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Protein

Phosphomannomutase

Gene

rfbB

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Involved in GDP-mannose biosynthesis which serves as the activated sugar nucleotide precursor for mannose residues in cell surface polysaccharides.

Catalytic activityi

Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate.

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei103 – 1031Phosphoserine intermediateBy similarity
Metal bindingi103 – 1031Magnesium; via phosphate groupBy similarity
Metal bindingi248 – 2481MagnesiumBy similarity
Metal bindingi250 – 2501MagnesiumBy similarity
Metal bindingi252 – 2521MagnesiumBy similarity

GO - Molecular functioni

  1. magnesium ion binding Source: InterPro
  2. phosphomannomutase activity Source: TIGR

GO - Biological processi

  1. carbohydrate metabolic process Source: TIGR
  2. GDP-mannose biosynthetic process Source: UniProtKB-UniPathway
  3. O antigen biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Lipopolysaccharide biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciVCHO:VC0242-MONOMER.
UniPathwayiUPA00126; UER00424.
UPA00281.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphomannomutase (EC:5.4.2.8)
Short name:
PMM
Gene namesi
Name:rfbB
Ordered Locus Names:VC_0242
OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Taxonomic identifieri243277 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
ProteomesiUP000000584 Componenti: Chromosome 1

Subcellular locationi

GO - Cellular componenti

  1. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 463463PhosphomannomutasePRO_0000147827Add
BLAST

Keywords - PTMi

Phosphoprotein

Interactioni

Protein-protein interaction databases

STRINGi243277.VC0242.

Structurei

3D structure databases

ProteinModelPortaliQ06951.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphohexose mutase family.Curated

Phylogenomic databases

eggNOGiCOG1109.
KOiK01840.
OMAiGWVHLRK.
OrthoDBiEOG6W9X55.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProiIPR005844. 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]
PfamiPF02878. 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]
PRINTSiPR00509. PGMPMM.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q06951-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKELTCFKAY DIRGQLGSEL DNEIAYRIGR SYGQFLKSEN DADKTVVVGG
60 70 80 90 100
DVRLTSEALK QALANGLMDA GINVIDIGVT GTEEIYFATF YLGVDGGIEV
110 120 130 140 150
TASHNPMDYN GMKLVREGSK PISGDTGLRE IQALAEKNEF MDVEVKGNYK
160 170 180 190 200
KVSLLPEYVD HLISYITPAK IKPMKLVINS GNGAAGHVID ELEKRFIELS
210 220 230 240 250
IPLEIIKVHH EEDGNFPNGI PNPLLPECRA DTANAVKEHK ADMGIAFDGD
260 270 280 290 300
FDRCFLFDEN GDFIEGYYIV GLLAEAFLQK EQGAKIIHDP RLSWNTIDVV
310 320 330 340 350
TKSGGVPVMS KTGHAFIKER MRKEDAIYGG EMSAHHYFRD FGYCDSGMIP
360 370 380 390 400
WLLITELLSL APDISLSKLI SAKRFLFPCS GEINFKVKQA KLIMEQVYLH
410 420 430 440 450
YYENSIHFSA IDGISLEFEG WRFNLRDSNT EPLLRLNVES KQNIALMNDK
460
VEELTKLIKK LDI
Length:463
Mass (Da):51,838
Last modified:February 1, 1995 - v1
Checksum:i7212EA3A64BFC6BE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59554 Genomic DNA. Translation: CAA42135.1.
AE003852 Genomic DNA. Translation: AAF93418.1.
PIRiS28469.
RefSeqiNP_229899.1. NC_002505.1.
WP_000661577.1. NC_002505.1.

Genome annotation databases

EnsemblBacteriaiAAF93418; AAF93418; VC_0242.
GeneIDi2614705.
KEGGivch:VC0242.
PATRICi20079528. VBIVibCho83274_0223.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59554 Genomic DNA. Translation: CAA42135.1.
AE003852 Genomic DNA. Translation: AAF93418.1.
PIRiS28469.
RefSeqiNP_229899.1. NC_002505.1.
WP_000661577.1. NC_002505.1.

3D structure databases

ProteinModelPortaliQ06951.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243277.VC0242.

Protocols and materials databases

DNASUi2614705.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF93418; AAF93418; VC_0242.
GeneIDi2614705.
KEGGivch:VC0242.
PATRICi20079528. VBIVibCho83274_0223.

Phylogenomic databases

eggNOGiCOG1109.
KOiK01840.
OMAiGWVHLRK.
OrthoDBiEOG6W9X55.

Enzyme and pathway databases

UniPathwayiUPA00126; UER00424.
UPA00281.
BioCyciVCHO:VC0242-MONOMER.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProiIPR005844. 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]
PfamiPF02878. 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]
PRINTSiPR00509. PGMPMM.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: El Tor O17 / Serotype O1.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 39315 / El Tor Inaba N16961.

Entry informationi

Entry nameiRFBB_VIBCH
AccessioniPrimary (citable) accession number: Q06951
Secondary accession number(s): Q9JQ14
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: January 7, 2015
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.