Characterization of the polyamine transport system in mouse neuroblastoma cells. Effects of sodium and system A amino acids.
Ovarian Neoplasms
Phase I dose-escalation study of F14512, a polyamine-vectorized topoisomerase II inhibitor, in patients with platinum-refractory or resistant ovarian cancer.
Prostatic Neoplasms
Selective exclusion by the polyamine transporter as a mechanism for differential radioprotection of amifostine derivatives.
Pulmonary Arterial Hypertension
ATP13A3 is a major component of the enigmatic mammalian polyamine transport system.
Sarcoma
The potential of a novel polyamine transport inhibitor in cancer chemotherapy.
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brenda
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brenda
genes sapABCDF encoding probable ABC transporter periplasmic-binding protein SapA, putrescine export system permease proteins SapB and SapC, putrescine export system ATP-binding proteins SapD and SapF
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
UniProt
brenda
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-
brenda
-
-
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brenda
-
-
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brenda
genes all5044, all5043, and all5042, encoding spermidine/putrescine import ATP-binding protein PotA, polyamine-binding protein of polyamine ABC transporter PotD, and permease protein of polyamine ABC transporter PotB; i.e. Anabaena sp. PCC 7120
UniProt
brenda
genes all5044, all5043, and all5042, encoding spermidine/putrescine import ATP-binding protein PotA, polyamine-binding protein of polyamine ABC transporter PotD, and permease protein of polyamine ABC transporter PotB; i.e. Anabaena sp. PCC 7120
UniProt
brenda
genes all5044, all5043, and all5042, encoding spermidine/putrescine import ATP-binding protein PotA, polyamine-binding protein of polyamine ABC transporter PotD, and permease protein of polyamine ABC transporter PotB; i.e. Anabaena sp. PCC 7120
UniProt
brenda
genes potA, potB, potC, and potD encoding spermidine/putrescine import ATP-binding protein PotA, spermidine/putrescine ABC transporter permease PotB, spermidine/putrescine ABC transporter permease protein PotC, and spermidine/putrescine-binding periplasmic protein PotD; isolated from a diseased pig in Sichuan province of China
UniProt
brenda
genes potA, potB, potC, and potD encoding spermidine/putrescine import ATP-binding protein PotA, spermidine/putrescine ABC transporter permease PotB, spermidine/putrescine ABC transporter permease protein PotC, and spermidine/putrescine-binding periplasmic protein PotD; isolated from a diseased pig in Sichuan province of China
UniProt
brenda
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brenda
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brenda
genes sapABCDF encoding probable ABC transporter periplasmic-binding protein SapA, putrescine export system permease proteins SapB and SapC, putrescine export system ATP-binding proteins SapD and SapF
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
UniProt
brenda
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evolution
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
SapABCDF is specifically distributed within gamma-proteobacteria
evolution
-
SapABCDF is specifically distributed within gamma-proteobacteria
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malfunction
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
deletion of sapBCDF significantly decreases putrescine levels in the cell culture supernatant, and the DELTAsapBCDF strain does not facilitate uptake of putrescine from the culture supernatant. Complementation of the deletion mutant with the sapBCDF genes restores putrescine levels in the culture supernatant. Putrescine concentration of the culture supernatant is not influenced by DELTAsapA but is affected by DELTAsapBCDF. The Escherichia coli DELTAsapBCDF strain does not show affected resistance to antimicrobial peptide LL-37t
malfunction
inactivation of the gene cluster potADB, encoding a polyamine ABC transporter disrupted diazotrophic growth, corroborates the importance of polyamine homeostasis in Nostoc sp. PCC 7120
malfunction
PotA deletion disrupts normal peptidoglycan synthesis and hampers cell elongation. In contrast to the wild-type, the mutant DELTApotA exhibits elongated chain length and abnormal cell division morphology. Phenotypic changes are attributed to be the upregulation of genes involved in peptidoglycan (PG) synthesis and hydrolysis in DELTApotA. Cultivation of strain SC-19 in presence of excessive spermidine or spermine displays attenuated growth
malfunction
-
