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THIL1_DICDI
ID   THIL1_DICDI             Reviewed;         414 AA.
AC   Q86AD9; Q55AV9;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Probable acetyl-CoA acetyltransferase;
DE            EC=2.3.1.9;
DE   AltName: Full=Acetoacetyl-CoA thiolase;
GN   ORFNames=DDB_G0271544;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Ohmachi T., Tanaka T.;
RT   "Cloning and expression of mitochondrial acetoacetyl-CoA thiolase from
RT   Dictyostelium discoideum.";
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=12097910; DOI=10.1038/nature00847;
RA   Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA   Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA   Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA   Noegel A.A.;
RT   "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL   Nature 418:79-85(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036,
CC         ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9;
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000305}.
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DR   EMBL; AB212872; BAD98242.1; -; mRNA.
DR   EMBL; AAFI02000006; EAL71636.1; -; Genomic_DNA.
DR   RefSeq; XP_645587.1; XM_640495.1.
DR   AlphaFoldDB; Q86AD9; -.
DR   SMR; Q86AD9; -.
DR   STRING; 44689.DDB0231621; -.
DR   PaxDb; Q86AD9; -.
DR   EnsemblProtists; EAL71636; EAL71636; DDB_G0271544.
DR   GeneID; 8618040; -.
DR   KEGG; ddi:DDB_G0271544; -.
DR   dictyBase; DDB_G0271544; acat.
DR   eggNOG; KOG1390; Eukaryota.
DR   HOGENOM; CLU_031026_0_1_1; -.
DR   InParanoid; Q86AD9; -.
DR   OMA; TNVCCTT; -.
DR   PhylomeDB; Q86AD9; -.
DR   BRENDA; 2.3.1.9; 1939.
DR   Reactome; R-DDI-70895; Branched-chain amino acid catabolism.
DR   Reactome; R-DDI-77108; Utilization of Ketone Bodies.
DR   Reactome; R-DDI-77111; Synthesis of Ketone Bodies.
DR   PRO; PR:Q86AD9; -.
DR   Proteomes; UP000002195; Chromosome 2.
DR   GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR   GO; GO:0005739; C:mitochondrion; IDA:dictyBase.
DR   GO; GO:0005777; C:peroxisome; IDA:dictyBase.
DR   GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IDA:dictyBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006696; P:ergosterol biosynthetic process; ISS:dictyBase.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 1.
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   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.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Metal-binding; Potassium; Reference proteome; Transferase.
FT   CHAIN           1..414
FT                   /note="Probable acetyl-CoA acetyltransferase"
FT                   /id="PRO_0000327943"
FT   ACT_SITE        110
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        370
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        400
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         205
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         205
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         244..246
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         249
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         266
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         268
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
FT   BINDING         269
FT                   /ligand="CoA"
FT                   /ligand_id="ChEBI:CHEBI:57287"
FT                   /evidence="ECO:0000250"
FT   BINDING         366
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   414 AA;  43466 MW;  B4D9267F4A4590CB CRC64;
     MISNLSKVLN SNVKRMYTTA KNLESVVIVS AVRTPIGSIG GSLSTIPGTK LSSITIEEAV
     KRAGIKPSDV DEAIIGNVIS ANLGQAPARQ CALGAGLEQK TITTTINKVC SSGMKAIVFG
     AQSIALGHSK TVVAGGFESM SQVPYYADKM RFGAKYGNQT FIDGLVRDGL ADAYNGSAMG
     VCGDDCADKY KITREQQDKF AVDSYLRALE AQKNGFFNDE IVQVPIVGRG GKVTYVVEDE
     EPKKVLFDKI PNLKPAFTPN GTVTPANASK LNDGASSVIL MSESHAKELG LKPLARIIGY
     ADAEQAPIEF PTAPALAIPK ALKNAGINMS QVDLFEINEA FAVVGLANAK ILDIDHNKLN
     VNGGAVALGH PIGSSGCRIV VTLTHLLQNK NLKYGVAAIC NGGGGSTALV LEKL
 
 
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