P29930 (COBO_PSEDE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cob(I)yrinic acid a,c-diamide adenosyltransferase
EC=2.5.1.17

Alternative name(s):
Cob(I)alamin adenosyltransferase
Corrinoid adenosyltransferase

Gene names

Name:

cobO

Organism

Pseudomonas denitrificans

Taxonomic identifier

43306 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas › Pseudomonas pertucinogena group

Protein attributes

Sequence length	214 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for both de novo synthesis of the corrin ring for the assimilation of exogenous corrinoids. Participates in the adenosylation of a variety of incomplete and complete corrinoids By similarity.
Catalytic activity	ATP + cob(I)yrinic acid a,c-diamide = triphosphate + adenosylcob(III)yrinic acid a,c-diamide. ATP + cobinamide = triphosphate + adenosylcobinamide.
Cofactor	Manganese.
Pathway	Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7.
Subunit structure	Monomer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the Cob(I)alamin adenosyltransferase family.

Ontologies

Keywords
Biological process	Cobalamin biosynthesis Porphyrin biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Manganese Nucleotide-binding
Molecular function	Transferase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	cobalamin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway porphyrin-containing compound biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cob(I)yrinic acid a,c-diamide adenosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.2
	Chain	2 – 214	213	Cob(I)yrinic acid a,c-diamide adenosyltransferase		PRO_0000089992
Regions
	Nucleotide binding	50 – 56	7	ATP By similarity
Experimental info
	Sequence conflict	14	1	E → K AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P29930 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: A110C89668990ECC	FASTA	214	24,028
	10 20 30 40 50 60 MSDETTVGGE APAEKDDARH AMKMAKKKAA REKIMATKTD EKGLIIVNTG KGKGKSTAGF 70 80 90 100 110 120 GMIFRHIAHG MPCAVVQFIK GAMATGEREL IEKHFGDVCQ FYTLGEGFTW ETQDRARDVA 130 140 150 160 170 180 MAEKAWEKAK ELIRDERNSM VLLDEINIAL RYDYIDVAEV VRFLKEEKPH MTHVVLTGRN 190 200 210 AKEDLIEVAD LVTEMELIKH PFRSGIKAQQ GVEF

References

[1]

"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." Crouzet J., Levy-Schil S., Cameron B., Cauchois L., Rigault S., Rouyez M.-C., Blanche F., Debussche L., Thibaut D. J. Bacteriol. 173:6074-6087(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

[2]

"Purification and partial characterization of Cob(I)alamin adenosyltransferase from Pseudomonas denitrificans." Debussche L., Couder M., Thibaut D., Cameron B., Crouzet J., Blanche F. J. Bacteriol. 173:6300-6302(1991) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, PROTEIN SEQUENCE OF 2-15.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M62866 Genomic DNA. Translation: AAA25781.1.
3D structure databases
ProteinModelPortal	P29930.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-123.
BRENDA	2.5.1.17. 5114.
UniPathway	UPA00148; UER00233.
Family and domain databases
InterPro	IPR003724. AdoCbl_synth_CblAdoTrfase_CobA. IPR025826. Co_AT_N_dom. [Graphical view]
Pfam	PF12557. Co_AT_N. 1 hit. PF02572. CobA_CobO_BtuR. 1 hit. [Graphical view]
PIRSF	PIRSF015617. Adensltrnsf_CobA. 1 hit.
TIGRFAMs	TIGR00708. cobA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

COBO_PSEDE

Accession

Primary (citable) accession number: P29930

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 66 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program