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Q8K9R9 (GMHA_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 73. 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
Synonyms:lpcA
Ordered Locus Names:BUsg_241
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length194 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule 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-Rule MF_00067

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00067

Subcellular location

Cytoplasm By similarity HAMAP-Rule 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.

Sequence similarities

Belongs to the SIS family. GmhA subfamily.

Contains 1 SIS domain.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasm
   LigandMetal-binding
Zinc
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processD-glycero-D-manno-heptose 7-phosphate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

lipopolysaccharide core region biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionD-sedoheptulose 7-phosphate isomerase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

carbohydrate binding

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 194194Phosphoheptose isomerase HAMAP-Rule MF_00067
PRO_0000136519

Regions

Domain37 – 194158SIS
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

Sequences

Sequence LengthMass (Da)Tools
Q8K9R9 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 803DA6B727B36B30

FASTA19421,631
        10         20         30         40         50         60 
MYKKIISSEL DAALKILKNF LKNEEQIENI EKAAILIAKS FKNKNKVISC GNGGSHCDAV 

        70         80         90        100        110        120 
HFSEELTGLY REKRPGYAAI PISDVGHISA IGNDFGYDQI FSRYIESIGL PNDVLLAIST 

       130        140        150        160        170        180 
SGNSINIINA IQTAHRKKMK VIVLTGNDGG QVKHLSDVEI CIPYHGYSDR IQEMHIKIIH 

       190 
ILILIIEKEM KKIN 

« Hide

References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013218 Genomic DNA. Translation: AAM67800.1.
RefSeqNP_660589.1. NC_004061.1.

3D structure databases

ProteinModelPortalQ8K9R9.
SMRQ8K9R9. Positions 1-192.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg241.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67800; AAM67800; BUsg_241.
GeneID1005442.
KEGGbas:BUsg241.
PATRIC21247285. VBIBucAph100086_0252.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0279.
KOK03271.
OMAHVFSRYV.
OrthoDBEOG6384PC.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-255-MONOMER.
UniPathwayUPA00041; UER00436.

Family and domain databases

HAMAPMF_00067. GmhA.
InterProIPR004515. Phosphoheptose_Isoase.
IPR001347. SIS.
[Graphical view]
PfamPF13580. SIS_2. 1 hit.
[Graphical view]
TIGRFAMsTIGR00441. gmhA. 1 hit.
PROSITEPS51464. SIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGMHA_BUCAP
AccessionPrimary (citable) accession number: Q8K9R9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2002
Last modified: May 14, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names