Phosphomannomutase - Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)

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Q06951 (RFBB_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 95. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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 serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]

Taxonomic identifier

243277 [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	GDP-mannose biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway O antigen biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway carbohydrate metabolic process Inferred from sequence or structural similarity Ref.2. Source: TIGR
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 sequence or structural similarity Ref.2. Source: TIGR
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

Phosphoserine intermediate By similarity

Metal binding

103

Magnesium; via phosphate group By similarity

Metal binding

248

Magnesium By similarity

Metal binding

250

Magnesium By similarity

Metal binding

252

Magnesium By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q06951 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 7212EA3A64BFC6BE
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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

« Hide

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] [Europe PMC] [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. Fraser C.M. Nature 406:477-483(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39315 / El Tor Inaba N16961.

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...
Protein-protein interaction databases
STRING	243277.VC0242.
Protocols and materials databases
DNASU	2614705.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAF93418; AAF93418; VC_0242.
GeneID	2614705.
KEGG	vch:VC0242.
PATRIC	20079528. VBIVibCho83274_0223.
Phylogenomic databases
eggNOG	COG1109.
KO	K01840.
OMA	AHDMRES.
ProtClustDB	CLSK873915.
Enzyme and pathway databases
UniPathway	UPA00126; UER00424. UPA00281.
Family and domain databases
Gene3D	3.40.120.10. 3 hits.
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]
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:	May 1, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents