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THIKA_CANTR
ID   THIKA_CANTR             Reviewed;         408 AA.
AC   P33290;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=3-ketoacyl-CoA thiolase A, peroxisomal;
DE            EC=2.3.1.16;
DE   AltName: Full=Acetyl-CoA acyltransferase A;
DE   AltName: Full=Beta-ketothiolase A;
DE   AltName: Full=Peroxisomal 3-oxoacyl-CoA thiolase A;
DE   AltName: Full=Thiolase IA;
DE   Flags: Precursor;
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].
RC   STRAIN=ATCC 20336 / pK233 / NCYC 997;
RX   PubMed=1362382; DOI=10.1111/j.1432-1033.1992.tb17505.x;
RA   Kurihara T., Ueda M., Kanayama N., Kondo J., Teranishi Y., Tanaka A.;
RT   "Peroxisomal acetoacetyl-CoA thiolase of an n-alkane-utilizing yeast,
RT   Candida tropicalis.";
RL   Eur. J. Biochem. 210:999-1005(1992).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA;
CC         Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16;
CC   -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000305}.
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DR   EMBL; D17320; BAA04142.1; -; Genomic_DNA.
DR   AlphaFoldDB; P33290; -.
DR   SMR; P33290; -.
DR   VEuPathDB; FungiDB:CTMYA2_042690; -.
DR   VEuPathDB; FungiDB:CTRG_01068; -.
DR   SABIO-RK; P33290; -.
DR   UniPathway; UPA00199; -.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR   InterPro; IPR020610; Thiolase_AS.
DR   InterPro; IPR020617; Thiolase_C.
DR   InterPro; IPR020613; Thiolase_CS.
DR   InterPro; IPR020616; Thiolase_N.
DR   Pfam; PF02803; Thiolase_C; 1.
DR   Pfam; PF00108; Thiolase_N; 1.
DR   PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR   SUPFAM; SSF53901; SSF53901; 2.
DR   TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
DR   PROSITE; PS00098; THIOLASE_1; 1.
DR   PROSITE; PS00737; THIOLASE_2; 1.
DR   PROSITE; PS00099; THIOLASE_3; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Fatty acid metabolism; Lipid metabolism; Peroxisome;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Peroxisome"
FT   CHAIN           ?..408
FT                   /note="3-ketoacyl-CoA thiolase A, peroxisomal"
FT                   /id="PRO_0000034075"
FT   ACT_SITE        112
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        366
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT   ACT_SITE        394
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
SQ   SEQUENCE   408 AA;  43262 MW;  4DC5212708875FA5 CRC64;
     MDRLNQLSGQ LKPNAKQSIL QKNPDDVVIV AAYRTAIGKG FKGSFRSVRS EFILTEFLKE
     FIKKTNIDPS LIEDVAIGNV LNQAAGATEH RGACLAAGIP YTAAFIAVNR FCSSGLMAIS
     DIANKIKTGE IECGLAGGAE SMSTNYRDPR VAPRIDPHLA DDAQMEKCLI PMGITNENVA
     NQFNISRERQ DEFAAKSYNK AAKAVAAGAF KSEILPIRSI IRNSDGTEKE IIVDTDEGPR
     EGVTAESLGK LRPAFDGTTT AGNASQVSDG AAAVLLMKRS LAEAKGYPII GKYVLCSTAG
     VPPEIMGVGP AYAIPEVLKR TGLTVDDIDV FEINEAFAAQ CLYSAEQVNV PEEKLNINGG
     AIALGHPLGE TGARQYATII PLLKPGQIGL TSMCIGSGMG SASILVRE
 
 
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