ID A0A0D2AIX6_9PEZI Unreviewed; 663 AA.
AC A0A0D2AIX6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
GN ORFNames=PV09_02921 {ECO:0000313|EMBL:KIW06485.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW06485.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIW06485.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW06485.1,
RC ECO:0000313|Proteomes:UP000053259};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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}.
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DR EMBL; KN847535; KIW06485.1; -; Genomic_DNA.
DR RefSeq; XP_016216354.1; XM_016356048.1.
DR AlphaFoldDB; A0A0D2AIX6; -.
DR STRING; 253628.A0A0D2AIX6; -.
DR GeneID; 27310894; -.
DR VEuPathDB; FungiDB:PV09_02921; -.
DR HOGENOM; CLU_014629_3_1_1; -.
DR InParanoid; A0A0D2AIX6; -.
DR OrthoDB; 5777at2759; -.
DR UniPathway; UPA00661; -.
DR Proteomes; UP000053259; 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; 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:SF250; PEROXISOMAL ACYL-COENZYME A OXIDASE 1; 1.
DR Pfam; PF01756; ACOX; 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|PIRNR:PIRNR000168};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000053259}.
FT DOMAIN 19..129
FT /note="Acyl-coenzyme A oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14749"
FT DOMAIN 483..630
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT ACT_SITE 421
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT BINDING 135
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT BINDING 174
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ SEQUENCE 663 AA; 75389 MW; 484B8DB4F3CC0716 CRC64;
MEGQTRNIPK EPVESDFGLF LWGKEKFLRR KATLKAFATD PIFSKGEVVY ASLPRKDVWA
RTVLQSKALI ELKLREGWSH TQFMEAIKMT DNFMPVQPQF RIFMSNLERQ MSDEQKKIWI
PKAERFEIFG SYAQTELGHG SNVQGIETTA TFDETTDEFV INSPTLSSTK YWIGTTGVWA
THSIVVAKLI IKGKNYGNHL FLTQIRDLDT QRLMPGVEIY ELGPKAFQGM LGTDNGAMQF
HNVRIPRSQM LARNAQVLRD GTYVKPKNEK HSYGSMVTVR ALMAEITAWD LLNAVVVAYH
YTTFRKQFRK DSNEKEETTV FDYASVRYRL LPLLAQATAL IVVGRNIKRG YDEYTEHNLK
TGDFSQLEDF HLQTVGAKVY STDITGRGIE TSRIACGGHG YSALSGFGRM YANAINAVTY
EGDNYVVGKQ VPRAILKHYR NKTESSLPTL SYLSALREGG RTMVPIKSAN DWFDEQTQKW
ALEQRLRNLV QQHIEDTDAG KDTSYSTHSL TMAHCDFVYF TQLMDVVNRL ETENRSYAPP
MRATARVFAL SVIQDPHHPS LAQALPLPMD EQKWLRDAYA AALDDYAKNH VASIIDAYGL
TEYELDSALA RSNQTPYEAL WEGAKKSEMS GAAMSYLWPV MIGARQIWKQ IEEEKQGHRT
SKL
//
