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Database: UniProt
Entry: Q63X89_BURPS
LinkDB: Q63X89_BURPS
Original site: Q63X89_BURPS 
ID   Q63X89_BURPS            Unreviewed;       595 AA.
AC   Q63X89;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   SubName: Full=Acyl-CoA dehydrogenase oxidoreductase protein {ECO:0000313|EMBL:CAH34641.1};
GN   OrderedLocusNames=BPSL0648 {ECO:0000313|EMBL:CAH34641.1};
OS   Burkholderia pseudomallei (strain K96243).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=272560 {ECO:0000313|EMBL:CAH34641.1, ECO:0000313|Proteomes:UP000000605};
RN   [1] {ECO:0000313|EMBL:CAH34641.1, ECO:0000313|Proteomes:UP000000605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243 {ECO:0000313|EMBL:CAH34641.1,
RC   ECO:0000313|Proteomes:UP000000605};
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.M., Atkins T.,
RA   Crossman L.C., Pitt T., Churcher C., Mungall K., Bentley S.D., Sebaihia M.,
RA   Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F.,
RA   Challis G.L., Cherevach I., Chillingworth T., Cronin A., Crosset B.,
RA   Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H.,
RA   Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C.,
RA   Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M.,
RA   Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S.,
RA   Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT   pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347}.
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DR   EMBL; BX571965; CAH34641.1; -; Genomic_DNA.
DR   RefSeq; WP_004526128.1; NZ_CP009538.1.
DR   RefSeq; YP_107277.1; NC_006350.1.
DR   AlphaFoldDB; Q63X89; -.
DR   STRING; 272560.BPSL0648; -.
DR   GeneID; 56527141; -.
DR   KEGG; bps:BPSL0648; -.
DR   PATRIC; fig|272560.51.peg.974; -.
DR   eggNOG; COG1960; Bacteria.
DR   Proteomes; UP000000605; Chromosome 1.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR   Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR   InterPro; IPR025878; Acyl-CoA_dh-like_C_dom.
DR   InterPro; IPR020953; Acyl-CoA_DH_N_bac.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   PANTHER; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR42803:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF12806; Acyl-CoA_dh_C; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   Pfam; PF12418; AcylCoA_DH_N; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000605}.
FT   DOMAIN          3..35
FT                   /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT                   /evidence="ECO:0000259|Pfam:PF12418"
FT   DOMAIN          44..159
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          164..273
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          283..451
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          471..591
FT                   /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12806"
SQ   SEQUENCE   595 AA;  65064 MW;  B28305D3540F920C CRC64;
     MGQYAAPLRD MQFVLHELLN VEAEVKQMPK HADLDADTIN QVLEEAGKFC SEVLFPLNQV
     GDREGCTYVG DGVVKTPTGF KEAYQQYIDA GWPALGCDPD YGGQGLPAFV NNALYEMLNS
     ANQAWTMYPG LSHGAYECLH AHGAPELQKL YLPKLVSGEW TGTMCLTEPH CGTDLGILRT
     KAEPNGDGTY SISGTKIFIS SGEHDFSKNI VHLVLARLPD APKGTKGISL FIVPKFVPDA
     SGEPGERNGV KCGSIEHKMG IHGNATCVMN LDNAKGWLIG EPNKGLNAMF VMMNAARLGV
     GMQGLGLTEV AYQNSLTYAK ERLQMRSLTG PKAPDKPADP IIVHPDVRRM LLTQKAYAEG
     ARAFTYWSAL QIDKALSHAD EAVRKEAEDL VALLTPIIKA FLTDNAFECT NHAMQIYGGH
     GFISEWGMEQ YVRDARINMI YEGTNSVQAL DLLGRKVLGD MGAKLKKFGK IVAEFAEAEG
     VKPEMSEFIT PLADIGEKVQ KLTMEIGMKA MQNPDEVGAA AVPYLRTVGH LVFSYFWARM
     ARIALDNEAS GDPFYKSKLA TARFYFARLL PETAASIRLA RAGAKSMMDV DEALF
//
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