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P84140

- G6PI_THELI

UniProt

P84140 - G6PI_THELI

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Protein

Glucose-6-phosphate isomerase

Gene
pgiA
Organism
Thermococcus litoralis
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-glucose 6-phosphate = D-fructose 6-phosphate.1 Publication

Cofactori

Binds 1 iron ion per subunit.2 Publications

Enzyme regulationi

Inhibited by mannose 6-phosphate, fructose 1-phosphate and fructose 1,6-bisphosphate. Its activity is also inhibited by Cobalt (II) ions < EDTA < nickel (II) ions < zinc (II) ions << cadmium (II) ions < copper (II) ions. Sodium and potassium ions and manganese ions show little or no effect on activity.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi89 – 891Iron
Metal bindingi91 – 911Iron
Metal bindingi98 – 981Iron
Metal bindingi137 – 1371Iron

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Gluconeogenesis, Glycolysis

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

SABIO-RKP84140.
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
OrganismiThermococcus litoralis
Taxonomic identifieri2265 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi89 – 891H → A: Loss of catalytic activity. 1 Publication
Mutagenesisi91 – 911H → A: Loss of catalytic activity. 1 Publication
Mutagenesisi98 – 981E → V: Loss of catalytic activity. 1 Publication
Mutagenesisi137 – 1371H → A: Loss of catalytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 190190Glucose-6-phosphate isomeraseUniRule annotationPRO_0000185360Add
BLAST

Interactioni

Subunit structurei

Homodimer.2 Publications

Structurei

Secondary structure

1
190
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 115
Turni13 – 153
Beta strandi22 – 276
Helixi28 – 303
Turni32 – 343
Helixi38 – 4710
Beta strandi51 – 588
Beta strandi67 – 748
Beta strandi98 – 1058
Beta strandi107 – 1126
Beta strandi118 – 1236
Beta strandi127 – 1315
Beta strandi136 – 1416
Beta strandi143 – 1453
Beta strandi147 – 1548
Helixi162 – 1676
Beta strandi170 – 18314

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J3PX-ray2.02A/B1-190[»]
1J3QX-ray1.85A/B1-190[»]
1J3RX-ray2.18A/B1-190[»]
ProteinModelPortaliP84140.
SMRiP84140. Positions 1-187.

Miscellaneous databases

EvolutionaryTraceiP84140.

Family & Domainsi

Sequence similaritiesi

Belongs to the archaeal-type GPI family.

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.

P84140-1 [UniParc]FASTAAdd to Basket

« Hide

MKYKEPFGVK LDFETGIIEN AKKSVRRLSD MKGYFIDEEA WKKMVEEGDP    50
VVYEVYAIEQ EEKEGDLNFA TTVLYPGKVG NEFFMTKGHY HSKIDRAEVY 100
FALKGKGGML LQTPEGEARF IEMEPGTIVY VPPYWAHRTI NTGDKPFIFL 150
ALYPADAGHD YGTIAEKGFS KIVVEENGKV VVKDNPKWRM 190
Length:190
Mass (Da):21,720
Last modified:September 13, 2004 - v1
Checksum:i0D91C56E61DD7D3F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB081724 Genomic DNA. No translation available.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB081724 Genomic DNA. No translation available.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1J3P X-ray 2.02 A/B 1-190 [» ]
1J3Q X-ray 1.85 A/B 1-190 [» ]
1J3R X-ray 2.18 A/B 1-190 [» ]
ProteinModelPortali P84140.
SMRi P84140. Positions 1-187.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00181 .
SABIO-RK P84140.

Miscellaneous databases

EvolutionaryTracei P84140.

Family and domain databases

Gene3Di 2.60.120.10. 1 hit.
HAMAPi MF_01410. G6P_isomerase_arch.
InterProi IPR010551. G6P_isomerase_prok.
IPR016758. G6P_isomerase_subgr.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view ]
Pfami PF06560. GPI. 1 hit.
[Graphical view ]
PIRSFi PIRSF019325. Glucose-6-phosphate_isomerase. 1 hit.
SUPFAMi SSF51182. SSF51182. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Characterization of the cupin-type phosphoglucose isomerase from the hyperthermophilic archaeon Thermococcus litoralis."
    Jeong J.-J., Fushinobu S., Ito S., Jeon B.S., Shoun H., Wakagi T.
    FEBS Lett. 535:200-204(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, SUBUNIT, MUTAGENESIS OF HIS-89; HIS-91; GLU-98 AND HIS-137.
  2. "Crystal structure of Thermococcus litoralis phosphoglucose isomerase."
    Jeong J.-J., Fushinobu S., Hidaka M., Shoun H., Wakagi T.
    Submitted (FEB-2004) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), COFACTOR, SUBUNIT.

Entry informationi

Entry nameiG6PI_THELI
AccessioniPrimary (citable) accession number: P84140
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: September 13, 2004
Last modified: June 11, 2014
This is version 47 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

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

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