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Information on EC 1.14.13.163 - 6-hydroxy-3-succinoylpyridine 3-monooxygenase
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EC Tree
1.14.13.163 6-hydroxy-3-succinoylpyridine 3-monooxygenaseIUBMB Comments
The enzyme catalyses a reaction in the nicotine degradation pathway of Pseudomonas species. One of the enzymes from the soil bacterium Pseudomonas putida S16 contains an FAD cofactor .
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Word Map
- 1.14.13.163
- pyrrolidine
- putida
- 2,5-dihydroxypyridine
- tumefaciens
-
agrobacterium
- arthrobacter
-
fad-binding
-
ochrobactrum
- wastes
- synthesis
-
nicotine-degrading
- flavoprotein
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
hsp hydroxylase, nicotine hydroxylase, 6-hydroxy-3-succinoylpyridine hydroxylase, nadh-dependent hsp hydroxylase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
6-hydroxy-3-succinoyl-pyridine 3-monooxygenase
6-hydroxy-3-succinoylpyridine hydroxylase
AWN88_01205
Hsh
HSP 3-monooxygenase
HSP hydroxylase
HSP monooxygenase
hspA
-
-
-
-
hspB
HSPH
NADH-dependent HSP hydroxylase
NIC
W7K_00670
6-hydroxy-3-succinoylpyridine hydroxylase
-
-
-
-
hspB
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2 = 2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2 = 2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
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-
-
-
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2 = 2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
catalytic mechanism, overview. In contrast to conclusions reported previously, the second product of the HspB reaction is shown to be succinate, with isotope labeling experiments providing direct evidence that the newly introduced oxygen atom of succinate is derived from H2O. Reduced HspB reacts with oxygen to form a C(4a)-(hydro)peroxyflavin intermediate before it is converted to the oxidized flavoenzyme species. The formed C(4a)-hydroperoxyflavin intermediate reacts with HSP to form an intermediate that is hydrolyzed to the products 2,5-dihydroxypyridine and succinate
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4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2 = 2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
catalytic mechanism, overview. In contrast to conclusions reported previously, the second product of the HspB reaction is shown to be succinate, with isotope labeling experiments providing direct evidence that the newly introduced oxygen atom of succinate is derived from H2O. Reduced HspB reacts with oxygen to form a C(4a)-(hydro)peroxyflavin intermediate before it is converted to the oxidized flavoenzyme species. The formed C(4a)-hydroperoxyflavin intermediate reacts with HSP to form an intermediate that is hydrolyzed to the products 2,5-dihydroxypyridine and succinate
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-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate,NADH:oxygen oxidoreductase (3-hydroxylating, succinate semialdehyde releasing)
The enzyme catalyses a reaction in the nicotine degradation pathway of Pseudomonas species. One of the enzymes from the soil bacterium Pseudomonas putida S16 contains an FAD cofactor [2].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
6-hydroxy-3-succinoylpyridine + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
oxidative decarboxylation of HSP to 2,5-dihydroxypyridine in presence of NADH and FAD
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
oxidative decarboxylation of HSP to 2,5-dihydroxypyridine in presence of NADH and FAD
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
the enzyme efficiently catalyzes the conversion of 6-hydroxy-3-succinoylpyridine (HSP) into 2,5-dihydroxypyridine (2,5-DHP) and succinic acid in the presence of NADH and FAD
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-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
Stenotrophomonas geniculata
-
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
Stenotrophomonas geniculata N1
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-
-
?
6-hydroxy-3-succinoylpyridine + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
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-
-
-
?
6-hydroxy-3-succinoylpyridine + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
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-
-
-
?
additional information
?
-
no activity with p-nitrophenol or 6-hydroxynicotinate as substrates
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-
?
additional information
?
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no activity with p-nitrophenol or 6-hydroxynicotinate as substrates
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?
additional information
?
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no activity with p-nitrophenol or 6-hydroxynicotinate as substrates
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-
?
additional information
?
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mass spectrometric analysis of substrates and products, with recombinant enzyme
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-
?
additional information
?
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mass spectrometric analysis of substrates and products, with recombinant enzyme
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-
?
additional information
?
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assay method optimization, overview. Product identification by LC-MS
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
-
?
