ID A0A410ULD0_9GAMM Unreviewed; 691 AA.
AC A0A410ULD0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:QAU25060.1};
GN ORFNames=EO087_14565 {ECO:0000313|EMBL:QAU25060.1};
OS Dyella sp. M7H15-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=2501295 {ECO:0000313|EMBL:QAU25060.1, ECO:0000313|Proteomes:UP000288967};
RN [1] {ECO:0000313|EMBL:QAU25060.1, ECO:0000313|Proteomes:UP000288967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M7H15-1 {ECO:0000313|EMBL:QAU25060.1,
RC ECO:0000313|Proteomes:UP000288967};
RA Gao Z.-H., Qiu L.-H., Yang Z.;
RT "Dyella phosphatilytica sp. nov. strain M7H15-1T., a phosphate solubilizing
RT bacterium isolated from forest soil and analysis of the complete genome
RT sequence.";
RL Submitted (JAN-2019) 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}.
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DR EMBL; CP035300; QAU25060.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A410ULD0; -.
DR KEGG; dye:EO087_14565; -.
DR OrthoDB; 5389341at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000288967; Chromosome.
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; 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; IPR013328; 6PGD_dom2.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000288967}.
FT DOMAIN 310..483
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 487..578
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT REGION 561..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 691 AA; 75620 MW; 600E3DCA06EB0CE3 CRC64;
MFEGLRFNHW KTSLDDDGIV TLTLDRANSS VNAISREVLD ELGQIVERLT IEKPTGVIIH
SAKSNGFAVG ADIKQFVEYA KHGTVQENIE NGQRVFESLA RLPCPTVAAV HGACMGGGTE
LILACRQRIA TDDDKTRIGL PEVMLGIHPG WGGSARLPRL IGAPEALAIM LTGKALSARR
AKSLGVIDRL ARPEELLAEA RSLLRHPHAR PLTQRATAWA TNSWLVRQIL APMVIKQTAT
KVRKEHYPAP FSLIDVWKRG GSDIQQRLKL EARSVAKLAN TSTAHNLIRI FFLQERLKSQ
GSGVDANIKH VHVVGAGVMG GDIAAWAAFK GFEVTLQDRE MKLIQPALDR ARTLYEKKLK
IPDKVEAASR RLRPDVEGAG VAKADLAIEA IFENAQAKEA LYATIEPQFQ NNEMLVSNTS
SIPLDALRKG LKAPQRFLGL HFFNPVAQMP LVEVVRHDQL DPAVEKRALA FCKAIDKLPV
AVKGTPGFLV NRILMPYLLE ALRLYNEGVP GPVLDKQAKS FGMPMGPIEL ADTVGLDVCA
SVGQELAPFL ELELPPGLED KLEAGKRGKK DGQGLYTWQD GKPQKPEVDP DYTPPPDLQE
RMILAMVNEA VACLGDGVVD DADLLDAGVI FGTGFAPFRG GPIQYVRSEG VENIRQKLES
LAKRYGERFT PKNGWDHPAL KQSTVELSVG H
//
