ID A0A1I5NM15_9ACTN Unreviewed; 426 AA.
AC A0A1I5NM15;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=SAMN05660464_2595 {ECO:0000313|EMBL:SFP22849.1};
OS Geodermatophilus dictyosporus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1523247 {ECO:0000313|EMBL:SFP22849.1, ECO:0000313|Proteomes:UP000198857};
RN [1] {ECO:0000313|Proteomes:UP000198857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44208 {ECO:0000313|Proteomes:UP000198857};
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; FOWQ01000003; SFP22849.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5NM15; -.
DR STRING; 1523247.SAMN05660464_2595; -.
DR OrthoDB; 9804716at2; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000198857; 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; SFLDG00178; 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|HAMAP-Rule:MF_00318};
KW Reference proteome {ECO:0000313|Proteomes:UP000198857};
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 426 AA; 44697 MW; 609007FA4AE65651 CRC64;
MPSIDAVGAR EILDSRGNPT VEVEVALDDG TIARAAVPSG ASTGAFEAVE LRDGGERYGG
KGVTKAVDGV LDVIGPELVG YEATEQRLVD QRLLDLDGTP DKSRLGANAL LGVSLAVARA
GADSTGLPLF RYVGGPSAHL LPVPMMNILN GGAHADSNVD VQEFMIAPIG AATFAEALST
GAECYHALKS VLKGRGLSTG LGDEGGFAPD LPTNRAALDL IAEAVEKAGY ALGTDIAFAL
DVAATEFHGE GGYDFEGQTR SAEYLVDYYR ELVDAYPIVS IEDPLSEEDW DGWVAMTAAL
GDRVQIVGDD LFVTNPARLA DGIGRGAANA LLVKVNQIGT LTETLDAVNL AHRNGYRCMM
SHRSGETEDT TIADLAVATD CGQIKTGAPA RSERVAKYNQ LLRIEEELDD AARYAGAAAF
PRLRTS
//
