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Q9KPY2 (GMHA_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoheptose isomerase

EC=5.3.1.28
Alternative name(s):
Sedoheptulose 7-phosphate isomerase
Gene names
Name:gmhA
Ordered Locus Names:VC_2230
OrganismVibrio cholerae
Taxonomic identifier666 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length191 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate By similarity. HAMAP MF_00067

Catalytic activity

D-sedoheptulose 7-phosphate = D-glycero-D-manno-heptose 7-phosphate. HAMAP MF_00067

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP MF_00067

Pathway

Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate: step 1/1. HAMAP MF_00067

Bacterial outer membrane biogenesis; LPS core biosynthesis. HAMAP MF_00067

Subunit structure

Homotetramer By similarity. HAMAP MF_00067

Subcellular location

Cytoplasm By similarity HAMAP MF_00067.

Miscellaneous

The reaction produces a racemic mixture of D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate By similarity. HAMAP MF_00067

Sequence similarities

Belongs to the SIS family. GmhA subfamily.

Contains 1 SIS domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 191191Phosphoheptose isomerase HAMAP MF_00067
PRO_0000136548

Regions

Domain37 – 191155SIS
Region52 – 543Substrate binding By similarity
Region93 – 942Substrate binding By similarity
Region119 – 1213Substrate binding By similarity

Sites

Metal binding611Zinc By similarity
Metal binding651Zinc By similarity
Metal binding1721Zinc By similarity
Metal binding1801Zinc By similarity
Binding site651Substrate By similarity
Binding site1241Substrate By similarity
Binding site1721Substrate By similarity

Secondary structure

........................... 191
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9KPY2 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: B5A57D89F437FED0

FASTA19120,646
        10         20         30         40         50         60 
MYQDLIRSEL TEAADVLQKF LSDDHNIAQI EAAAKLIADS FKQGGKVLSC GNGGSHCDAM 

        70         80         90        100        110        120 
HFAEELTGRY RENRPGYPGI AISDPSHLSC VSNDFGYDYV FSRYVEAVGA KGDVLFGLST 

       130        140        150        160        170        180 
SGNSGNILKA IEAAKAKGMK TIALTGKDGG KMAGLADVEI RVPHFGYADR IQEVHIKIIH 

       190 
IIIQLIEKEM A 

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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.
[2]"Novel pathways for biosynthesis of nucleotide-activated glycero-manno-heptose precursors of bacterial glycoproteins and cell surface polysaccharides."
Valvano M.A., Messner P., Kosma P.
Microbiology 148:1979-1989(2002) [PubMed: 12101286] [Abstract]
Cited for: BIOSYNTHESIS OF NUCLEOTIDE-ACTIVATED GLYCERO-MANNO-HEPTOSE.
[3]"Crystal structures of two putative phosphoheptose isomerases."
Seetharaman J., Rajashankar K.R., Solorzano V., Kniewel R., Lima C.D., Bonanno J.B., Burley S.K., Swaminathan S.
Proteins 63:1092-1096(2006) [PubMed: 16477602] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE003852 Genomic DNA. Translation: AAF95374.1.
PIRB82104.
RefSeqNP_231861.1. NC_002505.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1X94X-ray2.50A/B1-191[»]
ProteinModelPortalQ9KPY2.
SMRQ9KPY2. Positions 1-190.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2613270.
GenomeReviewsGene locus VC_2230 in contig AE003852_GR.
KEGGvch:VC2230.
PATRIC20083505. VBIVibCho83274_2127.
TIGRVC_2230.

Phylogenomic databases

HOGENOMHBG671955.
OMAANDLGYD.
PhylomeDBQ9KPY2.
ProtClustDBPRK00414.

Family and domain databases

HAMAPMF_00067. GmhA.
[Tree]
InterProIPR004515. Phosphoheptose_Isoase_subgr.
IPR020620. Phosphoheptose_isomerase.
IPR001347. SIS.
[Graphical view]
KOK03271.
PfamPF01380. SIS. 1 hit.
[Graphical view]
TIGRFAMsTIGR00441. GmhA. 1 hit.
PROSITEPS51464. SIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGMHA_VIBCH
AccessionPrimary (citable) accession number: Q9KPY2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families