ID A0A2A3GXC4_9ACTN Unreviewed; 708 AA.
AC A0A2A3GXC4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:PBC60439.1};
GN ORFNames=BKI49_28370 {ECO:0000313|EMBL:PBC60439.1};
OS Streptomyces sp. Tue6028.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2036037 {ECO:0000313|EMBL:PBC60439.1, ECO:0000313|Proteomes:UP000217789};
RN [1] {ECO:0000313|EMBL:PBC60439.1, ECO:0000313|Proteomes:UP000217789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tue6028 {ECO:0000313|EMBL:PBC60439.1,
RC ECO:0000313|Proteomes:UP000217789};
RA Greule A., Flemming S., Bechthold A.;
RT "The Draft Genome Sequence of Streptomyces sp. Tue6028 - Producer of
RT Polyketomycin and Foxicin.";
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}.
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:PBC60439.1}.
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DR EMBL; MLCE01000031; PBC60439.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3GXC4; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000217789; 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:UP000217789}.
FT DOMAIN 339..519
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 523..605
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 708 AA; 75260 MW; 6656B44DACAE821E CRC64;
MSTAELLKGA AELFPDEVVT SANVRHLDLP FGAGRFALIT LDNGFDHTKP TTFGPASLAN
LNTAIDQVEA EAAAGDIIGV GITGKPFIFA VGADLKGVEL LKKHEDALAI GKGGHEVFKR
LSALAVPTFA YYNGAAMGGG VEVGLHCTYR TVSKALPAFS LPEVFLGLVP GWGGCTILPN
LIGADKAVSV IIENSLNQNK QLKGKQVFEL GIADALFEGA DFLEQSLLWT ASVLKGDITV
ERPEIDRGEA WDQAVAKGRF IADGKVHGAA PAAYRALDII AAAKDGDLQK GYDAEDVALA
DLIMGGELRS GIYAFNLVQK RGKRPAGAPD KNLARPVTKV GVVGAGLMAS QLALLFLRRL
EVPVVLTDID QERVDKGVGY VHAEIDKLLG KGRINQDKAN RLKALVSGVL DKAEGFSDAD
FIIEAVFEEI GVKQQVFAEV EAVAPAHAIL ATNTSSLSVT EMASKLKNPE RVVGFHFFNP
VAILPLLEIV RGERTDDASL ATAFAVAKKL KKTAVLTKDA PAFVVNRILT RFMGEIQNVI
DEGTPVEIAE KAIEPLGLPM SPLVLLELVG PAIGLHVSET LNRAFPDRFT VSENLAAVVK
AGKRGFYVYD SGKPELDPEV AALLKQGDVV LTEEQVRARV LDAVAQEIGL MLDEGVVAEA
QDIDLCLITG AGWPFHLGGI TPYLDREGVS ERVNGKRFLE PGVASVPA
//
