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Information on EC 6.3.5.10 - adenosylcobyric acid synthase (glutamine-hydrolysing)
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6.3.5.10 adenosylcobyric acid synthase (glutamine-hydrolysing)IUBMB Comments
Requires Mg2+. NH3 can act instead of glutamine. This enzyme catalyses the four-step amidation sequence from cobyrinic acid a,c-diamide to cobyric acid via the formation of cobyrinic acid triamide, tetraamide and pentaamide intermediates.
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The expected taxonomic range for this enzyme is: Archaea, Bacteria
Synonyms
cobyric acid synthase, cobyric acid synthetase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5'-deoxy-5'-adenosylcobyrinic-acid-a,c-diamide:L-glutamine amido-ligase
-
-
-
-
Ado-cobyric acid synthase (glutamine hydrolyzing)
-
-
-
-
CbiP
CobQ
cobyric acid synthase
additional information
-
CobQ is a member of the dethiobiotin synthetase superfamily
CobQ
-
-
-
-
cobyric acid synthase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4 ATP + adenosylcobyrinic acid a,c-diamide + 4 L-glutamine + 4 H2O = 4 ADP + 4 phosphate + adenosylcobyric acid + 4 L-glutamate
4 ATP + adenosylcobyrinic acid a,c-diamide + 4 L-glutamine + 4 H2O = 4 ADP + 4 phosphate + adenosylcobyric acid + 4 L-glutamate
catalytic mechanism
-
4 ATP + adenosylcobyrinic acid a,c-diamide + 4 L-glutamine + 4 H2O = 4 ADP + 4 phosphate + adenosylcobyric acid + 4 L-glutamate
Requires Mg2+. NH3 can act instead of glutamine. This enzyme catalyses the four-step amidation sequence from cobyrinic acid a,c-diamide to cobyric acid via the formation of cobyrinic acid triamide, tetraamide and pentaamide intermediates
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
adenosylcobyrinic-acid-a,c-diamide:L-glutamine amido-ligase (ADP-forming)
Requires Mg2+. NH3 can act instead of glutamine. This enzyme catalyses the four-step amidation sequence from cobyrinic acid a,c-diamide to cobyric acid via the formation of cobyrinic acid triamide, tetraamide and pentaamide intermediates.
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CAS REGISTRY NUMBER
COMMENTARY
137672-90-3
-
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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
adenosylcobyrinic acid a,c-diamide + ATP + L-glutamine + H2O
adenosylcobyric acid + ADP + phosphate + L-glutamate
ATP + adenosylcobyrinic acid a,c-diamide + ammonia + H2O
ADP + phosphate + adenosylcobyric acid + ?
-
ammonia can replace L-glutamine as amide group donor, but L-glutamine is preferred
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
ATP + adenosylcobyrinic acid diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
four carboxylates attached to the corrinoid ring are amidated in a dissociative fashion. The four carboxylates are amidated in a sequence beginning with carboxylate e and followed in turn by carboxylates d, b, and g
-
-
?
ATP + adenosylcobyrinic acid pentaamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
ATP + adenosylcobyrinic acid tetraamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
ATP + adenosylcobyrinic acid triamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
cobinic acid a,c-diamide + ATP + L-glutamine + H2O
cobinamide + ADP + phosphate + L-glutamate
adenosylcobyrinic acid a,c-diamide + ATP + L-glutamine + H2O
adenosylcobyric acid + ADP + phosphate + L-glutamate
-
-
-
?
adenosylcobyrinic acid a,c-diamide + ATP + L-glutamine + H2O
adenosylcobyric acid + ADP + phosphate + L-glutamate
-
vitamin B12 biosynthesis
-
?
adenosylcobyrinic acid a,c-diamide + ATP + L-glutamine + H2O
adenosylcobyric acid + ADP + phosphate + L-glutamate
-
-
-
?
