ID   A0A1H1AN19_9ACTN        Unreviewed;       723 AA.
AC   A0A1H1AN19;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase / enoyl-CoA hydratase / 3-hydroxybutyryl-CoA epimerase {ECO:0000313|EMBL:SDQ41148.1};
GN   ORFNames=SAMN04489765_0308 {ECO:0000313|EMBL:SDQ41148.1};
OS   Tsukamurella pulmonis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Tsukamurellaceae;
OC   Tsukamurella.
OX   NCBI_TaxID=47312 {ECO:0000313|EMBL:SDQ41148.1, ECO:0000313|Proteomes:UP000183053};
RN   [1] {ECO:0000313|Proteomes:UP000183053}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44142 {ECO:0000313|Proteomes:UP000183053};
RA   Varghese N.;
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; FNLF01000002; SDQ41148.1; -; Genomic_DNA.
DR   RefSeq; WP_068537298.1; NZ_UHII01000001.1.
DR   AlphaFoldDB; A0A1H1AN19; -.
DR   STRING; 47312.SAMN04489765_0308; -.
DR   OrthoDB; 9771883at2; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000183053; 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}.
FT   DOMAIN          322..500
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          503..602
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   723 AA;  76462 MW;  71B65C807BC279C7 CRC64;
     MAENMIRWEQ DADGIVVLTM DDPTSSANTM NDLYRESMGA TIDRLEAEKD SITGVVLTSA
     KKTFFAGGNL NLIRQSTPEQ AQQVFDNVEN LKKDLRRLET LGKPVVAAIN GAALGGGLEI
     ALATHHRIAA DARGSQIGLP EVTLGLLPGG GGVTRTVRLL GLQGALMGVL LQGPRMKPAK
     AKDVGLVHEV VGTVEELVPA AKAWIKANPE GGVQPWDVKG YKIPGGSPSS PAIAANLPAF
     PANLRKQLKG APMPAPRAIM AAAVEGAMVD FDTASVIEGR YFTSLATGQV SKNMIKAFFF
     DLQHINGGGS RPEGYDKYTA KKVGVIGAGM MGAAIAYVSA KAGIEVVLKD IDLDAAKRGK
     AYSEKLEEKA LAKGRTTAEK SAELLARITP TVDAADFAGV DLVIEAAFES VEVKHKVFQE
     IEDIVEPDAV LGSNTSTLPI TILAEGVKRS EDFIGIHFFS PVDKMPLVEI IRGAKTSDAV
     LAKVIDYTLQ IKKTPIVVHD SRGFFTSRVI GTFVNEAIAA VGEGVNPVLI EQAGQQAGYP
     AAPLQLMDEL TLTLPQKIRK ETRAAAEAAG TPLPAHGSDA VVDAMVDAGR TGRKDGAGFY
     DYADGKRTGL WSGLSELFPG GNDIPLQDMI DRMLFAESLE TVRCFDEGVM DSVADANIGS
     IFGIGFPAWT GGVLQFINGY TAPDGTVGPK AFVARAQELT KYGEQFTPPA SLVAKAEAGE
     TYE
//