P0A9H5 (BTUR_ECOLI) 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:	btuR
Synonyms:	cobA
Ordered Locus Names:	b1270, JW1262

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	196 AA.
Sequence status	Complete.
Protein existence	Inferred 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.
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
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aerobic cobalamin biosynthetic process Inferred from mutant phenotype PubMed 7592411. Source: EcoCyc 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 sequence or structural similarity PubMed 7916712. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 196	196	Cob(I)yrinic acid a,c-diamide adenosyltransferase		PRO_0000065009
Regions
	Nucleotide binding	36 – 42	7	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0A9H5 [UniParc]. Last modified July 19, 2005. Version 1. Checksum: 4EE2FDD9C74FE8AE	FASTA	196	21,999
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Altered cobalamin metabolism in Escherichia coli btuR mutants affects btuB gene regulation." Lundrigan M.D., Kadner R.J. J. Bacteriol. 171:154-161(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M21528 Genomic DNA. Translation: AAA23530.1. U00096 Genomic DNA. Translation: AAC74352.1. AP009048 Genomic DNA. Translation: BAA14807.1.
PIR	A64875.
RefSeq	NP_415786.1. NC_000913.2. YP_489538.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P0A9H5.
SMR	P0A9H5. Positions 28-196.
ModBase	Search...
Protein-protein interaction databases
IntAct	P0A9H5. 14 interactions.
STRING	511145.b1270.
Proteomic databases
PaxDb	P0A9H5.
PRIDE	P0A9H5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC74352; AAC74352; b1270. BAA14807; BAA14807; BAA14807.
GeneID	12930581. 945839.
KEGG	ecj:Y75_p1244. eco:b1270.
PATRIC	32117798. VBIEscCol129921_1319.
Organism-specific databases
EchoBASE	EB0128.
EcoGene	EG10130. btuR.
Phylogenomic databases
eggNOG	COG2109.
HOGENOM	HOG000260311.
KO	K00798.
OMA	WHTMGEG.
ProtClustDB	PRK05986.
Enzyme and pathway databases
BioCyc	EcoCyc:COBALADENOSYLTRANS-MONOMER. ECOL316407:JW1262-MONOMER.
UniPathway	UPA00148; UER00233.
Gene expression databases
Genevestigator	P0A9H5.
Family and domain databases
InterPro	IPR003724. AdoCbl_synth_CblAdoTrfase_CobA. IPR025826. Co_AT_N_dom. IPR027417. P-loop_NTPase. [Graphical view]
Pfam	PF12557. Co_AT_N. 1 hit. PF02572. CobA_CobO_BtuR. 1 hit. [Graphical view]
PIRSF	PIRSF015617. Adensltrnsf_CobA. 1 hit.
SUPFAM	SSF52540. SSF52540. 1 hit.
TIGRFAMs	TIGR00708. cobA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

BTUR_ECOLI

Accession

Primary (citable) accession number: P0A9H5
Secondary accession number(s): P13040

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	May 29, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program