P39701 (COBC_SALTY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-ribazole phosphatase
EC=3.1.3.73

Alternative name(s):
Adenosylcobalamin phosphatase
Alpha-ribazole-5'-phosphate phosphatase

Gene names

Name:	cobC
Ordered Locus Names:	STM0643

Organism

Salmonella typhimurium

Taxonomic identifier

90371 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length	202 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Converts N1-(5-phospho-alpha-D-ribosyl)-5,6-dimethylbenzimidazole into N1-alpha-D-ribosyl-5,6-dimethylbenzimidazole. Also catalyzes the conversion of adenosylcobalamin 5'-phosphate to adenosylcobalamin (vitamin B12); involved in the assembly of the nucleotide loop of cobalamin. Ref.1
Catalytic activity	Adenosylcobalamin 5'-phosphate + H2O = coenzyme B12 + phosphate. Ref.1 Alpha-ribazole 5'-phosphate + H2O = alpha-ribazole + phosphate. Ref.1
Pathway	Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-ribazole from 5,6-dimethylbenzimidazole: step 2/2.
Subunit structure	Monomer.
Sequence similarities	Belongs to the phosphoglycerate mutase family.
Caution	Overexpression of the protein (in Ref.1) indicates that it may actually be longer by 32 amino acids.
Sequence caution	The sequence AAA62874.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cobalamin biosynthesis
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cobalamin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	alpha-ribazole phosphatase 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 – 202	202	Alpha-ribazole phosphatase		PRO_0000179956
Sites
	Active site	8	1	Tele-phosphohistidine intermediate By similarity
	Site	57	1	Interaction with carboxyl group of phosphoglycerates By similarity
Experimental info
	Sequence conflict	46 – 59	14	PFDRV…LERAR → HLTGCYRASWSARA Ref.1
	Sequence conflict	198	1	V → C in AAA62874. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P39701 [UniParc]. Last modified January 23, 2002. Version 3. Checksum: CBE887F066510B9D	FASTA	202	23,123
	10 20 30 40 50 60 MRLWLVRHGE TEANVAGLYS GHAPTPLTEK GIGQAKTLHT LLRHAPFDRV LCSELERARH 70 80 90 100 110 120 TARLVLEGRD VPQHILPELN EMYFGDWEMR HHRDLTHEDA ESYAAWCTDW QNAVPTNGEG 130 140 150 160 170 180 FQAFTRRVER FISRLDAFSD CQNLLIVSHQ GVLSLLIARL LTMPAASLWH FRVEQGCWSA 190 200 IDICEGFATL KVLNSRAVWR PE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The cobC gene of Salmonella typhimurium codes for a novel phosphatase involved in the assembly of the nucleotide loop of cobalamin." O'Toole G.A., Trzebiatowski J.R., Escalante-Semerena J.C. J. Biol. Chem. 269:26503-26511(1994) [PubMed: 7929373] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY. Strain: LT2.
[2]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K. Nature 413:852-856(2001) [PubMed: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U12808 Genomic DNA. Translation: AAA62874.1. Different initiation. AE006468 Genomic DNA. Translation: AAL19594.1.
PIR	A55367.
RefSeq	NP_459635.1. NC_003197.1.
3D structure databases
ProteinModelPortal	P39701.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1252163.
GenomeReviews	Gene locus STM0643 in contig AE006468_GR.
KEGG	stm:STM0643.
NMPDR	fig|99287.1.peg.623.
PATRIC	32379639. VBISalEnt20916_0679.
Phylogenomic databases
HOGENOM	HBG658938.
OMA	DQGCWST.
ProtClustDB	PRK15004.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-13213. STYP99287:STM0643-MONOMER.
BRENDA	3.1.3.73. 5542.
Family and domain databases
InterPro	IPR013078. His_Pase_superF_clade-1. IPR001345. PG/BPGM_mutase_AS. IPR017578. Ribazole_CobC. [Graphical view]
KO	K02226.
Pfam	PF00300. His_Phos_1. 1 hit. [Graphical view]
SMART	SM00855. PGAM. 1 hit. [Graphical view]
TIGRFAMs	TIGR03162. Ribazole_cobC. 1 hit.
PROSITE	PS00175. PG_MUTASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

COBC_SALTY

Accession

Primary (citable) accession number: P39701

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 23, 2002
Last modified:	January 25, 2012
This is version 80 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program