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Q664W9 (G6PI_YERPS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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:
Glucose-6-phosphate isomerase

Short name=GPI
EC=5.3.1.9
Alternative name(s):
Phosphoglucose isomerase
Short name=PGI
Phosphohexose isomerase
Short name=PHI
Gene names
Name:pgi
Ordered Locus Names:YPTB3649
OrganismYersinia pseudotuberculosis serotype I (strain IP32953) [Complete proteome] [HAMAP]
Taxonomic identifier273123 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length548 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

D-glucose 6-phosphate = D-fructose 6-phosphate. HAMAP-Rule MF_00473

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4. HAMAP-Rule MF_00473

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00473.

Sequence similarities

Belongs to the GPI family.

Ontologies

Keywords
   Biological processGluconeogenesis
Glycolysis
   Cellular componentCytoplasm
   Molecular functionIsomerase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processgluconeogenesis

Inferred from electronic annotation. Source: UniProtKB-HAMAP

glycolysis

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglucose-6-phosphate isomerase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 548548Glucose-6-phosphate isomerase HAMAP-Rule MF_00473
PRO_0000180776

Sites

Active site3551Proton donor By similarity
Active site3861 By similarity
Active site5141 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q664W9 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 3ED9D49B3A308A3B

FASTA54861,161
        10         20         30         40         50         60 
MKNINPSQTA AWKALQQHFE QMKDVTISSL FAKDDQRFNR FSATFDDQML VDFSKNRITS 

        70         80         90        100        110        120 
ETLEKLQDLA KETDLAGAIK SMFSGEKINR TEDRAVLHIA LRNRSNTPIV VDGKDVMPEV 

       130        140        150        160        170        180 
NAVLAKMKQF CDRVISGDWK GYTGKAITDV VNIGIGGSDL GPYMVTEALR PYKNHLNMHF 

       190        200        210        220        230        240 
VSNVDGTHIA EALKPLNPET TLFLVASKTF TTQETMTNAH SARDWFLSAA GDPAHVAKHF 

       250        260        270        280        290        300 
AALSTNAKAV GEFGIDTNNM FEFWDWVGGR YSLWSAIGLS IALSVGFEHF EQLLSGAHAM 

       310        320        330        340        350        360 
DKHFAETPAE KNLPVLLALI GIWYNNFFGA ETEAILPYDQ YMHRFPAYFQ QGNMESNGKY 

       370        380        390        400        410        420 
VDRNGHPVDY QTGPIIWGEP GTNGQHAFYQ LIHQGTKLIP CDFIAPAISH NPLSDHHAKL 

       430        440        450        460        470        480 
LSNFFAQTEA LAFGKSLEDV EAEFAAAGKT PEQVAHVAPF KVFEGNRPTN SILLREITPF 

       490        500        510        520        530        540 
SLGALIALYE HKIFTQGVIL NIYTFDQWGV ELGKQLANRI LPELADDQEV TSHDSSTNAL 


INRFKNWR 

« Hide

References

[1]"Insights into the evolution of Yersinia pestis through whole-genome comparison with Yersinia pseudotuberculosis."
Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O., Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L., Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C., Simonet M., Chenal-Francisque V., Souza B. expand/collapse author list , Dacheux D., Elliott J.M., Derbise A., Hauser L.J., Garcia E.
Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IP32953.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX936398 Genomic DNA. Translation: CAH22887.1.
RefSeqYP_072131.1. NC_006155.1.

3D structure databases

ProteinModelPortalQ664W9.
SMRQ664W9. Positions 7-548.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273123.YPTB3649.

Proteomic databases

PRIDEQ664W9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH22887; CAH22887; YPTB3649.
GeneID2956241.
KEGGyps:YPTB3649.
PATRIC18646680. VBIYerPse22266_4380.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0166.
HOGENOMHOG000261370.
KOK01810.
OMALKMHFVS.
OrthoDBEOG64R61J.
ProtClustDBPRK00179.

Enzyme and pathway databases

BioCycYPSE273123:GI1M-3761-MONOMER.
UniPathwayUPA00109; UER00181.

Family and domain databases

Gene3D1.10.1390.10. 1 hit.
HAMAPMF_00473. G6P_isomerase.
InterProIPR001672. G6P_Isomerase.
IPR023096. G6P_Isomerase_C.
IPR018189. Phosphoglucose_isomerase_CS.
[Graphical view]
PANTHERPTHR11469. PTHR11469. 1 hit.
PfamPF00342. PGI. 1 hit.
[Graphical view]
PRINTSPR00662. G6PISOMERASE.
PROSITEPS00765. P_GLUCOSE_ISOMERASE_1. 1 hit.
PS00174. P_GLUCOSE_ISOMERASE_2. 1 hit.
PS51463. P_GLUCOSE_ISOMERASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameG6PI_YERPS
AccessionPrimary (citable) accession number: Q664W9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: October 11, 2004
Last modified: February 19, 2014
This is version 57 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