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Database: UniProt
Entry: A1D2F8_NEOFI
LinkDB: A1D2F8_NEOFI
Original site: A1D2F8_NEOFI 
ID   A1D2F8_NEOFI            Unreviewed;       435 AA.
AC   A1D2F8;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 86.
DE   SubName: Full=3-ketoacyl-CoA ketothiolase (Kat1), putative {ECO:0000313|EMBL:EAW22601.1};
GN   ORFNames=NFIA_012900 {ECO:0000313|EMBL:EAW22601.1};
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW22601.1, ECO:0000313|Proteomes:UP000006702};
RN   [1] {ECO:0000313|Proteomes:UP000006702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC   NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000256|ARBA:ARBA00001958};
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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; DS027688; EAW22601.1; -; Genomic_DNA.
DR   RefSeq; XP_001264498.1; XM_001264497.1.
DR   AlphaFoldDB; A1D2F8; -.
DR   STRING; 331117.A1D2F8; -.
DR   EnsemblFungi; EAW22601; EAW22601; NFIA_012900.
DR   GeneID; 4591689; -.
DR   KEGG; nfi:NFIA_012900; -.
DR   VEuPathDB; FungiDB:NFIA_012900; -.
DR   eggNOG; KOG1389; Eukaryota.
DR   HOGENOM; CLU_031026_1_1_1; -.
DR   OMA; DYYWGMG; -.
DR   OrthoDB; 5481312at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
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; 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:SF10; KETOTHIOLASE (KAT1), PUTATIVE (AFU_ORTHOLOGUE AFUA_1G12650)-RELATED; 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.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006702};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003557}.
FT   DOMAIN          49..303
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          312..430
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        133
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        389
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        419
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   435 AA;  46094 MW;  76A0D5615F7C3576 CRC64;
     MAADRLSSLL NHLRPSGGSG VSAMYASSLA QPRFIILTNA STQKNPDDVV ITLALRTPLT
     KAAKGGFKDT ELDYMIYALL KEVVQKSKLD PALIEDVCLG NVNDGKAAYL VRAAALAAGI
     PHTAGASSVN RFCSSGLKAV QDIANQIQLG AIDVGVAVGA ELMSAGGDRL PRPFNEEVLK
     NQEAADCMQP MGQTSENVGA DFNITREMQD TYAAESFRRA EAAQKAGWFD DEIVPITTKV
     KDPKTGEVKT VTLTRDEGIR YGTTVEALNK IRPAFPQFGN RTTGGNASQV TDGAAAILLM
     RRSKAIELNQ PILAKFCGAT VAGVPPRVMG IGPTAAIPKL LSKFNLSKDD IDIYEINEAF
     ASMAVYCLKN LGLNHAKVNP RGGAIALGHP LGATGARQIC TILSEARRTK SKILVTSMCI
     GTGQGMAGLF VNEQI
//
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