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Database: UniProt
Entry: A0A0S1Y0J7_9BORD
LinkDB: A0A0S1Y0J7_9BORD
Original site: A0A0S1Y0J7_9BORD 
ID   A0A0S1Y0J7_9BORD        Unreviewed;       386 AA.
AC   A0A0S1Y0J7;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ALM83446.1};
GN   ORFNames=ASB57_11135 {ECO:0000313|EMBL:ALM83446.1};
OS   Bordetella sp. N.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1746199 {ECO:0000313|EMBL:ALM83446.1, ECO:0000313|Proteomes:UP000064621};
RN   [1] {ECO:0000313|EMBL:ALM83446.1, ECO:0000313|Proteomes:UP000064621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N {ECO:0000313|EMBL:ALM83446.1,
RC   ECO:0000313|Proteomes:UP000064621};
RA   Hou L.;
RT   "Draft genome of Bordetella sp. N.";
RL   Submitted (NOV-2015) 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; CP013111; ALM83446.1; -; Genomic_DNA.
DR   RefSeq; WP_057652292.1; NZ_CP013111.1.
DR   AlphaFoldDB; A0A0S1Y0J7; -.
DR   STRING; 1746199.ASB57_11135; -.
DR   OrthoDB; 9769473at2; -.
DR   Proteomes; UP000064621; Chromosome.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; 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; IPR006089; Acyl-CoA_DH_CS.
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; PTHR43884; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR43884:SF12; COMPLEX I ASSEMBLY FACTOR ACAD9, MITOCHONDRIAL-RELATED; 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   PIRSF; PIRSF016578; HsaA; 2.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 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:UP000064621}.
FT   DOMAIN          7..115
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          120..218
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          231..364
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   386 AA;  42721 MW;  388D01EB07CE4E19 CRC64;
     MSDASNDFQD IREAVRDLCA QFPAEYFRKI DAAQGYPEAF VDALTKAGWL AALIPQEYGG
     SGLGLTEASV IMEEINRAGG NSGACHGQMY NMGTLLRHGS EAQKQRYLPR IASGELRLQS
     MAVTEPTTGT DTTKLKTTAV KKGDRYVVNG QKVWISRVQH SDLMILLART TPIEQVQRKS
     EGMSIFLVDL HQAIGHGMEV RPIPNMVNHE TNELFFDNLE IPAENLIGEE GKGFKYILDG
     LNAERTLIAA ECIGDGYWFV DKVSAYVKER VVFGRPIGQN QGVQFPIARS FINVEAASLM
     RYEAARRFDA GLPCGTQANM AKLLAADASW EAANACLQFH GGFGFAHEYD VERKFRETRL
     YQVAPISTNL ILSYVAEHVL GLPRSF
//
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