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ACOX_KLULA
ID   ACOX_KLULA              Reviewed;         736 AA.
AC   Q6CKK7;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Acyl-coenzyme A oxidase;
DE            Short=Acyl-CoA oxidase;
DE            EC=1.3.3.6;
GN   Name=POX1; OrderedLocusNames=KLLA0F09933g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; Evidence={ECO:0000250};
CC   -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA oxidase family. {ECO:0000305}.
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DR   EMBL; CR382126; CAG98240.1; -; Genomic_DNA.
DR   RefSeq; XP_455532.1; XM_455532.1.
DR   AlphaFoldDB; Q6CKK7; -.
DR   SMR; Q6CKK7; -.
DR   STRING; 28985.XP_455532.1; -.
DR   EnsemblFungi; CAG98240; CAG98240; KLLA0_F09933g.
DR   GeneID; 2895011; -.
DR   KEGG; kla:KLLA0_F09933g; -.
DR   eggNOG; KOG0136; Eukaryota.
DR   HOGENOM; CLU_014629_3_1_1; -.
DR   InParanoid; Q6CKK7; -.
DR   OMA; VMPNIQI; -.
DR   UniPathway; UPA00661; -.
DR   Proteomes; UP000000598; Chromosome F.
DR   GO; GO:0005782; C:peroxisomal matrix; IEA:EnsemblFungi.
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; Reference proteome.
FT   CHAIN           1..736
FT                   /note="Acyl-coenzyme A oxidase"
FT                   /id="PRO_0000204699"
SQ   SEQUENCE   736 AA;  83144 MW;  32A5B2C0C7CA3E54 CRC64;
     MTRQSTVDQN QSTYNAKNFI TKERQESKLD IDQLNVFLEN GEQEAKLTHD LIEEIINDPI
     LKTDTDHYDI TKSQEREITA RRIARLSLYM EHDVKTKQRE FKDDLVKNLE RKDSKLLTNK
     DLSIFDRRLS LVANIDPGLS TRIGVHLGLF GNCIKGNGTD EQIHYWLQEK GALLLKGIYG
     CFAMTELGHG SNVAQLQTTA TYDPSSDTFK INTPDLLATK WWIGGAAHSA THTTAYARLI
     VNGKDYGVKT FVVPLRDEKT LNLLPGIMIG DIGAKMGRDG IDNGWIQFKN VVIPRQFMLQ
     RFTKVIPGSP PKVQTQPLLD QISGYSALLS GRVNMVMDSF RFGSKFAIIA TRYAVGRQQF
     GPEGNETQLI DYPLHQYRVL PQLALCYLVA PTAHKLMGTY ISTLMELHQA GADKAKLINV
     SNKLKDLFID SASLKATNTW LVAKLIDDLR QTCGGHGYSS YNGFGKGYND WVVQCTWEGD
     NNILSLTSAK SIVKKFADIS RGKNTTVTTD SLKYLTPQFI GKSLSKDLTF KFDNKKDFTE
     IWAVMIIRLI HHVVELISKG TKIDSLSKTL VQISKFHAIH SMLLTYQDKL NNESEASVKD
     AYTKGYLWKL YELFSLYFID QHLGEFLLLK VVTSDQMSQV LQPRLLQLLP EIRKECIALT
     DAFKLPDAMI NAPIGYYDGD IYHNYFNEVT NNNKLEPDGA GRPPYYPLLT SMLGRDDFQN
     RLGGSFESET LDSLLK
 
 
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