PotA deletion disrupts normal peptidoglycan synthesis and hampers cell elongation. In contrast to the wild-type, the mutant DELTApotA exhibits elongated chain length and abnormal cell division morphology. Phenotypic changes are attributed to be the upregulation of genes involved in peptidoglycan (PG) synthesis and hydrolysis in DELTApotA. Cultivation of strain SC-19 in presence of excessive spermidine or spermine displays attenuated growth
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malfunction
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inactivation of the gene cluster potADB, encoding a polyamine ABC transporter disrupted diazotrophic growth, corroborates the importance of polyamine homeostasis in Nostoc sp. PCC 7120
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malfunction
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inactivation of the gene cluster potADB, encoding a polyamine ABC transporter disrupted diazotrophic growth, corroborates the importance of polyamine homeostasis in Nostoc sp. PCC 7120
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malfunction
-
deletion of sapBCDF significantly decreases putrescine levels in the cell culture supernatant, and the DELTAsapBCDF strain does not facilitate uptake of putrescine from the culture supernatant. Complementation of the deletion mutant with the sapBCDF genes restores putrescine levels in the culture supernatant. Putrescine concentration of the culture supernatant is not influenced by DELTAsapA but is affected by DELTAsapBCDF. The Escherichia coli DELTAsapBCDF strain does not show affected resistance to antimicrobial peptide LL-37t
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metabolism
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
the enzyme complex SapBCDF exports putrescine from Escherichia coli cells to the culture supernatant, which is the natural function of the SapBCDF proteins, while PotABCD is a spermidine transporter of the ABC transporter family that takes up putrescine with lower affinity. Mechanism of polyamine export from bacterial cells to the intestinal lumen. PuuP is a putrescine importer dependent on proton-motive force and is indispensable when Escherichia coli grows on putrescine as a sole carbon or nitrogen source. PlaP is a proton-dependent putrescine importer that is important when Escherichia coli exhibits surface motility. PotE is responsible for both excretion and uptake of putrescine. PotE is a proton-dependent putrescine importer at neutral pH, but at acidic pH PotE is a putrescine-ornithine antiporter
metabolism
-
the enzyme complex SapBCDF exports putrescine from Escherichia coli cells to the culture supernatant, which is the natural function of the SapBCDF proteins, while PotABCD is a spermidine transporter of the ABC transporter family that takes up putrescine with lower affinity. Mechanism of polyamine export from bacterial cells to the intestinal lumen. PuuP is a putrescine importer dependent on proton-motive force and is indispensable when Escherichia coli grows on putrescine as a sole carbon or nitrogen source. PlaP is a proton-dependent putrescine importer that is important when Escherichia coli exhibits surface motility. PotE is responsible for both excretion and uptake of putrescine. PotE is a proton-dependent putrescine importer at neutral pH, but at acidic pH PotE is a putrescine-ornithine antiporter
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physiological function
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
the natural function of the SapBCDF enzyme complex is the export of putrescine, Escherichia coli can grow on putrescine as a sole carbon or nitrogen source
physiological function
the polyamine transport system PotABCD in Streptococcus suis can uptake polyamines preferably spermidine and spermine. Spermidine and putrescine have been found to be constituents of the cell wall peptidoglycan, these molecules maintain the integrity of the cell surface structure and normal cell growth. The known de novo synthesis pathway is not observed in strain SC-19 according to the genome of the strain. Regulatory roles of polyamine on polyamine transport and peptidoglycan (PG) synthesis. Polyamines function not only as feedback regulators of PotA by inhibiting PotA activity but also as regulators on potABCD and genes involved in PG synthesis. The binding of high-concentration spermidine to PotA decreases the ATPase activity and inhibits polyamine transport. PotD can downregulate the transcription of the potABCD operon. Thus, both receptor and ligand can function as feedback regulators of polyamine transport
physiological function
-
