P45515 (PDUO_CITFR) 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 ORFW
Organism	Citrobacter freundii
Taxonomic identifier	546 [NCBI]
Taxonomic lineage	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Citrobacter

Protein attributes

Sequence length	176 AA.
Sequence status	Complete.
Protein existence	Inferred 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 process	Cobalamin biosynthesis Porphyrin biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Transferase
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
	Chain	1 – 176	176	Cob(I)yrinic acid a,c-diamide adenosyltransferase		PRO_0000103801
Regions
	Nucleotide binding	6 – 14	9	ATP By similarity
	Nucleotide binding	131 – 136	6	ATP By similarity
Sites
	Binding site	24	1	ATP By similarity
	Binding site	155	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	P45515 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: AEB560DD05EF3EB5	FASTA	176	19,846
	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

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
ProteinModelPortal	P45515.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00148; UER00233.
Family and domain databases
Gene3D	1.20.1200.10. 1 hit.
InterPro	IPR016030. AdoCbl_synth_CblAdoTrfase-like. [Graphical view]
Pfam	PF01923. Cob_adeno_trans. 1 hit. [Graphical view]
ProDom	PD007457. AdoCbl_syn_CblAdoTrfase_PduO_N. 1 hit. [Graphical view] [Entries sharing at least one domain]
SUPFAM	SSF89028. AdoCbl_synth_CblAdoTrfase-like. 1 hit.
TIGRFAMs	TIGR00636. PduO_Nterm. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PDUO_CITFR

Accession

Primary (citable) accession number: P45515

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program