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Protein

Phosphoheptose isomerase

Gene

gmhA

Organism
Burkholderia pseudomallei (strain K96243)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate.1 Publication

Catalytic activityi

D-sedoheptulose 7-phosphate = D-glycero-D-manno-heptose 7-phosphate.1 Publication

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Pathwayi: D-glycero-D-manno-heptose 7-phosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate.
Proteins known to be involved in this subpathway in this organism are:
  1. Phosphoheptose isomerase (gmhA)
This subpathway is part of the pathway D-glycero-D-manno-heptose 7-phosphate biosynthesis, which is itself part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate, the pathway D-glycero-D-manno-heptose 7-phosphate biosynthesis and in Carbohydrate biosynthesis.

Pathwayi: capsule polysaccharide biosynthesis

This protein is involved in the pathway capsule polysaccharide biosynthesis, which is part of Capsule biogenesis.
View all proteins of this organism that are known to be involved in the pathway capsule polysaccharide biosynthesis and in Capsule biogenesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi64 – 641Zinc1 Publication
Metal bindingi68 – 681Zinc1 Publication
Binding sitei68 – 681Substrate
Binding sitei128 – 1281Substrate
Metal bindingi175 – 1751Zinc1 Publication
Binding sitei175 – 1751Substrate
Metal bindingi183 – 1831Zinc1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Capsule biogenesis/degradation, Carbohydrate metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciBPSE272560:GJNI-2870-MONOMER.
BRENDAi5.3.1.28. 1031.
UniPathwayiUPA00041; UER00436.
UPA00934.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoheptose isomerase (EC:5.3.1.28)
Alternative name(s):
Sedoheptulose 7-phosphate isomerase
Gene namesi
Name:gmhA
Ordered Locus Names:BPSL2795
OrganismiBurkholderia pseudomallei (strain K96243)
Taxonomic identifieri272560 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
Proteomesi
  • UP000000605 Componenti: Chromosome 1

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi61 – 611D → A: Less than 6% of wild-type activity. 1 Publication
Mutagenesisi64 – 641H → Q: Less than 10% of wild-type activity. 1 Publication
Mutagenesisi68 – 681E → Q: No activity. 1 Publication
Mutagenesisi98 – 981D → N: No activity. 1 Publication
Mutagenesisi124 – 1241T → A: No activity. 1 Publication
Mutagenesisi175 – 1751Q → E: No activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 197197Phosphoheptose isomerasePRO_0000136521Add
BLAST

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi272560.BPSL2795.

Structurei

Secondary structure

1
197
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 2421Combined sources
Helixi27 – 4519Combined sources
Beta strandi50 – 534Combined sources
Helixi57 – 7014Combined sources
Beta strandi73 – 753Combined sources
Beta strandi82 – 843Combined sources
Helixi89 – 9911Combined sources
Helixi101 – 1033Combined sources
Helixi106 – 1127Combined sources
Beta strandi118 – 1225Combined sources
Beta strandi124 – 1263Combined sources
Helixi129 – 14012Combined sources
Beta strandi144 – 1496Combined sources
Helixi156 – 1594Combined sources
Beta strandi161 – 1655Combined sources
Helixi171 – 19424Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2X3YX-ray2.40A/B/C/D/E/F/G/H1-197[»]
2XBLX-ray1.62A/B/C/D1-197[»]
ProteinModelPortaliQ93UJ2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ93UJ2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 197158SISAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni55 – 573Substrate binding
Regioni97 – 982Substrate binding
Regioni123 – 1253Substrate binding

Sequence similaritiesi

Belongs to the SIS family. GmhA subfamily.Curated
Contains 1 SIS domain.Curated

Phylogenomic databases

eggNOGiENOG4105F55. Bacteria.
COG0279. LUCA.
HOGENOMiHOG000237571.
KOiK03271.
OMAiQEAHIFI.
OrthoDBiEOG6384PC.

