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Database: UniProt
Entry: A0A1S8C865_9ACTN
LinkDB: A0A1S8C865_9ACTN
Original site: A0A1S8C865_9ACTN 
ID   A0A1S8C865_9ACTN        Unreviewed;       384 AA.
AC   A0A1S8C865;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:OMQ15097.1};
GN   ORFNames=A7K94_0211875 {ECO:0000313|EMBL:OMQ15097.1};
OS   Modestobacter sp. VKM Ac-2676.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Modestobacter.
OX   NCBI_TaxID=1678130 {ECO:0000313|EMBL:OMQ15097.1, ECO:0000313|Proteomes:UP000093049};
RN   [1] {ECO:0000313|EMBL:OMQ15097.1, ECO:0000313|Proteomes:UP000093049}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM Ac-2676 {ECO:0000313|EMBL:OMQ15097.1,
RC   ECO:0000313|Proteomes:UP000093049};
RA   Vasilenko O.V., Tarlachkov S.V., Ariskina E.V., Ariskina K.I., Avtukh A.N.,
RA   Evtushenko L.I.;
RT   "Draft genome sequence of Actynobacteria Modestobacter sp. strain VKM Ac-
RT   2676.";
RL   Submitted (JAN-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}.
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:OMQ15097.1}.
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DR   EMBL; MBFF02000355; OMQ15097.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S8C865; -.
DR   Proteomes; UP000093049; 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; 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:UP000093049}.
FT   DOMAIN          11..122
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          127..221
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          233..383
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   384 AA;  40713 MW;  A4918E285FFCD2BD CRC64;
     MGNNAGLYAL TEEHEAIREA VREIAEREIA PFAAEVDAES RYPVEAQKAL TAAGFHATHL
     PEAYGGEGAD AIATCIVIEE VARVDVSASL IPAVNKLGSV PLVLSASEEL KQLVLPSIAA
     GDAMISYGLS EREAGSDAAA MRTRARLEGD SWVLNGTKAW ITNASVSEWF TVMAVTDPER
     GAKGISAFVV HRDDPGFAVG PKEKKMGIKG SPTCELYLTD CTIPADRIVG EPGTGFTTAL
     RTLDVTRPTI GAQAVGVAQG ALDAAVAYTK DRRQFGSAVA DFQGVQFMLA DMDMKVQAAR
     HLVYVAAAAG DQGRPDVTRV SAAAKAFASD VAMQVTTDAV QLFGGAGYTQ DFPVERMMRD
     AKITQIYEGT NQVQRMVIAR SLLK
//
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