ID   G6PI_PONAB              Reviewed;         558 AA.
AC   Q5R4E3;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   22-FEB-2023, entry version 89.
DE   RecName: Full=Glucose-6-phosphate isomerase {ECO:0000250|UniProtKB:P06744};
DE            Short=GPI {ECO:0000250|UniProtKB:P06744};
DE            EC=5.3.1.9 {ECO:0000250|UniProtKB:P06745};
DE   AltName: Full=Autocrine motility factor {ECO:0000250|UniProtKB:P06744};
DE            Short=AMF {ECO:0000250|UniProtKB:P06744};
DE   AltName: Full=Neuroleukin {ECO:0000250|UniProtKB:P06744};
DE            Short=NLK {ECO:0000250|UniProtKB:P06744};
DE   AltName: Full=Phosphoglucose isomerase {ECO:0000250|UniProtKB:P06744};
DE            Short=PGI {ECO:0000250|UniProtKB:P06744};
DE   AltName: Full=Phosphohexose isomerase;
DE            Short=PHI {ECO:0000250|UniProtKB:P06744};
GN   Name=GPI {ECO:0000250|UniProtKB:P06744};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: In the cytoplasm, catalyzes the conversion of glucose-6-
CC       phosphate to fructose-6-phosphate, the second step in glycolysis, and
CC       the reverse reaction during gluconeogenesis (By similarity). Besides
CC       it's role as a glycolytic enzyme, also acts as a secreted cytokine:
CC       acts as an angiogenic factor (AMF) that stimulates endothelial cell
CC       motility. Acts as a neurotrophic factor, neuroleukin, for spinal and
CC       sensory neurons. It is secreted by lectin-stimulated T-cells and
CC       induces immunoglobulin secretion (By similarity).
CC       {ECO:0000250|UniProtKB:P06744, ECO:0000250|UniProtKB:P06745}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate;
CC         Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57634, ChEBI:CHEBI:58225;
CC         EC=5.3.1.9; Evidence={ECO:0000250|UniProtKB:P06744};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 2/4.
CC       {ECO:0000250|UniProtKB:P06744}.
CC   -!- SUBUNIT: Homodimer; in the catalytically active form. Monomer in the
CC       secreted form. {ECO:0000250|UniProtKB:P06744}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P06744}.
CC       Secreted {ECO:0000250|UniProtKB:P06744}.
CC   -!- PTM: Phosphorylation at Ser-185 by CK2 has been shown to decrease
CC       enzymatic activity and may contribute to secretion by a non-classical
CC       secretory pathway. {ECO:0000250|UniProtKB:P06744}.
CC   -!- PTM: ISGylated. {ECO:0000250|UniProtKB:P06744}.
CC   -!- SIMILARITY: Belongs to the GPI family. {ECO:0000305}.
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DR   EMBL; CR861307; CAH93373.1; -; mRNA.
DR   RefSeq; NP_001126984.1; NM_001133512.1.
DR   AlphaFoldDB; Q5R4E3; -.
DR   SMR; Q5R4E3; -.
DR   STRING; 9601.ENSPPYP00000011012; -.
DR   GeneID; 100174006; -.
DR   KEGG; pon:100174006; -.
DR   CTD; 2821; -.
DR   eggNOG; KOG2446; Eukaryota.
DR   InParanoid; Q5R4E3; -.
DR   OrthoDB; 1657888at2759; -.
DR   UniPathway; UPA00109; UER00181.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR   GO; GO:0004347; F:glucose-6-phosphate isomerase activity; ISS:UniProtKB.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0051156; P:glucose 6-phosphate metabolic process; ISS:UniProtKB.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd05015; SIS_PGI_1; 1.
DR   CDD; cd05016; SIS_PGI_2; 1.
DR   Gene3D; 1.10.1390.10; -; 1.
DR   HAMAP; MF_00473; G6P_isomerase; 1.
DR   InterPro; IPR001672; G6P_Isomerase.
DR   InterPro; IPR023096; G6P_Isomerase_C.
DR   InterPro; IPR018189; Phosphoglucose_isomerase_CS.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   InterPro; IPR035476; SIS_PGI_1.
DR   InterPro; IPR035482; SIS_PGI_2.
DR   PANTHER; PTHR11469; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR   PANTHER; PTHR11469:SF1; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR   Pfam; PF00342; PGI; 1.
DR   PRINTS; PR00662; G6PISOMERASE.
DR   SUPFAM; SSF53697; SIS domain; 1.
DR   PROSITE; PS00765; P_GLUCOSE_ISOMERASE_1; 1.
DR   PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1.
DR   PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytokine; Cytoplasm; Gluconeogenesis; Glycolysis;
KW   Hydroxylation; Isomerase; Phosphoprotein; Reference proteome; Secreted;
KW   Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P06744"
FT   CHAIN           2..558
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_0000180539"
FT   ACT_SITE        358
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   ACT_SITE        389
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   ACT_SITE        519
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   BINDING         159..160
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   BINDING         210..215
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   BINDING         354
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   BINDING         358
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   BINDING         389
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   BINDING         519
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P06744"
FT   MOD_RES         12
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P06744"
FT   MOD_RES         34
FT                   /note="N6-(2-hydroxyisobutyryl)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P06744"
FT   MOD_RES         107
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P06744"
FT   MOD_RES         109
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P06744"
FT   MOD_RES         142
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P06744"
FT   MOD_RES         185
FT                   /note="Phosphoserine; by CK2"
FT                   /evidence="ECO:0000250|UniProtKB:P06744"
FT   MOD_RES         250
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P6V0"
FT   MOD_RES         454
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   MOD_RES         454
FT                   /note="N6-malonyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         454
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   MOD_RES         455
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P06744"
SQ   SEQUENCE   558 AA;  63018 MW;  D8A5039C0E4C2B06 CRC64;
     MAALTRDPQF QKLQQWYREH GSELNLRRLF DANKDRFNHF SLTLNTNHGH ILVDYSKNLV
     TEDVMRMLVD LAKSRGVEAA RERMFNGEKI NYTEGRAVLH VALRNRSNTP ILVDGKDVMP
     EVNKVLDKMK SFCQRVRSGD WKGYTGKTIT DIINIGIGGS DLGPLMVTEA LKPYSSGGPR
     VWYVSNIDGT HIAKTLAQLN PESSVSIIAS KTFTTQETIT NAETAKEWFL QTAKDPSAVA
     KHFVALSTNT TKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHVGF DNFEQLLSGA
     HWMDQHFRTT PLEKNAPVLL ALLGIWYINC FGCETHAMLP YDQYLHRFAA YFQQGDMESN
     GKYITKSGTR VDHQTGPIVW GEPGTNGQHA FYQLIHQGTK MIPCDFLIPV QTQHPIRKGL
     HHKVLLANFL AQTEALMRGK STEEARKELQ AAGKSPEDLE RLLPHKVFEG NRPTNSIVFT
     KLTPFMLGAL VAMYEHKIFV QGIIWDINSF DQWGVELGKQ LAKKIEPELD GSAQVTSHDA
     STNGLINFIK QQREARIQ
//