ID A0A0J8TYQ3_COCIT Unreviewed; 693 AA.
AC A0A0J8TYQ3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Acyl-coenzyme A oxidase {ECO:0000256|PIRNR:PIRNR000168};
GN ORFNames=CISG_07253 {ECO:0000313|EMBL:KMU79087.1};
OS Coccidioides immitis RMSCC 3703.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=454286 {ECO:0000313|EMBL:KMU79087.1, ECO:0000313|Proteomes:UP000054559};
RN [1] {ECO:0000313|Proteomes:UP000054559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 3703 {ECO:0000313|Proteomes:UP000054559};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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; DS268170; KMU79087.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8TYQ3; -.
DR STRING; 454286.A0A0J8TYQ3; -.
DR Proteomes; UP000054559; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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; 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:UP000054559}.
FT DOMAIN 43..146
FT /note="Acyl-coenzyme A oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14749"
FT DOMAIN 505..675
FT /note="Acyl-CoA oxidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01756"
FT ACT_SITE 448
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-1"
FT BINDING 152
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
FT BINDING 191
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000168-2"
SQ SEQUENCE 693 AA; 78137 MW; A83FA9A72CEC5DE6 CRC64;
MADKPDWSAA LRPAPPGGAT IIAQERARSI IPVDQLAGYL LTPDFLERQD RVLKVLLKEP
VFKKANQANL SRPDRYKLGL ARGKKIRQLK EKLGWDEEDY HMAAYLCDDV LPYHLHTAMF
ITTVSQQGSD AQRARWVPRI ERWEIIGAYA QTELGHGSNV RGIELEARWD PETREFILHS
PHLTASKWWN GTMGRTATHA IAVAQLMLPV SGKGAETKYK SYGPHPFIVQ IRDSRTHQPP
ESIIIGDIGP KYGYASMDNG YMLFNNHRVP HDAMLSRYSR VDPETGKYTK PETPEVVYGS
LTHVRATLVM EARLALARAV TVAVRYLSIR RQFRDKDSDN PSDPEMPVLD YSTVQVRIFP
LLATAFALHY SGKAMGELYA RTRKNIEENG DFETLAELHS TSSGLKSLAT DLTAGGIEIC
RRAMGGHGFG ASGLVQLNAN YLSKPTVEGD NWMITQQVAR YLIKKAKALS ASAKSRAGTR
TEESLKRYLY ARQKTLNLKV YEDDNAILEA FEWRTAHLVF KAYEQREIQK KSWNSLLIDF
HKLSRAYSQS ILILNFHQAL QPNNPETARL DSTTRAVLRD LFLLFAFTTM DAEAREFSSS
GAVSNDALDA LSARILELMG RIRPHAVRLV DAWKIPDFLL DSALGRYDGK VYEDLFDRAH
RQNPLNAETF NPDYRSDEIV LGSEDAGQIL SKL
//
