Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q5R4E3 (G6PI_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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):
Autocrine motility factor
Short name=AMF
Neuroleukin
Short name=NLK
Phosphoglucose isomerase
Short name=PGI
Phosphohexose isomerase
Short name=PHI
Gene names
Name:GPI
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length558 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Besides it's role as a glycolytic enzyme, mammalian GPI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. GPI is also a neurotrophic factor (Neuroleukin) for spinal and sensory neurons By similarity. HAMAP-Rule MF_00473

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 in the catalytically active form, monomer in the secreted form By similarity.

Subcellular location

Cytoplasm. Secreted By similarity HAMAP-Rule MF_00473.

Post-translational modification

ISGylated By similarity. HAMAP-Rule MF_00473

Sequence similarities

Belongs to the GPI family.

Ontologies

Keywords
   Biological processAngiogenesis
Gluconeogenesis
Glycolysis
   Cellular componentCytoplasm
Secreted
   Molecular functionCytokine
Isomerase
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

gluconeogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

glycolysis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular space

Inferred from electronic annotation. Source: UniProtKB-KW

   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

Initiator methionine11Removed By similarity
Chain2 – 558557Glucose-6-phosphate isomerase HAMAP-Rule MF_00473
PRO_0000180539

Sites

Active site3581Proton donor By similarity
Active site3891 By similarity
Active site5191 By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue121N6-acetyllysine By similarity
Modified residue1091Phosphothreonine By similarity
Modified residue1421N6-acetyllysine By similarity
Modified residue1851Phosphoserine; by CK2 By similarity
Modified residue4541N6-malonyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5R4E3 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: D8A5039C0E4C2B06

FASTA55863,018
        10         20         30         40         50         60 
MAALTRDPQF QKLQQWYREH GSELNLRRLF DANKDRFNHF SLTLNTNHGH ILVDYSKNLV 

        70         80         90        100        110        120 
TEDVMRMLVD LAKSRGVEAA RERMFNGEKI NYTEGRAVLH VALRNRSNTP ILVDGKDVMP 

       130        140        150        160        170        180 
EVNKVLDKMK SFCQRVRSGD WKGYTGKTIT DIINIGIGGS DLGPLMVTEA LKPYSSGGPR 

       190        200        210        220        230        240 
VWYVSNIDGT HIAKTLAQLN PESSVSIIAS KTFTTQETIT NAETAKEWFL QTAKDPSAVA 

       250        260        270        280        290        300 
KHFVALSTNT TKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHVGF DNFEQLLSGA 

       310        320        330        340        350        360 
HWMDQHFRTT PLEKNAPVLL ALLGIWYINC FGCETHAMLP YDQYLHRFAA YFQQGDMESN 

       370        380        390        400        410        420 
GKYITKSGTR VDHQTGPIVW GEPGTNGQHA FYQLIHQGTK MIPCDFLIPV QTQHPIRKGL 

       430        440        450        460        470        480 
HHKVLLANFL AQTEALMRGK STEEARKELQ AAGKSPEDLE RLLPHKVFEG NRPTNSIVFT 

       490        500        510        520        530        540 
KLTPFMLGAL VAMYEHKIFV QGIIWDINSF DQWGVELGKQ LAKKIEPELD GSAQVTSHDA 

       550 
STNGLINFIK QQREARIQ 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR861307 mRNA. Translation: CAH93373.1.
RefSeqNP_001126984.1. NM_001133512.1.
UniGenePab.18209.

3D structure databases

ProteinModelPortalQ5R4E3.
SMRQ5R4E3. Positions 2-556.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5R4E3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100174006.
KEGGpon:100174006.

Organism-specific databases

CTD2821.

Phylogenomic databases

HOVERGENHBG002877.
InParanoidQ5R4E3.
KOK01810.

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...

Entry information

Entry nameG6PI_PONAB
AccessionPrimary (citable) accession number: Q5R4E3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 58 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways