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Entry: A0A1I1YH21_9ACTN
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ID   A0A1I1YH21_9ACTN        Unreviewed;       425 AA.
AC   A0A1I1YH21;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=SAMN05216574_102360 {ECO:0000313|EMBL:SFE18632.1};
OS   Blastococcus sp. DSM 46838.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Blastococcus.
OX   NCBI_TaxID=1798228 {ECO:0000313|EMBL:SFE18632.1, ECO:0000313|Proteomes:UP000198589};
RN   [1] {ECO:0000313|Proteomes:UP000198589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 46838 {ECO:0000313|Proteomes:UP000198589};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00001946,
CC         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}.
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DR   EMBL; FOND01000002; SFE18632.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1YH21; -.
DR   STRING; 1798228.SAMN05216574_102360; -.
DR   OrthoDB; 9804716at2; -.
DR   UniPathway; UPA00109; UER00187.
DR   Proteomes; UP000198589; 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   CDD; cd03313; enolase; 1.
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; IPR020809; Enolase_CS.
DR   InterPro; IPR020811; Enolase_N.
DR   NCBIfam; TIGR01060; eno; 1.
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   SFLD; SFLDF00002; enolase; 1.
DR   SFLD; SFLDS00001; Enolase; 1.
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.
DR   PROSITE; PS00164; ENOLASE; 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|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00318};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00318}; Reference proteome {ECO:0000313|Proteomes:UP000198589};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|HAMAP-Rule:MF_00318}.
FT   DOMAIN          4..133
FT                   /note="Enolase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01193"
FT   DOMAIN          138..422
FT                   /note="Enolase C-terminal TIM barrel"
FT                   /evidence="ECO:0000259|SMART:SM01192"
FT   ACT_SITE        204
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-1"
FT   ACT_SITE        334
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-1"
FT   BINDING         154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         163
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         241
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT   BINDING         282
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT   BINDING         282
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         309
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT   BINDING         309
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         334
FT                   /ligand="substrate"
FT                   /note="covalent; in inhibited form"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT   BINDING         361..364
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-2"
FT   BINDING         385
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT                   ECO:0000256|PIRSR:PIRSR001400-2"
SQ   SEQUENCE   425 AA;  44511 MW;  9EFAF3D014DE1C0A CRC64;
     MPSIDAVGAR EILDSRGNPT VEVEVALDDG TIARAAVPSG ASTGAFEAVE LRDGGDRYGG
     KGVTKAVDGV LDVIGPELVG YEATEQRLVD QRLIDLDGTP DKSRLGANAI LGVSLAVARA
     AADSTGLPLF RYVGGPSAHL LPVPMMNILN GGAHADSNVD VQEFMIAPIG AATFAEALAM
     GTETYHALKA VLKKDGLATG LGDEGGFAPN LSSNRAALDL IVRAVEQAGY AVGSDIAFAL
     DVAATEFHSD GAYAFEGRKL SAEEMTAYYA ELVDAYPIVS IEDPLDEEDW AGWVSMTQQL
     GDRVQIVGDD LFVTNPTRLA DGISRGAANA LLVKVNQIGT LTETLDAVNL AHRSGYRCMM
     SHRSGETEDT TIADLAVATD CGQIKTGAPA RSERVAKYNQ LLRIEEELDD AARYAGAGAF
     PRLAG
//
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