ID G3ARF9_SPAPN Unreviewed; 408 AA.
AC G3ARF9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN ORFNames=SPAPADRAFT_61847 {ECO:0000313|EMBL:EGW31280.1};
OS Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN [1] {ECO:0000313|EMBL:EGW31280.1, ECO:0000313|Proteomes:UP000000709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
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 Evidence={ECO:0000256|ARBA:ARBA00000617};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000256|ARBA:ARBA00004872}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
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DR EMBL; GL996503; EGW31280.1; -; Genomic_DNA.
DR RefSeq; XP_007376058.1; XM_007375996.1.
DR AlphaFoldDB; G3ARF9; -.
DR STRING; 619300.G3ARF9; -.
DR GeneID; 18874081; -.
DR KEGG; spaa:SPAPADRAFT_61847; -.
DR eggNOG; KOG1389; Eukaryota.
DR HOGENOM; CLU_031026_1_1_1; -.
DR InParanoid; G3ARF9; -.
DR OMA; TATCGVE; -.
DR OrthoDB; 5481312at2759; -.
DR Proteomes; UP000000709; 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; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR PANTHER; PTHR43853:SF8; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 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:0000256|RuleBase:RU003557};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000000709};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 14..280
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 288..406
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT REGION 201..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..221
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 99
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 366
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 394
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 408 AA; 43842 MW; E721499387DD0195 CRC64;
MTKAQHLQKN PDDVVIVAAY RSALAKGGKG SFKDTTTEVL LKTFTEEFLK KTKVDPSIIQ
DSAIGNVLKH RAGDFEHRGA LMAGGLPHTV PFVALNRQCS SGLMAISLIA NRIKCGEIEC
GLAGGVESMS KDYGPQAIPR IDPSLENDPE FIKNGTSMGI TNENIAAKFN ISRDYQDEFA
AQSYAKAEKA QREGKFKDEI LPLKVQIEDD DDDDDEDDDE DKPPKMKEIT VDKDEGIRPG
VTKEKLAKIK PAFKDDGVSH AGNSSQVTDG VALVLLMKRS FAEKHGFKPQ AKFVNCSVAG
VPPEIMGIGP AVAIPKVLKT TGLSVSDIDI YEINEAFAGQ CLYSIDTVGI DRKKVNLNGG
AIAMGHPLGC TGARQYATIL RIMKPGEIGV TSMCIGTGMG AASVLVRE
//