ID   A0A1I3YXY4_9ACTN        Unreviewed;       598 AA.
AC   A0A1I3YXY4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Butyryl-CoA dehydrogenase {ECO:0000313|EMBL:SFK36727.1};
GN   ORFNames=SAMN04488085_101253 {ECO:0000313|EMBL:SFK36727.1};
OS   Geodermatophilus ruber.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Geodermatophilus.
OX   NCBI_TaxID=504800 {ECO:0000313|EMBL:SFK36727.1, ECO:0000313|Proteomes:UP000199152};
RN   [1] {ECO:0000313|EMBL:SFK36727.1, ECO:0000313|Proteomes:UP000199152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45317 {ECO:0000313|EMBL:SFK36727.1,
RC   ECO:0000313|Proteomes:UP000199152};
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; FOSW01000001; SFK36727.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I3YXY4; -.
DR   STRING; 504800.SAMN04488085_101253; -.
DR   InParanoid; A0A1I3YXY4; -.
DR   OrthoDB; 9807883at2; -.
DR   Proteomes; UP000199152; 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; IPR013786; AcylCoA_DH/ox_N.
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:SF3; ACYL-COA DEHYDROGENASE-RELATED; 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; PF02771; Acyl-CoA_dh_N; 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|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199152}.
FT   DOMAIN          7..36
FT                   /note="Acyl-CoA dehydrogenase N-terminal bacteria"
FT                   /evidence="ECO:0000259|Pfam:PF12418"
FT   DOMAIN          41..158
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          164..267
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          294..460
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          478..594
FT                   /note="Acetyl-CoA dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12806"
SQ   SEQUENCE   598 AA;  65309 MW;  CA1AEC2822E3EFE5 CRC64;
     MPPSSLILSR RDLEFLLHEW LDVESLLERP QYAEHSRETF DAVLELAERI ATEHFAPHNR
     TADENEPRMV DGRVELIPEV SRALKVFADA GLMAGEFDEQ FGGMQLPHVV GQAVFAWFKA
     ANVGTAAYPF LTMANARLLL AHGSREQIDT YVGPMVEGRW FGTMALSEPQ AGSSLADITT
     RAERQDDGTY RLTGNKMWIS AGDHELTENI VHLVLAKVPG GPPGVKGISL FVVPKFLVRD
     DGSLGERNDV VLAGLNHKMG YRGTTNTLLN FGEGVHTPGG RAGAVGHLVG EEHRGLTYMF
     HMMNEARIGV GMGATALGYT GYLHALEYAR TRTQGRPPTD RNPSAPPVPI IEHTDVRRML
     LAAKSYVEGG LALGLYCARL VDEEQTAGSE ADRARAHLLL EMLTPIAKAW PSQWGPVADD
     LAIQVHGGYG YTRDYPVEQF YRDNRLNPIH EGTNGIQALD LLGRKVVMQD GAGLRLLAGT
     IAATTARAAG TDWAGFAVDL DAAVDRLTRV TATLWGVGDP AVTLANASAY LEAAGHVVVA
     WLWLEQALAT AGRTSDFHEG KRAAARYFAR YELPTVHTRL DLLESLDRTV LDLPESWL
//