ID A0A0S3EZM5_9SPHN Unreviewed; 725 AA.
AC A0A0S3EZM5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:ALR20863.1};
GN ORFNames=ATN00_11705 {ECO:0000313|EMBL:ALR20863.1};
OS Sphingobium baderi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1332080 {ECO:0000313|EMBL:ALR20863.1, ECO:0000313|Proteomes:UP000056968};
RN [1] {ECO:0000313|EMBL:ALR20863.1, ECO:0000313|Proteomes:UP000056968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DE-13 {ECO:0000313|EMBL:ALR20863.1,
RC ECO:0000313|Proteomes:UP000056968};
RA Cheng M., Meng Q., Yang Y., Chu C., Yan X., He J., Li S.;
RT "A Two-component Flavoprotein Monooxygenase System MeaXY Responsible for
RT para-Hydroxylation of 2-Methyl-6-ethylaniline and 2,6-Diethylaniline in
RT Sphingobium baderi DE-13.";
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}.
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DR EMBL; CP013264; ALR20863.1; -; Genomic_DNA.
DR RefSeq; WP_062064781.1; NZ_CP013264.1.
DR AlphaFoldDB; A0A0S3EZM5; -.
DR STRING; 1332080.ATN00_11705; -.
DR KEGG; sbd:ATN00_11705; -.
DR OrthoDB; 9771883at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000056968; 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 Reference proteome {ECO:0000313|Proteomes:UP000056968}.
FT DOMAIN 325..501
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 504..600
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 725 AA; 77153 MW; ECB96DFB9C8C2DD4 CRC64;
MSTIAFDIDG DGIATLTIDV PGQSMNVIGP DFITDLDAAI TRIASEEAIK GAVIASGKDS
GFMAGMDLKF LGAMLASAEG ERPAPADIFD KVFVLNQLFR RLETCGKPVA CAIEGTCVGG
GLELAMACHR RVVGDSPKTQ LGLPEILIGL FPGGGGSQRM TRLMGVQAAL MYMLQGKLFR
PAEAAMLKVV DEVVPQGTAL DTAKAWVKAN PTASVQPWDV KGFKIPGGAG GFNPAFVQTM
AGAVPMTLKQ TQRNMNAPIA LLSAVYEGAI LPIDQAIRIE SKYFAKVAAD PQASNMIRSL
FVNKQAAERG ARRPKDQPKA PTRKLAMLGA GMMGAGIATV AAQAGMEVVL FDRDLAYAEK
GKAHVEEQLS KRLGKGMTPE KMAETLARVT PTTDYAALAG ADFVIEAVFE DVAIKAEVTK
KVEEVLGADT IFGSNTSTLP ITKLAKAWSK PANFIGIHFF SPVEKMPLVE IILGRETGPA
AIAKALDFVA QIKKTPIVVN DSRGFYTSRC FGTYVQEGVE MVAEGVNPAL IENGGRQLGM
PVGPLAVGDE VSIELGNKIV LAAKKELGDA YVPQRSDELM AQMVELGRLG RKSAKGWYDY
PEGGKKHLWP GLADLFPLAA DQPDVEAVKE RLLYRQLIEC ARCFEEGVLE TPEDGDIGAI
FGWGFAPWTG GPFSHMDTVG IAHVVAVLDR LAAAHGERFA PTKQLREMAA SGATFYRPAP
SRAAA
//
