ID A0A2U2Z7Z7_9ACTN Unreviewed; 741 AA.
AC A0A2U2Z7Z7;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:PWI08410.1};
GN ORFNames=DIZ27_22285 {ECO:0000313|EMBL:PWI08410.1};
OS Streptomyces sp. NWU339.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2185284 {ECO:0000313|EMBL:PWI08410.1, ECO:0000313|Proteomes:UP000245372};
RN [1] {ECO:0000313|EMBL:PWI08410.1, ECO:0000313|Proteomes:UP000245372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NWU339 {ECO:0000313|EMBL:PWI08410.1,
RC ECO:0000313|Proteomes:UP000245372};
RA Adegboye M.F., Lobb B., Babalola O., Doxey A.C., Ma K.;
RT "Draft genomes of two novel cellulolytic Streptomyces strains isolated from
RT South African rhizosphere soils.";
RL Submitted (MAY-2018) 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:PWI08410.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QFRK01000019; PWI08410.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2Z7Z7; -.
DR OrthoDB; 9771883at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000245372; 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:UP000245372}.
FT DOMAIN 326..504
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 507..607
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 741 AA; 79331 MW; 878C199A372A7574 CRC64;
MTESTTIRWE QDDTGVVTLV LDDPDQSANT MNQAFRDSLA VITDRLEAEL RADPDSIRGI
ILTSAKKTFF AGGDLRDLIR VTPDTAQDLF DGGLAIKRQL RRVETLGKPV VAAINGAALG
GGYELALACH HRVALDAPGS RIGCPEVTLG LLPGGGGVVR TVRLLGIADA LLKVLLQGTQ
YSPRRALENG LVDEVADTHE ELLAKARAFI DAHPESAQPW DRPGYRIPGG TPSHPKFAAN
LPAFPANLRK QTNGAPYPAP RSILAAAVEG AQVDFETAQV IEARYFVELA AGQTSKNMIQ
AFFFDLQAVN AGANRPQGIE SRQVRKVAVL GAGMMGAGIA YSCARAGIDV VLKDVSLEAA
VKGKGYSEKL CAKAVAKGRT TQEKADALLA RITPTAEAQD LAGCDAVIEA VFEDTTLKHK
VFQEIQNVVA PDALLCSNTS TLPITALAEG VERQGDFIGL HFFSPVDKMP LVEIIKGERT
GDEALARAFD LVRQIKKTPI VVNDSRGFFT SRVIGQFINE GVAMVGEGIE PASIEQAAAQ
AGYPAKVLSL VDELTLTLPR KIRTESRRAV EEAGGTWTEH PADAVIDRMV DEYDRPGRAA
GAGFYTYKED GGRDALWPGL REHFTKPGHE IPFRDMQERM LFSEALDTVR LLEEGVLTSV
ADANIGSILG IGFPGWTGGV LQYINGYDGR AGGDARAGGE TGLPGFVARA RELAERYGER
FAPPALLVAK AEKGERFTDA G
//
