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P0A9H6 (BTUR_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 61. 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:btuR
Ordered Locus Names:c1735
OrganismEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier199310 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length196 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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.

Pathway

Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7.

Subcellular location

Cytoplasm Probable.

Sequence similarities

Belongs to the Cob(I)alamin adenosyltransferase family.

Ontologies

Keywords
   Biological processCobalamin biosynthesis
Porphyrin biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionTransferase
   Technical termComplete proteome
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

Chain1 – 196196Cob(I)yrinic acid a,c-diamide adenosyltransferase
PRO_0000065008

Regions

Nucleotide binding36 – 427ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A9H6 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: 4EE2FDD9C74FE8AE

FASTA19621,999
        10         20         30         40         50         60 
MSDERYQQRQ QRVKEKVDAR VAQAQDERGI IIVFTGNGKG KTTAAFGTAT RAVGHGKKVG 

        70         80         90        100        110        120 
VVQFIKGTWP NGERNLLEPH GVEFQVMATG FTWDTQNRES DTAACREVWQ HAKRMLADSS 

       130        140        150        160        170        180 
LDMVLLDELT YMVAYDYLPL EEVVQALNER PHQQTVIITG RGCHRDILEL ADTVSELRPV 

       190 
KHAFDAGVKA QIGIDY 

« Hide

References

[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014075 Genomic DNA. Translation: AAN80201.1.
RefSeqNP_753639.1. NC_004431.1.

3D structure databases

ProteinModelPortalP0A9H6.
SMRP0A9H6. Positions 28-196.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING199310.c1735.

Proteomic databases

PRIDEP0A9H6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN80201; AAN80201; c1735.
GeneID1035519.
KEGGecc:c1735.
PATRIC18281392. VBIEscCol75197_1615.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000260311.
KOK00798.
OMAKGERRNA.
OrthoDBEOG6GN76J.

Enzyme and pathway databases

BioCycECOL199310:C1735-MONOMER.
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 nameBTUR_ECOL6
AccessionPrimary (citable) accession number: P0A9H6
Secondary accession number(s): P13040
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: May 14, 2014
This is version 61 of the entry and version 1 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