ID   A0A1H8IN24_9ACTN        Unreviewed;       601 AA.
AC   A0A1H8IN24;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Acyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SAMN05660976_08088 {ECO:0000313|EMBL:SEN69779.1};
OS   Nonomuraea pusilla.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Nonomuraea.
OX   NCBI_TaxID=46177 {ECO:0000313|EMBL:SEN69779.1, ECO:0000313|Proteomes:UP000198953};
RN   [1] {ECO:0000313|EMBL:SEN69779.1, ECO:0000313|Proteomes:UP000198953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43357 {ECO:0000313|EMBL:SEN69779.1,
RC   ECO:0000313|Proteomes:UP000198953};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOBF01000033; SEN69779.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8IN24; -.
DR   STRING; 46177.SAMN05660976_08088; -.
DR   OrthoDB; 2769798at2; -.
DR   Proteomes; UP000198953; 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   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; 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; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
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:UP000198953}.
FT   DOMAIN          3..34
FT                   /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT                   /evidence="ECO:0000259|Pfam:PF12418"
FT   DOMAIN          162..271
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          286..448
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          467..597
FT                   /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12806"
SQ   SEQUENCE   601 AA;  65609 MW;  95E1FA6C5F1E0B69 CRC64;
     MGHYKSNMRD LEFNLFEVFG RREILGTGPF ADVDEDVARS ILDEVNRLAT GVLADSFEEG
     DRKPPVFDPK TSTVKIPEGF KKSFKALVDG GWAHLDLPAD LGGPGIPRSL AWATAEMVLG
     ANPALYMYAA GPNFAYTLWK LGTDEQKRFA ELAIERNWGA TMVLTEPDAG SDVGAGRTRA
     VRQADGSWHI EGVKRFITSA EHDMAENIFH LVLARPEGHG AGTKGLSMFL VPKFHVDLET
     GELGERNGVY VTNVEKKMGL KVSTTCELTF GDKHPAVGWL VGEVHEGIKQ MFMVIEHARM
     MVGTKAIATL STGYLNALEY AKARVQGADL TQMTDKSAPR VTITHHPDVR RELMLQKTYA
     EGMRALVLYT ATFQDAIQID PDDRHAQAMN DLLLPLVKGV GSERSYELLS RSLQTLGGSG
     YLQDYPIEQY IRDAKIDSLY EGTTAIQGLD LFFRKILRNQ GAAIGALLAE IGAFASSEAG
     NGRLKEERKL LADAAADVKA MGDTMAGWAI SSLESPREVY KVGLNTTRLL LALGDLVIGW
     LLLRQAEVAL AALAGGEDPF YQGKVAAASF FATNVLPRLA AERRVLEGTG LELMDLPEEA
     F
//