ID Q4SW55_TETNG Unreviewed; 255 AA. AC Q4SW55; DT 19-JUL-2005, integrated into UniProtKB/TrEMBL. DT 19-JUL-2005, sequence version 1. DT 02-SEP-2026, entry version 115. 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}; OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon OS nigroviridis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon. OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000008899.1, ECO:0000313|Proteomes:UP000007303}; RN [1] {ECO:0000313|Proteomes:UP000007303} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15496914; DOI=10.1038/nature03025; RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N., RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S., RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C., RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C., RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L., RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P., RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C., RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R., RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D., RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W., RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.; RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the RT early vertebrate proto-karyotype."; RL Nature 431:946-957(2004). RN [2] {ECO:0000313|Ensembl:ENSTNIP00000008899.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2026) to UniProtKB. 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:ARBA00093970}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15902; CC Evidence={ECO:0000256|ARBA:ARBA00093970}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15903; CC Evidence={ECO:0000256|ARBA:ARBA00093970}; 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:ARBA00093842}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17766; CC Evidence={ECO:0000256|ARBA:ARBA00093842}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17767; CC Evidence={ECO:0000256|ARBA:ARBA00093842}; 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 AlphaFoldDB; Q4SW55; -. DR STRING; 99883.ENSTNIP00000008899; -. DR Ensembl; ENSTNIT00000009070.1; ENSTNIP00000008899.1; ENSTNIG00000006151.1. DR KEGG; tng:GSTEN00011651G001; -. DR GeneTree; ENSGT00950000182926; -. DR HOGENOM; CLU_033323_1_1_1; -. DR OMA; MDDKHPY; -. DR OrthoDB; 354304at2759; -. DR Proteomes; UP000007303; Unassembled WGS sequence. DR GO; GO:0004082; F:bisphosphoglycerate mutase activity; IEA:UniProtKB-EC. DR GO; GO:0004619; F:phosphoglycerate mutase activity; IEA:UniProtKB-EC. DR GO; GO:0006096; P:glycolytic process; IEA:InterPro. DR CDD; cd07067; HP_PGM_like; 1. DR FunFam; 3.40.50.1240:FF:000007; Phosphoglycerate mutase; 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 NCBIfam; NF010713; PRK14115.1; 1. DR PANTHER; PTHR11931; PHOSPHOGLYCERATE MUTASE; 1. DR Pfam; PF00300; His_Phos_1; 1. 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU004511}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Reference proteome {ECO:0000313|Proteomes:UP000007303}. 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 188..189 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2" FT SITE 187 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR613078-3" SQ SEQUENCE 255 AA; 28755 MW; 47E3A7541419DBEE CRC64; MTAVHRLVIV RHGESSWNQE NRFCGWFDAD LSEKGVEEAK RGAQAIKEAG MKFDVCYTSV LKRAVKTLWT IMEGTDQMWL PVIRTWRLNE RHYGGLTGLN KAETAEKHGE EQVKIWRRSF DIPPPPMDKD HPYHKIISES RRYKNLKPGE LPTCESLKDT IARALPFWNE VIAPEIKAGK NVIIAAHGNS LRGIVKHLDG MSDAAIMELN LPTGIPIVYE LDADLKPVKP MSFLGDEETV RKAMEAVAAQ GKAKK //