ID   A0A1I4S2I1_9PSED        Unreviewed;       714 AA.
AC   A0A1I4S2I1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase / enoyl-CoA hydratase / 3-hydroxybutyryl-CoA epimerase {ECO:0000313|EMBL:SFM58433.1};
GN   ORFNames=SAMN04487858_104104 {ECO:0000313|EMBL:SFM58433.1};
OS   Pseudomonas sp. ok602.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1761898 {ECO:0000313|EMBL:SFM58433.1, ECO:0000313|Proteomes:UP000199362};
RN   [1] {ECO:0000313|Proteomes:UP000199362}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OK602 {ECO:0000313|Proteomes:UP000199362};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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: In the central section; belongs to the 3-hydroxyacyl-CoA
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00007005}.
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DR   EMBL; FOUL01000004; SFM58433.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4S2I1; -.
DR   STRING; 1761898.SAMN04487858_104104; -.
DR   OrthoDB; 5389341at2; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000199362; 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; 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.
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}.
FT   DOMAIN          318..496
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          499..599
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   714 AA;  76287 MW;  489CA2DD963FFDE2 CRC64;
     MTEAIRYETG QDRIVVLTLD MPGQSANTMN AMYRQAMAAC VARLQAEQAS ISGVIITSAK
     KTFFAGGDLN ELIKVDKAQA KAFYDMVLAL KQQLRTLETL GKPVVAAING AALGGGWEIC
     LACHHRVALD NASVQIGLPE VTLGLLPGGG GVVRMVRMLG LEKALPYLLE GKKIRPQQAL
     QAGLVDELAG DHAELMAKSR AWILANPQAV QRWDVKGYAI PGGTPAHPKV AQMLAIAPSV
     LRAKTQGCLP APEKILCAAV EGAQVDFDTA QLIETRYFTE LTTGQVAKNM IGTFWFQLNE
     INAGGSRPAG FAPHVTKKVG VLGAGMMGAG IAYVSAVAGI EVVLKDINLA AAEKGKAHSA
     ALLDQKVARG QLSAEQRDVT LARIHATEQD DDLAGCDLII EAVFEDRELK ARVSSAAQKI
     VGPDAVLASN TSTLPISGLA QAVPDQSKFI GLHFFSPVEK MPLVEIIKGA STSDETLARG
     FDFVLQIKKT PIVVNDSRGF FTSRVFGTFT NEGIAMLGEG IAAPMIETEA RKAGMPIGPL
     AISDEVSLSL MSHIRQQTAK DLHAEGKHLP EHPAVAVIDL LLNEYKRPGK AAGAGFYDYP
     AGAQKHLWPE LKKHFEKADG QISPQDVRDR LLFVQALETV RCVEEGVLLS TADANIGSIF
     GIGFAAWTGG ALQFINQYGV KDFVARAQYL AGQYGERFTP PALLLDKAAR EALF
//