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Database: UniProt
Entry: A0A0S8FML3_9GAMM
LinkDB: A0A0S8FML3_9GAMM
Original site: A0A0S8FML3_9GAMM 
ID   A0A0S8FML3_9GAMM        Unreviewed;       710 AA.
AC   A0A0S8FML3;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:KPK61003.1};
GN   ORFNames=AMJ59_03300 {ECO:0000313|EMBL:KPK61003.1};
OS   Gammaproteobacteria bacterium SG8_31.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=1703405 {ECO:0000313|EMBL:KPK61003.1, ECO:0000313|Proteomes:UP000051321};
RN   [1] {ECO:0000313|EMBL:KPK61003.1, ECO:0000313|Proteomes:UP000051321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_31 {ECO:0000313|EMBL:KPK61003.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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}.
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:KPK61003.1}.
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DR   EMBL; LJTI01000003; KPK61003.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8FML3; -.
DR   PATRIC; fig|1703405.3.peg.644; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000051321; 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          320..498
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          501..598
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   710 AA;  77784 MW;  DE8D6E891FD93649 CRC64;
     MSETIKYQKD EGGIVTLTID IADRSMNVLT PRFMRDLDAA VDRIVADDSV RGAIITSAKT
     SFIAGADLKE LVGVFGREMD EHQIYEFAGR YSQLYRKLET CGKPFVAAIN GTALGGGLEL
     CLACHHRVVL DNPKAAIGLP EVKVGLLPGA GGTQRLPRLI GIRESLPLML EGRHLKPPKA
     VELGICNELA TDVDDMMERA RRWLADVGDP VAPWDKKGFK VPGGSGGMHP AVVQTFMAGN
     AMVAEKTQHR YPAPISIMSC VYEGTQIPID KGLKVELQYF TKLLAGPVAR NMIRTLFIDK
     GAADKLARRP ADVPKSHVKK LGVLGAGMMG AGIAYVSAYA GQEVVLLDRA LEDAEKGKGY
     SRALLEKRVS RGRMTEDQAA AVLERIKPTT DYGDLAGCDL VIEAVFEDRA IKADVTEKTE
     AVIPETSIFA SNTSTLPITG LAQASRRPEQ FIGIHFFSPV DKMPLVEIIL GEKTGQEAIA
     RALDYVQQIR KTPILVNDSR GFYTSRVFST YVKEGMELLA EGVKPALIEN AAKMAGMPVG
     PLAVHDEVTI DLSYKILMQT KKDLGDDFLP TQADEVVRHF QEDLKRRGKR FGAGFYEYPE
     GARKYLWPGL AEEYPPAPEQ PDLEYIQRRL LYIQCVEAAR CMEEGVVPEP ADADVGSILG
     WGFPPWTGGT LSLIDTVGVR DFVDQCDALA EQHGPRFAPP DWLRQRSSAR
//
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