Q06951 (RFBB_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphomannomutase
Short name=PMM
EC=5.4.2.8

Gene names

Name:	rfbB
Ordered Locus Names:	VC_0242

Organism

Vibrio cholerae

Taxonomic identifier

666 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

Protein attributes

Sequence length	463 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Involved in GDP-mannose biosynthesis which serves as the activated sugar nucleotide precursor for mannose residues in cell surface polysaccharides.
Catalytic activity	Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate.
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Pathway	Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. Bacterial outer membrane biogenesis; LPS O-antigen biosynthesis.
Subcellular location	Cell membrane Probable.
Sequence similarities	Belongs to the phosphohexose mutase family.

Ontologies

Keywords
Biological process	Lipopolysaccharide biosynthesis
Cellular component	Cell membrane Membrane
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	lipopolysaccharide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: InterPro phosphomannomutase 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 – 463	463	Phosphomannomutase		PRO_0000147827
Sites
	Active site	103	1	Phosphoserine intermediate By similarity
	Metal binding	103	1	Magnesium; via phosphate group By similarity
	Metal binding	248	1	Magnesium By similarity
	Metal binding	250	1	Magnesium By similarity
	Metal binding	252	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q06951 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 7212EA3A64BFC6BE	FASTA	463	51,838
	10 20 30 40 50 60 MKELTCFKAY DIRGQLGSEL DNEIAYRIGR SYGQFLKSEN DADKTVVVGG DVRLTSEALK 70 80 90 100 110 120 QALANGLMDA GINVIDIGVT GTEEIYFATF YLGVDGGIEV TASHNPMDYN GMKLVREGSK 130 140 150 160 170 180 PISGDTGLRE IQALAEKNEF MDVEVKGNYK KVSLLPEYVD HLISYITPAK IKPMKLVINS 190 200 210 220 230 240 GNGAAGHVID ELEKRFIELS IPLEIIKVHH EEDGNFPNGI PNPLLPECRA DTANAVKEHK 250 260 270 280 290 300 ADMGIAFDGD FDRCFLFDEN GDFIEGYYIV GLLAEAFLQK EQGAKIIHDP RLSWNTIDVV 310 320 330 340 350 360 TKSGGVPVMS KTGHAFIKER MRKEDAIYGG EMSAHHYFRD FGYCDSGMIP WLLITELLSL 370 380 390 400 410 420 APDISLSKLI SAKRFLFPCS GEINFKVKQA KLIMEQVYLH YYENSIHFSA IDGISLEFEG 430 440 450 460 WRFNLRDSNT EPLLRLNVES KQNIALMNDK VEELTKLIKK LDI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Serotype conversion in Vibrio cholerae O1." Stroeher U.H., Karageorgos L.E., Morona R., Manning P.A. Proc. Natl. Acad. Sci. U.S.A. 89:2566-2570(1992) [PubMed: 1372980] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: El Tor O17 / Serotype O1.
[2]	"DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae." Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., Vamathevan J.J., Bass S. , Qin H., Dragoi I., Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M. Nature 406:477-483(2000) [PubMed: 10952301] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39315 / El Tor Inaba N16961 / Serotype O1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X59554 Genomic DNA. Translation: CAA42135.1. AE003852 Genomic DNA. Translation: AAF93418.1.
PIR	S28469.
RefSeq	NP_229899.1. NC_002505.1.
3D structure databases
ProteinModelPortal	Q06951.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2614705.
GenomeReviews	Gene locus VC_0242 in contig AE003852_GR.
KEGG	vch:VC0242.
PATRIC	20079528. VBIVibCho83274_0223.
TIGR	VC_0242.
Phylogenomic databases
HOGENOM	HBG644964.
OMA	ISADFGQ.
PhylomeDB	Q06951.
ProtClustDB	CLSK873915.
Family and domain databases
InterPro	IPR005844. A-D-PHexomutase_a/b/a-I. IPR016055. A-D-PHexomutase_a/b/a-I/II/III. IPR005845. A-D-PHexomutase_a/b/a-II. IPR005846. A-D-PHexomutase_a/b/a-III. IPR005843. A-D-PHexomutase_C. IPR016066. A-D-PHexomutase_CS. IPR005841. Alpha-D-phosphohexomutase_SF. [Graphical view]
Gene3D	G3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
KO	K01840.
Pfam	PF02878. PGM_PMM_I. 1 hit. PF02879. PGM_PMM_II. 1 hit. PF02880. PGM_PMM_III. 1 hit. PF00408. PGM_PMM_IV. 1 hit. [Graphical view]
PRINTS	PR00509. PGMPMM.
SUPFAM	SSF53738. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RFBB_VIBCH

Accession

Primary (citable) accession number: Q06951
Secondary accession number(s): Q9JQ14

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	January 25, 2012
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program