ID T0GUM2_9SPHN Unreviewed; 719 AA.
AC T0GUM2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=enoyl-CoA hydratase {ECO:0000256|ARBA:ARBA00012076};
DE EC=4.2.1.17 {ECO:0000256|ARBA:ARBA00012076};
GN ORFNames=L284_22745 {ECO:0000313|EMBL:EQB07681.1};
OS Novosphingobium lindaniclasticum LE124.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1096930 {ECO:0000313|EMBL:EQB07681.1, ECO:0000313|Proteomes:UP000015527};
RN [1] {ECO:0000313|EMBL:EQB07681.1, ECO:0000313|Proteomes:UP000015527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LE124 {ECO:0000313|EMBL:EQB07681.1,
RC ECO:0000313|Proteomes:UP000015527};
RX PubMed=24029761;
RA Saxena A., Nayyar N., Sangwan N., Kumari R., Khurana J.P., Lal R.;
RT "Genome Sequence of Novosphingobium lindaniclasticum LE124T, Isolated from
RT a Hexachlorocyclohexane Dumpsite.";
RL Genome Announc. 1:e00715-13(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35;
CC Evidence={ECO:0000256|ARBA:ARBA00023693};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC hydratase/isomerase family. {ECO:0000256|ARBA:ARBA00008750}.
CC -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-CoA
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00007005}.
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:EQB07681.1}.
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DR EMBL; ATHL01000153; EQB07681.1; -; Genomic_DNA.
DR AlphaFoldDB; T0GUM2; -.
DR PATRIC; fig|1096930.3.peg.4479; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000015527; Unassembled WGS sequence.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR CDD; cd06558; crotonase-like; 1.
DR Gene3D; 1.10.1040.50; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
DR InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR InterPro; IPR006108; 3HC_DH_C.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43612; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43612:SF3; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR Pfam; PF00378; ECH_1; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00067; 3HCDH; 1.
PE 3: Inferred from homology;
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000015527}.
FT DOMAIN 331..503
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 509..603
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT REGION 695..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 719 AA; 77661 MW; 77327D908098C045 CRC64;
MKEATMNDPA WTYLADRDLT LGPVSRVEPG EFTHWRTSRD QDGVFWAVID QQGSGTNTLS
QAVLEEFSRI LDLIEQRMPK ALVIRSAKRD GFLAGADIAE FRDVDDEAAI RERIAAAHGV
VDRLAALTIP TIAIMHGYAL GGGLEIALAC NQRNAVDGTR FGFPEVQIGL HPGLGGTARF
THLCDPIEAM SFMLTGKSIH DRQAKRMGLV DAVVPERHVE AAIAAAVRGD LDQAHQGLVG
RIKDSAPARR LAARQMRAQA EDRAPSRHYP APYALIDLWE EHGGDLDAMK QAEIASFARL
MLTDAAQNLI RVFFLRQKLK DLAGKDAGIA QVHVIGAGAM GGDIAAWCAW KGLRTSLSDV
SAEAIGAAVG RAAALYEKIA HGDRLKIRDA LDRLIPDTAA LGVTSADLVV EAAPEKAELK
RKLYADAEPR MKPGAILATN TSSIPLKELR EGLERPERLI GIHFFNPVSR LDLVEVVTHD
GTDEKVAARA RAFVGHIGKL PAAAGSAPGF IVNRVLTPYL AEALTLMDEG VPPEIIDKAA
TDFGMPVGPL ELADQVGLDI GLAVAEMLKR ELDWPIPDAP QWLRDKVKAR ELGKKTGKGI
YVWKDGKAVK GHTAKRAAET SNMDLADRLI LPMVNTAVAV LREGVTDDPE VIDAAMIFGT
GFAPFRGGPI HYARQRGAGE IVSALNDLAR RHGPRFEPDA GWSEGGRFEE DGPIAHETP
//
