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
//