Family and domain databases

HAMAPiMF_00067. GmhA.
InterProiIPR004515. Phosphoheptose_Isoase.
IPR001347. SIS.
[Graphical view]
PfamiPF13580. SIS_2. 1 hit.
[Graphical view]
PROSITEiPS51464. SIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q93UJ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENRELTYIT NSIAEAQRVM AAMLADERLL ATVRKVADAC IASIAQGGKV
60 70 80 90 100
LLAGNGGSAA DAQHIAGEFV SRFAFDRPGL PAVALTTDTS ILTAIGNDYG
110 120 130 140 150
YEKLFSRQVQ ALGNEGDVLI GYSTSGKSPN ILAAFREAKA KGMTCVGFTG
160 170 180 190
NRGGEMRELC DLLLEVPSAD TPKIQEGHLV LGHIVCGLVE HSIFGKQ
Length:197
Mass (Da):20,813
Last modified:November 23, 2004 - v2
Checksum:i22A249C834AC585B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti34 – 341R → Q in AAK49808 (PubMed:11119486).Curated
Sequence conflicti115 – 1151E → K in AAK49808 (PubMed:11119486).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF228583 Genomic DNA. Translation: AAK49808.1.
BX571965 Genomic DNA. Translation: CAH36804.1.
RefSeqiWP_011205222.1. NC_006350.1.
YP_109390.1. NC_006350.1.

Genome annotation databases

EnsemblBacteriaiCAH36804; CAH36804; BPSL2795.
GeneIDi3092932.
KEGGibps:BPSL2795.
PATRICi19265991. VBIBurPse99623_3191.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF228583 Genomic DNA. Translation: AAK49808.1.
BX571965 Genomic DNA. Translation: CAH36804.1.
RefSeqiWP_011205222.1. NC_006350.1.
YP_109390.1. NC_006350.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2X3YX-ray2.40A/B/C/D/E/F/G/H1-197[»]
2XBLX-ray1.62A/B/C/D1-197[»]
ProteinModelPortaliQ93UJ2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272560.BPSL2795.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAH36804; CAH36804; BPSL2795.
GeneIDi3092932.
KEGGibps:BPSL2795.
PATRICi19265991. VBIBurPse99623_3191.

Phylogenomic databases

eggNOGiENOG4105F55. Bacteria.
COG0279. LUCA.
HOGENOMiHOG000237571.
KOiK03271.
OMAiQEAHIFI.
OrthoDBiEOG6384PC.

Enzyme and pathway databases

UniPathwayiUPA00041; UER00436.
UPA00934.
BioCyciBPSE272560:GJNI-2870-MONOMER.
BRENDAi5.3.1.28. 1031.

Miscellaneous databases

EvolutionaryTraceiQ93UJ2.

Family and domain databases

HAMAPiMF_00067. GmhA.
InterProiIPR004515. Phosphoheptose_Isoase.
IPR001347. SIS.
[Graphical view]
PfamiPF13580. SIS_2. 1 hit.
[Graphical view]
PROSITEiPS51464. SIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Detection of bacterial virulence genes by subtractive hybridization: identification of capsular polysaccharide of Burkholderia pseudomallei as a major virulence determinant."
    Reckseidler S.L., DeShazer D., Sokol P.A., Woods D.E.
    Infect. Immun. 69:34-44(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K96243.
  3. "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] [Europe PMC] [Abstract]
    Cited for: BIOSYNTHESIS OF NUCLEOTIDE-ACTIVATED GLYCERO-MANNO-HEPTOSE.
  4. "The structure of sedoheptulose-7-phosphate isomerase from Burkholderia pseudomallei reveals a zinc binding site at the heart of the active site."
    Harmer N.J.
    J. Mol. Biol. 400:379-392(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH ZINC AND D-GLYCERO-ALPHA-D-MANNO-HEPTOSE 7-PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, REACTION MECHANISM, MUTAGENESIS OF ASP-61; HIS-64; GLU-68; ASP-98; THR-124 AND GLN-175.

Entry informationi

Entry nameiGMHA_BURPS
AccessioniPrimary (citable) accession number: Q93UJ2
Secondary accession number(s): Q63R78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: November 23, 2004
Last modified: November 11, 2015
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.