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C7BI06 (C7BI06_PHOAA) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphoheptose isomerase HAMAP-Rule MF_00067
EC=5.3.1.28 HAMAP-Rule MF_00067
Alternative name(s):
Sedoheptulose 7-phosphate isomerase HAMAP-Rule MF_00067
Gene names
Name:gmhA HAMAP-Rule MF_00067
Ordered Locus Names:PAU_03260 EMBL CAQ85348.1
OrganismPhotorhabdus asymbiotica subsp. asymbiotica (strain ATCC 43949 / 3105-77) (Xenorhabdus luminescens (strain 2)) [Complete proteome] [HAMAP]
Taxonomic identifier553480 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Photorhabdus ›

Protein attributes

Sequence length193 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. SAAS SAAS004515 HAMAP-Rule MF_00067

Catalytic activity

D-sedoheptulose 7-phosphate = D-glycero-D-manno-heptose 7-phosphate. SAAS SAAS004515 HAMAP-Rule MF_00067

Cofactor

Binds 1 zinc ion per subunit By similarity. SAAS SAAS004515 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. SAAS SAAS004515 HAMAP-Rule MF_00067

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00067

Subcellular location

Cytoplasm By similarity SAAS SAAS004515 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. HAMAP-Rule MF_00067

Sequence similarities

Belongs to the SIS family. GmhA subfamily. HAMAP-Rule MF_00067

Contains 1 SIS domain. SAAS SAAS004515 HAMAP-Rule MF_00067

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain37 – 193157SIS By similarity HAMAP-Rule MF_00067
Region52 – 543Substrate binding By similarity HAMAP-Rule MF_00067
Region93 – 942Substrate binding By similarity HAMAP-Rule MF_00067
Region119 – 1213Substrate binding By similarity HAMAP-Rule MF_00067

Sites

Metal binding611Zinc By similarity HAMAP-Rule MF_00067
Metal binding651Zinc By similarity HAMAP-Rule MF_00067
Metal binding1721Zinc By similarity HAMAP-Rule MF_00067
Metal binding1801Zinc By similarity HAMAP-Rule MF_00067
Binding site651Substrate By similarity HAMAP-Rule MF_00067
Binding site1241Substrate By similarity HAMAP-Rule MF_00067
Binding site1721Substrate By similarity HAMAP-Rule MF_00067

Sequences

Sequence LengthMass (Da)Tools
C7BI06 [UniParc].

Last modified September 22, 2009. Version 1.
Checksum: 24FE6F1251C01626

FASTA19320,888
        10         20         30         40         50         60 
MYQELIRSEL NEAADTLAKF LSDDANIKAI QKAAVLLADS FKAGGKVLSC GNGGSHCDAM 

        70         80         90        100        110        120 
HFAEELTGRY RENRPGYPAI AISDVSHLSC VSNDFGYEFV FSRYVEAVGK EGDVLLGIST 

       130        140        150        160        170        180 
SGNSGNIIKA IEAARLKGMK VITLTGKDGG KMAGTADVEI RVPHFGYADR IQEIHIKVIH 

       190 
ILIQLIEKEM IKA

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References

[1]"Comparative genomics of the emerging human pathogen Photorhabdus asymbiotica with the insect pathogen Photorhabdus luminescens."
Wilkinson P., Waterfield N.R., Crossman L., Corton C., Sanchez-Contreras M., Vlisidou I., Barron A., Bignell A., Clark L., Doggett J., Ormond D., Mayho M., Bason N., Smith F., Simmonds M., Arrowsmith C., Churcher C., Harris D. expand/collapse author list , Thompson N.R., Quail M., Parkhill J., Ffrench-Constant R.H.
BMC Genomics 10:302-302(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43949 / 3105-77.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FM162591 Genomic DNA. Translation: CAQ85348.1.
RefSeqYP_003042090.1. NC_012962.1.

3D structure databases

ProteinModelPortalC7BI06.
ModBaseSearch...

Protein-protein interaction databases

STRING291112.PAU_03260.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAQ85348; CAQ85348; PAU_03260.
GeneID13860054.
KEGGpay:PAU_03260.
PATRIC20500858. VBIPhoAsy71438_3667.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000237571.
KOK03271.
OMAFLAHKEA.
ProtClustDBPRK00414.

Enzyme and pathway databases

BioCycPASY291112:GJQ0-3376-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 nameC7BI06_PHOAA
AccessionPrimary (citable) accession number: C7BI06
Entry history
Integrated into UniProtKB/TrEMBL: September 22, 2009
Last sequence update: September 22, 2009
Last modified: May 1, 2013
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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