ID   G6PI_SCHPO              Reviewed;         550 AA.
AC   P78917; O94371;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   27-MAR-2024, entry version 144.
DE   RecName: Full=Glucose-6-phosphate isomerase;
DE            Short=GPI;
DE            EC=5.3.1.9 {ECO:0000250|UniProtKB:P06744};
DE   AltName: Full=Phosphoglucose isomerase;
DE            Short=PGI;
DE   AltName: Full=Phosphohexose isomerase;
DE            Short=PHI;
GN   Name=pgi1; ORFNames=SPBC1604.05;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=PR745;
RX   PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA   Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT   "Identification of open reading frames in Schizosaccharomyces pombe
RT   cDNAs.";
RL   DNA Res. 4:363-369(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-455, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
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.
CC       {ECO:0000250|UniProtKB:P06744}.
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:0000305}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P06744}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the GPI family. {ECO:0000305}.
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DR   EMBL; D89268; BAA13929.1; -; mRNA.
DR   EMBL; CU329671; CAA22338.1; -; Genomic_DNA.
DR   PIR; T39509; T39509.
DR   PIR; T43196; T43196.
DR   RefSeq; NP_596635.1; NM_001022556.2.
DR   AlphaFoldDB; P78917; -.
DR   SMR; P78917; -.
DR   BioGRID; 276182; 2.
DR   STRING; 284812.P78917; -.
DR   iPTMnet; P78917; -.
DR   MaxQB; P78917; -.
DR   PaxDb; 4896-SPBC1604-05-1; -.
DR   EnsemblFungi; SPBC1604.05.1; SPBC1604.05.1:pep; SPBC1604.05.
DR   GeneID; 2539625; -.
DR   KEGG; spo:SPBC1604.05; -.
DR   PomBase; SPBC1604.05; pgi1.
DR   VEuPathDB; FungiDB:SPBC1604.05; -.
DR   eggNOG; KOG2446; Eukaryota.
DR   HOGENOM; CLU_017947_3_1_1; -.
DR   InParanoid; P78917; -.
DR   OMA; DWYRQLW; -.
DR   PhylomeDB; P78917; -.
DR   Reactome; R-SPO-5628897; TP53 Regulates Metabolic Genes.
DR   Reactome; R-SPO-6798695; Neutrophil degranulation.
DR   Reactome; R-SPO-70171; Glycolysis.
DR   Reactome; R-SPO-70263; Gluconeogenesis.
DR   UniPathway; UPA00109; UER00181.
DR   PRO; PR:P78917; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IBA:GO_Central.
DR   GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR   GO; GO:0061621; P:canonical glycolysis; ISS:PomBase.
DR   GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR   GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..550
FT                   /note="Glucose-6-phosphate isomerase"
FT                   /id="PRO_0000180577"
FT   ACT_SITE        363
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P06744"
FT   ACT_SITE        394
FT                   /evidence="ECO:0000250|UniProtKB:P06744"
FT   ACT_SITE        516
FT                   /evidence="ECO:0000250|UniProtKB:P06744"
FT   BINDING         164..165
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   BINDING         215..220
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   BINDING         359
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   BINDING         363
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   BINDING         394
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   BINDING         516
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P06745"
FT   MOD_RES         455
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   CONFLICT        4
FT                   /note="S -> C (in Ref. 1; BAA13929)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        13..14
FT                   /note="QA -> EV (in Ref. 1; BAA13929)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        168
FT                   /note="G -> A (in Ref. 1; BAA13929)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        198
FT                   /note="A -> S (in Ref. 1; BAA13929)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        519
FT                   /note="A -> V (in Ref. 1; BAA13929)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        536
FT                   /note="D -> Y (in Ref. 1; BAA13929)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   550 AA;  60884 MW;  D882FC8D6C64B793 CRC64;
     MSFSLASTLP AWQAVQTHYE SVGKHLVLKE LFAKDSSRFE KFSFTFNGLK EEDGPILFDF
     SKNLITEETV ELLVKLAKEA NVEGLRDALF AGEHINFTED RAVFHPALRN VSEKPMKVNG
     QDVMPGVRKV LRHMKEFSDA VRSGAWKGYT GKPIKSIVNV GIGGSDLGPV MVTEALKPYG
     QENLELHFVS NIDGTHLAEA LKKCDPETTL FLIASKTFTT AETCTNAKSA KDWFLASAKD
     PSHVAKHFVA LSTNEKEVTA FGISAQNMFE FSDWVGGRYS VWSAIGLSVA LYIGYENFEA
     FLSGAHAMDE YFCSTPLEKN IPALAALISI WYSDFFGAQT HLVAPYDQYL HRFPAYLQQL
     SMESNGKAIT RSGDMVNYTT GKILWGEPGT NSQHSFFQLI HQGTKLIPAD FLIPIESHNP
     IDNNKHHRML FSNFAAQTEA LMLGKTPAEV KAEGTPDEIV PHKTFVGNRP SNSIIAKKIT
     PASLGALIAF YEWVTFTEGA VWNINSFDQF GVELGKKLAK NVLAQLETKG DVENHDSSTN
     GLINLFKNGF
//