the polyamine transport system PotABCD in Streptococcus suis can uptake polyamines preferably spermidine and spermine. Spermidine and putrescine have been found to be constituents of the cell wall peptidoglycan, these molecules maintain the integrity of the cell surface structure and normal cell growth. The known de novo synthesis pathway is not observed in strain SC-19 according to the genome of the strain. Regulatory roles of polyamine on polyamine transport and peptidoglycan (PG) synthesis. Polyamines function not only as feedback regulators of PotA by inhibiting PotA activity but also as regulators on potABCD and genes involved in PG synthesis. The binding of high-concentration spermidine to PotA decreases the ATPase activity and inhibits polyamine transport. PotD can downregulate the transcription of the potABCD operon. Thus, both receptor and ligand can function as feedback regulators of polyamine transport
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physiological function
-
the natural function of the SapBCDF enzyme complex is the export of putrescine, Escherichia coli can grow on putrescine as a sole carbon or nitrogen source
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additional information
ABC uptake transporters typically comprise one periplasmic solute-binding protein (SBP), two integral membrane proteins (transmembrane domains [TMD]) and two nucleotide-binding domains (NBD) that hydrolyze ATP in the cytoplasm, in which the TMD and NBD may be homo- or heterodimers
additional information
the putative potABCD operon is co-transcribed with gene murB encoding UDP-N-acetylenolpyruvoylglucosamine reductase, EC 1.3.1.98, also involved in peptidoglycan synthesis
additional information
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the putative potABCD operon is co-transcribed with gene murB encoding UDP-N-acetylenolpyruvoylglucosamine reductase, EC 1.3.1.98, also involved in peptidoglycan synthesis
additional information
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the putative potABCD operon is co-transcribed with gene murB encoding UDP-N-acetylenolpyruvoylglucosamine reductase, EC 1.3.1.98, also involved in peptidoglycan synthesis
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additional information
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ABC uptake transporters typically comprise one periplasmic solute-binding protein (SBP), two integral membrane proteins (transmembrane domains [TMD]) and two nucleotide-binding domains (NBD) that hydrolyze ATP in the cytoplasm, in which the TMD and NBD may be homo- or heterodimers
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additional information
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ABC uptake transporters typically comprise one periplasmic solute-binding protein (SBP), two integral membrane proteins (transmembrane domains [TMD]) and two nucleotide-binding domains (NBD) that hydrolyze ATP in the cytoplasm, in which the TMD and NBD may be homo- or heterodimers
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29000
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? * 43000 + ? * 31000 + ? * 29000 + ? * 39000, potA, potB, potC and potD subunits respectively, spermidine-preferential system, calculated from amino acid sequence
35000
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? * 38000 + ? * 45000 + ? * 31000 + ? * 35000, potF, potG, potH and potI subunits respectively, putrescine-specific system, calculated from amino acid sequence
38000
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? * 38000 + ? * 45000 + ? * 31000 + ? * 35000, potF, potG, potH and potI subunits respectively, putrescine-specific system, calculated from amino acid sequence
39000
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? * 43000 + ? * 31000 + ? * 29000 + ? * 39000, potA, potB, potC and potD subunits respectively, spermidine-preferential system, calculated from amino acid sequence
43000
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? * 43000 + ? * 31000 + ? * 29000 + ? * 39000, potA, potB, potC and potD subunits respectively, spermidine-preferential system, calculated from amino acid sequence
45000
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? * 38000 + ? * 45000 + ? * 31000 + ? * 35000, potF, potG, potH and potI subunits respectively, putrescine-specific system, calculated from amino acid sequence
31000
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? * 38000 + ? * 45000 + ? * 31000 + ? * 35000, potF, potG, potH and potI subunits respectively, putrescine-specific system, calculated from amino acid sequence
31000
-
? * 43000 + ? * 31000 + ? * 29000 + ? * 39000, potA, potB, potC and potD subunits respectively, spermidine-preferential system, calculated from amino acid sequence
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?
x * 49000, recombinant His-tagged PotA, SDS-PAGE, x * 38000, recombinant His-tagged PotD, SDS-PAGE
?
