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Database: UniProt
Entry: H5WPW0_9BURK
LinkDB: H5WPW0_9BURK
Original site: H5WPW0_9BURK 
ID   H5WPW0_9BURK            Unreviewed;       393 AA.
AC   H5WPW0;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:EHR72658.1};
GN   ORFNames=BurJ1DRAFT_3855 {ECO:0000313|EMBL:EHR72658.1};
OS   Burkholderiales bacterium JOSHI_001.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX   NCBI_TaxID=864051 {ECO:0000313|EMBL:EHR72658.1, ECO:0000313|Proteomes:UP000004674};
RN   [1] {ECO:0000313|EMBL:EHR72658.1, ECO:0000313|Proteomes:UP000004674}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JOSHI_001 {ECO:0000313|EMBL:EHR72658.1,
RC   ECO:0000313|Proteomes:UP000004674};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Zeytun A., Lu M., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Smith J., Lewis G.,
RA   Woyke T.;
RT   "Noncontiguous Finished sequence of Burkholderiales bacterium JOSHI_001.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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; CM001438; EHR72658.1; -; Genomic_DNA.
DR   AlphaFoldDB; H5WPW0; -.
DR   STRING; 864051.BurJ1DRAFT_3855; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_9_0_4; -.
DR   OrthoDB; 9770681at2; -.
DR   BioCyc; BBAC864051:G1H30-3841-MONOMER; -.
DR   Proteomes; UP000004674; Chromosome.
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; 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; PTHR43292; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43292:SF3; ACYL-COA DEHYDROGENASE FADE29; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_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:UP000004674}.
FT   DOMAIN          6..121
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          127..219
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          231..390
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   393 AA;  43780 MW;  2A9AD835CA31C4E7 CRC64;
     MDLNFTDEEI AFRAEIRQWV AQNLPKDISQ KVLSALRLSR DDMQRWAKIL GAKGWLGYGW
     PTQFGGPGWN SVQKHIFEEE CAIAGSPRIV PFGPVMVAPV IMAFGNAEQH KRFLPGIASG
     EVWWSQGYSE PGSGSDLASL KTRAERQGNS YIVNGQKTWT TLGQYGDWIF CLVRTSTDGK
     PQTGISFLLI DMKSKGITVR PIITMDGEHE VNEVFFDNVE VPAENLIGEE NKGWTYAKHL
     LSHERTNIAD VNRAKRELER VKRIAKAEGQ WDDQRFRDQI ALLEVDIVAL EMMVLRVLAA
     EKGGKQSLDV AGLLKIRGSE IQQRYTELMM LAAGPFTRPF VHEAMEAGWQ GDFAGAAAVA
     PLATTYFNMR KTTIYGGSNE VQRNIVAATV LGS
//
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