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Database: UniProt
Entry: A0A494Z3R0_9BACI
LinkDB: A0A494Z3R0_9BACI
Original site: A0A494Z3R0_9BACI 
ID   A0A494Z3R0_9BACI        Unreviewed;       382 AA.
AC   A0A494Z3R0;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:RKQ16649.1};
GN   ORFNames=D8M05_07185 {ECO:0000313|EMBL:RKQ16649.1};
OS   Oceanobacillus bengalensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=1435466 {ECO:0000313|EMBL:RKQ16649.1, ECO:0000313|Proteomes:UP000281813};
RN   [1] {ECO:0000313|EMBL:RKQ16649.1, ECO:0000313|Proteomes:UP000281813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCCC 1K00260 {ECO:0000313|EMBL:RKQ16649.1,
RC   ECO:0000313|Proteomes:UP000281813};
RX   PubMed=26303283; DOI=10.1007/s10482-015-0573-5;
RA   Yongchang O., Xiang W., Wang G.;
RT   "Oceanobacillus bengalensis sp. nov., a bacterium isolated from seawater of
RT   the Bay of Bengal.";
RL   Antonie Van Leeuwenhoek 108:1189-1196(2015).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|RuleBase:RU362125};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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:RKQ16649.1}.
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DR   EMBL; RBZO01000008; RKQ16649.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A494Z3R0; -.
DR   OrthoDB; 9802447at2; -.
DR   Proteomes; UP000281813; Unassembled WGS sequence.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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, ECO:0000256|RuleBase:RU362125};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362125};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000281813}.
FT   DOMAIN          6..117
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          122..218
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          231..379
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   382 AA;  41251 MW;  B3AD62D5F8029449 CRC64;
     MTIAITDELQ QMKIMIKNFV DNEVDAYAQQ IEDEDALPEH LVEKAKELGL FGISIPEAYG
     GIGLDAVGKA IVLEQLGRTH NGFVSLISAH TGIGSTGIVK LASNYLKQKY LPDMAAGRKI
     AAFALSEPGA GSDATNLATV AEKQGESWVL NGTKHFITNA PVADVFTVFA VTDKEKGAKG
     GITAFLVERD FPGLIVGKKD KKMGLRGSST AQVIFENCIV PEENVIGEVG MGYMNALKIL
     GEGRVGLAAR AVGSCDKLIE ISASYAKERV QFGKPIASNQ AIQWMLADMA TETEAARTLT
     MMAAEKIDSG KKVIKEAAMA KLFASEVFNK VADKAVQIHG GIGYIGEYPV ERFYRDARIT
     KIYEGTNEIQ RLIIARRILD EN
//
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