1.8.99.2: adenylyl-sulfate reductase
This is an abbreviated version!
For detailed information about adenylyl-sulfate reductase, go to the full flat file.
Word Map on EC 1.8.99.2
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1.8.99.2
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resection
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abdominoperineal
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rectal
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postoperative
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women
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anal
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perineal
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pelvic
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preoperative
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acute-phase
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5-year
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curative
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laparoscopic
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rust
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demographic
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radiotherapy
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oncological
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admission
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c-reactive
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population-based
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neoadjuvant
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anorectal
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puccinia
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sphincter
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intraoperative
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colostomy
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tritici
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verge
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chemoradiation
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chemoradiotherapy
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ontario
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circumferential
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haptoglobin
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flap
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poisson
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incontinence
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abdominis
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zoledronic
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stoma
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mesorectal
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dehiscence
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anastomosis
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exenteration
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synthesis
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analysis
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ileostomy
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levator
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agriculture
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environmental protection
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actuarial
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log-binomial
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orthoped
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race-specific
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psycinfo
- 1.8.99.2
-
resection
-
abdominoperineal
- rectal
-
postoperative
- women
-
anal
-
perineal
-
pelvic
-
preoperative
-
acute-phase
-
5-year
-
curative
-
laparoscopic
- rust
-
demographic
-
radiotherapy
-
oncological
-
admission
-
c-reactive
-
population-based
-
neoadjuvant
-
anorectal
- puccinia
-
sphincter
-
intraoperative
-
colostomy
- tritici
-
verge
-
chemoradiation
-
chemoradiotherapy
-
ontario
-
circumferential
- haptoglobin
- flap
-
poisson
- incontinence
-
abdominis
-
zoledronic
-
stoma
-
mesorectal
-
dehiscence
-
anastomosis
-
exenteration
- synthesis
- analysis
-
ileostomy
-
levator
- agriculture
- environmental protection
-
actuarial
-
log-binomial
-
orthoped
-
race-specific
-
psycinfo
Reaction
Synonyms
5'-adenylyl sulfate reductase, 5'-adenylylsulfate reductase, 5-adenylylsulfate reductase, AcAPR1, adenosine 5'-phosphosulfate reductase, adenosine phosphosulfate reductase, adenosine-5'-phosphosulfate reductase, adenylyl sulfate reductase, adenylylsulfate reductase, adenylylsulphate reductase, AdoPSO4 reductase, AMP,sulfite:flavin oxidoreductase, APR, APR1, APR2, APR3, AprA, AprB, AprBA, APS reductase, APS-reductase, APSR, AR, ATAPR2, Dde_1110, dissimilatory APS reductase, EAPR, EiAPR, FAD, FeS-enzyme adenosine-5'-phosphosulfate reductase, LMAPR, reductase, adenylylsulfate
ECTree
1.8.99.2 adenylyl-sulfate reductaseAdvanced search results
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Cloned on EC 1.8.99.2 - adenylyl-sulfate reductase
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CLONED (Commentary) 
ORGANISM
UNIPROT
LITERATURE
expressed in Eschericha coli as the N-terminal reductase domain (AcAPR1-N) and the C-terminal glutaredoxin domain (AcAPR1-C). Recombinant full-length ATP sulfurylase (AcATPS1) and recombinant full length adenosine-5'-phosphosulfate reductase (AcAPR1) from Allium cepa can form a physical association
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expressed in Escherichia coli
expression in Escherichia coli of a recombinant His-tagged protein and several mutants
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full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
gene apsA, PCR-based DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression in Escherichia coli
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genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
localized expression in plastids of Arabidopsis thaliana, transgenic plants accumulate sulfite, thiosulfate, cysteine and gluthatione
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overexpression in Escherichia coli
overexpression of a His-tagged recombinant protein in Escherichia coli
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full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
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full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
-
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
-
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
-
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
Desulforamulus reducens
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full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
-
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
full-length AprBA sequences from 20 phylogenetically distinct sulfate-reducing prokaryotes and sulfuroxidizing bacteria species are used for homology modeling. Based on the comparative models, there are no significant structural differences between dissimilatory APS reductases from sulfate-reducing prokaryotes and sulfur-oxidizing bacteria. This might be indicative for a similar catalytic process of APS reduction/sulfite oxidation
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genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
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genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
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genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
-
genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
-
genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
-
genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
-
genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
-
genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
genes aprA and aprB, DNA and amino acid sequence determination and phylogenetic analysis, AprBA tree topology and the composition/arrangement of the apr gene loci, overview
