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Database: UniProt
Entry: K1W376_TRIAC
LinkDB: K1W376_TRIAC
Original site: K1W376_TRIAC 
ID   K1W376_TRIAC            Unreviewed;      1046 AA.
AC   K1W376;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=acetyl-CoA C-acetyltransferase {ECO:0000256|ARBA:ARBA00012705};
DE            EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN   ORFNames=A1Q2_02328 {ECO:0000313|EMBL:EKD03348.1};
OS   Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Trichosporon.
OX   NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKD03348.1, ECO:0000313|Proteomes:UP000006757};
RN   [1] {ECO:0000313|EMBL:EKD03348.1, ECO:0000313|Proteomes:UP000006757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 8904 {ECO:0000313|EMBL:EKD03348.1,
RC   ECO:0000313|Proteomes:UP000006757};
RX   PubMed=23193141; DOI=10.1128/EC.00264-12;
RA   Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT   "Genome sequence of the Trichosporon asahii environmental strain CBS
RT   8904.";
RL   Eukaryot. Cell 11:1586-1587(2012).
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000256|ARBA:ARBA00010982}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKD03348.1}.
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DR   EMBL; AMBO01000256; EKD03348.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1W376; -.
DR   STRING; 1220162.K1W376; -.
DR   eggNOG; KOG1391; Eukaryota.
DR   HOGENOM; CLU_291737_0_0_1; -.
DR   InParanoid; K1W376; -.
DR   OrthoDB; 5481312at2759; -.
DR   Proteomes; UP000006757; Unassembled WGS sequence.
DR   GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
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   NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR   PANTHER; PTHR18919:SF107; 3-KETOACYL-COA THIOLASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 1.
DR   Pfam; PF02803; Thiolase_C; 1.
DR   Pfam; PF00108; Thiolase_N; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
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 {ECO:0000313|EMBL:EKD03348.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006757};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EKD03348.1}.
FT   DOMAIN          704..915
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          924..1045
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   REGION          1..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          114..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          199..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          398..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          527..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..91
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..226
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        233..257
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..489
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        549..572
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1046 AA;  110362 MW;  7F67A17837A35442 CRC64;
     MSTSRSTATP AKRSRPCSFT SSTLSPIAES PVPSPDQDAL PAVKRLWLLR SDTGEGSSSR
     DQAGKTASTG PGGDTEAISL LASSTSQPTE ELDEGAVIKA LLSAKALATQ FLKARRTGPP
     VKREAAADNG PQLEDSDPVP PAPPMRPVEP RARRIPHVSF RPTPRPFPEL AAGAKKPAGH
     QRSRSEPLAL EALDGAAAGT SSDVSSSLPP LASDSLGSSM LSDTRPVAVS RPQARATKTQ
     ASTGRAEGPD VTSAETVSNQ QKTIYRSFVD GTRTLVYRSS EHKFTTQGFI MRDLARVLHQ
     PRPAVDAVHL PFPKEQMDRH PQLDKNHRGA VTSRSSSIHT VALMSSSSAA TQKRGRGLAA
     AFPSLSPIAK SPPSLLQLEL PPPLLHLESP PPLLHLESPP PLLDLGSPPP AKKKKIRHVS
     WAPVRTLSHL VPGGNNAPLG VSTDPVTTAK NATTRSSSGG VLGSTAQSSQ STTAPSLSAL
     PPLSAPAPST TATVLLSTSL PTHSVAHDTG SGDDEIDSVL QELISANARA QGPLQRRAGK
     RRREEQSTTA PQRQMSPPVE WNANSPTPRS SGVRAAGLSA RISSDRALLP RHPTAGEENL
     SRSHKSGQAP RPASRCQVLG SQVEIFNSLV RGNRVVELDV RSMEHKFSTQ EHIMFHIVRK
     LDLPSTLPGC AGRVSELEQD LGLATTDRLG LNDCQVLVRS KPGVTQTDNS TPYLARHVGE
     RIGLDHTVPA LTVNRLCGSG FQSLITAAQH IKLGEADTCV TGGAEAMSMS PFTLSGSNRT
     GMRFGQDQKL EDSLFATLTD LNPRGEKTPM GITAENLGKK YGITRQDADN YALQSQQRYA
     QGLKDGAFKD EIAPITLKTR KGDVVVDADE HPKPQTTIEA LNKLPSVFIP KTGTVSPGNA
     SGISDGGAAN IVMGENAVKA TGAKPLARVV SYAWSACEPS IMGIGPVASV HKALERAGLS
     LGQMDLIDIN EAFATQWLAV AKELDLPNDK SNMFGGAIAV GHPLAASGAR IIANLVHNLH
     RLDKKYALGG ACIGGGQGIA VILERV
//
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