ID A0A095SFK8_9GAMM Unreviewed; 430 AA.
AC A0A095SFK8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=T9A_00399 {ECO:0000313|EMBL:KGD63079.1};
OS Alcanivorax jadensis T9.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alcanivorax.
OX NCBI_TaxID=1177181 {ECO:0000313|EMBL:KGD63079.1, ECO:0000313|Proteomes:UP000029443};
RN [1] {ECO:0000313|EMBL:KGD63079.1, ECO:0000313|Proteomes:UP000029443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T9 {ECO:0000313|EMBL:KGD63079.1,
RC ECO:0000313|Proteomes:UP000029443};
RA Lai Q., Shao Z.;
RT "Genome Sequence of alkane-degrading Bacterium Alcanivorax jadensis T9.";
RL Submitted (SEP-2012) 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:KGD63079.1}.
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DR EMBL; ARXU01000001; KGD63079.1; -; Genomic_DNA.
DR RefSeq; WP_035244633.1; NZ_ARXU01000001.1.
DR AlphaFoldDB; A0A095SFK8; -.
DR STRING; 1177181.T9A_00399; -.
DR PATRIC; fig|1177181.3.peg.408; -.
DR eggNOG; COG0148; Bacteria.
DR OrthoDB; 9804716at2; -.
DR UniPathway; UPA00109; UER00187.
DR Proteomes; UP000029443; 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 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 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 341
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 ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT BINDING 289
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT BINDING 289
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 316
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT BINDING 316
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 341
FT /ligand="substrate"
FT /note="covalent; in inhibited form"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318"
FT BINDING 368..371
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-2"
FT BINDING 392
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00318,
FT ECO:0000256|PIRSR:PIRSR001400-2"
SQ SEQUENCE 430 AA; 45887 MW; 7DC0A10CC1322D57 CRC64;
MSKIVDIKAR EILDSRGNPT IEADVILESG ASGSACAPSG ASTGSREALE LRDGDKARYL
GKGVTKAVGN VNSAIRELLV GMEAGDQKAL DKAMIDADGT ENKAKFGANA ILAVSLAAAK
AAAVDQGKPL YEYISDLQDD DNEYSLPVPM MNIINGGEHA DNNVDIQEFM IQPVGAPTVA
EAIRYGAEIF HALKSVLKKR GLNTAVGDEG GFAPDLPSNE AALEAIMEAI EIAGYKAGDD
VTLALDCAAS EFYKDGKYVL AGEGRSMDSE EFASYLAELC DRYPIISIED GMDESDWDGW
KILTEKLGKK IQLVGDDLFV TNTKILKRGI DEGVANSILI KFNQIGSLSE TLDAIKMAKD
AGYTAVISHR SGETADSTIA DLAVATAAGQ IKTGSLCRSD RVAKYNRLIR IEQELGRAAY
HGRKEFKFLG
//
