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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
 
 
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