ID A0A0N1KJE7_9GAMM Unreviewed; 730 AA.
AC A0A0N1KJE7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=enoyl-CoA hydratase {ECO:0000256|ARBA:ARBA00012076};
DE EC=4.2.1.17 {ECO:0000256|ARBA:ARBA00012076};
GN ORFNames=M992_0979 {ECO:0000313|EMBL:KPD03689.1};
OS Moellerella wisconsensis ATCC 35017.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Moellerella.
OX NCBI_TaxID=1354267 {ECO:0000313|EMBL:KPD03689.1, ECO:0000313|Proteomes:UP000053226};
RN [1] {ECO:0000313|EMBL:KPD03689.1, ECO:0000313|Proteomes:UP000053226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35017 {ECO:0000313|EMBL:KPD03689.1,
RC ECO:0000313|Proteomes:UP000053226};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (JUL-2015) 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}.
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:KPD03689.1}.
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DR EMBL; LGAA01000009; KPD03689.1; -; Genomic_DNA.
DR RefSeq; WP_053907558.1; NZ_LGAA01000009.1.
DR AlphaFoldDB; A0A0N1KJE7; -.
DR OrthoDB; 5389341at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000053226; Unassembled WGS sequence.
DR GO; GO:0036125; C:fatty acid beta-oxidation multienzyme complex; IEA:InterPro.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008692; F:3-hydroxybutyryl-CoA epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0004165; F:delta(3)-delta(2)-enoyl-CoA isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0004300; F:enoyl-CoA hydratase activity; IEA:UniProtKB-EC.
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; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR InterPro; IPR012799; FadB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR02437; FadB; 1.
DR PANTHER; PTHR43612:SF8; FATTY ACID OXIDATION COMPLEX SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43612; TRIFUNCTIONAL ENZYME SUBUNIT ALPHA; 1.
DR Pfam; PF00725; 3HCDH; 2.
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.
DR PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE 3: Inferred from homology;
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:KPD03689.1};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:KPD03689.1};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:KPD03689.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053226}.
FT DOMAIN 315..494
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 496..592
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 627..688
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 730 AA; 80192 MW; 49D6C4ECE5C456B5 CRC64;
MLYQSDTIEV RWVKTGIAEL IFNALGPINK LDTQTVASLD EAVAILEQHP ELQGLILRST
KSAFIVGADI KEFLSLFDAP KEQLIEWLKY ANGIFNRIED LPIPTVSAIN GYALGGGCEC
VLATDFRIVT PDARIGLPET KLGIMPGFGG SVRLPRLIGC DNALEIITAG KDIGANEALK
LGLVNAIVAT EQLQRSALKL IEQAIAGSID WKKARQPKLS PLQLSPLEQS MSFNVAKGMV
IKVAGKHYPA PLTAVTTIEK AANCARNEAL QHETAAFIPL AHSTVAQALV SIFLNDQYIK
TLNKKYTQQE SPPNKVMVLG AGIMGGGIAY QSASKGVSVL MKDINDHSLQ LGIQEAEKLL
NNQFERGKLS ALKMAKILSS IHPSLDYHGS KDVDIVIEAV IENPKIKAAV LAEAEALISP
ESIITSNTST IPITKLANAL LRPENFCGMH FFNPVHRMPL VEVIRGEKTS DDTLAKVVAY
AIKMGKTPIV VNDCPGFFVN RVLFPYFAGF SLLLQDGADF NQIDKVMETE FGWPMGPAYL
LDVVGIDTAH HAQQVMAVGF PERMTKSTRD AIDILYEQQR FGQKNNQGFY QYQKDKKGKP
IKLADPIVEQ LINPNQQPKK SFTSEQIIQR MMIPMINEVV RCLEEGIIQS PAEADIALVY
GLGFPPFHGG IFRYIETLGL ANYVQSTEQY SYLGPLYQVP EGLKQRSITN NRYYPQPATV
AINVKKSMRG
//
