ID A0A0Q7K486_9ACTN Unreviewed; 700 AA.
AC A0A0Q7K486;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:KQX66905.1};
GN ORFNames=ASD06_05525 {ECO:0000313|EMBL:KQX66905.1};
OS Angustibacter sp. Root456.
OC Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae.
OX NCBI_TaxID=1736539 {ECO:0000313|EMBL:KQX66905.1, ECO:0000313|Proteomes:UP000051170};
RN [1] {ECO:0000313|EMBL:KQX66905.1, ECO:0000313|Proteomes:UP000051170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root456 {ECO:0000313|EMBL:KQX66905.1,
RC ECO:0000313|Proteomes:UP000051170};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQX66905.1, ECO:0000313|Proteomes:UP000051170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root456 {ECO:0000313|EMBL:KQX66905.1,
RC ECO:0000313|Proteomes:UP000051170};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQX66905.1}.
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DR EMBL; LMER01000014; KQX66905.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q7K486; -.
DR STRING; 1736539.ASD06_05525; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000051170; 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:UP000051170}.
FT DOMAIN 331..510
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 514..595
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 700 AA; 74204 MW; 8D38CE4972D81813 CRC64;
MAAATSDERV TSFHVRDVAL PGGAGTMALI TMDNGFDHTK PTTLGAQGLL NLKAALDAVS
PRAASGEIVA VGITGKPFIF AVGADLKDVG NLSTREQALT IARFGHDQLR RLGELAVPSF
GFVNGAAMGG GVEVALHCTY RTISSGVPAV ALPETFLGLV PGWGGNYLLP NLIGVANALK
VIIENPLSQN RMLKGPQAFQ LGLADAMFEP ADFLEQSLQW AAAVVRGEIV VQRPEVDRDE
ATWAAAVKTA QGFAHMKTGG AAPAPYRALD IVTAARTCSR DEGFALEDAA LADLIMSEEF
RSGVYSFNLV QGRAKRPAGA PDKSLARKVT KVGIVGAGLM ASQLALLFAQ RLEVPVVLTD
LDQGRVDKGV GYVHGEVDKL LGKGRVNPDK ANRLKSLVTG STSKDGFADA DFVIEAVFEQ
MSVKQQVFAE VEAIVSPECV LATNTSSLSI TEMASQLQHP ERVVGFHFFN PVAVMPLLEI
VKGEQTDDAT LATAFATGKT LRKTTILVKD SPSFIVNRLL GRFMGEVSRV VDEGTPVEVA
DGAFAGLAPM PPFVLLALVG PAIALHNSET LARAFPDRFY VSQNLRRVVE AGKPGFYVWD
GPKPSLDPEV AALFETPAEP VVLDREQVRE KVLSALADEA RRMLDEGVVA APEDLDLAMI
TGAGFSFWNG GLTPLLDRTG VAERTSGKRF LTPGVASLPA
//
