G6PI_PONAB
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 03-AUG-2022, entry version 86.
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 PRIDE; Q5R4E3; -.
DR GeneID; 100174006; -.
DR KEGG; pon:100174006; -.
DR CTD; 2821; -.
DR eggNOG; KOG2446; Eukaryota.
DR InParanoid; Q5R4E3; -.
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; PTHR11469; 1.
DR Pfam; PF00342; PGI; 1.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF53697; SSF53697; 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
