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B4EUT1 (GMHA_PROMH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:PMI0349
OrganismProteus mirabilis (strain HI4320) [Complete proteome] [HAMAP]
Taxonomic identifier529507 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeProteus

Protein attributes

Sequence length192 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 – 192192Phosphoheptose isomerase HAMAP-Rule MF_00067
PRO_1000092284

Regions

Domain37 – 192156SIS
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
B4EUT1 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 93C044E549B39254

FASTA19220,852
        10         20         30         40         50         60 
MYQDLIRGEL TEAADTLSRF LQDDANIEAI QKAAVLLADS FKAGGKVLSC GNGGSHCDAM 

        70         80         90        100        110        120 
HFAEELTGRY RENRPGYPAI AISDVSHISC VSNDFGYEYV FSRYVEAVGK EGDVLLGIST 

       130        140        150        160        170        180 
SGNSGNIIKA ISAAREKGMK VITLTGKDGG KMAGSADIEI RVPHFGYADR IQEIHIKVIH 

       190 
ILIQLIEKEM EK 

« Hide

References

[1]"Complete genome sequence of uropathogenic Proteus mirabilis, a master of both adherence and motility."
Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S., Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T., Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Walker D., Whithead S. expand/collapse author list , Thomson N.R., Rather P.N., Parkhill J., Mobley H.L.T.
J. Bacteriol. 190:4027-4037(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HI4320.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM942759 Genomic DNA. Translation: CAR40905.1.
RefSeqYP_002150122.1. NC_010554.1.

3D structure databases

ProteinModelPortalB4EUT1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING529507.PMI0349.

Proteomic databases

PRIDEB4EUT1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR40905; CAR40905; PMI0349.
GeneID6800936.
KEGGpmr:PMI0349.
PATRIC20515345. VBIProMir120933_0332.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0279.
HOGENOMHOG000237571.
KOK03271.
OMAHVFSRYV.
OrthoDBEOG6384PC.

Enzyme and pathway databases

BioCycPMIR529507:GJIW-346-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_PROMH
AccessionPrimary (citable) accession number: B4EUT1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: May 14, 2014
This is version 38 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