adenosylcobyrinic acid a,c-diamide + ATP + L-glutamine + H2O
adenosylcobyric acid + ADP + phosphate + L-glutamate
Pseudomonas denitrificans (nom. rej.) SC510 RifT
-
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
-
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
cobinamide biosynthesis
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
-
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
cobinamide biosynthesis
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
-
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
biosynthesis of vitamin B12, cobalamin biosynthetic pathway
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
cobalamin biosynthetic pathway, involved in coenzyme B12 synthesis
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
CobQ is involved in the biosynthesis of adenosylcobalamin, i.e. vitamin B12, aerobic pathway
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
involved in cobalamin biosynthesis
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
CobQ amidates the side chains b, d, e, and g generating adenosylcobyric acid, requires glutamine as the amide donor
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
CobQ catalyzes amidations at positions b, d, e and g
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
CobQ contains an unusual Triad family, class I, glutamine amidotransferase domain with conserved Cys and His residues, but lacking the Glu residue of the catalytic triad, domain organization, model of substrate binding, catalytic mechanism, CobQ catalyzes amidation of the carboxyls b, d, e, and g in a strict order, one ATP molecule and one glutamine molecule are consumed for each amidation reaction
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
enzyme catalyzes the stepwise amidation of carboxyl groups b, d, e, and g of cobyrinic acid a,c-diamide, four-step amidation sequence from cobyrinic acid a,c-diamide to cobyric acid via the formation of corbyrinic acid triamide, tetraamide, and pentaamide intermediates, the amidations are carried out in a specific order, enzyme is specific to coenzyme forms of substrates, no amidation of the carboxyl group at position f, L-glutamine is the preferred amide group donor
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
Pseudomonas denitrificans (nom. rej.) SC510 Rifr(pXL617)
cobalamin biosynthetic pathway, involved in coenzyme B12 synthesis
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
Pseudomonas denitrificans (nom. rej.) SC510 Rifr(pXL617)
CobQ catalyzes amidations at positions b, d, e and g
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
Pseudomonas denitrificans (nom. rej.) SC510 RifT
-
biosynthesis of vitamin B12, cobalamin biosynthetic pathway
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
Pseudomonas denitrificans (nom. rej.) SC510 RifT
-
enzyme catalyzes the stepwise amidation of carboxyl groups b, d, e, and g of cobyrinic acid a,c-diamide, four-step amidation sequence from cobyrinic acid a,c-diamide to cobyric acid via the formation of corbyrinic acid triamide, tetraamide, and pentaamide intermediates, the amidations are carried out in a specific order, enzyme is specific to coenzyme forms of substrates, no amidation of the carboxyl group at position f, L-glutamine is the preferred amide group donor
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
-
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
CbiP is involved in the biosynthesis of adenosylcobalamin, i.e. vitamin B12, anaerobic pathway
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
involved in the de novo cobinamide biosynthesis pathway
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
CbiP catalyzes b, d, e, and g amidation
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
-
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
involved in the de novo cobinamide biosynthesis pathway
-
-
?
ATP + adenosylcobyrinic acid pentaamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
-
-
-
?
ATP + adenosylcobyrinic acid pentaamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
four carboxylates attached to the corrinoid ring are amidated in a dissociative fashion. The four carboxylates are amidated in a sequence beginning with carboxylate e and followed in turn by carboxylates d, b, and g
-
-
?
ATP + adenosylcobyrinic acid tetraamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
two-step amidation
-
-
?
ATP + adenosylcobyrinic acid tetraamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
four carboxylates attached to the corrinoid ring are amidated in a dissociative fashion. The four carboxylates are amidated in a sequence beginning with carboxylate e and followed in turn by carboxylates d, b, and g
-
-
?
ATP + adenosylcobyrinic acid triamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
three-step amidation
-
-
?
ATP + adenosylcobyrinic acid triamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
four carboxylates attached to the corrinoid ring are amidated in a dissociative fashion. The four carboxylates are amidated in a sequence beginning with carboxylate e and followed in turn by carboxylates d, b, and g
-
-
?
cobinic acid a,c-diamide + ATP + L-glutamine + H2O
cobinamide + ADP + phosphate + L-glutamate
-
-
-
?
cobinic acid a,c-diamide + ATP + L-glutamine + H2O
cobinamide + ADP + phosphate + L-glutamate
Pseudomonas denitrificans (nom. rej.) SC510 RifT
-
-
-
?
additional information
?
-
-
no amidation of adenosylcobyric acid, hydrogenobyrinic acid a,c-diamide, monocyano or diaqua form of cobyrinic acid a,c-diamide
-
-
?
additional information
?
-
Pseudomonas denitrificans (nom. rej.) SC510 RifT
-
no amidation of adenosylcobyric acid, hydrogenobyrinic acid a,c-diamide, monocyano or diaqua form of cobyrinic acid a,c-diamide
-
-
?
