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ACOX2_CANTR
ID   ACOX2_CANTR             Reviewed;         724 AA.
AC   P11356;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Acyl-coenzyme A oxidase 2;
DE            Short=Acyl-CoA oxidase 2;
DE            EC=1.3.3.6;
DE   AltName: Full=PXP-2;
GN   Name=POX2;
OS   Candida tropicalis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3692174; DOI=10.1016/0378-1119(87)90027-8;
RA   Okazaki K., Tan H., Fukui S., Kubota I., Kamiryo T.;
RT   "Peroxisomal acyl-coenzyme A oxidase multigene family of the yeast Candida
RT   tropicalis; nucleotide sequence of a third gene and its protein product.";
RL   Gene 58:37-44(1987).
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC   -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC   -!- SUBCELLULAR LOCATION: Peroxisome.
CC   -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. {ECO:0000305}.
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DR   EMBL; M18259; AAA34361.1; -; Genomic_DNA.
DR   PIR; A27331; OXCKP2.
DR   AlphaFoldDB; P11356; -.
DR   SMR; P11356; -.
DR   VEuPathDB; FungiDB:CTMYA2_049320; -.
DR   VEuPathDB; FungiDB:CTRG_02374; -.
DR   SABIO-RK; P11356; -.
DR   UniPathway; UPA00661; -.
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; -; 1.
DR   Gene3D; 2.40.110.10; -; 1.
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.
DR   PANTHER; PTHR10909; PTHR10909; 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; SSF47203; 2.
DR   SUPFAM; SSF56645; SSF56645; 1.
PE   3: Inferred from homology;
KW   FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism; Oxidoreductase;
KW   Peroxisome.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..724
FT                   /note="Acyl-coenzyme A oxidase 2"
FT                   /id="PRO_0000204695"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   724 AA;  81936 MW;  B2A145C5DDAF7379 CRC64;
     MAMLSQPNDG HDHPEKKDPD TTPKQVAGVI SSQDPPHPAK DVAEERARTD WDLKEMHEFL
     EGDEAKSEQI LRLYQSIERD PILQTRPEQF DYTQKQEREL VANRINQMTK FLETEPYGKF
     RRRLQLMTVI DPSLGIRMLV NIGLFLNCVR GNGTQKQFDF WSNKKEAGIV KQLYGCFGMT
     ELGHGSNVAG CETTATFDEK TDEFIIDTPH IGATKWWIGG AAHSATHTVC YARLIVKDVD
     YGVKTFIVPL RDSRHSLLPG IAIGDIGAKM GRQGVDNGWI QFTEVRVPRF FMLQRWCKVD
     RQGNVTLPPL EQLSYISLLE GRVGMATDSY RIGARYTTIA LRYAVGRRQF SKKAGEPETK
     LIDYTLHQRR LLPYLALTYA AAVGTDRLER QHEELLANLD IALAKKDKLL LKNTITGTKS
     MFVDSGSLKS TLTWLAADLI NETRQACGGH GYSSYNGFGK TYDDWVVQCT WEGDNNVLAM
     SAGKTIIKTV QQVLNGKELK DSTLEFLNAA PELSKAKKAV IRIRDHVDDV DRVLKAIAGL
     ISKFSKDLIP ISYQSWDSIG AQRVILSKLR CHYYLLETFN ERLNDKIKAK SPARPHLENI
     IKLYYVTNIL GPFIDEFLRF GVISPQVAKY ITYEYPQKLC ANIRPYVIGL TDSFQQPDNF
     INSLIGKYDG NIYTNYLESV KDVNDPSNYK APYSEALEAM LNRSALENRE RSERGKAAAD
     ILSK
 
 
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