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Protein

Glucose-6-phosphate isomerase

Gene

pgiA

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-glucose 6-phosphate = D-fructose 6-phosphate.

Cofactori

Fe cationBy similarityNote: Binds 1 Fe cation per subunit.By similarity

Enzyme regulationi

Inhibited by mannose 6-phosphate, fructose 1-phosphate and fructose 1,6-bisphosphate.

pH dependencei

Optimum pH is 7.0.

Temperature dependencei

Optimum temperature is 90-96 degrees Celsius. Highly thermostable.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi88 – 881IronBy similarity
Metal bindingi90 – 901IronBy similarity
Metal bindingi97 – 971IronBy similarity
Metal bindingi136 – 1361IronBy similarity

GO - Molecular functioni

  1. glucose-6-phosphate isomerase activity Source: UniProtKB-HAMAP
  2. iron ion binding Source: InterPro

GO - Biological processi

  1. gluconeogenesis Source: UniProtKB-HAMAP
  2. glycolytic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Gluconeogenesis, Glycolysis

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-11807.
SABIO-RKP83194.
UniPathwayiUPA00109; UER00181.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose-6-phosphate isomerase (EC:5.3.1.9)
Short name:
GPI
Alternative name(s):
Phosphoglucose isomerase
Short name:
PGI
Phosphohexose isomerase
Short name:
PHI
Gene namesi
Name:pgiA
Ordered Locus Names:PF0196
OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifieri186497 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
ProteomesiUP000001013: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 189189Glucose-6-phosphate isomerasePRO_0000185357Add
BLAST

Proteomic databases

PRIDEiP83194.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi186497.PF0196.

Structurei

Secondary structure

1
189
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 105Combined sources
Turni12 – 143Combined sources
Beta strandi22 – 265Combined sources
Helixi27 – 304Combined sources
Turni31 – 333Combined sources
Helixi37 – 4610Combined sources
Beta strandi50 – 578Combined sources
Beta strandi66 – 738Combined sources
Beta strandi91 – 944Combined sources
Beta strandi97 – 11115Combined sources
Beta strandi117 – 1226Combined sources
Beta strandi127 – 1304Combined sources
Beta strandi135 – 1406Combined sources
Beta strandi142 – 1443Combined sources
Beta strandi146 – 1538Combined sources
Helixi161 – 1666Combined sources
Beta strandi169 – 1757Combined sources
Beta strandi178 – 1836Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QXJX-ray1.80A/B1-189[»]
1QXRX-ray1.70A/B1-189[»]
1QY4X-ray1.80A/B1-189[»]
1X7NX-ray1.89A1-189[»]
1X82X-ray1.50A1-189[»]
1X8EX-ray2.80A/B1-189[»]
2GC0X-ray2.00A/B1-187[»]
2GC1X-ray1.95A/B1-187[»]
2GC2X-ray2.10A/B1-187[»]
2GC3X-ray2.10A/B1-187[»]
3SXWX-ray1.80A1-189[»]
4LTAX-ray2.04A/B1-189[»]
4LUKX-ray1.41A1-189[»]
4LULX-ray1.89A/B1-189[»]
4LUMX-ray1.79A/B1-189[»]
ProteinModelPortaliP83194.
SMRiP83194. Positions 1-189.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP83194.

Family & Domainsi

Sequence similaritiesi

Belongs to the archaeal-type GPI family.Curated

Phylogenomic databases

eggNOGiCOG2140.
HOGENOMiHOG000243903.
KOiK06859.
OMAiYPADAGH.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
HAMAPiMF_01410. G6P_isomerase_arch.
InterProiIPR010551. G6P_isomerase_prok.
IPR016758. G6P_isomerase_subgr.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF06560. GPI. 1 hit.
[Graphical view]
PIRSFiPIRSF019325. Glucose-6-phosphate_isomerase. 1 hit.
SUPFAMiSSF51182. SSF51182. 1 hit.

Sequencei

Sequence statusi: Complete.

