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-APR-2018, entry version 8.
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: 2-phospho-D-glycerate = phosphoenolpyruvate +
CC       H(2)O. {ECO:0000256|HAMAP-Rule:MF_00318}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00318};
CC   -!- ENZYME 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}.
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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.
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
//