ID   A0A1X7G1F6_9ACTN        Unreviewed;       608 AA.
AC   A0A1X7G1F6;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:SMF62310.1};
GN   ORFNames=SAMN02745830_04802 {ECO:0000313|EMBL:SMF62310.1};
OS   Streptomyces sp. Amel2xC10.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1305826 {ECO:0000313|EMBL:SMF62310.1, ECO:0000313|Proteomes:UP000192930};
RN   [1] {ECO:0000313|EMBL:SMF62310.1, ECO:0000313|Proteomes:UP000192930}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Amel2xC10 {ECO:0000313|EMBL:SMF62310.1,
RC   ECO:0000313|Proteomes:UP000192930};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-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; FWZW01000011; SMF62310.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7G1F6; -.
DR   OrthoDB; 9807883at2; -.
DR   Proteomes; UP000192930; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR   CDD; cd01153; ACAD_fadE5; 1.
DR   Gene3D; 2.40.110.20; -; 1.
DR   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR   InterPro; IPR025878; Acyl-CoA_dh-like_C_dom.
DR   InterPro; IPR020953; Acyl-CoA_DH_N_bac.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   InterPro; IPR034188; FadE5-like.
DR   PANTHER; PTHR42803; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR42803:SF1; BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF12806; Acyl-CoA_dh_C; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF12418; AcylCoA_DH_N; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 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:UP000192930}.
FT   DOMAIN          3..34
FT                   /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT                   /evidence="ECO:0000259|Pfam:PF12418"
FT   DOMAIN          162..272
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          286..452
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          471..604
FT                   /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12806"
SQ   SEQUENCE   608 AA;  66152 MW;  4966A076235F1DB3 CRC64;
     MGHYKPNLRD IEFNLFEVLG RDKLYGSGPF EEMDTETAKS ILEELTRLAE NELAESFIDA
     DRNPPVFDPV TNTAPVPASF KKSYQAFMDS EYWRLGLPEG IGGTTAPPSL IWAYAELILG
     ANPAVWMYSS GPAFAGILYD EGNDVQKKIA QVAVEKQWGS TMVLTEPDAG SDVGAGRTKA
     VPQEDGSWHI EGVKRFITSG EHDMSENILH YVLARPEGAG PGTKGLSLFL VPKFLFDFET
     GELGERNGVY ATNVEHKMGL KASNTCEMTF GDQHPAKGWL IGDKHDGIRQ MFRIIEFARM
     MVGTKAISTL STGYLNALEY AKERVQGPDL ANFMDKAAPK VTITHHPDVR RSLMTQKAYA
     EGMRALVLYT ASVQDTIAVK EAAGEDTKAD HALNDLLLPI VKGYGSEKGY EQLAQSLQTF
     GGSGFLQEYP IEQYIRDAKI DTLYEGTTAI QGQDFFFRKI VRNQGAALNT LAEDIKKFLA
     LGTGGEDLAG AREHLAKAAV ELEAIVGLML TDLAATEQDV KNIYKVGLNS TRLLLASGDV
     VVGYLLLKGA AVAAEKLETA SAKDKAFYTG KIAAAKFFAA NVLPGVTLAR KIAAGVELDL
     MELDEAAF
//