ID A0A0G9HJM2_9GAMM Unreviewed; 685 AA.
AC A0A0G9HJM2;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:APG06588.1};
GN ORFNames=BJI69_16115 {ECO:0000313|EMBL:APG06588.1}, Y883_05790
GN {ECO:0000313|EMBL:KLD67892.1};
OS Luteibacter rhizovicinus DSM 16549.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Luteibacter.
OX NCBI_TaxID=1440763 {ECO:0000313|EMBL:APG06588.1, ECO:0000313|Proteomes:UP000182987};
RN [1] {ECO:0000313|EMBL:KLD67892.1, ECO:0000313|Proteomes:UP000035585}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16549 {ECO:0000313|EMBL:KLD67892.1,
RC ECO:0000313|Proteomes:UP000035585};
RX PubMed=25481407; DOI=10.1007/s10482-014-0344-8;
RA Naushad S., Adeolu M., Wong S., Sohail M., Schellhorn H.E., Gupta R.S.;
RT "A phylogenomic and molecular marker based taxonomic framework for the
RT order Xanthomonadales: proposal to transfer the families Algiphilaceae and
RT Solimonadaceae to the order Nevskiales ord. nov. and to create a new family
RT within the order Xanthomonadales, the family Rhodanobacteraceae fam. nov.,
RT containing the genus Rhodanobacter and its closest relatives.";
RL Antonie Van Leeuwenhoek 107:467-485(2015).
RN [2] {ECO:0000313|EMBL:APG06588.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LJ96 {ECO:0000313|EMBL:APG06588.1};
RX PubMed=28123952;
RA Aamot H.U., Hofgaard I.S., Lysoe E.;
RT "Complete genome sequence of Luteibacter rhizovicinus strain LJ96T,
RT isolated from the rhizosphere of barley (Hordeum vulgare L.) in Denmark.";
RL Genom Data 11:104-105(2016).
RN [3] {ECO:0000313|Proteomes:UP000182987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LJ96T {ECO:0000313|Proteomes:UP000182987};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-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}.
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DR EMBL; CP017480; APG06588.1; -; Genomic_DNA.
DR EMBL; JPLB01000017; KLD67892.1; -; Genomic_DNA.
DR RefSeq; WP_046966835.1; NZ_JPLB01000017.1.
DR AlphaFoldDB; A0A0G9HJM2; -.
DR STRING; 1440763.BJI69_16115; -.
DR KEGG; lrz:BJI69_16115; -.
DR PATRIC; fig|1440763.5.peg.858; -.
DR OrthoDB; 5389341at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000035585; Unassembled WGS sequence.
DR Proteomes; UP000182987; 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; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
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"
SQ SEQUENCE 685 AA; 74179 MW; 25BEFC38C708EDAB CRC64;
MFEGLRFKHW KTNVGDDGIV VLTFDREGAS ANALSREALD ELDTIVERLA IENPRGVVIH
SAKPSGFAVG ADIREFVEYA QTGTVLANIE NGQRVFENLA RLSCPTVAAI HGACMGGGTE
LALACRQRIA VDDDATKIGL PEVMLGIHPG WGGTARLPRL IGAPDALPAM LTGKPFNARR
AKAVGLVDRL ARADELLAEA RHLIKRPHQR PFAQRAKAWA TNTLPARAIL APMVRKQTAA
KVRKEHYPAP FALIDTWARG GSSIQQRLKL EAKSVAKLAT TPTARNLIRI FFLQERLKGL
GGGTDHGIKH VHVVGAGTMG GDIAAWSALK GFDVTLQDRE LRFIEPAIKR ARTLFEKKLK
ASAKVDAAVG RLRADVDGKG VAEADLAIEA IFENPEAKHA LYAAIEPQFQ ADEILASNTS
SIPLDELRQG LKAPQRFLGL HFFNPVAQMP LVEVVRHDAL DPAIEKRALA FCKAIGKLPV
PVKGTPGFLV NRILMPYLME AMRLYNEGVP GPVLDREAKK FGMPMGPIEL ADTVGLDVCA
SVGKELAPFL GLEIPHGLEE KIAANKRGKK DGEGLYVWKE GKADKPDVDP DYVPPADIQD
RMILPMVNEA IACLAEGVVD DADLLDAGVI FGTGFAPFRG GPIQYVRTEG VAAVRERLAK
LEAKHGVRFA KKEGWDNPEL TLSPA
//
