ID A0A162Z843_9BURK Unreviewed; 430 AA.
AC A0A162Z843;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=LPB072_13970 {ECO:0000313|EMBL:AOW13784.1}, LPB72_01850
GN {ECO:0000313|EMBL:OAD44252.1};
OS Hydrogenophaga crassostreae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Hydrogenophaga.
OX NCBI_TaxID=1763535 {ECO:0000313|EMBL:AOW13784.1, ECO:0000313|Proteomes:UP000185680};
RN [1] {ECO:0000313|EMBL:OAD44252.1, ECO:0000313|Proteomes:UP000185657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LPB0072 {ECO:0000313|EMBL:OAD44252.1,
RC ECO:0000313|Proteomes:UP000185657};
RA Shin S.-K., Yi H.;
RT "Draft genome sequence of Hydrogenophaga sp. LPB0072.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AOW13784.1, ECO:0000313|Proteomes:UP000185680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LPB0072 {ECO:0000313|EMBL:AOW13784.1,
RC ECO:0000313|Proteomes:UP000185680};
RA Kim E., Yi H.;
RT "Hydorgenophaga sp. LPB0072 isolated from gastropod.";
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00318}.
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DR EMBL; CP017476; AOW13784.1; -; Genomic_DNA.
DR EMBL; LVWD01000001; OAD44252.1; -; Genomic_DNA.
DR RefSeq; WP_066084712.1; NZ_LVWD01000001.1.
DR AlphaFoldDB; A0A162Z843; -.
DR STRING; 1763535.LPB072_13970; -.
DR KEGG; hyl:LPB072_13970; -.
DR OrthoDB; 4577602at2; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000185657; Unassembled WGS sequence.
DR Proteomes; UP000185680; Chromosome.
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 Pyruvate {ECO:0000313|EMBL:AOW13784.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000185680};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|HAMAP-Rule:MF_00318}.
FT DOMAIN 5..135
FT /note="Enolase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01193"
FT DOMAIN 143..428
FT /note="Enolase C-terminal TIM barrel"
FT /evidence="ECO:0000259|SMART:SM01192"
FT ACT_SITE 209
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-1"
FT ACT_SITE 342
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-1"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT BINDING 290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT BINDING 290
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT BINDING 317
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT BINDING 317
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT BINDING 342
FT /ligand="substrate"
FT /note="covalent; in inhibited form"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT BINDING 393
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
SQ SEQUENCE 430 AA; 44784 MW; 86EF57F4F02A6C33 CRC64;
MNTQISAVRA RQILDSRGRP TVEADVTLAD GSFGRASVPS GASTGSAEAH ELRDGDATTY
AGLGVLKAVA HANSEIAAAL AGLDAREQHK VDLAMRSLDG TPQLARLGAN AVLAVSIAVA
RAAAASLRQP LFERVREIAG LSGLSMPVPM VNILSGGLHA GRGMDVQDFL AMPVRATSIA
DAIHIISRVR NAATEEARAR GLPTLLADEG GVSPGLPSGR DALEMMLRIT ERAGLKPGDD
VVIAIDVAAA SLQQPDGSYA LTREGRTANA VEMTEMLAGW VRDYPVVSIE DGLGEEDWSA
WAELTQQVGH RTQLVGDDLF TTHPDRLARG VRERVANGVL VKANQNGTLS GTIDLIAQAK
AAGYATIVSA RSGETEDAFM SDLAVGSGAG QIKIGSLRTS STVAKYNQLL RIEEACSAPY
AGISALVGRP
//