P83194-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MYKEPFGVKV DFETGIIEGA KKSVRRLSDM EGYFVDERAW KELVEKEDPV
60 70 80 90 100
VYEVYAVEQE EKEGDLNFAT TVLYPGKVGK EFFFTKGHFH AKLDRAEVYV
110 120 130 140 150
ALKGKGGMLL QTPEGDAKWI SMEPGTVVYV PPYWAHRTVN IGDEPFIFLA
160 170 180
IYPADAGHDY GTIAEKGFSK IVIEENGEVK VVDNPRWKK
Length:189
Mass (Da):21,476
Last modified:March 1, 2002 - v1
Checksum:iC5D8380C59F2A785
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111D → N AA sequence (PubMed:11533028)Curated
Sequence conflicti28 – 281S → P AA sequence (PubMed:11344151)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF381250 Genomic DNA. Translation: AAL27992.1.
AE009950 Genomic DNA. Translation: AAL80320.1.
RefSeqiNP_577925.1. NC_003413.1.

Genome annotation databases

EnsemblBacteriaiAAL80320; AAL80320; PF0196.
GeneIDi1468028.
KEGGipfu:PF0196.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF381250 Genomic DNA. Translation: AAL27992.1.
AE009950 Genomic DNA. Translation: AAL80320.1.
RefSeqiNP_577925.1. NC_003413.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QXJX-ray1.80A/B1-189[»]
1QXRX-ray1.70A/B1-189[»]
1QY4X-ray1.80A/B1-189[»]
1X7NX-ray1.89A1-189[»]
1X82X-ray1.50A1-189[»]
1X8EX-ray2.80A/B1-189[»]
2GC0X-ray2.00A/B1-187[»]
2GC1X-ray1.95A/B1-187[»]
2GC2X-ray2.10A/B1-187[»]
2GC3X-ray2.10A/B1-187[»]
3SXWX-ray1.80A1-189[»]
4LTAX-ray2.04A/B1-189[»]
4LUKX-ray1.41A1-189[»]
4LULX-ray1.89A/B1-189[»]
4LUMX-ray1.79A/B1-189[»]
ProteinModelPortaliP83194.
SMRiP83194. Positions 1-189.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi186497.PF0196.

Proteomic databases

PRIDEiP83194.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL80320; AAL80320; PF0196.
GeneIDi1468028.
KEGGipfu:PF0196.

Phylogenomic databases

eggNOGiCOG2140.
HOGENOMiHOG000243903.
KOiK06859.
OMAiYPADAGH.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00181.
BioCyciMetaCyc:MONOMER-11807.
SABIO-RKP83194.

Miscellaneous databases

EvolutionaryTraceiP83194.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
HAMAPiMF_01410. G6P_isomerase_arch.
InterProiIPR010551. G6P_isomerase_prok.
IPR016758. G6P_isomerase_subgr.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF06560. GPI. 1 hit.
[Graphical view]
PIRSFiPIRSF019325. Glucose-6-phosphate_isomerase. 1 hit.
SUPFAMiSSF51182. SSF51182. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The phosphoglucose isomerase from the hyperthermophilic archaeon Pyrococcus furiosus is a unique glycolytic enzyme that belongs to the cupin superfamily."
    Verhees C.H., Huynen M.A., Ward D.E., Schiltz E., de Vos W.M., van der Oost J.
    J. Biol. Chem. 276:40926-40932(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20, CHARACTERIZATION.
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
  2. "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
    Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
    Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
  3. "Novel type of glucose-6-phosphate isomerase in the hyperthermophilic archaeon Pyrococcus furiosus."
    Hansen T., Oehlmann M., Schoenheit P.
    J. Bacteriol. 183:3428-3435(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-28, CHARACTERIZATION.
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.

Entry informationi

Entry nameiG6PI_PYRFU
AccessioniPrimary (citable) accession number: P83194
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: March 1, 2002
Last modified: January 7, 2015
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.