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C6UX01 (C6UX01_ECO5T) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

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:lpcA EMBL ACT70142.1
Synonyms:gmhA HAMAP-Rule MF_00067
Ordered Locus Names:ECSP_0254 EMBL ACT70142.1
OrganismEscherichia coli O157:H7 (strain TW14359 / EHEC) [Complete proteome] [HAMAP] EMBL ACT70142.1
Taxonomic identifier544404 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

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. 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. HAMAP-Rule MF_00067

Contains SIS domain. SAAS SAAS004515

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Domain37 – 192156SIS 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
C6UX01 [UniParc].

Last modified September 22, 2009. Version 1.
Checksum: 7A2C05E1079108B4

FASTA19220,815
        10         20         30         40         50         60 
MYQDLIRNEL NEAAETLANF LKDDANIHAI QRAAVLLADS FKAGGKVLSC GNGGSHCDAM 

        70         80         90        100        110        120 
HFAEELTGRY RENRPGYPAI AISDVSHISC VGNDFGFNDI FSRYVEAVGR EGDVLLGIST 

       130        140        150        160        170        180 
SGNSANVIKA IAAAREKGMK VITLTGKDGG KMAGTADIEI RVPHFGYADR IQEIHIKVIH 

       190 
ILIQLIEKEM VK 

« Hide

References

[1]"Analysis of the genome of the Escherichia coli O157:H7 2006 spinach-associated outbreak isolate indicates candidate genes that may enhance virulence."
Kulasekara B.R., Jacobs M., Zhou Y., Wu Z., Sims E., Saenphimmachak C., Rohmer L., Ritchie J.M., Radey M., McKevitt M., Freeman T.L., Hayden H., Haugen E., Gillett W., Fong C., Chang J., Beskhlebnaya V., Waldor M.K. expand/collapse author list , Samadpour M., Whittam T.S., Kaul R., Brittnacher M., Miller S.I.
Infect. Immun. 77:3713-3721(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TW14359 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001368 Genomic DNA. Translation: ACT70142.1.
RefSeqYP_003076218.1. NC_013008.1.

3D structure databases

ProteinModelPortalC6UX01.
SMRC6UX01. Positions 1-192.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING544404.ECSP_0254.

Proteomic databases

PRIDEC6UX01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACT70142; ACT70142; ECSP_0254.
GeneID8214820.
KEGGetw:ECSP_0254.
PATRIC18384342. VBIEscCol9396_0253.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0279.
HOGENOMHOG000237571.
KOK03271.
OMAFLAHKEA.
OrthoDBEOG6384PC.
ProtClustDBPRK00414.

Enzyme and pathway databases

BioCycECOL544404:GKCX-254-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 nameC6UX01_ECO5T
AccessionPrimary (citable) accession number: C6UX01
Entry history
Integrated into UniProtKB/TrEMBL: September 22, 2009
Last sequence update: September 22, 2009
Last modified: February 19, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)