G6PI_SCHPO
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 03-AUG-2022, entry version 138.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 4896.SPBC1604.05.1; -.
DR iPTMnet; P78917; -.
DR MaxQB; P78917; -.
DR PaxDb; P78917; -.
DR PRIDE; P78917; -.
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; IGVWYIN; -.
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; ISS:PomBase.
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; ISS:PomBase.
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; 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 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
