ID A0A145WY78_9GAMM Unreviewed; 714 AA.
AC A0A145WY78;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=enoyl-CoA hydratase {ECO:0000256|ARBA:ARBA00012076};
DE EC=4.2.1.17 {ECO:0000256|ARBA:ARBA00012076};
GN ORFNames=AMD27_03115 {ECO:0000313|EMBL:AMW77983.1};
OS Acinetobacter sp. TGL-Y2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1407071 {ECO:0000313|EMBL:AMW77983.1, ECO:0000313|Proteomes:UP000076238};
RN [1] {ECO:0000313|Proteomes:UP000076238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TGL-Y2 {ECO:0000313|Proteomes:UP000076238};
RA Zhang G.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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: Belongs to the enoyl-CoA hydratase/isomerase family.
CC {ECO:0000256|RuleBase:RU003707}.
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}.
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DR EMBL; CP015110; AMW77983.1; -; Genomic_DNA.
DR RefSeq; WP_067656227.1; NZ_CP015110.1.
DR AlphaFoldDB; A0A145WY78; -.
DR STRING; 1407071.AMD27_03115; -.
DR KEGG; acv:AMD27_03115; -.
DR OrthoDB; 5389341at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000076238; Chromosome.
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; 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; IPR018376; Enoyl-CoA_hyd/isom_CS.
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; PS00166; ENOYL_COA_HYDRATASE; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000076238}.
FT DOMAIN 320..498
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 501..601
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 714 AA; 77010 MW; 78475AC52590C1E0 CRC64;
MSAIQFEKNA DGIVILTLDS PNQSANTMNG DFRVALEDTV AKLKAESGIT GIIFKSAKKT
FFAGGDLDEL IQAQPEHATE FFGMIQKMKA EFRYIETLGV PVVAALNGTA LGGGWEIALG
CHYRIALNDP KAKFGLPEVT LGLLPGGGGI VRMVRLLGLQ NAFPFLMEGK QFGVDKAKSL
GLIHDTAESN EELFEKAIAW VKANPPSIKA SQQPFDVKGY KIPGGTPSSP QVAQVLAIAP
AMLRDKTKGC YPAPEAIMSA AVEGAQVDVD TALTIESRYF TYLATGQISK NMIGTFWHGL
NAIKSGASRP QNVEKWQATK LGVLGAGMMG AGIAYSSAIK GIQVVLKDVS QEAADKGKAY
SQKLLDKRVS QGRMTAEKRD QVLSLITATA SSEDLKGCDL IIEAVFENQE LKAKVTQEAE
KHLIAGGVMA SNTSTLPISG LAQASQNAKN FIGLHFFSPV DKMQLVEIIK GKETSAETLA
KAYDYVQQIG KTPIVVNDSR GFFTSRVFGT FVQEGLRLLS EGVHPAKIEM AALKAGMPIG
PLAIQDEVSL TLSEHVTSET RKALQAEGKD LPRSGADEVI ETMIHQFNRK GKAAGSGFYD
YPQDGKKHLW DGLTHWKKDN DISEQEIIDR FLFVQSLDTL RCLEEGVLES VVDGNIGSIF
GIGFAPWTGG ALQFLNQYGL SKAVTRAQAL EAKYGERFKA PQLLLDKAKS GEKI
//
