(data stored in ACNUC1104 zone)

SWISSPROT: KASA_STRCO

ID   KASA_STRCO              Reviewed;         467 AA.
AC   Q02059; Q93IZ1;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   17-JAN-2003, sequence version 2.
DT   11-DEC-2019, entry version 116.
DE   RecName: Full=Actinorhodin polyketide putative beta-ketoacyl synthase 1;
DE            EC=2.3.1.-;
DE   AltName: Full=actI ORF1;
GN   OrderedLocusNames=SCO5087; ORFNames=SCBAC28G1.13;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-467.
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=1527048;
RA   Fernandez-Moreno M.A., Martinez E., Boto L., Hopwood D.A., Malpartida F.;
RT   "Nucleotide sequence and deduced functions of a set of cotranscribed genes
RT   of Streptomyces coelicolor A3(2) including the polyketide synthase for the
RT   antibiotic actinorhodin.";
RL   J. Biol. Chem. 267:19278-19290(1992).
CC   -!- PATHWAY: Antibiotic biosynthesis; actinorhodin biosynthesis.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC       synthases family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA45043.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AL939122; CAC44200.1; -; Genomic_DNA.
DR   EMBL; X63449; CAA45043.1; ALT_INIT; Genomic_DNA.
DR   PIR; S25840; S25840.
DR   RefSeq; NP_629237.1; NC_003888.3.
DR   RefSeq; WP_003973891.1; NC_003888.3.
DR   PDB; 1QXG; Model; -; A=45-461.
DR   PDB; 1TQY; X-ray; 2.00 A; A/C/E/G=45-467.
DR   PDBsum; 1QXG; -.
DR   PDBsum; 1TQY; -.
DR   SMR; Q02059; -.
DR   IntAct; Q02059; 1.
DR   STRING; 100226.SCO5087; -.
DR   PRIDE; Q02059; -.
DR   EnsemblBacteria; CAC44200; CAC44200; CAC44200.
DR   GeneID; 1100528; -.
DR   KEGG; sco:SCO5087; -.
DR   PATRIC; fig|100226.15.peg.5167; -.
DR   eggNOG; ENOG4105C0Q; Bacteria.
DR   eggNOG; COG0304; LUCA.
DR   HOGENOM; HOG000060166; -.
DR   InParanoid; Q02059; -.
DR   KO; K05551; -.
DR   OMA; TACSIGN; -.
DR   PhylomeDB; Q02059; -.
DR   UniPathway; UPA00173; -.
DR   EvolutionaryTrace; Q02059; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IBA:GO_Central.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR000794; Beta-ketoacyl_synthase.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR11712; PTHR11712; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF53901; SSF53901; 1.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q02059.
DR   SWISS-2DPAGE; Q02059.
KW   3D-structure; Acyltransferase; Antibiotic biosynthesis; Reference proteome;
KW   Transferase.
FT   CHAIN           1..467
FT                   /note="Actinorhodin polyketide putative beta-ketoacyl
FT                   synthase 1"
FT                   /id="PRO_0000180342"
FT   ACT_SITE        212
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT   STRAND          48..57
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   STRAND          60..62
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   HELIX           63..72
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   STRAND          77..79
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   STRAND          92..94
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   HELIX           100..103
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   HELIX           107..112
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   HELIX           115..131
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   TURN            135..137
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   HELIX           140..142
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   STRAND          143..148
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   HELIX           154..165
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   TURN            166..169
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   HELIX           175..177
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   TURN            180..182
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   HELIX           183..186
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   HELIX           190..199
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   STRAND          205..208
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   HELIX           211..213
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   HELIX           214..227
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   STRAND          232..240
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   HELIX           245..253
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   HELIX           264..266
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   STRAND          283..291
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   HELIX           292..297
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   STRAND          304..313
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   HELIX           326..339
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   HELIX           343..345
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   STRAND          348..350
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   HELIX           357..370
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   HELIX           372..377
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   HELIX           384..387
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   TURN            391..393
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   HELIX           394..408
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   STRAND          419..421
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   STRAND          430..432
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   STRAND          439..447
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   TURN            448..450
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   STRAND          451..458
FT                   /evidence="ECO:0000244|PDB:1TQY"
FT   HELIX           460..465
FT                   /evidence="ECO:0000244|PDB:1TQY"
SQ   SEQUENCE   467 AA;  49504 MW;  6B5BEE32B5241C60 CRC64;
     MPLDAAPVDP ASRGPVSAFE PPSSHGADDD DDHRTNASKE LFGLKRRVVI TGVGVRAPGG
     NGTRQFWELL TSGRTATRRI SFFDPSPYRS QVAAEADFDP VAEGFGPREL DRMDRASQFA
     VACAREAFAA SGLDPDTLDP ARVGVSLGSA VAAATSLERE YLLLSDSGRD WEVDAAWLSR
     HMFDYLVPSV MPAEVAWAVG AEGPVTMVST GCTSGLDSVG NAVRAIEEGS ADVMFAGAAD
     TPITPIVVAC FDAIRATTAR NDDPEHASRP FDGTRDGFVL AEGAAMFVLE DYDSALARGA
     RIHAEISGYA TRCNAYHMTG LKADGREMAE TIRVALDESR TDATDIDYIN AHGSGTRQND
     RHETAAYKRA LGEHARRTPV SSIKSMVGHS LGAIGSLEIA ACVLALEHGV VPPTANLRTS
     DPECDLDYVP LEARERKLRS VLTVGSGFGG FQSAMVLRDA ETAGAAA
//

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