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Database: UniProt
Entry: F2LDS5_BURGS
LinkDB: F2LDS5_BURGS
Original site: F2LDS5_BURGS 
ID   F2LDS5_BURGS            Unreviewed;       694 AA.
AC   F2LDS5;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase, NAD-binding protein {ECO:0000313|EMBL:AEA61000.1};
GN   OrderedLocusNames=bgla_1g23730 {ECO:0000313|EMBL:AEA61000.1};
OS   Burkholderia gladioli (strain BSR3).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=999541 {ECO:0000313|EMBL:AEA61000.1, ECO:0000313|Proteomes:UP000008316};
RN   [1] {ECO:0000313|EMBL:AEA61000.1, ECO:0000313|Proteomes:UP000008316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSR3 {ECO:0000313|EMBL:AEA61000.1,
RC   ECO:0000313|Proteomes:UP000008316};
RX   PubMed=21478339; DOI=10.1128/JB.00420-11;
RA   Seo Y.S., Lim J., Choi B.S., Kim H., Goo E., Lee B., Lim J.S., Choi I.Y.,
RA   Moon J.S., Kim J., Hwang I.;
RT   "Complete genome sequence of Burkholderia gladioli BSR3.";
RL   J. Bacteriol. 193:3149-3149(2011).
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}.
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DR   EMBL; CP002599; AEA61000.1; -; Genomic_DNA.
DR   RefSeq; WP_013698328.1; NC_015381.1.
DR   AlphaFoldDB; F2LDS5; -.
DR   STRING; 999541.bgla_1g23730; -.
DR   KEGG; bgd:bgla_1g23730; -.
DR   eggNOG; COG1024; Bacteria.
DR   eggNOG; COG1250; Bacteria.
DR   HOGENOM; CLU_009834_16_3_4; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000008316; Chromosome 1.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-KW.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
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; PTHR23309; 3-HYDROXYACYL-COA DEHYROGENASE; 1.
DR   PANTHER; PTHR23309:SF9; PEROXISOMAL BIFUNCTIONAL ENZYME; 1.
DR   Pfam; PF00725; 3HCDH; 2.
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   4: Predicted;
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140}.
FT   DOMAIN          295..471
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          476..568
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   DOMAIN          604..690
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
SQ   SEQUENCE   694 AA;  74515 MW;  E1D554673F80811A CRC64;
     MAVDYTTRDG VAVITLNNPP VNGLGYSTRV GVMDGLDRAL QDPAVTAIVL TGAGRAFSGG
     ADITEFNTPK ALQEPSLHTL IAAVEASAKP VVAAVHSVVM GGGLELALGA HYRIAAPGTQ
     VALPEVKIGL LPGAGGTQRL PRALGLETAL NMIVSGAAVP SEQLAKSGLF DEMAEGDLLE
     AAVALARRVG AKPGPHPRVR DRKIEHPNAA GFIQFARNSA RAAAPQYPAP HKCIDAIEAG
     VLKGFDQGLI DEREGFVALV QTPESRALRH AFFGERAASK IPDVPADTPV REIRKLGVIG
     AGTMGGGITI NFLNAGLPVT LLETKQEALE RGLATIRKNY EVQVKKGKLS EEKLEARMAL
     ISPTLSYEDL KDADLIIEAV FEELGVKEQV FRKLDEVAKP GAILASNTST LDVNKIAAFT
     RRPQDVVGMH FFSPANVMKL LEVVRGEHTA KDVLATVMQL AKKIRKTAVV SGVCDGFIGN
     RMVEQYIRQA LFMLEEGALP AQVDRAIEAF GFAMGPFRMS DLAGNDIGWA IRKRRYLEQP
     ELHYSKIADR LCELGRFGQK TGGGWYDYQA GERRAKPSKL VDEMVLAYSK EAGVERRKIA
     DEEIVERLVY ALVNEGAKIL EEGIASKASD IDMVYLTGYG FPLWRGGPML YADTVGLYNV
     ERAMRRYAAG ANGDAWQPAP SIAKLAAAGK GFNG
//
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