ACTI1_STRCO
ID ACTI1_STRCO Reviewed; 467 AA.
AC Q02059; Q93IZ1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 17-JAN-2003, sequence version 2.
DT 25-MAY-2022, entry version 126.
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; DOI=10.1016/s0021-9258(18)41772-3;
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};
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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; 1TQY; X-ray; 2.00 A; A/C/E/G=45-467.
DR PDBsum; 1TQY; -.
DR AlphaFoldDB; Q02059; -.
DR SMR; Q02059; -.
DR IntAct; Q02059; 1.
DR STRING; 100226.SCO5087; -.
DR GeneID; 1100528; -.
DR KEGG; sco:SCO5087; -.
DR PATRIC; fig|100226.15.peg.5167; -.
DR eggNOG; COG0304; Bacteria.
DR HOGENOM; CLU_000022_69_2_11; -.
DR InParanoid; Q02059; -.
DR OMA; MNNNFAF; -.
DR PhylomeDB; Q02059; -.
DR UniPathway; UPA00173; -.
DR EvolutionaryTrace; Q02059; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 CDD; cd00834; KAS_I_II; 1.
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;
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 REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT STRAND 48..57
FT /evidence="ECO:0007829|PDB:1TQY"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 63..72
FT /evidence="ECO:0007829|PDB:1TQY"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1TQY"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 107..112
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 115..131
FT /evidence="ECO:0007829|PDB:1TQY"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:1TQY"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 154..165
FT /evidence="ECO:0007829|PDB:1TQY"
FT TURN 166..169
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:1TQY"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 190..199
FT /evidence="ECO:0007829|PDB:1TQY"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 214..227
FT /evidence="ECO:0007829|PDB:1TQY"
FT STRAND 232..240
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 245..253
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:1TQY"
FT STRAND 283..291
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 292..297
FT /evidence="ECO:0007829|PDB:1TQY"
FT STRAND 304..313
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 326..339
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:1TQY"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 357..370
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 372..377
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 384..387
FT /evidence="ECO:0007829|PDB:1TQY"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 394..408
FT /evidence="ECO:0007829|PDB:1TQY"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:1TQY"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:1TQY"
FT STRAND 439..447
FT /evidence="ECO:0007829|PDB:1TQY"
FT TURN 448..450
FT /evidence="ECO:0007829|PDB:1TQY"
FT STRAND 451..458
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 460..465
FT /evidence="ECO:0007829|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
