ID A0A0D8QV27_RAOPL Unreviewed; 330 AA. AC A0A0D8QV27; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 07-APR-2021, entry version 24. DE RecName: Full=Phosphopyruvate hydratase {ECO:0000256|ARBA:ARBA00012058}; DE EC=4.2.1.11 {ECO:0000256|ARBA:ARBA00012058}; DE Flags: Fragment; GN Name=eno {ECO:0000313|EMBL:KJG35071.1}; GN ORFNames=UA70_15505 {ECO:0000313|EMBL:KJG35071.1}; OS Raoultella planticola (Klebsiella planticola). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Raoultella. OX NCBI_TaxID=575 {ECO:0000313|EMBL:KJG35071.1, ECO:0000313|Proteomes:UP000032530}; RN [1] {ECO:0000313|EMBL:KJG35071.1, ECO:0000313|Proteomes:UP000032530} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GCSL-DIFS-295 {ECO:0000313|EMBL:KJG35071.1, RC ECO:0000313|Proteomes:UP000032530}; RA Timme R., Allard M.W., Strain E., Evans P.S., Brown E.; RT "Whole genome shotgun sequencing of cultured foodborne pathogen."; RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; CC Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, CC ChEBI:CHEBI:58702; EC=4.2.1.11; CC Evidence={ECO:0000256|ARBA:ARBA00000767}; 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 -!- SIMILARITY: Belongs to the enolase family. CC {ECO:0000256|ARBA:ARBA00009604}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KJG35071.1}. 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; JZSG01000899; KJG35071.1; -; Genomic_DNA. DR PATRIC; fig|575.7.peg.5521; -. DR UniPathway; UPA00109; UER00187. DR Proteomes; UP000032530; Unassembled WGS sequence. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. 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 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; PTHR11902; 1. DR Pfam; PF00113; Enolase_C; 1. DR Pfam; PF03952; Enolase_N; 1. DR PRINTS; PR00148; ENOLASE. DR SMART; SM01192; Enolase_C; 1. DR SUPFAM; SSF51604; SSF51604; 1. DR SUPFAM; SSF54826; SSF54826; 1. DR TIGRFAMs; TIGR01060; eno; 1. DR PROSITE; PS00164; ENOLASE; 1. PE 3: Inferred from homology; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:KJG35071.1}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}. FT DOMAIN 42..329 FT /note="Enolase_C" FT /evidence="ECO:0000259|SMART:SM01192" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:KJG35071.1" SQ SEQUENCE 330 AA; 35188 MW; 7F44B7E9E7FD576F CRC64; NKSNFGANAI LAVSLANAKA AAASKGQPLY EHIAELNGTP GKYSMPVPMM NIINGGEHAD NNVDIQEFMI QPVGAKSLKE AVRMGSEVFH NLAKVLKAKG MNTAVGDEGG YAPNLGSNAE ALAVIAEAVK AAGYELGKDI TLAMDCAASE FYKDGKYVLA GEGNKAFTSE EFTHFLEELT KQYPIVSIED GLDESDWDGF AYQTKVLGDK IQLVGDDLFV TNTKILKEGI EKGIVNSILI KFNQIGSLTE TLAAIKMAKD AGYTAVISHR SGETEDATIA DLAVGTAAGQ IKTGSMSRSD RVAKYNQLIR IEEALGEKAP YNGRKEIKGQ //