ID A0A6P4XTR2_PANPR Unreviewed; 341 AA. AC A0A6P4XTR2; DT 02-DEC-2020, integrated into UniProtKB/TrEMBL. DT 02-DEC-2020, sequence version 1. DT 14-DEC-2022, entry version 9. DE RecName: Full=phosphopyruvate hydratase {ECO:0000256|ARBA:ARBA00012058}; DE EC=4.2.1.11 {ECO:0000256|ARBA:ARBA00012058}; DE AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000256|ARBA:ARBA00031125}; GN Name=ENO2 {ECO:0000313|RefSeq:XP_019320208.1}; OS Panthera pardus (Leopard) (Felis pardus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Pantherinae; OC Panthera. OX NCBI_TaxID=9691 {ECO:0000313|Proteomes:UP000515130, ECO:0000313|RefSeq:XP_019320208.1}; RN [1] {ECO:0000313|RefSeq:XP_019320208.1} RP IDENTIFICATION. RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_019320208.1}; RG RefSeq; RL Submitted (APR-2022) to UniProtKB. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000256|ARBA:ARBA00005031}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC -!- SIMILARITY: Belongs to the enolase family. CC {ECO:0000256|ARBA:ARBA00009604}. 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 RefSeq; XP_019320208.1; XM_019464663.1. DR AlphaFoldDB; A0A6P4XTR2; -. DR GeneID; 109276099; -. DR CTD; 2026; -. DR UniPathway; UPA00109; UER00187. DR Proteomes; UP000515130; Unplaced. DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-EC. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR CDD; cd03313; enolase; 1. DR Gene3D; 3.20.20.120; -; 1. DR Gene3D; 3.30.390.10; -; 1. DR InterPro; IPR000941; Enolase. DR InterPro; IPR036849; Enolase-like_C_sf. DR InterPro; IPR029017; Enolase-like_N. DR InterPro; IPR020810; Enolase_C. DR InterPro; IPR020809; Enolase_CS. DR InterPro; IPR020811; Enolase_N. DR PANTHER; PTHR11902; ENOLASE; 1. DR Pfam; PF00113; Enolase_C; 1. DR Pfam; PF03952; Enolase_N; 1. DR PRINTS; PR00148; ENOLASE. DR SMART; SM01192; Enolase_C; 1. DR SMART; SM01193; Enolase_N; 1. DR SUPFAM; SSF51604; Enolase C-terminal domain-like; 1. DR SUPFAM; SSF54826; Enolase N-terminal domain-like; 1. DR PROSITE; PS00164; ENOLASE; 1. PE 3: Inferred from homology; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152}; KW Lyase {ECO:0000256|ARBA:ARBA00023239}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}. FT DOMAIN 1..41 FT /note="Enolase_N" FT /evidence="ECO:0000259|SMART:SM01193" FT DOMAIN 49..338 FT /note="Enolase_C" FT /evidence="ECO:0000259|SMART:SM01192" SQ SEQUENCE 341 AA; 37159 MW; 19F8274B712F4A9A CRC64; MLELDGTENK SKFGANAILG VSLAVCKAGA AERELPLYRH IAQLAGNSDL ILPVPAFNVI NGGSHAGNKL AMQEFMILPV GAESFRDAMR LGAEVYHTLK GVIKDKYGKD ATNVGDEGGF APNILENSEA LELVKEAIDK AGYTEKIVIG MDVAASEFHR DGKYDLDFKS PADPSRYITG DQLGALYQDF VRDYPVVSIE DPFDQDDWAA WSKFTANVGI QIVGDDLTVT NPKRIERAVE EKACNCLLLK VNQIGSVTEA IQACKLAQEN GWGVMVSHRS GETEDTFIAD LVVGLCTGQI KTGAPCRSER LAKYNQLMRI EEELGDEARF AGHNFRNPSV L //