ID A0A1Q7JZ12_9ARCH Unreviewed; 415 AA. AC A0A1Q7JZ12; DT 12-APR-2017, integrated into UniProtKB/TrEMBL. DT 12-APR-2017, sequence version 1. DT 13-NOV-2019, entry version 12. 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; unclassified Thaumarchaeota. OX NCBI_TaxID=1805392 {ECO:0000313|EMBL:OLC81152.1}; RN [1] {ECO:0000313|EMBL:OLC81152.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=27843720; RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., RA Singh A., Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., RA Northen T., Pan C., 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- CC phosphoglycerate into phosphoenolpyruvate. It is essential for the CC degradation of carbohydrates via glycolysis. {ECO:0000256|HAMAP- CC 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; Evidence={ECO:0000256|HAMAP- CC 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 CC the 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|HAMAP- CC 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 CC of enolase possibly depends on the covalent binding to the CC substrate; once secreted, it remains attached to the cell surface. CC {ECO:0000256|HAMAP-Rule:MF_00318}. CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000256|HAMAP- CC Rule:MF_00318}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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|HAMAP-Rule:MF_00318}; KW Lyase {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 Enolase_N. {ECO:0000259|SMART:SM01193}. FT DOMAIN 130 414 Enolase_C. {ECO:0000259|SMART:SM01192}. FT REGION 358 361 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00318, ECO:0000256|PIRSR: FT PIRSR001400-2}. FT ACT_SITE 199 199 Proton donor. {ECO:0000256|HAMAP-Rule: FT MF_00318, ECO:0000256|PIRSR:PIRSR001400- FT 1}. FT ACT_SITE 331 331 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_00318, ECO:0000256|PIRSR:PIRSR001400- FT 1}. FT METAL 235 235 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00318}. FT METAL 280 280 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00318}. FT METAL 306 306 Magnesium. {ECO:0000256|HAMAP-Rule: FT MF_00318}. FT BINDING 146 146 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00318, ECO:0000256|PIRSR:PIRSR001400- FT 2}. FT BINDING 156 156 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00318, ECO:0000256|PIRSR:PIRSR001400- FT 2}. FT BINDING 280 280 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00318, ECO:0000256|PIRSR:PIRSR001400- FT 2}. FT BINDING 306 306 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00318, ECO:0000256|PIRSR:PIRSR001400- FT 2}. FT BINDING 331 331 Substrate (covalent); in inhibited form. FT {ECO:0000256|HAMAP-Rule:MF_00318}. FT BINDING 382 382 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00318, ECO:0000256|PIRSR:PIRSR001400- FT 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 //