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Q87L81 (G6PI_VIBPA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 67. 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:VP2731
OrganismVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) [Complete proteome] [HAMAP]
Taxonomic identifier223926 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length550 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

glycolytic process

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 – 550550Glucose-6-phosphate isomerase HAMAP-Rule MF_00473
PRO_0000180764

Sites

Active site3561Proton donor By similarity
Active site3871 By similarity
Active site5151 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q87L81 [UniParc].

Last modified May 23, 2003. Version 1.
Checksum: 1895C049D2D41B65

FASTA55060,913
        10         20         30         40         50         60 
MLKNINPTQT QAWKALTAHF ESAQDMDLKE LFAQDAARFD KYSARFGSDI LVDYSKNLIN 

        70         80         90        100        110        120 
EETLKHLFAL ANETELKSAI EAMFSGEAIN QTEGRAVLHT ALRNRTNTPV MVDGEDVMPA 

       130        140        150        160        170        180 
VNAVLEKMKS FTDRVIGGEW KGYTGKAITD IVNIGIGGSD LGPYMVTEAL APYKNHLNLH 

       190        200        210        220        230        240 
FVSNVDGTHI VETLKKVNPE TTLFLIASKT FTTQETMTNA HTARDWFLES AGDQAHVAKH 

       250        260        270        280        290        300 
FAALSTNATA VSEFGIDTAN MFEFWDWVGG RYSLWSAIGL SIALAVGYDN FVELLDGAHE 

       310        320        330        340        350        360 
MDKHFVSTDL ESNIPVILAL IGIWYNNFHG AESEAILPYD QYMHRFAAYF QQGNMESNGK 

       370        380        390        400        410        420 
YVDREGNAVT YQTGPIIWGE PGTNGQHAFY QLIHQGTKLI PCDFIAPAIS HNPAGDHHQK 

       430        440        450        460        470        480 
LMSNFFAQTE ALAFGKSEET VKEELVKAGK NAEEVAAIAP FKVFEGNRPT NSILVKQITP 

       490        500        510        520        530        540 
RTLGNLIAMY EHKIFVQGVI WNIFSFDQWG VELGKQLANQ ILPELADASQ INSHDSSTNG 

       550 
LINAFKAFKA 

« Hide

References

[1]"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RIMD 2210633.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000031 Genomic DNA. Translation: BAC60994.1.
RefSeqNP_799110.1. NC_004603.1.

3D structure databases

ProteinModelPortalQ87L81.
SMRQ87L81. Positions 8-546.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING223926.VP2731.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC60994; BAC60994; BAC60994.
GeneID1190281.
KEGGvpa:VP2731.
PATRIC20143672. VBIVibPar50997_2628.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0166.
HOGENOMHOG000261370.
KOK01810.
OMANCHFVAN.
OrthoDBEOG64R61J.

Enzyme and pathway databases

BioCycVPAR223926:GHK4-2825-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_VIBPA
AccessionPrimary (citable) accession number: Q87L81
Entry history
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: May 23, 2003
Last modified: June 11, 2014
This is version 67 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