Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P45515 (PDUO_CITFR) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 64. 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
ORFW
OrganismCitrobacter freundii
Taxonomic identifier546 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCitrobacterCitrobacter freundii complex

Protein attributes

Sequence length176 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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 Potential.

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
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 – 176176Cob(I)yrinic acid a,c-diamide adenosyltransferase
PRO_0000103801

Regions

Nucleotide binding6 – 149ATP By similarity
Nucleotide binding131 – 1366ATP By similarity

Sites

Binding site241ATP By similarity
Binding site1551ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P45515 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: AEB560DD05EF3EB5

FASTA17619,846
        10         20         30         40         50         60 
MYRIYTRTGD NGTTALFGGS RIDKDDIRVE AYGTVDELIS QLGVCYASTR QAELRQELHA 

        70         80         90        100        110        120 
MQKMLFVLGA ELASDQKGLT RLKQRIGEED IQALEQLIDR NMAQSGPLKE FVIPGKNLAS 

       130        140        150        160        170 
AQLHVARTLT RRLERILIAM GRTLTLRDEA RRYINRLSDA LFSMARIEET TPDVCA 

« Hide

References

[1]Daniel R., Gottschalk G.
Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 6750 / DSM 30040 / NCIB 8173 / M8BK.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U09771 Genomic DNA. Translation: AAB48846.1.

3D structure databases

ProteinModelPortalP45515.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00148; UER00233.

Family and domain databases

Gene3D1.20.1200.10. 1 hit.
InterProIPR016030. AdoCbl_synth_CblAdoTrfase-like.
[Graphical view]
PfamPF01923. Cob_adeno_trans. 1 hit.
[Graphical view]
ProDomPD007457. AdoCbl_syn_CblAdoTrfase_PduO_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF89028. SSF89028. 1 hit.
TIGRFAMsTIGR00636. PduO_Nterm. 1 hit.
ProtoNetSearch...

Entry information

Entry namePDUO_CITFR
AccessionPrimary (citable) accession number: P45515
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 16, 2013
This is version 64 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