NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1655697 [NCBI, ExPASy, EBI, Israel, Japan]
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).

[2]

CHARACTERIZATION, AND PROTEIN SEQUENCE OF 2-11.
PubMed=1655696 [NCBI, ExPASy, EBI, Israel, Japan]
Blanche F., Debussche L., Famechon A., Thibaut D., Cameron B., Crouzet J.;
"A bifunctional protein from Pseudomonas denitrificans carries cobinamide kinase and cobinamide phosphate guanylyltransferase activities.";
J. Bacteriol. 173:6052-6057(1991).

Comments

FUNCTION: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate.
CATALYTIC ACTIVITY: ATP or GTP + adenosylcobinamide = adenosylcobinamide phosphate + ADP or GDP.
CATALYTIC ACTIVITY: GTP + adenosylcobinamide phosphate = diphosphate + adenosylcobinamide-GDP.
PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinic acid a,c-diamide: step 5/7 .
PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinic acid a,c-diamide: step 6/7 .
SUBUNIT: Homodimer.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M62866; AAA25778.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

Q05599; 1CBU. [HSSP ENTRY / PDB]

ModBase

P29931.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-143; -.

Ontologies

GO:0043752;	Molecular function: adenosylcobinamide kinase activity (inferred from electronic annotation from InterPro).
GO:0043753;	Molecular function: adenosylcobinamide-phosphate guanylyltransferase activity (inferred from electronic annotation from InterPro).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005525;	Molecular function: GTP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0009236;	Biological process: cobalamin biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR003203; CobU.
Graphical view of domain structure.

Pfam

PF02283; CobU; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF006135; CobU; 1.

ProDom

PD011091; CobU; 1.
[Domain structure / List of seq. sharing at least 1 domain]

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Cobalamin biosynthesis; Direct protein sequencing; GTP-binding; Kinase; Multifunctional enzyme; Nucleotide-binding; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 174`	`173`	`Bifunctional adenosylcobalamin biosynthesis protein cobP.`	`PRO_0000089993`
`NP_BIND`	`13 20`	`8`	`ATP (Potential).`
`ACT_SITE`	`54 54`		`GMP-histidine intermediate (By similarity).`

Sequence information

Length: 174 AA [This is the length of the unprocessed precursor]

Molecular weight: 19442 Da [This is the MW of the unprocessed precursor]

CRC64: 71580200BC9DC4DC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSSLSAGPVL VLGGARSGKS SFSERLVEAS GFTMHYVATG RAWDDEMRER IDHHRTRRGE 

        70         80         90        100        110        120 
GWTTHEEPLD LVGILRRIDD PSHVVLIDCL TLWVTNLMLE ERDMTAEFAA LVAYLPEARA 

       130        140        150        160        170 
RLVFVSNEVG LGIVPENRMA REFRDHAGRL HQIVAEKSAE VYFVAAGLPL KMKG

P29931 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools