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B1WYG5 (GMHA_CYAA5) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 28. 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:cce_0043
OrganismCyanothece sp. (strain ATCC 51142) [Complete proteome] [HAMAP]
Taxonomic identifier43989 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaChroococcalesCyanothece

Protein attributes

Sequence length196 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 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

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

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasm
   LigandMetal-binding
Zinc
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processlipopolysaccharide 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: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

sugar binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 196196Phosphoheptose isomerase HAMAP MF_00067
PRO_1000092269

Regions

Domain31 – 196166SIS
Region46 – 483Substrate binding By similarity
Region88 – 892Substrate binding By similarity
Region114 – 1163Substrate binding By similarity

Sites

Metal binding551Zinc By similarity
Metal binding591Zinc By similarity
Metal binding1661Zinc By similarity
Metal binding1741Zinc By similarity
Binding site591Substrate By similarity
Binding site1191Substrate By similarity
Binding site1661Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B1WYG5 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: DB512B6BCEA64E3C

FASTA19621,641
        10         20         30         40         50         60 
MNYWIQHRLN CLEQAFNPKY CRALEHTIGI VARQFKAGNK LLICGNGGSA ADAQHIAAEF 

        70         80         90        100        110        120 
VGRFQLHRKG LPAIALGTNP ATLTAWSNDY EFETVFARQV EAFAQPGDIL WGISTSGKSA 

       130        140        150        160        170        180 
NVIRAMEMAK DLGLLTIGMA GNNGGMLKDL TDYPLFVSEY HTPYIQEIHL ITYHRICEQV 

       190 
EAQLFAKAGL EAQIAV 

« Hide

References

[1]"The genome of Cyanothece 51142, a unicellular diazotrophic cyanobacterium important in the marine nitrogen cycle."
Welsh E.A., Liberton M., Stoeckel J., Loh T., Elvitigala T., Wang C., Wollam A., Fulton R.S., Clifton S.W., Jacobs J.M., Aurora R., Ghosh B.K., Sherman L.A., Smith R.D., Wilson R.K., Pakrasi H.B.
Proc. Natl. Acad. Sci. U.S.A. 105:15094-15099(2008) [PubMed: 18812508] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51142.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000806 Genomic DNA. Translation: ACB49395.1.
RefSeqYP_001801461.1. NC_010546.1.

3D structure databases

ProteinModelPortalB1WYG5.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1WYG5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6167307.
GenomeReviewsGene locus cce_0043 in contig CP000806_GR.
KEGGcyt:cce_0043.
PATRIC21538560. VBICyaSp130209_0132.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG671955.
OMAHITIIHI.
ProtClustDBCLSK2301919.

Family and domain databases

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

Entry information

Entry nameGMHA_CYAA5
AccessionPrimary (citable) accession number: B1WYG5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 20, 2008
Last modified: January 25, 2012
This is version 28 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

SIMILARITY comments

Index of protein domains and families