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FADA4_MYCLE
ID   FADA4_MYCLE             Reviewed;         393 AA.
AC   P46707;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Probable acetyl-CoA acetyltransferase;
DE            EC=2.3.1.9;
DE   AltName: Full=Acetoacetyl-CoA thiolase;
GN   Name=fadA4; OrderedLocusNames=ML1158; ORFNames=B1549_C1_166;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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         Evidence={ECO:0000255|PROSITE-ProRule:PRU10020};
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000305}.
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DR   EMBL; U00014; AAA50881.1; -; Genomic_DNA.
DR   EMBL; AL583921; CAC31539.1; -; Genomic_DNA.
DR   PIR; S72804; S72804.
DR   RefSeq; NP_301848.1; NC_002677.1.
DR   RefSeq; WP_010908172.1; NC_002677.1.
DR   AlphaFoldDB; P46707; -.
DR   SMR; P46707; -.
DR   STRING; 272631.ML1158; -.
DR   PRIDE; P46707; -.
DR   EnsemblBacteria; CAC31539; CAC31539; CAC31539.
DR   KEGG; mle:ML1158; -.
DR   PATRIC; fig|272631.5.peg.2090; -.
DR   Leproma; ML1158; -.
DR   eggNOG; COG0183; Bacteria.
DR   HOGENOM; CLU_031026_0_0_11; -.
DR   OMA; ICPSIAI; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0003985; F:acetyl-CoA C-acetyltransferase 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   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.
DR   PROSITE; PS00099; THIOLASE_3; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..393
FT                   /note="Probable acetyl-CoA acetyltransferase"
FT                   /id="PRO_0000206457"
FT   ACT_SITE        88
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        349
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT   ACT_SITE        379
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
SQ   SEQUENCE   393 AA;  40529 MW;  9055A3BC878D47E1 CRC64;
     MTTSVIVTGA RTPIGKLMGS LKDFSASDLG AITIAAALKK ANVAPSIVQY VIIGQVLTAG
     AGQMPARQAA VAAGIGWDVP ALTINKMCLS GLDAIALADQ LIRAGEFDVV VAGGQESMTK
     APHLLMDSRS GYKYGDVTIV DHLAYDGLHD VFTNQPMGAL TEQRNDVEKF TRQEQDEFAA
     RSHQKAAAAW KDGVFADEVV PVSIPQSKGD SLQFTEDEGI RANTSAESLA GLKPAFRCGG
     TITPGSASQI SDGAATVVVM NKEKAQQLGL TWLVEIGAHG VVAGPDSTLQ SQPANAIKKA
     VDREGISVEQ LDVVEINEAF AAVALASARE LGIAPELVNV NGGAIAVGHP LGMSGARITL
     HVALELARRG SGYGVAALCG AGGQGDALIL RAV
 
 
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