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Database: UniProt
Entry: A0A101AIP9_9MYCO
LinkDB: A0A101AIP9_9MYCO
Original site: A0A101AIP9_9MYCO 
ID   A0A101AIP9_9MYCO        Unreviewed;       657 AA.
AC   A0A101AIP9;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Acyl-CoA oxidase {ECO:0000313|EMBL:KUI23442.1};
GN   ORFNames=AU193_01475 {ECO:0000313|EMBL:KUI23442.1};
OS   Mycobacterium sp. GA-1285.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1772282 {ECO:0000313|EMBL:KUI23442.1, ECO:0000313|Proteomes:UP000053702};
RN   [1] {ECO:0000313|EMBL:KUI23442.1, ECO:0000313|Proteomes:UP000053702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GA-1285 {ECO:0000313|EMBL:KUI23442.1,
RC   ECO:0000313|Proteomes:UP000053702};
RG   TB Trials Study Group;
RA   Sutton G., Brinkac L., Sanka R., Adams M., Lau E.L., Macaden R.,
RA   Grewal H.M.S.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:KUI23442.1}.
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DR   EMBL; LQIS01000001; KUI23442.1; -; Genomic_DNA.
DR   RefSeq; WP_064420546.1; NZ_LQIS01000001.1.
DR   AlphaFoldDB; A0A101AIP9; -.
DR   STRING; 1772282.AU193_01475; -.
DR   OrthoDB; 1144545at2; -.
DR   Proteomes; UP000053702; Unassembled WGS sequence.
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}.
FT   DOMAIN          25..124
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          130..240
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          274..435
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          494..624
FT                   /note="Acyl-CoA oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01756"
SQ   SEQUENCE   657 AA;  72747 MW;  B2ED0CE4F192541E CRC64;
     MTTTAEHLRN ALDGRWRDVK NRMREELSNE IFRPHYTPNT VIARTKVAEQ LKIMAAMGAA
     EDGFKKEHGG NGDVGAAVTQ IEMLAMSDLS LMVKAGVQWG LFGGAIENLG TERHHEKYVK
     PVIDCELLGC YAMTETGHGS NVQALETTAT YDPATEEFVI DSPTPTARKD YIGGAAETAR
     IAAVFAQLIT PDGEGHGVHC VLVPIRDEDG NDLPGVTTSD CHYKGGLPGV DNGRIQFDKV
     RVPRENLLNR YGDVAPDGTY SSPIESPGRR FFTMLGTLVR GRVTVGGSAA AAARVALDIA
     TRYGLLRRQF EAPGEDHEVV IMDYLVHQRR LLPLIAESYA LQFAQNELVA KCHDLQSAED
     PDPEEQRELE GRAAGLKAAN TWHATRAIQE AREACGGAGY MAENRLIALK ADTDVFTTFE
     GDNHVLTQLV AKQLLTAYAD DVKSMSPVEW VRFAANFAGE RVLKRTAAET IMQTILDTRQ
     DNEEEGSLFN RGTQVQMFED REEYMISTVA RRLQGKSKEM SEFDAFNAVQ DHVLHCAQAH
     IDRVILEAFV AGIDACEDEE ARKILNMVCD LYALSVIEKD RAWFIEHRFI STERAKAVTR
     GVNERCRTLR PYAELLVDGF GIPEQLRYAE MLHPERIPDA DEHVEQDAIS AGTIGPK
//
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