ID PGAM1_PONAB Reviewed; 254 AA. AC Q5RFB8; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 13-SEP-2023, entry version 89. DE RecName: Full=Phosphoglycerate mutase 1 {ECO:0000250|UniProtKB:P18669}; DE EC=5.4.2.11 {ECO:0000250|UniProtKB:P18669}; DE EC=5.4.2.4 {ECO:0000250|UniProtKB:P18669}; DE AltName: Full=BPG-dependent PGAM 1; DE AltName: Full=Phosphoglycerate mutase isozyme B; DE Short=PGAM-B; GN Name=PGAM1 {ECO:0000250|UniProtKB:P18669}; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Pongo. OX NCBI_TaxID=9601; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RG The German cDNA consortium; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3- CC phosphoglyceratea crucial step in glycolysis, by using 2,3- CC bisphosphoglycerate. Also catalyzes the interconversion of (2R)-2,3- CC bisphosphoglycerate and (2R)-3-phospho-glyceroyl phosphate. CC {ECO:0000250|UniProtKB:P18669}. 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:0000250|UniProtKB:P18669}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15903; CC Evidence={ECO:0000250|UniProtKB:P18669}; 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:0000250|UniProtKB:P18669}; CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P18669}. CC -!- PTM: Acetylated at Lys-253, Lys-253 and Lys-254 under high glucose CC condition. Acetylation increases catalytic activity. Under glucose CC restriction SIRT1 levels dramatically increase and it deacetylates the CC enzyme (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG- CC dependent PGAM subfamily. {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; CR857242; CAH89539.1; -; mRNA. DR RefSeq; NP_001127164.1; NM_001133692.2. DR AlphaFoldDB; Q5RFB8; -. DR SMR; Q5RFB8; -. DR STRING; 9601.ENSPPYP00000002936; -. DR GeneID; 100174215; -. DR KEGG; pon:100174215; -. DR CTD; 5223; -. DR eggNOG; KOG0235; Eukaryota. DR InParanoid; Q5RFB8; -. DR OrthoDB; 1008469at2759; -. DR Proteomes; UP000001595; Unplaced. DR GO; GO:0046538; F:2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; ISS:UniProtKB. DR GO; GO:0004082; F:bisphosphoglycerate mutase activity; ISS:UniProtKB. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. 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:SF15; PHOSPHOGLYCERATE MUTASE 1; 1. DR Pfam; PF00300; His_Phos_1; 2. DR PIRSF; PIRSF000709; 6PFK_2-Ptase; 1. DR SMART; SM00855; PGAM; 1. DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1. DR PROSITE; PS00175; PG_MUTASE; 1. PE 2: Evidence at transcript level; KW Acetylation; Glycolysis; Hydrolase; Isomerase; Phosphoprotein; KW Reference proteome. FT CHAIN 1..254 FT /note="Phosphoglycerate mutase 1" FT /id="PRO_0000179827" FT ACT_SITE 11 FT /note="Tele-phosphohistidine intermediate" FT /evidence="ECO:0000250|UniProtKB:P18669" FT ACT_SITE 89 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250|UniProtKB:P18669" FT BINDING 10..17 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00950" FT BINDING 23..24 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00950" FT BINDING 62 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00950" FT BINDING 89..92 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00950" FT BINDING 100 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00950" FT BINDING 116..117 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00950" FT BINDING 187..188 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P00950" FT SITE 186 FT /note="Transition state stabilizer" FT /evidence="ECO:0000250|UniProtKB:P00950" FT MOD_RES 14 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P18669" FT MOD_RES 23 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P18669" FT MOD_RES 26 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P18669" FT MOD_RES 31 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P18669" FT MOD_RES 106 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9DBJ1" FT MOD_RES 118 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9DBJ1" FT MOD_RES 251 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P18669" FT MOD_RES 251 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9DBJ1" FT MOD_RES 253 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P18669" FT MOD_RES 254 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P18669" SQ SEQUENCE 254 AA; 28778 MW; E650852BEBB23AF8 CRC64; MAAYKLVLIR HGESAWNLEN RFSGWYDADL SPAGHEEAKR GGQALRDAGY EFDICFTSVQ KRAIRTLWTV LDAIDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEA QVKIWRRSYD VPPPPMEPDH PFYSNISKDR RYADLTEDQL PSCESLKDTI ARALPFWNEE IVPQIKEGKR VLIAAHGNSL RGIVKHLEGL SEEAIMELNL PTGIPIVYEL DKNSKPIKPM QFLGDEETVR KAMEAVAAQG KAKK //