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Database: UniProt
Entry: A0A0C1UYY8_9ACTN
LinkDB: A0A0C1UYY8_9ACTN
Original site: A0A0C1UYY8_9ACTN 
ID   A0A0C1UYY8_9ACTN        Unreviewed;       314 AA.
AC   A0A0C1UYY8;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:KIE52730.1};
DE   Flags: Fragment;
GN   ORFNames=MB55_07485 {ECO:0000313|EMBL:KIE52730.1};
OS   marine actinobacterium MedAcidi-G3.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1550402 {ECO:0000313|EMBL:KIE52730.1, ECO:0000313|Proteomes:UP000031370};
RN   [1] {ECO:0000313|EMBL:KIE52730.1, ECO:0000313|Proteomes:UP000031370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mizuno C.M., Rodriguez-Valera F., Ghai R.;
RT   "Novel reconstructed genomes of marine planktonic Acidimicrobiales.";
RL   Submitted (SEP-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}.
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:KIE52730.1}.
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DR   EMBL; JUEP01000013; KIE52730.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C1UYY8; -.
DR   STRING; 1550402.MB55_07485; -.
DR   Proteomes; UP000031370; 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; ISOVALERYL-COA DEHYDROGENASE, 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   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|RuleBase:RU362125}.
FT   DOMAIN          1..50
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          55..148
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          161..309
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KIE52730.1"
SQ   SEQUENCE   314 AA;  33424 MW;  B3B85133702FDD1B CRC64;
     YAVAMEEISA VDGGISNMMS GSNSPVAAGI NAYGSLKQKE SVLPKLCSGE WMGSFHLTEP
     HTGSDASAIT TKAVRDGDEF VLDGHKAFIT GGQTSDVAMI VAITNPEAGK SGLSAFVTPT
     DNPGYQVIAR EAKLGHRTND LCQVRFDAMR VPESDLLGEE GRGLAIALSG LSVGRIAVAA
     QAVGGARQAL RLAKEYAELR DTFGKPIIEH QTIAFLLAEM ATKVEAARQM YLHAATLQDT
     GLDSAAAASM AKLFASEVAE WVASKAIQIH GGAGFLEDHL VEKIYRDVRV YQIYEGTSEI
     QKLVISRHLD ALEM
//
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