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P13377 (G6PI_TRYBB) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 78. 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, glycosomal

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
OrganismTrypanosoma brucei brucei
Taxonomic identifier5702 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma

Protein attributes

Sequence length607 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

Subunit structure

Homodimer.

Subcellular location

Glycosome HAMAP-Rule MF_00473.

Sequence similarities

Belongs to the GPI family.

Ontologies

Keywords
   Biological processGluconeogenesis
Glycolysis
   Cellular componentGlycosome
Peroxisome
   Molecular functionIsomerase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processgluconeogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

glycolytic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentglycosome

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 – 607607Glucose-6-phosphate isomerase, glycosomal HAMAP-Rule MF_00473
PRO_0000180548

Regions

Motif605 – 6073Microbody targeting signal Potential

Sites

Active site4111Proton donor By similarity
Active site4421 By similarity
Active site5711 By similarity

Secondary structure

.............................................................................................. 607
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13377 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: AB237B7261CF2B74

FASTA60767,518
        10         20         30         40         50         60 
MSSYLDDLRI DLAASPASGG SASIAVGSFN IPYEVTRRLK GVGADADTTL TSCASWTQLQ 

        70         80         90        100        110        120 
KLYEQYGDEP IKKHFEADSE RGQRYSVKVS LGSKDENFLF LDYSKSHIND EIKCALLRLA 

       130        140        150        160        170        180 
EERGIRQFVQ SVFRGERVNT TENRPVLHIA LRNRSNRPIY VDGKDVMPAV NKVLDQMRSF 

       190        200        210        220        230        240 
SEKVRTGEWK GHTGKAIRHV VNIGIGGSDL GPVMATEALK PFSQRDLSLH FVSNVDGTHI 

       250        260        270        280        290        300 
AEVLKSIDIE ATLFIVASKT FTTQETITNA LSARRALLDY LRSRGIDEKG SVAKHFVALS 

       310        320        330        340        350        360 
TNNQKVKEFG IDEENMFQFW DWVGGRYSMW SAIGLPIMIS IGYENFVELL TGAHVIDEHF 

       370        380        390        400        410        420 
ANAPPEQNVP LLLALVGVWY INFFGAVTHA ILPYDQYLWR LPAYLQQLDM ESNGKYVTRS 

       430        440        450        460        470        480 
GKTVSTLTGP IIFGEAGTNG QHAFYQLIHQ GTNLIPCDFI GAIQSQNKIG DHHKIFMSNF 

       490        500        510        520        530        540 
FAQTEALMIG KSPSEVRREL EAAGERSAEK INALLPHKTF IGGRPSNTLL IKSLTPRALG 

       550        560        570        580        590        600 
AIIAMYEHKV LVQGAIWGID SYDQWGVELG KVLAKSILPQ LRPGMRVNNH DSSTNGLINM 


FNELSHL 

« Hide

References

[1]"Glucosephosphate isomerase from Trypanosoma brucei. Cloning and characterization of the gene and analysis of the enzyme."
Marchand M., Kooystra U., Wierenga R.K., Lambeir A.-M., van Beeumen J., Opperdoes F.R., Michels P.A.M.
Eur. J. Biochem. 184:455-464(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: 427.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X15540 Genomic DNA. Translation: CAA33547.1.
PIRNUUTB. S06113.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AOLmodel-A157-562[»]
2O2CX-ray1.58A/B/C1-607[»]
2O2DX-ray1.90A/B/C1-607[»]
3CV0X-ray2.00B601-607[»]
ProteinModelPortalP13377.
SMRP13377. Positions 38-606.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP13377.
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

EvolutionaryTraceP13377.

Entry information

Entry nameG6PI_TRYBB
AccessionPrimary (citable) accession number: P13377
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: June 11, 2014
This is version 78 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