(data stored in SCRATCH zone)

SWISSPROT: B4SRW3_STRM5

ID   B4SRW3_STRM5            Unreviewed;       431 AA.
AC   B4SRW3;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   16-JAN-2019, entry version 57.
DE   SubName: Full=Acetyl-CoA acetyltransferase {ECO:0000313|EMBL:ACF49833.1};
DE            EC=2.3.1.16 {ECO:0000313|EMBL:ACF49833.1};
GN   OrderedLocusNames=Smal_0128 {ECO:0000313|EMBL:ACF49833.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF49833.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF49833.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF49833.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thiolase family.
CC       {ECO:0000256|RuleBase:RU003557}.
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DR   EMBL; CP001111; ACF49833.1; -; Genomic_DNA.
DR   STRING; 391008.Smal_0128; -.
DR   EnsemblBacteria; ACF49833; ACF49833; Smal_0128.
DR   KEGG; smt:Smal_0128; -.
DR   eggNOG; ENOG4105CHU; Bacteria.
DR   eggNOG; COG0183; LUCA.
DR   HOGENOM; HOG000012240; -.
DR   KO; K00626; -.
DR   OMA; AWESEDY; -.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020617; Thiolase_C.
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.
PE   3: Inferred from homology;
DR   PRODOM; B4SRW3.
DR   SWISS-2DPAGE; B4SRW3.
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557,
KW   ECO:0000313|EMBL:ACF49833.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Transferase {ECO:0000256|RuleBase:RU003557,
KW   ECO:0000313|EMBL:ACF49833.1}.
FT   DOMAIN       12    282       Thiolase_N. {ECO:0000259|Pfam:PF00108}.
FT   DOMAIN      291    431       Thiolase_C. {ECO:0000259|Pfam:PF02803}.
FT   ACT_SITE     96     96       Acyl-thioester intermediate.
FT                                {ECO:0000256|PIRSR:PIRSR000429-1}.
FT   ACT_SITE    388    388       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000429-1}.
FT   ACT_SITE    418    418       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000429-1}.
SQ   SEQUENCE   431 AA;  45771 MW;  A6788BB93BE0A907 CRC64;
     MPGISMPNAR PVAILGGVRI PFCRQNTAYS DVGNLGMSVR TLGALVERFG LHGQQLGEVA
     MGAVIKHSSD WNLGREATLS SGLSPLTPGI TLQRACGTSL DSIITVANKI ALGQIESGIG
     GGSDTTSDVP IVYGKKLRAR LLAANRAKST GDKIRALTAG FKFSELKPEF PGVAEPRTGK
     SMGDHCEDMA KEWNISRDSQ DEWAVSSHKK LAAAYERGFF SDLIAPFRGV ERDNILRADT
     SLEKLATLKP AFDKVSGRGT LTAANSTPLT DGAAAVLLAS EEWARAHGHE PQAYLRDAHV
     SAVDFVHGEG LLMAPTVAVP EMLKRNGLTL QDFDIYEIHE AFAAQVLCTL RAWESEDYCR
     NRLGLDAPMG RIDPDKINLL GSSLATGHPF AATGARVIAT AAKQLAERGG GRALVSICTA
     GGMGVVAIVE R
//

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