(data stored in ACNUC7421 zone)

SWISSPROT: A0A0H2ZK25_PSEAB

ID   A0A0H2ZK25_PSEAB        Unreviewed;       401 AA.
AC   A0A0H2ZK25;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   30-AUG-2017, entry version 11.
DE   SubName: Full=Beta-ketoadipyl CoA thiolase PcaF {ECO:0000313|EMBL:ABJ15177.1};
GN   Name=pcaF {ECO:0000313|EMBL:ABJ15177.1};
GN   OrderedLocusNames=PA14_02790 {ECO:0000313|EMBL:ABJ15177.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15177.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15177.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15177.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- SIMILARITY: Belongs to the thiolase family.
CC       {ECO:0000256|RuleBase:RU003557}.
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DR   EMBL; CP000438; ABJ15177.1; -; Genomic_DNA.
DR   RefSeq; WP_003110233.1; NC_008463.1.
DR   EnsemblBacteria; ABJ15177; ABJ15177; PA14_02790.
DR   KEGG; pau:PA14_02790; -.
DR   KO; K07823; -.
DR   OMA; TDMRWGA; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0019619; P:3,4-dihydroxybenzoate catabolic process; IEA:InterPro.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR012793; PcaF.
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   TIGRFAMs; TIGR02430; pcaF; 1.
DR   PROSITE; PS00098; THIOLASE_1; 1.
DR   PROSITE; PS00737; THIOLASE_2; 1.
DR   PROSITE; PS00099; THIOLASE_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0H2ZK25.
DR   SWISS-2DPAGE; A0A0H2ZK25.
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   Transferase {ECO:0000256|RuleBase:RU003557}.
FT   DOMAIN        5    268       Thiolase_N. {ECO:0000259|Pfam:PF00108}.
FT   DOMAIN      277    400       Thiolase_C. {ECO:0000259|Pfam:PF02803}.
FT   ACT_SITE     91     91       Acyl-thioester intermediate.
FT                                {ECO:0000256|PIRSR:PIRSR000429-1}.
FT   ACT_SITE    357    357       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000429-1}.
FT   ACT_SITE    387    387       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000429-1}.
SQ   SEQUENCE   401 AA;  42074 MW;  A064241A93FFBB7F CRC64;
     MSREVFICDA VRTPIGRFGG SLSAVRADDL AAVPLKALVE RNPGVDWSAL DEVFLGCANQ
     AGEDNRNVAR MALLLAGLPE SVPGVTLNRL CASGMDAIGT AFRAIACGEM ELAIAGGVES
     MSRAPYVMGK ADSAFGRGQK IEDTTIGWRF VNPLMKEQYG IDPMPQTADN VADDYRVSRA
     DQDAFALRSQ QRAGRAQAAG FFAEEIVPVT IRGRKGDTLV EYDEHPRPDT TLEALARLKP
     VNGPEKTVTA GNASGVNDGA AALVLASAEA VEKHGLTPRA RVLGMASAGV APRIMGIGPV
     PAVRKLLRRL DLAIDAFDVI ELNEAFASQG LACLRELGVA DDSEKVNPNG GAIALGHPLG
     MSGARLVLTA LHQLEKSGGR RGLATMCVGV GQGLALAIER V
//

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