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Database: UniProt
Entry: A0A0P7BRF6_9BACT
LinkDB: A0A0P7BRF6_9BACT
Original site: A0A0P7BRF6_9BACT 
ID   A0A0P7BRF6_9BACT        Unreviewed;       769 AA.
AC   A0A0P7BRF6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Acyl-CoA oxidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AFM12_16635 {ECO:0000313|EMBL:KPM46865.1};
OS   Jiulongibacter sediminis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Jiulongibacter.
OX   NCBI_TaxID=1605367 {ECO:0000313|EMBL:KPM46865.1, ECO:0000313|Proteomes:UP000050454};
RN   [1] {ECO:0000313|EMBL:KPM46865.1, ECO:0000313|Proteomes:UP000050454}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JN14-9 {ECO:0000313|EMBL:KPM46865.1,
RC   ECO:0000313|Proteomes:UP000050454};
RA   Liu Y., Du J., Shao Z.;
RT   "The draft genome sequence of Leadbetterella sp. JN14-9.";
RL   Submitted (JUL-2015) 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:KPM46865.1}.
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DR   EMBL; LGTQ01000013; KPM46865.1; -; Genomic_DNA.
DR   RefSeq; WP_055150543.1; NZ_LGTQ01000013.1.
DR   AlphaFoldDB; A0A0P7BRF6; -.
DR   STRING; 1605367.AFM12_16635; -.
DR   PATRIC; fig|1605367.3.peg.760; -.
DR   OrthoDB; 1144545at2; -.
DR   Proteomes; UP000050454; 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   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:UP000050454}.
FT   DOMAIN          168..269
FT                   /note="Acyl-CoA dehydrogenase/oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02771"
FT   DOMAIN          278..386
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          421..577
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
FT   DOMAIN          625..757
FT                   /note="Acyl-CoA oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01756"
SQ   SEQUENCE   769 AA;  86069 MW;  A0968A4D60CC8418 CRC64;
     MKYSPGIISV LPLFYIGWSD SVLSPSEMKS IQDKIKGMDF LSYDDQYTLI SWTDQKNPPS
     EETFKSWLDA IKSQSAQMKV SDKISLVDLG LQMAKTSSGA KNEIWDAPKV RKSIEELEAA
     LGVSHQLSKL SFYQSISPEA EHEIEEEKAF DPRAMQSLLD GPYAPLKEKA KKLIMDSFFD
     ISKEVRDKEE MRNLVLDQVK ALARQGYGAY AYPEEYGGAN SPGGNTAIFE TLAMGNISLL
     IKFGVQFGLF GGAIFQLGTK KHHDKYLKDT GTLELAGCFA MTETGHGSNV RDLETTAVYN
     PDDKTITVHS PTVAAGKEYI GNALHSKMAV VFAQLMVNNK NQGIHAVLVP LRDEKHETLP
     GITVKDNGYK MGLNGVDNGR IWFDNVTVPL ENLLDKYGGI DENGNYQSSI KKESKRFFTM
     LGALVGGRVS LALASNTAAK KSLDIAIRYS LKRRQFSNLN EDQETLILDY PTHQWRLFPL
     MAKSYGLTFA TETLREKFAG AYGGSEEMRE VETLAAGLKS YASWHATDTI QECREACGGK
     GYLAENEFAD LKADTDIFTT FEGDNHVLLQ LVAKALLTDL KQEFNDGGFM AVARHVLQRM
     SSSVLTLNPV NTRNTNAEHL LSIDFMQSAM TFRSQKLLFS LSDRMRSFIG KKLAPPEIFL
     RTQTHMVSLA KAWVEAFIFE EFVKKLNSLP ESKEKEALRI MLQIFSLHAI YEDKGWFLEN
     DFISGDKSKA IRKVLNKLMR QVRPQAHLYV EAFGIPEVLR KAKIATFAE
//
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