Q05600 (CBIB_SALTY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cobalamin biosynthesis protein CbiB

Gene names

Name:	cbiB
Ordered Locus Names:	STM2034

Organism

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]

Taxonomic identifier

99287 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella choleraesuis › Salmonella enterica I › Salmonella typhimurium

Protein attributes

Sequence length	319 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group. However, the true cosubstrate could be (R)-1-amino-2-propanol O-2-phosphate, leading to cobinamide phosphate. HAMAP-Rule MF_00024
Pathway	Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 4/7. HAMAP-Rule MF_00024
Subcellular location	Cell membrane; Multi-pass membrane protein Potential HAMAP-Rule MF_00024.
Sequence similarities	Belongs to the CobD/CbiB family.

Ontologies

Keywords
Biological process	Cobalamin biosynthesis
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cobalamin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cobalamin-transporting ATPase activity Inferred from electronic annotation. Source: HAMAP threonine-phosphate decarboxylase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 319	319	Cobalamin biosynthesis protein CbiB HAMAP-Rule MF_00024		PRO_0000150937
Regions
	Transmembrane	3 – 23	21	Helical; Potential
	Transmembrane	56 – 76	21	Helical; Potential
	Transmembrane	82 – 102	21	Helical; Potential
	Transmembrane	153 – 173	21	Helical; Potential
	Transmembrane	296 – 316	21	Helical; Potential

Sequences

	Sequence		Length	Mass (Da)
	Q05600 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 540FDF93E0796214	FASTA	319	35,370
	10 20 30 40 50 60 MTILAWCIAW VLDFIIGDPQ HWPHPVRWIG RLITFVQRIV RRYCPGDKAL RIGGGVMWVV 70 80 90 100 110 120 VVGATWGVAW GVLALAQRIH PWFGWSVEVW MIFTTLAGRS LAHAAQEVER PLRKNDLAES 130 140 150 160 170 180 RIKLSWIVGR DTSQLQPAQI NRAVVETVAE NTVDGIIAPL FFLFLGGAPL AMAYKAVNTL 190 200 210 220 230 240 DSMVGYKHEK YRAIGMVSAR MDDVANYLPA RLSWLLLGIA AGLCRLSGWR ALRIGWRDRY 250 260 270 280 290 300 NHSSPNCAWS EACVAGALGI QLGGPNNYFG ERVDKPWIGD AQRDISVDDI SRTIRLMWVA 310 STLALALLIA ARCGLSGVA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the cobalamin (vitamin B12) biosynthetic genes of Salmonella typhimurium." Roth J.R., Lawrence J.G., Rubenfield M., Kieffer-Higgins S., Church G.M. J. Bacteriol. 175:3303-3316(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[3]	"CobD, a novel enzyme with L-threonine-O-3-phosphate decarboxylase activity, is responsible for the synthesis of (R)-1-amino-2-propanol O-2-phosphate, a proposed new intermediate in cobalamin biosynthesis in Salmonella typhimurium LT2." Brushaber K.R., O'Toole G.A., Escalante-Semerena J.C. J. Biol. Chem. 273:2684-2691(1998) [PubMed] [Europe PMC] [Abstract] Cited for: POSSIBLE COSUBSTRATE. Strain: LT2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L12006 Genomic DNA. Translation: AAA27253.1. AE006468 Genomic DNA. Translation: AAL20938.1.
RefSeq	NP_460979.1. NC_003197.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	99287.STM2034.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAL20938; AAL20938; STM2034.
GeneID	1253555.
KEGG	stm:STM2034.
PATRIC	32382651. VBISalEnt20916_2156.
Phylogenomic databases
HOGENOM	HOG000290070.
KO	K02227.
OMA	REFGWAS.
ProtClustDB	PRK01209.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-13228. SENT99287:GCTI-2046-MONOMER.
UniPathway	UPA00148; UER00235.
Family and domain databases
HAMAP	MF_00024. CobD_CbiB.
InterPro	IPR004485. Cobalamin_biosynth_CobD/CbiB. [Graphical view]
Pfam	PF03186. CobD_Cbib. 1 hit. [Graphical view]
TIGRFAMs	TIGR00380. cobD. 1 hit.
ProtoNet	Search...

Entry information

Entry name

CBIB_SALTY

Accession

Primary (citable) accession number: Q05600

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	May 29, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program