MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
Description | RecName: Full=Actinorhodin polyketide putative beta-ketoacyl synthase 1; EC=2.3.1.-; AltName: Full=actI ORF1; |
![]() |
|
MyHits synonyms | KASA_STRCO , Q02059 , Q93IZ1 , 6B5BEE32B5241C60 |
![]() Legends: 1, ACT_SITE {ECO:0000255|PROSITE-ProRule:PRU10022}; 2, ipat:B_KETOACYL_SYNTHASE [T]; 3, STRAND {ECO:0000244|PDB:1TQY}; 4, HELIX {ECO:0000244|PDB:1TQY}; 5, TURN {ECO:0000244|PDB:1TQY}.
| |
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 15-MAR-2017, entry version 109. 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., RA Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., RA Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., RA Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., RA Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., RA Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., RA Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., RA Hopwood D.A.; RT "Complete genome sequence of the model actinomycete Streptomyces RT coelicolor 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., RA Malpartida F.; RT "Nucleotide sequence and deduced functions of a set of cotranscribed RT genes of Streptomyces coelicolor A3(2) including the polyketide RT synthase for the antibiotic actinorhodin."; RL J. Biol. Chem. 267:19278-19290(1992). CC -!- PATHWAY: Antibiotic biosynthesis; actinorhodin biosynthesis. CC -!- SIMILARITY: Belongs to the beta-ketoacyl-ACP synthases family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA45043.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- 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 ProteinModelPortal; Q02059; -. DR SMR; Q02059; -. DR IntAct; Q02059; 1. DR STRING; 100226.SCO5087; -. DR PRIDE; Q02059; -. DR EnsemblBacteria; CAC44200; CAC44200; CAC44200. DR GeneID; 1100528; -. DR GeneID; 29663939; -. DR KEGG; sco:SCO5087; -. DR PATRIC; 23740014; VBIStrCoe124346_5167. DR eggNOG; ENOG4105C0Q; Bacteria. DR eggNOG; COG0304; LUCA. DR HOGENOM; HOG000060166; -. DR InParanoid; Q02059; -. DR KO; K05551; -. DR OMA; MGPNNTI; -. DR OrthoDB; POG091H018O; -. DR PhylomeDB; Q02059; -. DR UniPathway; UPA00173; -. DR EvolutionaryTrace; Q02059; -. DR Proteomes; UP000001973; Chromosome. DR GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW. DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.47.10; -; 2. 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 Pfam; PF00109; ketoacyl-synt; 1. DR Pfam; PF02801; Ketoacyl-synt_C; 1. DR SMART; SM00825; PKS_KS; 1. DR SUPFAM; SSF53901; SSF53901; 2. DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Antibiotic biosynthesis; KW Complete proteome; Reference proteome; Transferase. FT CHAIN 1 467 Actinorhodin polyketide putative beta- FT ketoacyl synthase 1. FT /FTId=PRO_0000180342. FT ACT_SITE 212 212 {ECO:0000255|PROSITE-ProRule:PRU10022}. FT STRAND 48 57 {ECO:0000244|PDB:1TQY}. FT STRAND 60 62 {ECO:0000244|PDB:1TQY}. FT HELIX 63 72 {ECO:0000244|PDB:1TQY}. FT STRAND 77 79 {ECO:0000244|PDB:1TQY}. FT STRAND 92 94 {ECO:0000244|PDB:1TQY}. FT HELIX 100 103 {ECO:0000244|PDB:1TQY}. FT HELIX 107 112 {ECO:0000244|PDB:1TQY}. FT HELIX 115 131 {ECO:0000244|PDB:1TQY}. FT TURN 135 137 {ECO:0000244|PDB:1TQY}. FT HELIX 140 142 {ECO:0000244|PDB:1TQY}. FT STRAND 143 148 {ECO:0000244|PDB:1TQY}. FT HELIX 154 165 {ECO:0000244|PDB:1TQY}. FT TURN 166 169 {ECO:0000244|PDB:1TQY}. FT HELIX 175 177 {ECO:0000244|PDB:1TQY}. FT TURN 180 182 {ECO:0000244|PDB:1TQY}. FT HELIX 183 186 {ECO:0000244|PDB:1TQY}. FT HELIX 190 199 {ECO:0000244|PDB:1TQY}. FT STRAND 205 208 {ECO:0000244|PDB:1TQY}. FT HELIX 211 213 {ECO:0000244|PDB:1TQY}. FT HELIX 214 227 {ECO:0000244|PDB:1TQY}. FT STRAND 232 240 {ECO:0000244|PDB:1TQY}. FT HELIX 245 253 {ECO:0000244|PDB:1TQY}. FT HELIX 264 266 {ECO:0000244|PDB:1TQY}. FT STRAND 283 291 {ECO:0000244|PDB:1TQY}. FT HELIX 292 297 {ECO:0000244|PDB:1TQY}. FT STRAND 304 313 {ECO:0000244|PDB:1TQY}. FT HELIX 326 339 {ECO:0000244|PDB:1TQY}. FT HELIX 343 345 {ECO:0000244|PDB:1TQY}. FT STRAND 348 350 {ECO:0000244|PDB:1TQY}. FT HELIX 357 370 {ECO:0000244|PDB:1TQY}. FT HELIX 372 377 {ECO:0000244|PDB:1TQY}. FT HELIX 384 387 {ECO:0000244|PDB:1TQY}. FT TURN 391 393 {ECO:0000244|PDB:1TQY}. FT HELIX 394 408 {ECO:0000244|PDB:1TQY}. FT STRAND 419 421 {ECO:0000244|PDB:1TQY}. FT STRAND 430 432 {ECO:0000244|PDB:1TQY}. FT STRAND 439 447 {ECO:0000244|PDB:1TQY}. FT TURN 448 450 {ECO:0000244|PDB:1TQY}. FT STRAND 451 458 {ECO:0000244|PDB:1TQY}. FT HELIX 460 465 {ECO:0000244|PDB:1TQY}. CC -------------------------------------------------------------------------- CC The following FT lines are automated annotations from the MyHits database. CC -------------------------------------------------------------------------- FT MYHIT 48 462 ismart:PKS_KS [T] FT MYHIT 303 417 ipfam:Ketoacyl-synt_C [T] FT MYHIT 46 294 ipfam:ketoacyl-synt [T] FT MYHIT 203 219 ipat:B_KETOACYL_SYNTHASE [T] 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 // |