ID A0A1Q7JZ12_9ARCH Unreviewed; 415 AA. AC A0A1Q7JZ12; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 27-NOV-2024, entry version 29. DE RecName: Full=Enolase {ECO:0000256|HAMAP-Rule:MF_00318}; DE EC=4.2.1.11 {ECO:0000256|HAMAP-Rule:MF_00318}; DE AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000256|HAMAP-Rule:MF_00318}; DE AltName: Full=2-phosphoglycerate dehydratase {ECO:0000256|HAMAP-Rule:MF_00318}; GN Name=eno {ECO:0000256|HAMAP-Rule:MF_00318}; GN ORFNames=AUJ08_07805 {ECO:0000313|EMBL:OLC81152.1}; OS Thaumarchaeota archaeon 13_1_40CM_3_50_5. OC Archaea; Nitrososphaerota. OX NCBI_TaxID=1805392 {ECO:0000313|EMBL:OLC81152.1, ECO:0000313|Proteomes:UP000186022}; RN [1] {ECO:0000313|EMBL:OLC81152.1, ECO:0000313|Proteomes:UP000186022} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=27843720; RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A., RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C., RA Banfield J.F.; RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal RT heterotrophy are prevalent below the grass root zone."; RL PeerJ 4:E2687-E2687(2016). CC -!- FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate (2- CC PG) into phosphoenolpyruvate (PEP). It is essential for the degradation CC of carbohydrates via glycolysis. {ECO:0000256|HAMAP-Rule:MF_00318}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2R)-2-phosphoglycerate = phosphoenolpyruvate + H2O; CC Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, CC ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00318}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00318}; CC Note=Binds a second Mg(2+) ion via substrate during catalysis. CC {ECO:0000256|HAMAP-Rule:MF_00318}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR001400-3}; CC Note=Mg(2+) is required for catalysis and for stabilizing the dimer. CC {ECO:0000256|PIRSR:PIRSR001400-3}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000256|ARBA:ARBA00005031, CC ECO:0000256|HAMAP-Rule:MF_00318}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00318}. CC Secreted {ECO:0000256|HAMAP-Rule:MF_00318}. Cell surface CC {ECO:0000256|HAMAP-Rule:MF_00318}. Note=Fractions of enolase are CC present in both the cytoplasm and on the cell surface. CC {ECO:0000256|HAMAP-Rule:MF_00318}. CC -!- SIMILARITY: Belongs to the enolase family. CC {ECO:0000256|ARBA:ARBA00009604, ECO:0000256|HAMAP-Rule:MF_00318}. 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:OLC81152.1}. 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; MNFY01000295; OLC81152.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1Q7JZ12; -. DR UniPathway; UPA00109; UER00187. DR Proteomes; UP000186022; Unassembled WGS sequence. DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule. DR Gene3D; 3.20.20.120; Enolase-like C-terminal domain; 1. DR Gene3D; 3.30.390.10; Enolase-like, N-terminal domain; 1. DR HAMAP; MF_00318; Enolase; 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; IPR020811; Enolase_N. DR PANTHER; PTHR11902; ENOLASE; 1. DR PANTHER; PTHR11902:SF1; ENOLASE; 1. DR Pfam; PF00113; Enolase_C; 1. DR Pfam; PF03952; Enolase_N; 1. DR PIRSF; PIRSF001400; Enolase; 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. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00318}; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP- KW Rule:MF_00318}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00318}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00318, ECO:0000256|PIRSR:PIRSR001400- KW 3}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00318, KW ECO:0000256|PIRSR:PIRSR001400-3}; KW Secreted {ECO:0000256|HAMAP-Rule:MF_00318}. FT DOMAIN 4..125 FT /note="Enolase N-terminal" FT /evidence="ECO:0000259|SMART:SM01193" FT DOMAIN 130..414 FT /note="Enolase C-terminal TIM barrel" FT /evidence="ECO:0000259|SMART:SM01192" FT ACT_SITE 199 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318, FT ECO:0000256|PIRSR:PIRSR001400-1" FT ACT_SITE 331 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318, FT ECO:0000256|PIRSR:PIRSR001400-1" FT BINDING 146 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2" FT BINDING 155 FT /ligand="(2R)-2-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58289" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318" FT BINDING 156 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2" FT BINDING 235 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318, FT ECO:0000256|PIRSR:PIRSR001400-3" FT BINDING 280 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318, FT ECO:0000256|PIRSR:PIRSR001400-3" FT BINDING 280 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2" FT BINDING 306 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318, FT ECO:0000256|PIRSR:PIRSR001400-3" FT BINDING 306 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2" FT BINDING 331 FT /ligand="(2R)-2-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58289" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318" FT BINDING 358..361 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2" FT BINDING 360 FT /ligand="(2R)-2-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58289" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318" FT BINDING 361 FT /ligand="(2R)-2-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58289" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318" FT BINDING 382 FT /ligand="(2R)-2-phosphoglycerate" FT /ligand_id="ChEBI:CHEBI:58289" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318" FT BINDING 382 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001400-2" SQ SEQUENCE 415 AA; 44917 MW; 38BAF3E23474F1AF CRC64; MPSITSVRGR IIFNSRGSKS IEIDVVTDNR FMGRACAPSG ASVGKFEAQS FPDNKVEKAL AAFNGNSKKF VGLQAESLQE VFDALRSIDK TDNYATIGGS VAYALSIAAV DSAAKALNIP LFKLLKASKP FSFPFPLGNI LGGGAHAGPG TPDIQEILAC PVGAKSIVEA LEMNFKLHAE TRKVIESIDR RFTYGRGDEG AWAPNVNNDR ALEIVEKAVK NCGYTLGKDM AIGIDFASSS FWDEKNNVYD YARQGIKRDA GEQIEFANRL IRDYRLIYTE DPVHEGDFQS MATLTKKNPG IFVTGDDMLV TNACKVKEAV KYGACSGAIL KVNQAGSLYD AMKFAEECDK NDIKIITSHR SGESIDSHIS HIAIATGSKM IKTGVLGGER VAKLNELVRL TEYDLIEGMA ELSSA //