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P84140 (G6PI_THELI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 46. 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:pgiA
OrganismThermococcus litoralis
Taxonomic identifier2265 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus

Protein attributes

Sequence length190 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 1 iron ion per subunit. Ref.1 Ref.2

Enzyme regulation

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. Ref.1

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4. HAMAP-Rule MF_01410

Subunit structure

Homodimer. Ref.1 Ref.2

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01410.

Sequence similarities

Belongs to the archaeal-type GPI family.

Ontologies

Keywords
   Biological processGluconeogenesis
Glycolysis
   Cellular componentCytoplasm
   LigandIron
Metal-binding
   Molecular functionIsomerase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_processgluconeogenesis

Traceable author statement Ref.1. Source: UniProtKB

glycolysis

Traceable author statement Ref.1. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglucose-6-phosphate isomerase activity

Inferred from direct assay Ref.1. Source: UniProtKB

iron ion binding

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 190190Glucose-6-phosphate isomerase HAMAP-Rule MF_01410
PRO_0000185360

Sites

Metal binding891Iron
Metal binding911Iron
Metal binding981Iron
Metal binding1371Iron

Experimental info

Mutagenesis891H → A: Loss of catalytic activity. Ref.1
Mutagenesis911H → A: Loss of catalytic activity. Ref.1
Mutagenesis981E → V: Loss of catalytic activity. Ref.1
Mutagenesis1371H → A: Loss of catalytic activity. Ref.1

Secondary structure

.................................. 190
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P84140 [UniParc].

Last modified September 13, 2004. Version 1.
Checksum: 0D91C56E61DD7D3F

FASTA19021,720
        10         20         30         40         50         60 
MKYKEPFGVK LDFETGIIEN AKKSVRRLSD MKGYFIDEEA WKKMVEEGDP VVYEVYAIEQ 

        70         80         90        100        110        120 
EEKEGDLNFA TTVLYPGKVG NEFFMTKGHY HSKIDRAEVY FALKGKGGML LQTPEGEARF 

       130        140        150        160        170        180 
IEMEPGTIVY VPPYWAHRTI NTGDKPFIFL ALYPADAGHD YGTIAEKGFS KIVVEENGKV 

       190 
VVKDNPKWRM 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB081724 Genomic DNA. No translation available.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1J3PX-ray2.02A/B1-190[»]
1J3QX-ray1.85A/B1-190[»]
1J3RX-ray2.18A/B1-190[»]
ProteinModelPortalP84140.
SMRP84140. Positions 1-187.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP84140.
UniPathwayUPA00109; UER00181.

Family and domain databases

Gene3D2.60.120.10. 1 hit.
HAMAPMF_01410. G6P_isomerase_arch.
InterProIPR010551. G6P_isomerase_prok.
IPR016758. G6P_isomerase_subgr.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamPF06560. GPI. 1 hit.
[Graphical view]
PIRSFPIRSF019325. Glucose-6-phosphate_isomerase. 1 hit.
SUPFAMSSF51182. SSF51182. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP84140.

Entry information

Entry nameG6PI_THELI
AccessionPrimary (citable) accession number: P84140
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: September 13, 2004
Last modified: February 19, 2014
This is version 46 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways