ID A0A151C1Z3_9MICO Unreviewed; 646 AA.
AC A0A151C1Z3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Acyl-CoA oxidase {ECO:0000313|EMBL:KYH46141.1};
GN ORFNames=AZH51_10920 {ECO:0000313|EMBL:KYH46141.1};
OS Branchiibius sp. NY16-3462-2.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC Branchiibius.
OX NCBI_TaxID=1807500 {ECO:0000313|EMBL:KYH46141.1, ECO:0000313|Proteomes:UP000075667};
RN [1] {ECO:0000313|EMBL:KYH46141.1, ECO:0000313|Proteomes:UP000075667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NY16-3462-2 {ECO:0000313|EMBL:KYH46141.1};
RA Lapierre P., Halse T.A., Shea J., Musser K.A., Escuyer V.E.;
RT "Draft genome assembly of Branchiibius sp. 15-3462-2 from a clinical sputum
RT sample.";
RL Submitted (MAR-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:KYH46141.1}.
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DR EMBL; LVCF01000001; KYH46141.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151C1Z3; -.
DR STRING; 1807500.AZH51_10920; -.
DR Proteomes; UP000075667; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000075667}.
FT DOMAIN 62..140
FT /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02771"
FT DOMAIN 144..253
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 287..449
FT /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00441"
FT DOMAIN 511..645
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
SQ SEQUENCE 646 AA; 70690 MW; 4725B43F41053EAB CRC64;
MSNTLTETPE AGVPADARAD QLRALLDGPW RELRERFRAE IEPQMVLGEP GRSIEENRAR
VTAQLLSLAE KGYGRIGFLT QYGGEYDYGA SCVLFEMQAY GDLSLTVKTG VQFGLFGGAV
QRLGTQRHHA AYLEDIMTGK LLGSFAMTEE GHGSNVQRLE TTLTYDVEAG DFVLHSPTPS
SIKTYIGNAA RDAQMAVVFA QLIVPSGSQG VHAVLVPVRD GDGNPLPGVT IGDNGPKAGL
PGVDNGTFFF DHVRVPRENL LNAYGDVAED GSYTSPIEGE NKRFFTMLGT LVRGRVCVGG
GAAASAKKAL VIALRYGTQR RQFEAPGVEQ EAVILDYLAH QRKLFPRLAR SYALSFAQNE
LTSRLQALQG EQAHPDEQGQ RELEGLVAGM KALSTWHAID TIQTCREACG GAGYMGENEL
GQMRADTDVF ATFEGDNTVL LQLVAKGLLT EYKETFSDLD AADLIGLITR QVGDTIVEKT
AGRAGLQKLV DAVTPRNDET ALDNRGWQLW MFRERADHLL ETLGKRLRRA TRENAFELFN
NAQDHVLEAA RAHIEEFILT EATTAWQSMP KGPARDLLDK VIDLYALSSI EADKAWFLEH
GRLTDKRSRL VTASVNDLCQ ALRPEVDTLT RALGVPEQLI VAPIAQ
//
