ID B9B3C4_9BURK Unreviewed; 710 AA.
AC B9B3C4;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Peroxisomal bifunctional enzyme (Pbe) (Pbfe) {ECO:0000313|EMBL:EEE00939.1};
DE EC=1.1.1.35 {ECO:0000313|EMBL:EEE00939.1};
DE EC=4.2.1.17 {ECO:0000313|EMBL:EEE00939.1};
DE EC=5.3.3.8 {ECO:0000313|EMBL:EEE00939.1};
GN ORFNames=BURMUCGD1_0334 {ECO:0000313|EMBL:EEE00939.1};
OS Burkholderia multivorans CGD1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=513051 {ECO:0000313|EMBL:EEE00939.1, ECO:0000313|Proteomes:UP000005493};
RN [1] {ECO:0000313|EMBL:EEE00939.1, ECO:0000313|Proteomes:UP000005493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGD1 {ECO:0000313|EMBL:EEE00939.1,
RC ECO:0000313|Proteomes:UP000005493};
RX PubMed=23105085; DOI=10.1128/JB.01306-12;
RA Varga J.J., Losada L., Zelazny A.M., Brinkac L., Harkins D., Radune D.,
RA Hostetler J., Sampaio E.P., Ronning C.M., Nierman W.C., Greenberg D.E.,
RA Holland S.M., Goldberg J.B.;
RT "Draft Genome Sequence Determination for Cystic Fibrosis and Chronic
RT Granulomatous Disease Burkholderia multivorans Isolates.";
RL J. Bacteriol. 194:6356-6357(2012).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EEE00939.1}.
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DR EMBL; ACFB01000003; EEE00939.1; -; Genomic_DNA.
DR RefSeq; WP_006398160.1; NZ_ACFB01000003.1.
DR AlphaFoldDB; B9B3C4; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000005493; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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; 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 Isomerase {ECO:0000313|EMBL:EEE00939.1};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lyase {ECO:0000313|EMBL:EEE00939.1}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000313|EMBL:EEE00939.1};
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; 75474 MW; 928D4E58D732484B CRC64;
MNSPAFSAPS NGTVTRERRD KVLVVTIDHP PVNALSADVR RGLADALDAA QADDAIRAVL
IVGAGRNFIA GADIREFGKP PVPPSLPDVC ARIESSAKPV VVALHGATLG GGLEVALAAH
YRLAVPGAKL GLPEVTLGLL PGAGGTQRAP RLIGAKAALD LMLTGRHASA EEALALGLVD
RLAHSDDTLA EGLAYAQELV SLGAPARRTR DAQALADRAA AQAAIDAARA ELPKKSRGLF
SPAKIVDAVE AALAQPFDAG MKLERSLFLQ CIDSPQRAGL VHAFFAEREA AKVPEARRGT
ARPIERIGVV GGGTMGAGIA IAALDAGLPV TMIERDEAAL ARGRAHVEKV YDALVAKGRM
TSAAQAARIA RLKGSTSYDA LAQVDVVIEA VFEDMAVKQA VFAELARVCK PGAVLATNTS
YLDIDALAAS IDRPADVIGL HFFSPANVMK LLEIVVPARA SADVVATAFA LARQLKKMPV
RAGVCDGFIG NRILAVYRTA ADYLMEDGAS PYQIDRAVRE FGFPMGPFQV VDLAGGDIGW
ATRKRRAATR DPRARYVEIS DRLCERGWFG QKTGRGYYLY PDGARVGTPD PEVEAIVEQE
RAKKGIVPRA FTDDEILRRY LAAMINEGAN VVHEKIALRP LDVDAVFLHG YGFPRYRGGP
MHHADTVGLA NVLADIRAFA EEDPLFWKPS PLLVELVERG ANFASLNRID
//
