PMGY_SCHPO
ID PMGY_SCHPO Reviewed; 211 AA.
AC P36623;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Phosphoglycerate mutase;
DE Short=PGAM;
DE EC=5.4.2.11;
DE AltName: Full=BPG-dependent PGAM;
DE AltName: Full=MPGM;
DE AltName: Full=Phosphoglyceromutase;
GN Name=gpm1; ORFNames=SPAC26F1.06;
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 [MRNA], PARTIAL PROTEIN SEQUENCE, AND SUBUNIT.
RC STRAIN=CMI 39917;
RX PubMed=8110200; DOI=10.1042/bj2970603;
RA Nairn J., Price N.C., Fothergill-Gilmore L.A., Walker G.E.,
RA Fothergill J.E., Dunbar B.;
RT "The amino acid sequence of the small monomeric phosphoglycerate mutase
RT from the fission yeast Schizosaccharomyces pombe.";
RL Biochem. J. 297:603-608(1994).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-37; SER-62; TYR-96 AND
RP SER-166, AND IDENTIFICATION BY 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).
RN [4]
RP STRUCTURE BY NMR.
RX PubMed=11237600; DOI=10.1006/jmbi.2000.4390;
RA Uhrinova S., Uhrin D., Nairn J., Price N.C., Fothergill-Gilmore L.A.,
RA Barlow P.N.;
RT "Solution structure and dynamics of an open beta-sheet, glycolytic enzyme,
RT monomeric 23.7 kDa phosphoglycerate mutase from Schizosaccharomyces
RT pombe.";
RL J. Mol. Biol. 306:275-290(2001).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.11;
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8110200}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000305}.
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DR EMBL; X75385; CAA53154.1; -; mRNA.
DR EMBL; CU329670; CAA97363.1; -; Genomic_DNA.
DR PIR; S43369; S43214.
DR RefSeq; NP_594889.1; NM_001020318.2.
DR PDB; 1FZT; NMR; -; A=1-211.
DR PDBsum; 1FZT; -.
DR AlphaFoldDB; P36623; -.
DR BMRB; P36623; -.
DR SMR; P36623; -.
DR BioGRID; 278562; 5.
DR IntAct; P36623; 1.
DR MINT; P36623; -.
DR STRING; 4896.SPAC26F1.06.1; -.
DR iPTMnet; P36623; -.
DR MaxQB; P36623; -.
DR PaxDb; P36623; -.
DR PRIDE; P36623; -.
DR EnsemblFungi; SPAC26F1.06.1; SPAC26F1.06.1:pep; SPAC26F1.06.
DR GeneID; 2542085; -.
DR KEGG; spo:SPAC26F1.06; -.
DR PomBase; SPAC26F1.06; gpm1.
DR VEuPathDB; FungiDB:SPAC26F1.06; -.
DR eggNOG; KOG0235; Eukaryota.
DR HOGENOM; CLU_033323_1_4_1; -.
DR InParanoid; P36623; -.
DR OMA; RMLPYWY; -.
DR PhylomeDB; P36623; -.
DR BRENDA; 5.4.2.11; 5613.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-70171; Glycolysis.
DR Reactome; R-SPO-70263; Gluconeogenesis.
DR SABIO-RK; P36623; -.
DR UniPathway; UPA00109; UER00186.
DR EvolutionaryTrace; P36623; -.
DR PRO; PR:P36623; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IMP:PomBase.
DR GO; GO:0004619; F:phosphoglycerate mutase activity; IDA:PomBase.
DR GO; GO:0061621; P:canonical glycolysis; ISO:PomBase.
DR GO; GO:0006094; P:gluconeogenesis; ISO:PomBase.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR HAMAP; MF_01039; PGAM_GpmA; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR InterPro; IPR005952; Phosphogly_mut1.
DR PANTHER; PTHR11931; PTHR11931; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR TIGRFAMs; TIGR01258; pgm_1; 2.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycolysis; Isomerase;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..211
FT /note="Phosphoglycerate mutase"
FT /id="PRO_0000179838"
FT ACT_SITE 15
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT ACT_SITE 93
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 14..21
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 27..28
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 66
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 93..96
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 120..121
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT BINDING 164..165
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT SITE 163
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT MOD_RES 37
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 96
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:1FZT"
FT HELIX 19..23
FT /evidence="ECO:0007829|PDB:1FZT"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1FZT"
FT HELIX 36..52
FT /evidence="ECO:0007829|PDB:1FZT"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:1FZT"
FT HELIX 65..78
FT /evidence="ECO:0007829|PDB:1FZT"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:1FZT"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:1FZT"
FT HELIX 104..120
FT /evidence="ECO:0007829|PDB:1FZT"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:1FZT"
FT HELIX 133..148
FT /evidence="ECO:0007829|PDB:1FZT"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:1FZT"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:1FZT"
FT HELIX 164..175
FT /evidence="ECO:0007829|PDB:1FZT"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:1FZT"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:1FZT"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:1FZT"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:1FZT"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:1FZT"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:1FZT"
SQ SEQUENCE 211 AA; 23765 MW; 4B937820E2FA5C15 CRC64;
MTTEAAPNLL VLTRHGESEW NKLNLFTGWK DPALSETGIK EAKLGGERLK SRGYKFDIAF
TSALQRAQKT CQIILEEVGE PNLETIKSEK LNERYYGDLQ GLNKDDARKK WGAEQVQIWR
RSYDIAPPNG ESLKDTAERV LPYYKSTIVP HILKGEKVLI AAHGNSLRAL IMDLEGLTGD
QIVKRELATG VPIVYHLDKD GKYVSKELID N
