ID S2JQQ2_MUCC1 Unreviewed; 692 AA.
AC S2JQQ2;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
GN ORFNames=HMPREF1544_08343 {ECO:0000313|EMBL:EPB84908.1};
OS Mucor circinelloides f. circinelloides (strain 1006PhL) (Mucormycosis
OS agent) (Calyptromyces circinelloides).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=1220926 {ECO:0000313|EMBL:EPB84908.1, ECO:0000313|Proteomes:UP000014254};
RN [1] {ECO:0000313|Proteomes:UP000014254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1006PhL {ECO:0000313|Proteomes:UP000014254};
RG The Broad Institute Genomics Platform;
RA Cuomo C., Earl A., Findley K., Lee S.C., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome sequence of Mucor circinelloides f. circinelloides 1006PhL.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; KE124026; EPB84908.1; -; Genomic_DNA.
DR AlphaFoldDB; S2JQQ2; -.
DR STRING; 1220926.S2JQQ2; -.
DR VEuPathDB; FungiDB:HMPREF1544_08343; -.
DR eggNOG; KOG0136; Eukaryota.
DR InParanoid; S2JQQ2; -.
DR OMA; NDGATHN; -.
DR OrthoDB; 5777at2759; -.
DR UniPathway; UPA00661; -.
DR Proteomes; UP000014254; 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:SF250; PEROXISOMAL ACYL-COENZYME A OXIDASE 1; 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:UP000014254}.
FT DOMAIN 42..164
FT /note="Acyl-coenzyme A oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14749"
FT DOMAIN 166..275
FT /note="Acyl-CoA oxidase/dehydrogenase middle"
FT /evidence="ECO:0000259|Pfam:PF02770"
FT DOMAIN 516..686
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT BINDING 170
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT BINDING 209
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ SEQUENCE 692 AA; 77978 MW; EAA4C290538AA65C CRC64;
MSKANAVERL EQIKQQLNLS PSPMSLQAPK DMQKERSSAS FNIEALSHFW MGGKEKFERR
KKALDFIEKD AELVVQAPKN ILEFGREEMR EYAMGQINRI VRLGREINDR EFLEDISRAV
ILYSESFALR IGVHEALFRN VVQMLGNKQQ QEEWIENVNE FKIIGCFAMT ELGHSSALRD
IETTATFDVE TDEFIIHSPN ITSTKWWIGM AGQTATHTVV IAQTFIHGKN VGLNWFIVQL
RDTVTGKVVP GVQAGDVGSK VGHQGVDNGW IQFNQKRIPR TNMLTKWVSM DRSGEFQPAP
NPAVMYATLI PERFSLVTIT LTLVTQALTI ATRYGVVRRQ GSKNQQIMDY QSHYVKLLPA
ISFMYMVQNS FKTLDDQFAI LTAGGEMDPI VYLNHMGDMH SISASLKGLS GAYATEILEI
CRRSCGGHAY SAYNALGNLI SDFGVMTTGG GDNVVLLQQA ARYLLYRLNQ KLEFDEYPEL
KYQSATHYIA RAKELLQIKN WSVNVIADAT KDFALIEEAL HVILVKRLNS IQQALNDGAT
HNDLLLESVR VAELHCAAFL FSVNARQFAS VSDSDMDPSV QLIMRQMTAL WGLHILRVYG
DQGYMEGFLS PKQLKDIEKE YLELCKSMRY EVIGLTDGFG LPDFVLKAPI AKYDGNIYQA
YFETLLQAPG STGVAPYHAK LIKPLTEKFE SK
//