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x * 49000, recombinant His-tagged PotA, SDS-PAGE, x * 38000, recombinant His-tagged PotD, SDS-PAGE
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oligomer
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? * 38000 + ? * 45000 + ? * 31000 + ? * 35000, potF, potG, potH and potI subunits respectively, putrescine-specific system, calculated from amino acid sequence
oligomer
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? * 43000 + ? * 31000 + ? * 29000 + ? * 39000, potA, potB, potC and potD subunits respectively, spermidine-preferential system, calculated from amino acid sequence
additional information
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the enzyme is a ATP-binding cassette transporter
additional information
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the enzyme is a ATP-binding cassette transporter
additional information
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the PotD protein consists of two domains with an alterating beta-alpha-beta topology
additional information
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the spermidine-preferential uptake system consists of 4 proteins, that are all necessary for spermidine uptake: PotA, PotB, PotC and PotD. The calculated molecular weights are 43000 Da for PotA, 31000 Da for PotB, 29000 Da for PotC and 39000 Da for PotD. The putrescine-uptake system consists of the 4 proteins: PotF, PotG, PotH and PotI. All 4 proteins are necessary for maximal putrescine transport. PotF is a 38000 Da putrescine binding protein, PotG is a 45000 Da membrane-associated ATPase, PotH and PotI are 31000-35000 Da channel-forming proteins
additional information
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the enzyme is a ATP-binding cassette transporter
additional information
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the enzyme is a ATP-binding cassette transporter
additional information
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the enzyme is a ATP-binding cassette transporter
additional information
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the enzyme is a ATP-binding cassette transporter
additional information
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the enzyme is a ATP-binding cassette transporter
additional information
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the enzyme is a ATP-binding cassette transporter
additional information
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the enzyme is a ATP-binding cassette transporter
additional information
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PotA protein and PotD protein are absolutely necessary for spermidine uptake in conjugation with the two channel forming proteins PotB and PotC
additional information
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the enzyme is a ATP-binding cassette transporter
additional information
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the enzyme is a ATP-binding cassette transporter
additional information
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the enzyme is a ATP-binding cassette transporter
additional information
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the enzyme is a ATP-binding cassette transporter
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C26A
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no loss of ATPase activity
C276A
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no loss of ATPase activity
C54T
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mutated PotA protein loses both ATPase and spermidine uptake activity
D172N
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potA subunit, inactive mutant
E297D
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potA subunit, spermidine uptake activity is greately reduced
E297K
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potA subunit, spermidine uptake activity is reduced
E297Q
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potA subunit, spermidine uptake activity is greately reduced
F27L
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potA subunit, spermidine uptake activity is reduced
F47L
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potA subunit, spermidine uptake activity is reduced
L60F
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potA subunit, spermidine uptake activity is reduced
L76P
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spermidine uptake activity is reduced
additional information
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construction of mutants truncated at the carboxylic terminal domain of the potA subunit, these mutants have reduced activity
additional information
Q47622; P0AGH3; P0AGH5; P0AAH4; P0AAH8
generation of several sap gene deletion mutants, phenotypes, overview. Deletion of sapBCDF significantly decreases putrescine levels in the cell culture supernatant, and the DELTAsapBCDF strain does not facilitate uptake of putrescine from the culture supernatant. Complementation of the deletion mutant with the sapBCDF genes restores putrescine levels in the culture supernatant. Putrescine concentration of the culture supernatant is not influenced by DELTAsapA but is affected by DELTAsapBCDF. The Escherichia coli DELTAsapBCDF strain does not show affected resistance to antimicrobial peptide LL-37t
additional information
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generation of several sap gene deletion mutants, phenotypes, overview. Deletion of sapBCDF significantly decreases putrescine levels in the cell culture supernatant, and the DELTAsapBCDF strain does not facilitate uptake of putrescine from the culture supernatant. Complementation of the deletion mutant with the sapBCDF genes restores putrescine levels in the culture supernatant. Putrescine concentration of the culture supernatant is not influenced by DELTAsapA but is affected by DELTAsapBCDF. The Escherichia coli DELTAsapBCDF strain does not show affected resistance to antimicrobial peptide LL-37t
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additional information
inactivation of the gene cluster potADB
additional information
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inactivation of the gene cluster potADB
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additional information
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inactivation of the gene cluster potADB
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Sugiyama, S.; Matsuo, Y.; Maenaka, K.; Vassylyev, D.G.; Matsushima, M.; Kashiwagi, K.; Igarashi, K.; Mirikawa, K.
The 1.8-A X-ray structure of the Escherichia coli PotD protein complexed with spermidine and the mechanism of polyamine binding
Protein Sci.
5
1984-1990
1996
Escherichia coli
brenda
Kashiwagi, K.; Miyamoto, S.; Nukui, E.; Kobayashi, H.; Igarashi, K.
