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Q5QWW0 (G6PI_IDILO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. 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:IL0570
OrganismIdiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR) [Complete proteome] [HAMAP]
Taxonomic identifier283942 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesIdiomarinaceaeIdiomarina

Protein attributes

Sequence length489 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 – 489489Glucose-6-phosphate isomerase HAMAP-Rule MF_00473
PRO_0000180654

Sites

Active site3091Proton donor By similarity
Active site3401 By similarity
Active site4591 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5QWW0 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 785139F668BE9602

FASTA48954,110
        10         20         30         40         50         60 
MIKNGPYLAL DTSYQKLSVD ELLETAGKRL PEHFDDYRQQ LCRGEYRNIS EDRPVTHVLS 

        70         80         90        100        110        120 
RSVHAVAKQS NRKTRFVDTV QKLRSGRRLG STGKPITDVV NIGVGGSDLG PQMGAFALRE 

       130        140        150        160        170        180 
FANDAALHNL QVHFVSSMDG GQLYAVLPIV DPETTLFIIS SKSFGTVDTF ANVDTVRKWI 

       190        200        210        220        230        240 
EPELTQEQWL ENHVIGVSAN AQGMTDYGIP PAQQFTFGDG VGGRFSLWSA LGLSIALTTG 

       250        260        270        280        290        300 
IRPFERMLEG AKAMDEHFLD APLNENLPVL LALYGVYNRE QLGINNLAIL PYDGRLRMLP 

       310        320        330        340        350        360 
NYLQQLDMES NGKQYTAENE AIDYPTGPII WGGFGPNGQH AFFQHLHQGY DQFTADFVTV 

       370        380        390        400        410        420 
LKREAPGFSD ATRSGLAEQQ RLAVANCLAH RRLMSDGSEN ADSPSDHYPG GHPSNLLIMD 

       430        440        450        460        470        480 
ELTPESFGAL IAAYEHKVFT QGVIWGLNSF DQPGVEKGKK IAMDVLRVLD GESDESFDES 


TDAVIQRMR 

« Hide

References

[1]"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy."
Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. expand/collapse author list , Aizawa S., Shibata S., Malahoff A., Alam M.
Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-735 / DSM 15497 / L2-TR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017340 Genomic DNA. Translation: AAV81411.1.
RefSeqYP_154960.1. NC_006512.1.

3D structure databases

ProteinModelPortalQ5QWW0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING283942.IL0570.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV81411; AAV81411; IL0570.
GeneID3172033.
KEGGilo:IL0570.
PATRIC22139161. VBIIdiLoi21852_0572.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0166.
HOGENOMHOG000261370.
KOK01810.
OMALKMHFVS.
OrthoDBEOG64R61J.

Enzyme and pathway databases

BioCycILOI283942:GI0U-570-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_IDILO
AccessionPrimary (citable) accession number: Q5QWW0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: January 4, 2005
Last modified: February 19, 2014
This is version 58 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