ID A2W757_9BURK Unreviewed; 710 AA.
AC A2W757; A0A0D5J672;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000313|EMBL:EAY67803.1};
GN ORFNames=BDAG_00495 {ECO:0000313|EMBL:EAY67803.1};
OS Burkholderia dolosa AU0158.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=350701 {ECO:0000313|EMBL:EAY67803.1, ECO:0000313|Proteomes:UP000053482};
RN [1] {ECO:0000313|Proteomes:UP000053482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU0158 {ECO:0000313|Proteomes:UP000053482};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L.,
RA Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E., Brockman W., Rounsley S., Young S., LaButti K., Pushparaj V.,
RA DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P.,
RA Pearson M., Howarth C., Kodira C., Zeng Q., Yandava C., Oleary S.,
RA Alvarado L., Lory S., LiPuma J.;
RT "The Genome Sequence of Burkholderia dolosa (strain AU0158).";
RL Submitted (DEC-2005) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH482380; EAY67803.1; -; Genomic_DNA.
DR RefSeq; WP_006763298.1; NZ_CP009795.1.
DR AlphaFoldDB; A2W757; -.
DR GeneID; 64460025; -.
DR PATRIC; fig|350701.8.peg.259; -.
DR HOGENOM; CLU_009834_16_3_4; -.
DR OrthoDB; 5287258at2; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000053482; Unassembled WGS sequence.
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 307..482
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 487..580
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT DOMAIN 616..700
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
SQ SEQUENCE 710 AA; 75756 MW; 86F866E95C1A0EF2 CRC64;
MHSPASPAPE AGTVTRERRG DVLVVTIDHP PVNALSADVR RGLADALDAA QADDAIRAVL
VVGAGRNFIA GADIREFGKP PVPPSLPDVC ERIESSAKPV VVALHGATLG GGLEVALAAH
YRLALPGAKL GLPEVTLGLL PGAGGTQRTP RLIGAKAALD LMLTGRHASA DEALALGLVD
RIAQSDDTLA EGLAYAHELV SLDAPPRRTR DADGLSDRAA AQAAIDAARA ELPKKSRGLF
SPAKIVDAIE AALTQPFDAG MKLERSLFLQ CVDSPQRAGL VHAFFAEREA AKVPEARRAS
ARPVERIGVV GGGTMGAGIA VAALDAGLPV TMIERDEASL ARGRAHVEKV YDGLVAKGRM
TPAARAARLE RLTGSTSYDA LAQADVVIEA VFEDMTVKKA VFAELARVCK PRAMLATNTS
YLDIDELAAS IDRPADVIGL HFFSPAHVMK LLEIVVPARV DAEVVATAFA LAKQLKKTPV
RAGVCDGFIG NRILAVYRTA ADYLMEDGAS PYQIDRAVRE FGFPMGPFQV VDLAGGDIGW
AARKRRAATR DPRARYVEIS DRLCERGWFG QKTGRGYYLY PDGARVGTPD PDVDAIVAHE
RAKKGIVPRT FTDDEILRRY LAAMINEGAN VVHEKIALRP LDVDAVFLHG YGFPRYRGGP
MHYADTVGLA NVLADIRAFA DEDPLFWKPS PLLVELVERG ANFASLNRID
//