Functions of PotA and PotD proteins in spermidine-preferential uptake system in Escherichia coli
J. Biol. Chem.
268
19358-19363
1993
Escherichia coli
brenda
Meksuriyen, D.; Fukuchi-Shimogori, T.; Tomitori, H.; Kashiwagi, K.; Toida, T.; Imanari, T.; Kawai, G.; Igarashi, K.
Formation of a complex containing ATP, Mg2+, and spermine. Structural evidence and biological significance
J. Biol. Chem.
273
30939-30944
1998
Escherichia coli
brenda
Kashiwagi, K.; Endo, H.; Kobayashi, H.; Igarashi, K.
Spermidine-preferential uptake system in Escherichia coli. ATP hydrolysis by PotA protein and its association with membranes
J. Biol. Chem.
270
25377-25382
1995
Escherichia coli
brenda
Sugiyama, S.; Vassylyev, D.G.; Matsushima, M.; Kashiwagi, K.; Igarashi, K.; Morikawa, K.
Crystal structure of potD, the primary receptor of the poylamine transport system in Escherichia coli
J. Biol. Chem.
271
9519-9525
1996
Escherichia coli
brenda
Kashiwagi, K.; Pistocchi, R.; Shibuya, S.; Sugiyama, S; Morikawa, K.; Igarashi, K.
Spermidine-preferential uptake system in Escherichia coli. Identification of amino acids involved in polyamine binding in PotD proteins
J. Biol. Chem.
271
12205-12208
1996
Escherichia coli
brenda
Igarashi, K.; Kashiwagi, K.
Polyamine transport in bacteria and yeast
Biochem. J.
344
633-642
1999
Archaeoglobus fulgidus, Borreliella burgdorferi, Escherichia coli, Haemophilus influenzae, Mycoplasma genitalium, Mycoplasma pneumoniae, Treponema pallidum
brenda
Kashiwagi, K.; Innami, A.; Zenda, R.; Tomitori, H.; Igarashi, K.
The ATPase activity and the functional domain of PotA, a component of the sermidine-preferential uptake system in Escherichia coli
J. Biol. Chem.
277
24212-24219
2002
Escherichia coli
brenda
Igarashi, K.; Ito, K.; Kashiwagi, K.
Polyamine uptake systems in Escherichia coli
Res. Microbiol.
152
271-278
2001
Escherichia coli
brenda
Sugiyama, Y.; Nakamura, A.; Matsumoto, M.; Kanbe, A.; Sakanaka, M.; Higashi, K.; Igarashi, K.; Katayama, T.; Suzuki, H.; Kurihara, S.
A novel putrescine exporter SapBCDF of Escherichia coli
J. Biol. Chem.
291
26343-26351
2016
Escherichia coli (Q47622 AND P0AGH3 AND P0AGH5 AND P0AAH4 AND P0AAH8), Escherichia coli MG1655 (Q47622 AND P0AGH3 AND P0AGH5 AND P0AAH4 AND P0AAH8)
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brenda
Liu, W.; Tan, M.; Zhang, C.; Xu, Z.; Li, L.; Zhou, R.
Functional characterization of murB-potABCD operon for polyamine uptake and peptidoglycan synthesis in Streptococcus suis
Microbiol. Res.
207
177-187
2018
Streptococcus suis (A0A142UTH4 AND A0A0K2E5X6 AND G7SFQ8 AND A0A116LEI2), Streptococcus suis, Streptococcus suis SC-19 (A0A142UTH4 AND A0A0K2E5X6 AND G7SFQ8 AND A0A116LEI2)
brenda
Burnat, M.; Li, B.; Kim, S.; Michael, A.; Flores, E.
Homospermidine biosynthesis in the cyanobacterium Anabaena requires a deoxyhypusine synthase homologue and is essential for normal diazotrophic growth
Mol. Microbiol.
109
763-780
2018
Nostoc sp. PCC 7120 = FACHB-418 (Q8YM92 AND Q8YM93 AND Q8YM94), Nostoc sp. PCC 7120 = FACHB-418 UTEX 2576 (Q8YM92 AND Q8YM93 AND Q8YM94), Nostoc sp. PCC 7120 = FACHB-418 SAG 25.82 (Q8YM92 AND Q8YM93 AND Q8YM94)
brenda