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Database: UniProt
Entry: A0A0B4RE06_9BACL
LinkDB: A0A0B4RE06_9BACL
Original site: A0A0B4RE06_9BACL 
ID   A0A0B4RE06_9BACL        Unreviewed;       379 AA.
AC   A0A0B4RE06;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Acyl-CoA dehydrogenase domain-containing protein {ECO:0000313|EMBL:AIY06389.1};
GN   ORFNames=Plano_2424 {ECO:0000313|EMBL:AIY06389.1};
OS   Planococcus sp. PAMC 21323.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX   NCBI_TaxID=1526927 {ECO:0000313|EMBL:AIY06389.1, ECO:0000313|Proteomes:UP000031496};
RN   [1] {ECO:0000313|EMBL:AIY06389.1, ECO:0000313|Proteomes:UP000031496}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 21323 {ECO:0000313|EMBL:AIY06389.1,
RC   ECO:0000313|Proteomes:UP000031496};
RA   Jung J.-H., Joe M.-H., Cho Y.-J., Lee S.G., Han S.J., Lim S., Choi J.-i.;
RT   "Complete genome sequence of Planococcus sp. PAMC21323 isolated from the
RT   Antarctica.";
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP009129; AIY06389.1; -; Genomic_DNA.
DR   RefSeq; WP_038704737.1; NZ_CP009129.1.
DR   AlphaFoldDB; A0A0B4RE06; -.
DR   STRING; 1526927.Plano_2424; -.
DR   KEGG; pln:Plano_2424; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_0_2_9; -.
DR   OrthoDB; 9802447at2; -.
DR   Proteomes; UP000031496; Chromosome.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   CDD; cd01158; SCAD_SBCAD; 1.
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; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 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:UP000031496}.
FT   DOMAIN          6..117
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          122..217
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          229..376
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   379 AA;  41767 MW;  0093EC8B8E72A57C CRC64;
     MNFQLSEEHQ MIRKMVRDFA NKEVAPTAEE RDEEERFDRE IFDKMAELGL TGIPWPEEYG
     GIGSDYLAYC IAVEELSRVC ASTGVTLSAH TSLAGWPVYT FGTEEQKQKY LRPMAEGTKI
     GAYGLTEPSA GSDAGSMRTS AREDGDHYVL NGSKIFITNG GIADIYVVFA VTDPESKHKG
     TTAFIVEKDF EGFSVGKKER KLGIRSSPTT EIIFDNCRVP KENVLGELGQ GFKIAMQTLD
     GGRNGIAAQA VGIAQGALDA SIDYAKEREQ FGKPILVNQG VSFKLADMAT SIEASRLLTY
     QAAWLESNKL SYSKESAMAK LMAGDTAMKV TVEAVQVFGG YGYTKDYPVE RYMRDAKITQ
     IYEGTQEVQR LVISRMVTK
//
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