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Database: UniProt
Entry: A0A0M8V3U1_9ACTN
LinkDB: A0A0M8V3U1_9ACTN
Original site: A0A0M8V3U1_9ACTN 
ID   A0A0M8V3U1_9ACTN        Unreviewed;       736 AA.
AC   A0A0M8V3U1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:KOV57610.1};
GN   ORFNames=ADL01_40130 {ECO:0000313|EMBL:KOV57610.1};
OS   Streptomyces sp. NRRL WC-3618.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1519490 {ECO:0000313|EMBL:KOV57610.1, ECO:0000313|Proteomes:UP000037738};
RN   [1] {ECO:0000313|EMBL:KOV57610.1, ECO:0000313|Proteomes:UP000037738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL WC-3618 {ECO:0000313|EMBL:KOV57610.1,
RC   ECO:0000313|Proteomes:UP000037738};
RA   Noorani M.;
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: 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:KOV57610.1}.
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DR   EMBL; LGDW01000492; KOV57610.1; -; Genomic_DNA.
DR   RefSeq; WP_053747007.1; NZ_LGDW01000492.1.
DR   AlphaFoldDB; A0A0M8V3U1; -.
DR   PATRIC; fig|1519490.3.peg.8731; -.
DR   OrthoDB; 9771883at2; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000037738; 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   Reference proteome {ECO:0000313|Proteomes:UP000037738}.
FT   DOMAIN          323..500
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          503..603
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   736 AA;  78912 MW;  333135265B78EA9A CRC64;
     MTQSTTIRWE QDRTGLVTLV LDDPDQSANT MNQAFRDSLA VVTDRLEAEK ETIRGVIITS
     AKKTFFAGGD LRDLIRVTPD TAQELLDGGL AIKRDLRRIE TLGKPVVAAL NGAALGGGYE
     IALACHHRVA LDAPGSKIGC PEVTLGLLPG GGGVVRTVRM LGIADALLKV LLQGTQYSPQ
     RALQNGLVDE VAATQDELMA KARAFIDANP VSQQPWDKPG YRIPGGTPAN PRFAANLPAF
     PANLRKQTNG APYPAPRSIL AAAVEGAQVD FETAQVIEAR YFVELAAGQT SKNMIQAFFF
     DLQAVNSGAN RPKGIEPRPV RRVAVLGAGM MGAGIAYSCA RAGIEVVLKD VSAEAAARGK
     NYSEKLCAKA VSRGRSTQEK ADELLARITP TADPQDVAGC DAVIEAVFED PALKHKVFQE
     IQHLVEPDAL LCSNTSTLPI TALAEGVERQ ADFVGLHFFS PVDKMPLVEI IKGERTGQEA
     LARAFDLVRQ IRKTPIVVND SRGFFTSRVI GHFINEGVAM VGEGIEPASV EQAAAQAGYP
     AKVLSLMDEL TLTLPRRIRA ESKRAVEEAG GTWVTHPAEA VIDRMVDEFG RTGRSGGGGF
     YEYGQDGRRT RLWPGLREHF GREGAASEEG AEGAEGVRIP FKDMQERMLF SEALDTVRLL
     EEGVLTSVAD ANIGSIFGIG FPGWTGGVLQ YINGYEGGLP GFVARSRELA QRYGERFAPP
     ALLVEKAAKG EGFVDG
//
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