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P42861 (G6PI_LEIME) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 64. 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
OrganismLeishmania mexicana
Taxonomic identifier5665 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmania

Protein attributes

Sequence length605 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 HAMAP-Rule MF_00473.

Sequence similarities

Belongs to the GPI family.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

glycolysis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglucose-6-phosphate isomerase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 605605Glucose-6-phosphate isomerase HAMAP-Rule MF_00473
PRO_0000180546

Sites

Active site4101Proton donor By similarity
Active site4411 By similarity
Active site5691 By similarity

Secondary structure

............................................................................................ 605
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P42861 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 5C43210BF13FED71

FASTA60567,287
        10         20         30         40         50         60 
MSDYFSKLKE HVVESTEING CTPSIATATF NAPYEVARKT KMLGVTDSSL LNLPAWKRLQ 

        70         80         90        100        110        120 
SLYEKYGNDS ILSHFEKDHQ RFQRYSIEID LHSDDNFLFL DYSKSHINDE IKDALVALAE 

       130        140        150        160        170        180 
ERGVRAFAKA MFDGQRVNST ENRAVLHVAL RNRSNRPIIV DGKDVMSDVN NVLAQMKDFT 

       190        200        210        220        230        240 
ERVRSGEWKG QTGKSIYNIV NIGIGGSDLG PVMVTEALKP FSKRDLHCFF VSNVDGTHMA 

       250        260        270        280        290        300 
EVLKQVNLEE TIFIIASKTF TTQETLTNAM SARNALMSYL KENGISTDGA VAKHFVALST 

       310        320        330        340        350        360 
NTEKVREFGI DTVNMFAFWD WVGGRYSVWS AIGLSVMLSI GYDNFVEFLT GAHVMDNHFA 

       370        380        390        400        410        420 
STPTEQNLPM MLALVGIWYN NFFGSETQAV LPYDQYLWRL PAYLQQLDME SNGKGVTKKS 

       430        440        450        460        470        480 
GAVAVQTGPI VFGEAGTNGQ HAFYQLIHQG TKIIPCDFIG CVQTQNRVGD HHRTLMSNFF 

       490        500        510        520        530        540 
AQTEALMVGK NAEEVRQELV KSGMSGDAIE NMIPHKTFTG SRPSNSILVN ALTPRALGAI 

       550        560        570        580        590        600 
IAMYEHKVLV QGAIWGINSY DQWGVELGKV LAKSILPQLK SGNIVSDHDG STNGLINMFN 


TRAHL 

« Hide

References

[1]"Subcellular distribution and characterization of glucosephosphate isomerase in Leishmania mexicana mexicana."
Nyame K., Do Thi C.D., Opperdoes F.R., Michels P.A.M.
Mol. Biochem. Parasitol. 67:269-279(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NHOM/BZ/84/BEL46.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X78206 Genomic DNA. Translation: CAA55042.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q50X-ray2.60A44-604[»]
1T10X-ray2.35A1-605[»]
ProteinModelPortalP42861.
SMRP42861. Positions 44-604.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP42861.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

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...

Other

EvolutionaryTraceP42861.

Entry information

Entry nameG6PI_LEIME
AccessionPrimary (citable) accession number: P42861
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 19, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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