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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
adenosylcobyrinic acid a,c-diamide + ATP + L-glutamine + H2O
adenosylcobyric acid + ADP + phosphate + L-glutamate
-
vitamin B12 biosynthesis
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
cobinamide biosynthesis
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
cobinamide biosynthesis
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
-
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
biosynthesis of vitamin B12, cobalamin biosynthetic pathway
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
cobalamin biosynthetic pathway, involved in coenzyme B12 synthesis
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
CobQ is involved in the biosynthesis of adenosylcobalamin, i.e. vitamin B12, aerobic pathway
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
involved in cobalamin biosynthesis
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
Pseudomonas denitrificans (nom. rej.) SC510 Rifr(pXL617)
cobalamin biosynthetic pathway, involved in coenzyme B12 synthesis
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
Pseudomonas denitrificans (nom. rej.) SC510 RifT
-
biosynthesis of vitamin B12, cobalamin biosynthetic pathway
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
CbiP is involved in the biosynthesis of adenosylcobalamin, i.e. vitamin B12, anaerobic pathway
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
involved in the de novo cobinamide biosynthesis pathway
-
-
?
ATP + adenosylcobyrinic acid a,c-diamide + L-glutamine + H2O
ADP + phosphate + adenosylcobyric acid + L-glutamate
-
involved in the de novo cobinamide biosynthesis pathway
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0027
adenosylcobyrinic acid diamide
-
30°C, pH 7.5
20.4
ammonia
-
pH 7.5, adenosylcobyrinic acid a,c-diamide as substrate
0.0007
adenosylcobyrinic acid pentaamide
-
30°C, pH 7.5
0.0008
adenosylcobyrinic acid tetraamide
-
30°C, pH 7.5
0.001
adenosylcobyrinic acid triamide
-
30°C, pH 7.5
0.011
ATP
-
pH 7.5, adenosylcobyrinic acid a,c-diamide as substrate
0.035
ATP
-
pH 7.5, adenosylcobyrinic acid triamide as substrate
0.088
ATP
-
pH 7.5, adenosylcobyrinic acid pentaamide as substrate
0.12
ATP
-
pH 7.5, adenosylcobyrinic acid tetraamide as substrate
0.033
L-glutamine
-
pH 7.5, adenosylcobyrinic acid triamide as substrate
0.045
L-glutamine
-
pH 7.5, adenosylcobyrinic acid a,c-diamide as substrate
0.049
L-glutamine
-
pH 7.5, adenosylcobyrinic acid pentaamide as substrate
0.064
L-glutamine
-
pH 7.5, adenosylcobyrinic acid tetraamide as substrate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.6
adenosylcobyrinic acid diamide
-
30°C, pH 7.5
8.4
adenosylcobyrinic acid pentaamide
-
30°C, pH 7.5
3.6
adenosylcobyrinic acid tetraamide
-
30°C, pH 7.5
2.4
adenosylcobyrinic acid triamide
-
30°C, pH 7.5
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.083
-
pH 7.5, adenosylcobyrinic acid a,c-diamide as substrate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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). A0A075FKV3_9ARCH
90
0
10237
TrEMBL
-
A0A6J4IL75_9PSEU
uncultured Actinomycetospora sp
510
0
57217
TrEMBL
-
A0A3B0V750_9ZZZZ
170
0
18431
TrEMBL
other Location (Reliability: 2)
A0A1W1D3R7_9ZZZZ
460
0
52018
TrEMBL
other Location (Reliability: 3)
A0A1W1BGL0_9ZZZZ
462
0
51982
TrEMBL
other Location (Reliability: 4)
A0A1W1BBA2_9ZZZZ
450
0
51081
TrEMBL
other Location (Reliability: 1)
A0A160VC82_9ZZZZ
513
