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P29930 (COBO_PSEDE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismPseudomonas denitrificans
Taxonomic identifier43306 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length214 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processCobalamin biosynthesis
Porphyrin biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Manganese
Nucleotide-binding
   Molecular functionTransferase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcobalamin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

porphyrin-containing compound biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cob(I)yrinic acid a,c-diamide adenosyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 214213Cob(I)yrinic acid a,c-diamide adenosyltransferase
PRO_0000089992

Regions

Nucleotide binding50 – 567ATP By similarity

Experimental info

Sequence conflict141E → K AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P29930 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A110C89668990ECC

FASTA21424,028
        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 

« Hide

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

ProteinModelPortalP29930.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-123.
BRENDA2.5.1.17. 5114.
UniPathwayUPA00148; UER00233.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR003724. AdoCbl_synth_CblAdoTrfase_CobA.
IPR025826. Co_AT_N_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF12557. Co_AT_N. 1 hit.
PF02572. CobA_CobO_BtuR. 1 hit.
[Graphical view]
PIRSFPIRSF015617. Adensltrnsf_CobA. 1 hit.
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00708. cobA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCOBO_PSEDE
AccessionPrimary (citable) accession number: P29930
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 69 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways