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Q59000 (G6PI_METJA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:MJ1605
OrganismMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]
Taxonomic identifier243232 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus

Protein attributes

Sequence length401 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the isomerization of glucose-6-P to fructose-6-P. Ref.2 Ref.3

Catalytic activity

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

Enzyme regulation

Competively inhibited by 6-phosphogluconate and erythrose 4-phosphate. Ref.2

Pathway

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

Subunit structure

Homodimer. Ref.2

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00473.

Sequence similarities

Belongs to the GPI family.

Biophysicochemical properties

Kinetic parameters:

KM=0.04 mM for F6P (at pH 6.3 and 50 degrees Celsius) Ref.2

KM=1 mM for G6P (at pH 6.3 and 50 degrees Celsius)

Vmax=9 µmol/min/mg enzyme for G6P (at pH 6.3 and 50 degrees Celsius)

Vmax=21 µmol/min/mg enzyme for F6P (at pH 6.3 and 50 degrees Celsius)

pH dependence:

Optimum pH is 6.3. 50% remaining activity is observed at pH 5.3 and pH 7.

Temperature dependence:

Optimum temperature is 89 degrees Celsius. It does not lose activity upon incubation at 80 degrees Celsius for about 120 min and still has a half-life at 95 degrees Celsius of 40 min. At 100 degrees Celsius, an almost complete loss of activity is observed after 30 min.

Ontologies

Keywords
   Biological processGluconeogenesis
Glycolysis
   Cellular componentCytoplasm
   Molecular functionIsomerase
   Technical termComplete proteome
Reference 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 direct assay Ref.2. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 401401Glucose-6-phosphate isomerase HAMAP-Rule MF_00473
PRO_0000180780

Sites

Active site2611Proton donor By similarity
Active site2821 By similarity
Active site3921 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q59000 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: D5B766A9F2230ED9

FASTA40145,675
        10         20         30         40         50         60 
MLSYDYENAL KVGEISLEDI NKVDFANAYS NLMEKLDNGV VGFRDVIYDE NLDKYKSLNG 

        70         80         90        100        110        120 
YENVVVIGMG GSILGTMAIY YAISPFNNNA YFIDNSDPEK TLSILKKVDL NESIIYIISK 

       130        140        150        160        170        180 
SGNTLETLVN YYLIKKRIEK LNSFKGKLVF ITNGGKLKRE AEKNNYDIFS IPENVPGRFS 

       190        200        210        220        230        240 
VFTAVGLAPL YSLGVDISKI LEGAREMDKI CQNEDILKNP ALLNGVIHYL YDKRGKDISV 

       250        260        270        280        290        300 
IMSYVESLKY FGDWYKQLIG ESLGKNKHGI TPLLSIGAKD QHSLLQLYMD GKKDKIITFM 

       310        320        330        340        350        360 
VAKKYRLDEE IEFEDINDEK ISCRYSDIIR SQQKATEIAL TNNGVPNVRI TLDEINEMAM 

       370        380        390        400 
GALLYMYEMQ VGFMGELYNI NAYNQPAVEE EKKICWRLIK Q 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii."
Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. expand/collapse author list , Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.
Science 273:1058-1073(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
[2]"Glucose-6-phosphate isomerase from the hyperthermophilic archaeon Methanococcus jannaschii: characterization of the first archaeal member of the phosphoglucose isomerase superfamily."
Rudolph B., Hansen T., Schonheit P.
Arch. Microbiol. 181:82-87(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A GLUCOSE-6-PHOSPHATE ISOMERASE, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT.
[3]"Methylglyoxal is an intermediate in the biosynthesis of 6-deoxy-5-ketofructose-1-phosphate: a precursor for aromatic amino acid biosynthesis in Methanocaldococcus jannaschii."
White R.H., Xu H.
Biochemistry 45:12366-12379(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A GLUCOSE-6-PHOSPHATE ISOMERASE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L77117 Genomic DNA. Translation: AAB99624.1.
PIRD64500.
RefSeqNP_248615.1. NC_000909.1.

3D structure databases

ProteinModelPortalQ59000.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243232.MJ1605.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB99624; AAB99624; MJ_1605.
GeneID1452514.
KEGGmja:MJ_1605.

Phylogenomic databases

eggNOGCOG0166.
KOK01810.
OMADWYRQLW.
ProtClustDBPRK00973.

Enzyme and pathway databases

SABIO-RKQ59000.
UniPathwayUPA00109; UER00181.

Family and domain databases

HAMAPMF_00473. G6P_isomerase.
InterProIPR001672. G6P_Isomerase.
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_METJA
AccessionPrimary (citable) accession number: Q59000
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: November 1, 1996
Last modified: February 19, 2014
This is version 80 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

Methanococcus jannaschii

Methanococcus jannaschii: entries and gene names