ID A0A0F4JWD3_9ACTN Unreviewed; 712 AA.
AC A0A0F4JWD3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:KJY38048.1};
GN ORFNames=VR44_04390 {ECO:0000313|EMBL:KJY38048.1};
OS Streptomyces katrae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68223 {ECO:0000313|EMBL:KJY38048.1, ECO:0000313|Proteomes:UP000033551};
RN [1] {ECO:0000313|EMBL:KJY38048.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL ISP-5550 {ECO:0000313|EMBL:KJY38048.1};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-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:KJY38048.1}.
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DR EMBL; JZWV01000080; KJY38048.1; -; Genomic_DNA.
DR RefSeq; WP_045946024.1; NZ_JZWV01000080.1.
DR AlphaFoldDB; A0A0F4JWD3; -.
DR STRING; 68223.GCA_002028425_05441; -.
DR PATRIC; fig|68223.7.peg.447; -.
DR eggNOG; COG1024; Bacteria.
DR eggNOG; COG1250; Bacteria.
DR OrthoDB; 9771883at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000033551; 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 340..520
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 524..606
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 712 AA; 75758 MW; 32B6490E8B2713FC CRC64;
MSTTAELLKG AAELFPDEVV TSAHVRHLDL PFGAGRFALI TLDNGFDHTK PTTFGPQSLA
NLNAAIDQVE QEATAGTIVG AGITGKPFIF AVGADLKGVE LLKKHDEALA IGKGGHDVFK
RLSALAVPTF AYYNGAAMGG GVEVGLHCSY RTVSKAIPAF SLPEVFLGLV PGWGGCAILP
NLIGAERAVS VIIENSLNQN RQLKGKQVFE LGIADAIFEG ADFLEQSLIW TAKVLKGETE
VVRAEVERGE AWDAAVAKGR SIADSKVHGA APAAYRALEI IAAAKDGDLQ AGFDAEDKAL
ADLIMGGELR SGIYAFNLVQ KRGKRPAGAP DKSLARPVTK VGVVGAGLMA SQLALLFLRR
LEVPVVLTDI DQERVDKGVG YVHAEIQKLL DKGRINQDKA NRLTALVTGV LDKAEGFADA
DFIIEAVFEE MSVKQKVFAE VEAVAPAHAI LATNTSSLSV SEMASKLQHP ERVVGFHFFN
PVAILPLLEI VRGERTDDAS LATAFGVAKK LKKTAVLTKD APAFVVNRIL TRFMGEIQNV
IDEGTPVATA EKAIEPLGLP MSPLVLLELV GPAIGLHVSE TLNRSFPERF TVSPNLKRVV
EAGKRGFYVY SAENGFKPEL DPEVAALLVQ GDSVLTEEQV RDRVLDAVAQ EIGLMLEEGV
VAEAQDIDLC LITGAGWPFH LGGITPYLDR EGVSERVNGK KFLAPGVASV PA
//
