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Database: UniProt
Entry: A0A0M2ZLE9_9MYCO
LinkDB: A0A0M2ZLE9_9MYCO
Original site: A0A0M2ZLE9_9MYCO 
ID   A0A0M2ZLE9_9MYCO        Unreviewed;       390 AA.
AC   A0A0M2ZLE9; A0A1A0QA57;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:ORA60453.1};
GN   ORFNames=BST23_23070 {ECO:0000313|EMBL:ORA60453.1};
OS   Mycolicibacterium elephantis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=81858 {ECO:0000313|EMBL:ORA60453.1, ECO:0000313|Proteomes:UP000192772};
RN   [1] {ECO:0000313|EMBL:ORA60453.1, ECO:0000313|Proteomes:UP000192772}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FI-09383 {ECO:0000313|EMBL:ORA60453.1,
RC   ECO:0000313|Proteomes:UP000192772};
RA   Tortoli E., Trovato A., Cirillo D.M.;
RT   "The new phylogeny of genus Mycobacterium.";
RL   Submitted (FEB-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:ORA60453.1}.
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DR   EMBL; MVHP01000037; ORA60453.1; -; Genomic_DNA.
DR   RefSeq; WP_046751606.1; NZ_MVHP01000037.1.
DR   AlphaFoldDB; A0A0M2ZLE9; -.
DR   STRING; 81858.BST23_23070; -.
DR   OrthoDB; 8876745at2; -.
DR   Proteomes; UP000192772; 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; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 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}.
FT   DOMAIN          9..120
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          124..220
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          235..381
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   390 AA;  41755 MW;  3EC152B65D5AF293 CRC64;
     MTTPEVSDDD FREILAQTRH FVRTAVVPRE QEILREDRVP DDLREQAKKM GLFGYAIPQQ
     WGGLGLNLAQ DVELAMELGY TSLALRSMFG TNNGIAGQVL VGFGTDEQKA RWLEPIASGD
     VVASFALTEP GAGSNPSGLR TKAVADGDDW VISGQKRFIT NAPTANLFVV FARTRPADDA
     GPGIAVFLVP ADTAGVQVGA KDAKMGQEGA WTADVSFDDV RVPAEALVGG SEDIGYRAAM
     ISLARGRVHI AALAVGTAQR ALDESVAYAA TATQGGTPIG NFQLVQAMLA DQQTGVLAGR
     ALVRDAARKW VDDEDRRVAP SAAKLYCTEM AGQVADLAVQ IHGGSGYMRE VAVERIYRDV
     RLLRLYEGTS EIQRLIIGSN LVKTAQKEHA
//
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