ID Q6FUX8_CANGA Unreviewed; 247 AA. AC Q6FUX8; DT 19-JUL-2004, integrated into UniProtKB/TrEMBL. DT 19-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 115. DE RecName: Full=Phosphoglycerate mutase {ECO:0000256|RuleBase:RU004511}; DE EC=5.4.2.11 {ECO:0000256|RuleBase:RU004511}; GN Name=GPM1 {ECO:0000313|CGD:CAL0129130}; GN OrderedLocusNames=CAGL0E06358g {ECO:0000313|CGD:CAL0129130, GN ECO:0000313|EMBL:CAG58885.1}; OS Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / OS NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces. OX NCBI_TaxID=284593 {ECO:0000313|EMBL:CAG58885.1, ECO:0000313|Proteomes:UP000002428}; RN [1] {ECO:0000313|EMBL:CAG58885.1, ECO:0000313|Proteomes:UP000002428} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65 RC {ECO:0000313|Proteomes:UP000002428}; RX PubMed=15229592; DOI=10.1038/nature02579; RG Genolevures; RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S., RA Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J., RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., RA Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S., RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L., RA Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., RA Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A., RA Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., RA Wincker P., Souciet J.L.; RT "Genome evolution in yeasts."; RL Nature 430:35-44(2004). 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; Evidence={ECO:0000256|ARBA:ARBA00000380, CC ECO:0000256|RuleBase:RU004511}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000256|ARBA:ARBA00004798, CC ECO:0000256|RuleBase:RU004511}. CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG- CC dependent PGAM subfamily. {ECO:0000256|ARBA:ARBA00006717, CC ECO:0000256|RuleBase:RU004511}. 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; CR380951; CAG58885.1; -; Genomic_DNA. DR RefSeq; XP_445966.1; XM_445966.1. DR AlphaFoldDB; Q6FUX8; -. DR STRING; 284593.Q6FUX8; -. DR EnsemblFungi; CAGL0E06358g-T; CAGL0E06358g-T-p1; CAGL0E06358g. DR GeneID; 2887384; -. DR KEGG; cgr:CAGL0E06358g; -. DR CGD; CAL0129130; GPM1. DR VEuPathDB; FungiDB:CAGL0E06358g; -. DR eggNOG; KOG0235; Eukaryota. DR HOGENOM; CLU_033323_1_1_1; -. DR InParanoid; Q6FUX8; -. DR OMA; RMLPYWY; -. DR UniPathway; UPA00109; UER00186. DR Proteomes; UP000002428; Chromosome E. DR GO; GO:0009986; C:cell surface; IDA:CGD. DR GO; GO:0005829; C:cytosol; IDA:CGD. DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:EnsemblFungi. DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-EC. DR GO; GO:0006094; P:gluconeogenesis; IEA:EnsemblFungi. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR CDD; cd07067; HP_PGM_like; 1. DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 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 NCBIfam; TIGR01258; pgm_1; 1. DR PANTHER; PTHR11931; PHOSPHOGLYCERATE MUTASE; 1. DR PANTHER; PTHR11931:SF0; PHOSPHOGLYCERATE MUTASE; 1. DR Pfam; PF00300; His_Phos_1; 2. DR PIRSF; PIRSF000709; 6PFK_2-Ptase; 2. DR SMART; SM00855; PGAM; 1. DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1. DR PROSITE; PS00175; PG_MUTASE; 1. PE 3: Inferred from homology; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU004511}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU004511}; KW Reference proteome {ECO:0000313|Proteomes:UP000002428}. FT ACT_SITE 9 FT /note="Tele-phosphohistidine intermediate" FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1" FT ACT_SITE 87 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1" FT BINDING 8..15 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2" FT BINDING 21..22 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2" FT BINDING 60 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2" FT BINDING 87..90 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2" FT BINDING 98 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2" FT BINDING 114..115 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2" FT BINDING 183..184 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2" FT SITE 182 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR613078-3" SQ SEQUENCE 247 AA; 27590 MW; 3A8975790206941B CRC64; MPKLVLVRHG QSEWNEKNLF TGWVDVRLSA KGEQEAARAG ELLKEKNVHP DILYTSKLSR AIQTANIALS KADRLWIPVK RSWRLNERHY GALQGKDKAE TLETYGEEKF NTWRRSFDVP PPVIEADSPY SQKNDERYRD VDPNVLPQTE SLALVIDRLL PYWEDVIAKD LLAGKTVMIA AHGNSLRGLV KHLEGISDAD IAKLNIPTGI PLVFELDENL KPSKPSYYLD PEAAAAGAAA VAAQGKK //