ID   A0A1Q7JZ12_9ARCH        Unreviewed;       415 AA.
AC   A0A1Q7JZ12;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   12-OCT-2022, entry version 20.
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}.
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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   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|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   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   BINDING         280
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT   BINDING         280
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   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   BINDING         306
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         331
FT                   /ligand="substrate"
FT                   /note="covalent; in inhibited form"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT   BINDING         358..361
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         382
FT                   /ligand="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
//