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Database: UniProt
Entry: X8DSI2_9MYCO
LinkDB: X8DSI2_9MYCO
Original site: X8DSI2_9MYCO 
ID   X8DSI2_9MYCO            Unreviewed;       382 AA.
AC   X8DSI2;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Acyl-CoA dehydrogenase, C-terminal domain protein {ECO:0000313|EMBL:EUA71592.1};
GN   ORFNames=I540_2486 {ECO:0000313|EMBL:EUA71592.1};
OS   Mycobacteroides abscessus subsp. bolletii 1513.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacteroides; Mycobacteroides abscessus.
OX   NCBI_TaxID=1299321 {ECO:0000313|EMBL:EUA71592.1, ECO:0000313|Proteomes:UP000023351};
RN   [1] {ECO:0000313|EMBL:EUA71592.1, ECO:0000313|Proteomes:UP000023351}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1513 {ECO:0000313|EMBL:EUA71592.1,
RC   ECO:0000313|Proteomes:UP000023351};
RA   Zelazny A., Olivier K., Holland S., Lenaerts A., Ordway D., DeGroote M.A.,
RA   Parker T., Sizemore C., Tallon L.J., Sadzewicz L.K., Sengamalay N.,
RA   Fraser C.M., Hine E., Shefchek K.A., Das S.P., Tettelin H.;
RL   Submitted (DEC-2013) 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:EUA71592.1}.
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DR   EMBL; JAOJ01000002; EUA71592.1; -; Genomic_DNA.
DR   AlphaFoldDB; X8DSI2; -.
DR   PATRIC; fig|1299321.3.peg.2405; -.
DR   Proteomes; UP000023351; 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; cd00567; ACAD; 1.
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; 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:SF44; BLR1022 PROTEIN; 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.
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          6..117
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          123..216
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          234..369
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   382 AA;  41144 MW;  AF8BB07376DB58F9 CRC64;
     MDFSLTDEQQ LLKHSISDFL SNRYALDTSR RAARSDIGWQ PQVWKSFAEE LGILAAPLPE
     DRGGLGGGAE EVLVICEVLG RHLVVEPFIG TVVLGGGLLR RSNAEVAYDL IEGIASGDVV
     TGFAALEPTS GQSFHSVQTT ARRDGPDWVL DGEKIVVSDA PLATHVIISA RTSGDAADTS
     GLTLFVVPFD PAAPAQGIEA HHYRTIDDHH ASDLVISGLR VPDSARISEV DQAWPLIEAA
     LDEATAATVA EAVGMLRKVL ADTIEYTKQR QQFGVAISNF QALQHRMVNM HIEVEQSVAA
     SYLASLNLDG PRRTRAVSAA KATISRAARL VGQEAVQLHG GMGMTEELAI GHYFKRLTVI
     ESEFGNRDFH TARYGIARST QG
//
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