ID A0A0R0CPT5_9GAMM Unreviewed; 428 AA.
AC A0A0R0CPT5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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 ECO:0000313|EMBL:KRG67886.1};
GN ORFNames=ABB29_15210 {ECO:0000313|EMBL:KRG67886.1};
OS Pseudoxanthomonas dokdonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=344882 {ECO:0000313|EMBL:KRG67886.1, ECO:0000313|Proteomes:UP000052052};
RN [1] {ECO:0000313|EMBL:KRG67886.1, ECO:0000313|Proteomes:UP000052052}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21858 {ECO:0000313|EMBL:KRG67886.1,
RC ECO:0000313|Proteomes:UP000052052};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-2015) 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 -!- SUBUNIT: Component of the RNA degradosome, which is a multiprotein
CC complex involved in RNA processing and mRNA degradation.
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:KRG67886.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LDJL01000018; KRG67886.1; -; Genomic_DNA.
DR RefSeq; WP_057660573.1; NZ_LDJL01000018.1.
DR AlphaFoldDB; A0A0R0CPT5; -.
DR STRING; 344882.ABB29_15210; -.
DR PATRIC; fig|344882.3.peg.1424; -.
DR OrthoDB; 9804716at2; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000052052; 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:UP000052052};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|HAMAP-Rule:MF_00318}.
FT DOMAIN 4..134
FT /note="Enolase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01193"
FT DOMAIN 139..425
FT /note="Enolase C-terminal TIM barrel"
FT /evidence="ECO:0000259|SMART:SM01192"
FT ACT_SITE 205
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-1"
FT ACT_SITE 337
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-1"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT BINDING 285
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT BINDING 285
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT BINDING 312
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 337
FT /ligand="substrate"
FT /note="covalent; in inhibited form"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT BINDING 364..367
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 388
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-2"
SQ SEQUENCE 428 AA; 45686 MW; 3DDE0711AD484831 CRC64;
MTNIAKIHAR EILDSRGNPT LEAEVTLADG SFGRAMVPSG ASTGTKEAVE LRDGDKTRYL
GKGVRTAVDN VNNAIATALK GFDALDQEGL DRRLIELDGT ENKGRLGANA LLGVSLANAH
AVAASKKMPL WQHLANGRAV TLPVPMMNII NGGAHADNNV DLQEFMVLPV GFDSFAESLR
AGTEIFHALK SVLKGHGLST AVGDEGGFAP DFRSNVEALD TILEAIGKAG YKAGEDIQLG
LDVASSEFYD NGKYHLVGEG KRLTSEQFTD FLADWAAQYP IITIEDGMAE DDWAGWKLLT
DRIGKKVQLV GDDLFVTNPR IFKEGIESGT ANAILIKVNQ IGTLSETLEA IAMADHAGYA
AIVSHRSGET EDTTIADIAV ATTATQIKTG SLCRSDRVAK YNQLLRIEEA LGAAARYAGR
NAFVSLKQ
//