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate + 2 NADH + 2 H+ + O2
2,5-dihydroxypyridine + succinate semialdehyde + 2 NAD+ + H2O
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the enzyme is not significantly affected by Ni2+, Ca2+, K+, and Na+ at 5 mM. The enzyme is no metalloenzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no inhibition by Twen-20, Tween-40, and Tween-80 at 1% w/v
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6-hydroxy-3-succinoylpyridine
acts as an initial effector and strongly stimulates NADH oxidation
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
stopped-flow spectroscopy and kinetic analysis
-
0.0359
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate
Stenotrophomonas geniculata
pH 8, 25°C
0.173
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate
-
pH 8.0, 25°C, recombinant His-tagged enzyme
0.201
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate
pH 8.0, 25°C, recombinant His-tagged enzyme
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.74
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate
-
pH 8.0, 25°C, recombinant His-tagged enzyme
21.6
4-(6-hydroxypyridin-3-yl)-4-oxobutanoate
pH 8.0, 25°C, recombinant His-tagged enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from soil samples obtained from a field under continuous tobacco cropping in Henan, P.R. China
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brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
strain SJY uses nicotine as a sole source of carbon, nitrogen, and energy
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
-
phylogenetic analysis reveals that HspB is the most closely related to two p-nitrophenol 4-monooxygenases, and the experimental results exhibit that p-nitrophenol is a substrate of HspB
evolution
sequence alignment and phylogenetic analysis suggests that the VPP pathway, which evolved independently from nicotinic acid degradation, might have a closer relationship with the pyrrolidine pathway
evolution
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phylogenetic analysis reveals that HspB is the most closely related to two p-nitrophenol 4-monooxygenases, and the experimental results exhibit that p-nitrophenol is a substrate of HspB
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metabolism
6-hydroxy-3-succinoylpyridine hydroxylase catalyzes a central step of nicotine degradation. 6-Hydroxy-3-succinoylpyridine (HSP) is a key intermediate connecting the two pathways, pyridine pathway and pyrrolidine pathway, detailed overview
metabolism
6-hydroxy-3-succinoylpyridine hydroxylase catalyzes a central step of nicotine degradation. 6-Hydroxy-3-succinoylpyridine (HSP) is a key intermediate connecting the two pathways, pyridine pathway and pyrrolidine pathway, overview
metabolism
strain SJY1 efficiently degrades nicotine via a variant of the pyridine and pyrrolidine pathways (the VPP pathway), highlighting bacterial metabolic diversity in relation to nicotine degradation, a 97-kbp DNA fragment containing six nicotine degradation-related genes is obtained by gap closing from the genome sequence of strain SJY1, gene vppD gene encodes an NADH-dependent flavin-containing monooxygenase, which catalyzes the hydroxylation of 6-hydroxy-3-succinoylpyridine to 2,5-dihydroxypyridine. Nicotine degradation pathway in strain SJY1, detailed overview
metabolism
-
6-hydroxy-3-succinoylpyridine hydroxylase catalyzes a central step of nicotine degradation. 6-Hydroxy-3-succinoylpyridine (HSP) is a key intermediate connecting the two pathways, pyridine pathway and pyrrolidine pathway, detailed overview
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metabolism
-
6-hydroxy-3-succinoylpyridine hydroxylase catalyzes a central step of nicotine degradation. 6-Hydroxy-3-succinoylpyridine (HSP) is a key intermediate connecting the two pathways, pyridine pathway and pyrrolidine pathway, overview
-
physiological function
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strain S33 can transform nicotine into renewable hydroxylated-pyridine intermediates by a special pathway, in which at least three intermediates, 6-hydroxy-L-nicotine, 6-hydroxy-3-succinoylpyridine, and 2,5-dihydroxypyridine, have potential to be further chemically modified into useful compounds. Strain S33 is able to transform nicotine to 6-hydroxy-pseudooxynicotine first via the pyridine pathway through 6-hydroxy-L-nicotine and 6-hydroxy-N-methylmyosmine, and then, it turns to the pyrrolidine pathway with the formation of 6-hydroxy-3-succinoylpyridine and 2,5-dihydroxypyridine
physiological function
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6-hydroxy-3-succinoyl-pyridine (HSP) 3-monooxygenase (HspB) is a flavoprotein essential to the pyrrolidine pathway of nicotine degradation, it catalyzes pyridine-ring beta-hydroxylation, resulting in carbon-carbon cleavage and production of 2,5-dihydroxypyridine
physiological function
the key enzyme HSP hydroxylase is involved in the fused nicotine degradation pathway of the pyridine and pyrrolidine pathways
physiological function
-
strain S33 can transform nicotine into renewable hydroxylated-pyridine intermediates by a special pathway, in which at least three intermediates, 6-hydroxy-L-nicotine, 6-hydroxy-3-succinoylpyridine, and 2,5-dihydroxypyridine, have potential to be further chemically modified into useful compounds. Strain S33 is able to transform nicotine to 6-hydroxy-pseudooxynicotine first via the pyridine pathway through 6-hydroxy-L-nicotine and 6-hydroxy-N-methylmyosmine, and then, it turns to the pyrrolidine pathway with the formation of 6-hydroxy-3-succinoylpyridine and 2,5-dihydroxypyridine
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physiological function
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the key enzyme HSP hydroxylase is involved in the fused nicotine degradation pathway of the pyridine and pyrrolidine pathways
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physiological function
-
6-hydroxy-3-succinoyl-pyridine (HSP) 3-monooxygenase (HspB) is a flavoprotein essential to the pyrrolidine pathway of nicotine degradation, it catalyzes pyridine-ring beta-hydroxylation, resulting in carbon-carbon cleavage and production of 2,5-dihydroxypyridine
-
additional information
-
free H2O2 does not catalyze the HspB enzyme reaction
additional information
the ativity of VppD is 10fold higher than the activity of the hydroxylase (HspB) from Pseudomonas putida strain S16
additional information
-
free H2O2 does not catalyze the HspB enzyme reaction
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A0P1GWL9_9RHOB
208
0
23549
TrEMBL
-
A0A6V7BV08_9XANT
318
0
36210
TrEMBL
-
A0A2S6UVF6_9PROT
401
1
45564
TrEMBL
-
A0A5J4PGN9_9ZZZZ
211
0
24611
TrEMBL
other Location (Reliability: 2)
A0A2S6U000_9PROT
403
1
45432
TrEMBL
-
A0A011PHW2_9PROT
206
0
23724
TrEMBL
-
A0A5J4Q8R6_9ZZZZ
55
0
6258
TrEMBL
other Location (Reliability: 3)
A0A5J4QAB2_9ZZZZ
212
0
24761
TrEMBL
other Location (Reliability: 2)