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P08059 (G6PI_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 110. 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):
Autocrine motility factor
Short name=AMF
Neuroleukin
Short name=NLK
Phosphoglucose isomerase
Short name=PGI
Phosphohexose isomerase
Short name=PHI
Gene names
Name:GPI
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

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

Subcellular location

Cytoplasm. Secreted HAMAP-Rule MF_00473.

Post-translational modification

ISGylated By similarity. HAMAP-Rule MF_00473

Sequence similarities

Belongs to the GPI family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed HAMAP-Rule MF_00473
Chain2 – 558557Glucose-6-phosphate isomerase HAMAP-Rule MF_00473
PRO_0000180540

Sites

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

Amino acid modifications

Modified residue21N-acetylalanine HAMAP-Rule MF_00473
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

Experimental info

Sequence conflict156 – 1572Missing in CAA82246. Ref.3
Sequence conflict3441Y → H in AAA31048. Ref.5
Sequence conflict347 – 39852RFAAY…LIHQG → ALLPTSSRVTWSPTGSTSPS PAPVWTTRRAPLCGGSQGPM ASMPSTSSS in CAA82246. Ref.3
Sequence conflict481 – 4822KL → NV in CAA82246. Ref.3
Sequence conflict5501K → M in CAA82246. Ref.3

Secondary structure

................................................................................................ 558
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08059 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 84DA1B15CF0C702F

FASTA55863,126
        10         20         30         40         50         60 
MAALTQNPQF KKLQTWYHEH RSDLNLRRLF EGDKDRFNHF SLNLNTNHGR ILLDYSKNLV 

        70         80         90        100        110        120 
TEAVMQMLVD LAKSRGVEAA RERMFNGEKI NFTEDRAVLH VALRNRSNTP ILVDGKDVMP 

       130        140        150        160        170        180 
EVNRVLEKMK SFCKRVRSGE WKGYSGKSIT DVINIGIGGS DLGPLMVTEA LKPYSAEGPR 

       190        200        210        220        230        240 
VWFVSNIDGT HIAKTLATLN PESSLFIIAS KTFTTQETIT NAETAKEWFL QSAKDPSAVA 

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

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

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

       430        440        450        460        470        480 
HHKILLANFL AQTEALMKGK STEEARKELQ AAGKSPEDFE KLLPHKVFEG NRPTNSIVFT 

       490        500        510        520        530        540 
KLTPFILGAL IAMYEHKIFV QGVIWDINSF DQWGVELGKQ LAKKIEPELD GSSPVTSHDS 

       550 
STNGLINFIK QEREARSQ 

« Hide

References

[1]"The neurotrophic factor neuroleukin is 90% homologous with phosphohexose isomerase."
Chaput M., Claes V., Portetelle D., Clutdts I., Cravador A., Burny A., Gras H., Tartar A.
Nature 332:454-455(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Burny A.
Submitted (AUG-1988) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Structure of the gene encoding pig phosphoglucose isomerase."
Claes V., Kettmann R., Burny A.
Gene 150:235-241(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Sequence analysis of the pig phosphoglucose isomerase gene promoter region."
Claes V., Taquet A.N., Kettmann R., Burny A.
Biochim. Biophys. Acta 1087:339-340(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-17.
Strain: Belgian Landrace.
[5]"A partial cDNA clone for porcine glucosephosphate isomerase: isolation, characterization and use in detection of restriction fragment length polymorphisms."
Davies W., Harbitz I., Hauge J.G.
Anim. Genet. 18:233-240(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 238-357.
[6]"Three-dimensional structure of pig muscle phosphoglucose isomerase at 6-A resolution."
Muirhead H., Shaw P.J.
J. Mol. Biol. 89:195-203(1974) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (6.0 ANGSTROMS).
[7]"Glucose-6-phosphate isomerase."
Achari A., Marshall S.E., Muirhead H., Palmieri R.H., Noltmann E.A.
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 293:145-157(1981) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), PROTEIN SEQUENCE OF 554-558.
[8]"Crystal structure of phosphoglucose isomerase from pig muscle and its complex with 5-phosphoarabinonate."
Davies C., Muirhead H.
Proteins 49:577-579(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) ALONE AND IN COMPLEX WITH 5-PHOSPHOARABINONATE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X07382 mRNA. Translation: CAA30295.1.
Z28396 expand/collapse EMBL AC list , Z28397, Z28398, Z28399, Z28400, Z28401, Z28402, Z28403, Z28404 Genomic DNA. Translation: CAA82246.1.
X53719 mRNA. Translation: CAA37755.1.
M54975 mRNA. Translation: AAA31048.1.
PIRI47142.
NUPG. S00895.
RefSeqNP_999495.1. NM_214330.1.
UniGeneSsc.81817.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GZDX-ray2.50A2-558[»]
1GZVX-ray3.51A2-558[»]
ProteinModelPortalP08059.
SMRP08059. Positions 2-555.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000003094.

Proteomic databases

PaxDbP08059.
PRIDEP08059.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID397602.
KEGGssc:397602.

Organism-specific databases

CTD2821.

Phylogenomic databases

eggNOGCOG0166.
HOGENOMHOG000261370.
HOVERGENHBG002877.
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...

Other

EvolutionaryTraceP08059.

Entry information

Entry nameG6PI_PIG
AccessionPrimary (citable) accession number: P08059
Secondary accession number(s): Q29556
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 110 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways