ID A0A1Q7JZ12_9ARCH Unreviewed; 415 AA. AC A0A1Q7JZ12; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 25-MAY-2022, entry version 18. 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; Thaumarchaeota. 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 CC into phosphoenolpyruvate. It is essential for the degradation of CC carbohydrates via glycolysis. {ECO:0000256|HAMAP-Rule:MF_00318}. 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; 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 -!- ACTIVITY REGULATION: The covalent binding to the substrate causes CC inactivation of the enzyme, and possibly serves as a signal for the CC export of the protein. {ECO:0000256|HAMAP-Rule:MF_00318}. 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. The export of CC enolase possibly depends on the covalent binding to the substrate; once CC secreted, it remains attached to the cell surface. {ECO:0000256|HAMAP- CC 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 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; -; 1. DR Gene3D; 3.30.390.10; -; 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; PTHR11902; 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; SSF51604; 1. DR SUPFAM; SSF54826; SSF54826; 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}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00318}; KW Secreted {ECO:0000256|HAMAP-Rule:MF_00318}. FT DOMAIN 4..125 FT /note="Enolase_N" FT /evidence="ECO:0000259|SMART:SM01193" FT DOMAIN 130..414 FT /note="Enolase_C" FT /evidence="ECO:0000259|SMART:SM01192" FT REGION 358..361 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318, FT ECO:0000256|PIRSR:PIRSR001400-2" 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 METAL 235 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318" FT METAL 280 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318" FT METAL 306 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318" FT BINDING 146 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318, FT ECO:0000256|PIRSR:PIRSR001400-2" FT BINDING 156 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318, FT ECO:0000256|PIRSR:PIRSR001400-2" FT BINDING 280 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318, FT ECO:0000256|PIRSR:PIRSR001400-2" FT BINDING 306 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318, FT ECO:0000256|PIRSR:PIRSR001400-2" FT BINDING 331 FT /note="Substrate; covalent; in inhibited form" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318" FT BINDING 382 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318, FT 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 //