ID A5XD88_DROME Unreviewed; 255 AA. AC A5XD88; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 08-NOV-2023, entry version 76. DE RecName: Full=Phosphoglycerate mutase {ECO:0000256|RuleBase:RU004511}; DE EC=5.4.2.11 {ECO:0000256|RuleBase:RU004511}; DE EC=5.4.2.4 {ECO:0000256|RuleBase:RU004511}; DE Flags: Fragment; GN Name=Pglym78 {ECO:0000313|EMBL:ABH06874.1}; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227 {ECO:0000313|EMBL:ABH06874.1}; RN [1] {ECO:0000313|EMBL:ABH06874.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Hfl_16 {ECO:0000313|EMBL:ABH06874.1}; RA Flowers J.M., Sezgin E., Kumagai S., Duvernell D.D., Matzkin L.M., RA Schmidt P.S., Eanes W.F.; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ABH06874.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Hfl_16 {ECO:0000313|EMBL:ABH06874.1}; RX PubMed=17379620; DOI=10.1093/molbev/msm057; RA Flowers J., Sezgin E., Kumagai S., Duvernell D., Matzkin L., Schmidt P., RA Eanes W.; RT "Adaptive evolution of metabolic pathways in Drosophila."; RL Mol. Biol. Evol. 24:1347-1354(2007). 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|RuleBase:RU004511}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2R)-3-phospho-glyceroyl phosphate = (2R)-2,3- CC bisphosphoglycerate + H(+); Xref=Rhea:RHEA:17765, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58248; EC=5.4.2.4; CC Evidence={ECO:0000256|ARBA:ARBA00000505, 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; DQ864239; ABH06874.1; -; Genomic_DNA. DR AlphaFoldDB; A5XD88; -. DR PeptideAtlas; A5XD88; -. DR VEuPathDB; VectorBase:FBgn0014869; -. DR HOGENOM; CLU_033323_1_1_1; -. DR ExpressionAtlas; A5XD88; baseline and differential. DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; IEA:UniProtKB-EC. DR GO; GO:0004082; F:bisphosphoglycerate mutase activity; IEA:UniProtKB-EC. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW. 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; 1. 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}. FT ACT_SITE 12 FT /note="Tele-phosphohistidine intermediate" FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1" FT ACT_SITE 90 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1" FT BINDING 11..18 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2" FT BINDING 63 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2" FT BINDING 90..93 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2" FT BINDING 101 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2" FT BINDING 117..118 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2" FT BINDING 189..190 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2" FT SITE 188 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR613078-3" FT NON_TER 255 FT /evidence="ECO:0000313|EMBL:ABH06874.1" SQ SEQUENCE 255 AA; 28672 MW; F29E2A8D085F93AD CRC64; MGGKYKIVMV RHGESEWNQK NQFCGWYDAN LSEKGQEEAL AARKAVKDAG LEFDVAHTSV LTRAQVTLAS ILKASGHKEI PIQKTWRLNE RHYGGLTGLN KAETAAKYGE AQVQIWRRSF DTPPPPMEPG HPYYENIVKD PRYAEGPKPE EFPQFESLKL TIERTLPYWN DVIIPQMKEG KRILIAAHGN SLRGIVKHLD NLSEDAIMAL NLPTGIPFVY ELDENFKPVV SMQFLGDEET VKKAIEAVAA QGKAK //