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Database: UniProt
Entry: F5YZX4_MYCSD
LinkDB: F5YZX4_MYCSD
Original site: F5YZX4_MYCSD 
ID   F5YZX4_MYCSD            Unreviewed;       649 AA.
AC   F5YZX4;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Acyl-CoA dehydrogenase {ECO:0000313|EMBL:AEF35578.1};
GN   OrderedLocusNames=JDM601_1578 {ECO:0000313|EMBL:AEF35578.1};
OS   Mycolicibacter sinensis (strain JDM601) (Mycobacterium sinense).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacter.
OX   NCBI_TaxID=875328 {ECO:0000313|EMBL:AEF35578.1, ECO:0000313|Proteomes:UP000009224};
RN   [1] {ECO:0000313|EMBL:AEF35578.1, ECO:0000313|Proteomes:UP000009224}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JDM601 {ECO:0000313|EMBL:AEF35578.1,
RC   ECO:0000313|Proteomes:UP000009224};
RX   PubMed=21685274; DOI=10.1128/JB.05291-11;
RA   Zhang Z.Y., Sun Z.Q., Wang Z.L., Wen Z.L., Sun Q.W., Zhu Z.Q., Song Y.Z.,
RA   Zhao J.W., Wang H.H., Zhang S.L., Guo X.K.;
RT   "Complete genome sequence of a novel clinical isolate, the nontuberculous
RT   Mycobacterium strain JDM601.";
RL   J. Bacteriol. 193:4300-4301(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009347}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
CC       {ECO:0000256|ARBA:ARBA00006288}.
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DR   EMBL; CP002329; AEF35578.1; -; Genomic_DNA.
DR   RefSeq; WP_013828514.1; NC_015576.1.
DR   AlphaFoldDB; F5YZX4; -.
DR   STRING; 875328.JDM601_1578; -.
DR   KEGG; mjd:JDM601_1578; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_014629_4_0_11; -.
DR   OrthoDB; 1144545at2; -.
DR   Proteomes; UP000009224; Chromosome.
DR   GO; GO:0005777; C:peroxisome; IEA:InterPro.
DR   GO; GO:0003997; F:acyl-CoA oxidase activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; 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; 2.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR012258; Acyl-CoA_oxidase.
DR   InterPro; IPR002655; Acyl-CoA_oxidase_C.
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; PTHR10909:SF378; ACYL-COENZYME A OXIDASE-LIKE PROTEIN; 1.
DR   PANTHER; PTHR10909; ELECTRON TRANSPORT OXIDOREDUCTASE; 1.
DR   Pfam; PF01756; ACOX; 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; PIRSF000168; Acyl-CoA_oxidase; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 2.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009224}.
FT   DOMAIN          18..123
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          129..243
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          277..441
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          501..630
FT                   /note="Acyl-CoA oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01756"
SQ   SEQUENCE   649 AA;  71242 MW;  A59F07AE4A5AAC26 CRC64;
     MTISAALCDT LDGRWRAVKN RVRATLSDEK FRPHHTPNTV IARAKVAEQL RIMAGTGVAA
     DSFRKEHGGT GDVGAAVSMI EMLAMSDLSL MVKAGVQWGL FGGAVENLGT ERHHRAYVQK
     IIDLDLLGCF AMTETGHGSD VQALETTATY DPATEEFVID SATGTARKDY IGGAAETATI
     AAVFAQLRTP GPGGEEQGHG VHCLLVPIRD SEGNDLPGVT TSDCHYKGGL PGVDNGRIVF
     DHVRVPRENL LNRYADVDPD GSYRSSIESD GRRFFTMIGT LIRGRVSVGG SAGAAARVAL
     DIATRYALQR RQFSAPSDDG AEHEVLIMDY LVHQRRLLPL IARSYALQFA QNELVSKCHD
     LQTADDPDPE EQRELEARAA GLKAANTWHA SRAIQEAREA CGGAGYMAEN RLIALRADTD
     VFTTFEGDNH VLTQLVAKQL LTAYADDIAG MSPVDWVRFA AETVSDRVLK RTAAETIIQT
     FVDARQDSEE EGSLFNRGTQ LHMFTDREEY LLTSVARRLR AKSEEMSDFD AFNAVQDHVL
     HAAAAHIDRV VLEAFVAGIE SCPDAAAREL LELVCDLYAL SVIEDDKAWY IEHRYLSTDR
     AKAVTRGIND RCRKLRPHAE TLVDGFGIPE QLRYAEMLHP EHLAETARR
//
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