0
55280
TrEMBL
Mitochondrion (Reliability: 3)
A0A3B1ABW8_9ZZZZ
493
0
53580
TrEMBL
other Location (Reliability: 5)
A0A075HXP5_9ARCH
238
0
26951
TrEMBL
-
A0A1W1BXS3_9ZZZZ
446
0
50601
TrEMBL
other Location (Reliability: 2)
A0A3B1AAZ3_9ZZZZ
486
0
52822
TrEMBL
other Location (Reliability: 4)
A0A075GXG8_9ARCH
238
0
26931
TrEMBL
-
A0A6J4JXP4_9BACT
459
0
50492
TrEMBL
-
A0A8K1DD91_9ARCH
227
0
25375
TrEMBL
-
A0A484H6A8_9ZZZZ
514
0
54228
TrEMBL
other Location (Reliability: 2)
A0A3B0XUC6_9ZZZZ
492
0
53847
TrEMBL
other Location (Reliability: 4)
A0A075I5A8_9ARCH
267
0
30196
TrEMBL
-
A0A447NR75_SALET
93
0
10385
TrEMBL
-
A0A3B1A6K4_9ZZZZ
482
0
52050
TrEMBL
other Location (Reliability: 5)
A0A2P2C7K7_9ZZZZ
498
0
51996
TrEMBL
other Location (Reliability: 5)
A0A2P2CCG5_9ZZZZ
496
0
51921
TrEMBL
other Location (Reliability: 3)
A0A075HX82_9ARCH
238
0
26840
TrEMBL
-
A0A075H1W2_9ARCH
238
0
27008
TrEMBL
-
A0A3B0VZQ7_9ZZZZ
503
0
55232
TrEMBL
other Location (Reliability: 3)
J6H4D6_9FUSO
489
0
55057
TrEMBL
-
A0A6J4U6Y2_9ACTN
395
0
42945
TrEMBL
-
A0A3B1D1J2_9ZZZZ
524
0
57439
TrEMBL
Mitochondrion (Reliability: 5)
A0A3B0SPZ5_9ZZZZ
489
0
52289
TrEMBL
Mitochondrion (Reliability: 2)
A0A3B1D329_9ZZZZ
55
0
5867
TrEMBL
Mitochondrion (Reliability: 4)
A0A3B0S904_9ZZZZ
474
0
50548
TrEMBL
Mitochondrion (Reliability: 3)
A0A3B1BCB4_9ZZZZ
488
0
52484
TrEMBL
Mitochondrion (Reliability: 4)
W6QQ40_PSEP5
Pseudomonas pseudoalcaligenes (strain CECT 5344)
256
0
28445
TrEMBL
-
A0A3B1A8N8_9ZZZZ
493
0
53854
TrEMBL
other Location (Reliability: 2)
A0A3B0UYV3_9ZZZZ
515
0
54412
TrEMBL
Mitochondrion (Reliability: 3)
A0A3B0SNB5_9ZZZZ
487
0
52687
TrEMBL
other Location (Reliability: 5)
A0A3B1BD31_9ZZZZ
487
0
52491
TrEMBL
Mitochondrion (Reliability: 4)
A0A1W1CRT3_9ZZZZ
102
0
10848
TrEMBL
other Location (Reliability: 5)
A0A3B1CR79_9ZZZZ
434
0
47455
TrEMBL
Mitochondrion (Reliability: 5)
A0A160TI50_9ZZZZ
486
0
51483
TrEMBL
Mitochondrion (Reliability: 5)
A0A447JGB2_SALET
93
0
10387
TrEMBL
-
A0A075HJI2_9ARCH
238
0
26817
TrEMBL
-
A0A6J4LWC7_9ACTN
499
0
53816
TrEMBL
-
A0A3B0XA42_9ZZZZ
497
0
54257
TrEMBL
other Location (Reliability: 3)
A0A1W1CY33_9ZZZZ
442
0
49476
TrEMBL
other Location (Reliability: 2)
A0A1W1BZ01_9ZZZZ
464
0
51858
TrEMBL
other Location (Reliability: 3)
F9EJM6_FUSNU
128
0
15201
TrEMBL
-
A0A170PLX3_9ZZZZ
515
0
55833
TrEMBL
other Location (Reliability: 2)
A0A3B0XQV7_9ZZZZ
498
0
54204
TrEMBL
Mitochondrion (Reliability: 5)
A0A3B0TZR8_9ZZZZ
494
0
54522
TrEMBL
other Location (Reliability: 3)
A0A087RZV7_9ARCH
182
0
20501
TrEMBL
-
A0A3B0YXY1_9ZZZZ
489
0
52674
TrEMBL
Mitochondrion (Reliability: 4)
A0A1W1D1J4_9ZZZZ
446
0
50070
TrEMBL
other Location (Reliability: 2)
A0A3B0Z7A1_9ZZZZ
159
0
16940
TrEMBL
other Location (Reliability: 5)
A0A3B1AM52_9ZZZZ
396
0
42491
TrEMBL
Mitochondrion (Reliability: 5)
A0A3B0RKH5_9ZZZZ
484
0
51527
TrEMBL
other Location (Reliability: 3)
A0A3B0TSI1_9ZZZZ
492
0
52757
TrEMBL
Mitochondrion (Reliability: 4)
F0HVV6_LACDL
261
0
28244
TrEMBL
-
A0A3B1CY20_9ZZZZ
482
0
53483
TrEMBL
Mitochondrion (Reliability: 5)
A0A3B1DFM2_9ZZZZ
509
0
57264
TrEMBL
other Location (Reliability: 4)
A0A3B0QW92_9ZZZZ
504
0
53496
TrEMBL
Mitochondrion (Reliability: 5)
A0A160U3E4_9ZZZZ
494
0
52541
TrEMBL
Mitochondrion (Reliability: 4)
A0A1W1CRN1_9ZZZZ
374
0
42245
TrEMBL
other Location (Reliability: 1)
COBQ_SINSX
Sinorhizobium sp
485
0
51982
Swiss-Prot
other Location (Reliability: 3)
GATD_STRR6
260
0
29193
Swiss-Prot
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
51982
2 * 51982, CobQ sequence calculation, 2 * 57000
