ACTI2_STRCO
ID ACTI2_STRCO Reviewed; 407 AA.
AC Q02062;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Actinorhodin polyketide putative beta-ketoacyl synthase 2;
DE EC=2.3.1.-;
DE AltName: Full=actI ORF2;
GN OrderedLocusNames=SCO5088; ORFNames=SCBAC28G1.14;
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 [GENOMIC DNA].
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).
RN [2]
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).
CC -!- MISCELLANEOUS: This putative ketoacyl synthase lacks the active site
CC cysteine.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000305}.
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DR EMBL; X63449; CAA45044.1; -; Genomic_DNA.
DR EMBL; AL939122; CAC44201.1; -; Genomic_DNA.
DR PIR; S25841; S25841.
DR RefSeq; NP_629238.1; NC_003888.3.
DR RefSeq; WP_011030048.1; NZ_VNID01000008.1.
DR PDB; 1TQY; X-ray; 2.00 A; B/D/F/H=2-407.
DR PDBsum; 1TQY; -.
DR AlphaFoldDB; Q02062; -.
DR SMR; Q02062; -.
DR IntAct; Q02062; 1.
DR STRING; 100226.SCO5088; -.
DR GeneID; 1100529; -.
DR KEGG; sco:SCO5088; -.
DR PATRIC; fig|100226.15.peg.5168; -.
DR eggNOG; COG0304; Bacteria.
DR HOGENOM; CLU_000022_69_2_11; -.
DR InParanoid; Q02062; -.
DR OMA; TDHMTRL; -.
DR PhylomeDB; Q02062; -.
DR EvolutionaryTrace; Q02062; -.
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; 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; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Antibiotic biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..407
FT /note="Actinorhodin polyketide putative beta-ketoacyl
FT synthase 2"
FT /id="PRO_0000180349"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:1TQY"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 18..26
FT /evidence="ECO:0007829|PDB:1TQY"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1TQY"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:1TQY"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:1TQY"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 70..85
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:1TQY"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 109..121
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 139..148
FT /evidence="ECO:0007829|PDB:1TQY"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 163..176
FT /evidence="ECO:0007829|PDB:1TQY"
FT STRAND 180..188
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 193..200
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:1TQY"
FT STRAND 230..238
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 239..245
FT /evidence="ECO:0007829|PDB:1TQY"
FT STRAND 251..261
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 273..284
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:1TQY"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 302..316
FT /evidence="ECO:0007829|PDB:1TQY"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 326..329
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 337..351
FT /evidence="ECO:0007829|PDB:1TQY"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:1TQY"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:1TQY"
FT STRAND 382..390
FT /evidence="ECO:0007829|PDB:1TQY"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:1TQY"
FT STRAND 394..402
FT /evidence="ECO:0007829|PDB:1TQY"
SQ SEQUENCE 407 AA; 42550 MW; 59FC75A5A0D94632 CRC64;
MSVLITGVGV VAPNGLGLAP YWSAVLDGRH GLGPVTRFDV SRYPATLAGQ IDDFHAPDHI
PGRLLPQTDP STRLALTAAD WALQDAKADP ESLTDYDMGV VTANACGGFD FTHREFRKLW
SEGPKSVSVY ESFAWFYAVN TGQISIRHGM RGPSSALVAE QAGGLDALGH ARRTIRRGTP
LVVSGGVDSA LDPWGWVSQI ASGRISTATD PDRAYLPFDE RAAGYVPGEG GAILVLEDSA
AAEARGRHDA YGELAGCAST FDPAPGSGRP AGLERAIRLA LNDAGTGPED VDVVFADGAG
VPELDAAEAR AIGRVFGREG VPVTVPKTTT GRLYSGGGPL DVVTALMSLR EGVIAPTAGV
TSVPREYGID LVLGEPRSTA PRTALVLARG RWGFNSAAVL RRFAPTP