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Database: UniProt
Entry: A0A221R5I5_9MICC
LinkDB: A0A221R5I5_9MICC
Original site: A0A221R5I5_9MICC 
ID   A0A221R5I5_9MICC        Unreviewed;       391 AA.
AC   A0A221R5I5;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ASN51590.1};
GN   ORFNames=CGQ25_05505 {ECO:0000313|EMBL:ASN51590.1};
OS   Sinomonas sp. R1AF57.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Sinomonas.
OX   NCBI_TaxID=2020377 {ECO:0000313|EMBL:ASN51590.1, ECO:0000313|Proteomes:UP000199767};
RN   [1] {ECO:0000313|EMBL:ASN51590.1, ECO:0000313|Proteomes:UP000199767}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R1AF57 {ECO:0000313|EMBL:ASN51590.1,
RC   ECO:0000313|Proteomes:UP000199767};
RA   Sastre D.E., Santos L., Kagohara E., Andrade L.H.;
RT   "Draft Genome Sequence of Sinomonas sp., Isolated from Brazilian Amazon
RT   Soils with Potential for Applications in Biocatalysis.";
RL   Submitted (JUL-2017) 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; CP022463; ASN51590.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A221R5I5; -.
DR   Proteomes; UP000199767; 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   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; 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:UP000199767}.
FT   DOMAIN          7..119
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          123..229
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          241..389
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   REGION          128..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   391 AA;  41953 MW;  D2ACFB9791C3E0CE CRC64;
     MVDFQLSDEY KELSDTVREF ADEVVAPVAG KHDEEHSFPY EVIAQMGELG LFGLPFPEEY
     GGMGGDFFAL ALALEQLGRV DQSVAITLEA GVSLGAMPIY KWGTEEQKQT WLPDLAAGKK
     LAGFGLTEPE AGSDAGGTKT TARLEDGPGG KQWVLNGSKE FITNSGTDIT SFVTVSAVTG
     TGQRDDGSPR KEISTIIVPS GTPGFRAEKA YNKVGWNASD THPLSFKDVR VPEENLLGER
     GRGYANFLTA LDEGRIAIAA LGTGAAQGCV DLSVKYAKER SAFGHHIGTY QAIQFKIARM
     QARAHTARLA YYDAAARMLA GKPFKTHAAI AKMVAGEAAM DNARDATQVF GGYGFINESA
     VARHYRDSKI LEIGEGTTEV QLMLIARELG L
//
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