57000
57000
2 * 51982, CobQ sequence calculation, 2 * 57000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
homodimer
2 * 51982, CobQ sequence calculation, 2 * 57000
homodimer
Pseudomonas denitrificans (nom. rej.) SC510 Rifr(pXL617)
-
2 * 51982, CobQ sequence calculation, 2 * 57000
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
mutant strain JE6738 with in-frame deletion of cbiP, deficient in cobinamide biosynthesis, auxotrophic for adenosylcorbyric acid
additional information
-
mutant strain JE6738 with in-frame deletion of cbiP, deficient in cobinamide biosynthesis, auxotrophic for adenosylcorbyric acid
-
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
20% w/v and 1 mM dithiothreitol are necessary to stabilize enzyme during purification
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C or 0°C, purified enzyme, 0.1 M Tris hydrochloride, pH 7.5, 48 h, 100% loss of activity
-
-20°C, purified enzyme, 50 mM Tris hydrochloride, pH 7.5, 0.1 M sodium chloride, 1 mM dithiothreitol, 20% glycerol, several weeks, stable
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cbiP gene
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Crouzet, J.; Levy-Schil, S.; Cameron, B.; Cauchois, L.; Rigault, S.; Rouyez, M.C.; Blanche, F.; Debussche, L.; Thibaut, D.
Nucleotide sequence and genetic analysis of a 13.1-kilobase-pair Pseudomonas denitrificans DNA fragment containing five cob genes and identification of structural genes encoding Cob(I)alamin adenosyltransferase, cobyric acid synthase, and bifunctional cobinamide kinase-cobinamide phosphate guanylyltransferase
J. Bacteriol.
173
6074-6087
1991
Pseudomonas denitrificans (nom. rej.) (P29932), Pseudomonas denitrificans (nom. rej.), Pseudomonas denitrificans (nom. rej.) SC510 Rifr(pXL617) (P29932)
brenda
Warren, M.J.; Raux, E.; Schubert, H.L.; Escalante-Semerena, J.C.
The biosynthesis of adenosylcobalamin (vitamin B12)
Nat. Prod. Rep.
19
390-412
2002
Salmonella enterica, Pseudomonas denitrificans (nom. rej.)
brenda
Blanche F.; Maton, L.; Debussche, L.; Thibaut, D.
Purification and characterization of cob(II)yrinic acid a,c-diamide reductase from Pseudomonas denitrificans
J. Bacteriol.
174
7452-7454
1992
Pseudomonas denitrificans (nom. rej.)
brenda
Blanche, F.; Couder, M.; Debussche, L.; Thibaut, D.; Cameron, B.; Cruzet, J.
Biosynthesis of vitamin B12: stepwise amidation of carboxyl groups b, d, e, and g of cobyrinic acid a,c-diamide is catalyzed by one enzyme in Pseudomonas denitrificans
J. Bacteriol.
173
6046-6051
1991
Pseudomonas denitrificans (nom. rej.)
brenda
Galperin, M.Y.; Grishin, N.V.
The synthetase domains of cobalamin biosynthesis amidotransferases cobB and cobQ belong to a new family of ATP-dependent amidoligases, related to dethiobiotin synthetase
Proteins
41
238-247
2000
Escherichia coli, Pseudomonas denitrificans (nom. rej.)
brenda
Woodson, J.D.; Zayas, C.L.; Escalante-Semerena, J.C.
A new pathway for salvaging the coenzyme B12 precursor cobinamide in archaea requires cobinamide-phosphate synthase (CbiB) enzyme activity
J. Bacteriol.
185
7193-7201
2003
Salmonella enterica, Halobacterium sp., Salmonella enterica TR6583
brenda
Williams, L.; Fresquet, V.; Santander, P.J.; Raushel, F.M.
The multiple amidation reactions catalyzed by cobyric acid synthetase from Salmonella typhimurium are sequential and dissociative
J. Am. Chem. Soc.
129
294-295
2007
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
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