ID I2JUG1_DEKBR Unreviewed; 707 AA.
AC I2JUG1;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 2.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
GN ORFNames=AWRI1499_3511 {ECO:0000313|EMBL:EIF46613.1};
OS Brettanomyces bruxellensis AWRI1499.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Brettanomyces.
OX NCBI_TaxID=1124627 {ECO:0000313|EMBL:EIF46613.1, ECO:0000313|Proteomes:UP000004997};
RN [1] {ECO:0000313|EMBL:EIF46613.1, ECO:0000313|Proteomes:UP000004997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AWRI1499 {ECO:0000313|EMBL:EIF46613.1,
RC ECO:0000313|Proteomes:UP000004997};
RX PubMed=22470482; DOI=10.1371/journal.pone.0033840;
RA Curtin C.D., Borneman A.R., Chambers P.J., Pretorius I.S.;
RT "De-Novo Assembly and Analysis of the Heterozygous Triploid Genome of the
RT Wine Spoilage Yeast Dekkera bruxellensis AWRI1499.";
RL PLoS ONE 7:E33840-E33840(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-CoA + O2 = a (2E)-enoyl-CoA + H2O2;
CC Xref=Rhea:RHEA:38959, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.3.6;
CC Evidence={ECO:0000256|ARBA:ARBA00001201};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00004846}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
CC {ECO:0000256|ARBA:ARBA00006288, ECO:0000256|PIRNR:PIRNR000168}.
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:EIF46613.1}.
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DR EMBL; AHIQ01000201; EIF46613.1; -; Genomic_DNA.
DR UniPathway; UPA00661; -.
DR Proteomes; UP000004997; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0003997; F:acyl-CoA oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0033540; P:fatty acid beta-oxidation using acyl-CoA oxidase; IEA:UniProtKB-UniPathway.
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; IPR029320; Acyl-CoA_ox_N.
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; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR PANTHER; PTHR10909; ELECTRON TRANSPORT OXIDOREDUCTASE; 1.
DR PANTHER; PTHR10909:SF352; PEROXISOMAL ACYL-COENZYME A OXIDASE 3; 1.
DR Pfam; PF01756; ACOX; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF14749; Acyl-CoA_ox_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|PIRNR:PIRNR000168, ECO:0000256|PIRSR:PIRSR000168-2};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR000168};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000004997}.
FT DOMAIN 28..139
FT /note="Acyl-coenzyme A oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14749"
FT DOMAIN 154..263
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 510..685
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 458
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT BINDING 158
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT BINDING 197
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT UNSURE 503
FT /note="I or L"
FT /evidence="ECO:0000313|EMBL:EIF46613.1"
SQ SEQUENCE 707 AA; 79043 MW; E2C7156A78BF1E40 CRC64;
MSYTVSSNSV EPNPGSMIQE ERRSTSFNVQ KMFEFLEGSK QKAVDTLSIM QQLERDPILR
TSLRYYEYGT EKHREETAAK ISRMAQYIEK DAPDMQXFQN RLNLIAVVDP QLGTRIGVHL
GLFLGAIRGN GTDNQFNYWA FERGAAYIKG IYGCFAMTEL AHGSNVAALE TTATYNRKRK
CFIINTPHVG ATKWWIGGAA HSATHTACFA RLKVDGKDYG VKVFVVPLRD TAHMLQPGIA
LGDIGEKMGR NGIDNGWIQF SHVEIPKEYM LSKFATISDD GEVIEPPLAQ LAYSALLGGR
VTMVTDSFRT SERFITIALR YSVGRRQFKQ GKAASNNKKM PQSESQIIDH PLHQHRLLPL
LAWXYAMGIA SNQIQSDYKA TLSMLESGVR TQDMKVLGVA IKKLKQLFAD SASLKSTCTW
KCLQLIEECR QACGGHGYSA YSGFGKGYAD HAVQCTWEGD NNILAQNAGR ITVQQVAKML
KTDMKPTGNF SFLAGKSKIG HXLDAEDISD LSKLLLALET LIXRLSSNCL DLLSKNEQNW
DSISTEKKSL SHLYAIQYML SKGIQRLXEX RQSNNGGINT PIKLLLSLFA LSGIKEYADV
FLQFDVLSTQ TYAKLKERIG TLCLEIRPMV IGMTDSFKFS DFFINSVLGC YNGDIYNDYW
KAVNSLNDAF DTKAPYSHDL EAMLKRPTVA QRENFEKGSK VLQKLSN
//
