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Q02059 (KASA_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Actinorhodin polyketide putative beta-ketoacyl synthase 1

EC=2.3.1.-
Alternative name(s):
actI ORF1
Gene names
Ordered Locus Names:SCO5087
ORF Names:SCBAC28G1.13
OrganismStreptomyces coelicolor
Taxonomic identifier1902 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length467 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Pathway

Antibiotic biosynthesis; actinorhodin biosynthesis.

Sequence similarities

Belongs to the beta-ketoacyl-ACP synthases family.

Sequence caution

The sequence CAA45043.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processAntibiotic biosynthesis
   Molecular functionAcyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processantibiotic biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functiontransferase activity, transferring acyl groups

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 467467Actinorhodin polyketide putative beta-ketoacyl synthase 1
PRO_0000180342

Sites

Active site2121 By similarity

Secondary structure

........................................................................ 467
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q02059 [UniParc].

Last modified January 17, 2003. Version 2.
Checksum: 6B5BEE32B5241C60

FASTA46749,504
        10         20         30         40         50         60 
MPLDAAPVDP ASRGPVSAFE PPSSHGADDD DDHRTNASKE LFGLKRRVVI TGVGVRAPGG 

        70         80         90        100        110        120 
NGTRQFWELL TSGRTATRRI SFFDPSPYRS QVAAEADFDP VAEGFGPREL DRMDRASQFA 

       130        140        150        160        170        180 
VACAREAFAA SGLDPDTLDP ARVGVSLGSA VAAATSLERE YLLLSDSGRD WEVDAAWLSR 

       190        200        210        220        230        240 
HMFDYLVPSV MPAEVAWAVG AEGPVTMVST GCTSGLDSVG NAVRAIEEGS ADVMFAGAAD 

       250        260        270        280        290        300 
TPITPIVVAC FDAIRATTAR NDDPEHASRP FDGTRDGFVL AEGAAMFVLE DYDSALARGA 

       310        320        330        340        350        360 
RIHAEISGYA TRCNAYHMTG LKADGREMAE TIRVALDESR TDATDIDYIN AHGSGTRQND 

       370        380        390        400        410        420 
RHETAAYKRA LGEHARRTPV SSIKSMVGHS LGAIGSLEIA ACVLALEHGV VPPTANLRTS 

       430        440        450        460 
DPECDLDYVP LEARERKLRS VLTVGSGFGG FQSAMVLRDA ETAGAAA 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)."
Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. expand/collapse author list , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.
Nature 417:141-147(2002) [PubMed: 12000953] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-471 / A3(2) / M145.
[2]"Nucleotide sequence and deduced functions of a set of cotranscribed genes of Streptomyces coelicolor A3(2) including the polyketide synthase for the antibiotic actinorhodin."
Fernandez-Moreno M.A., Martinez E., Boto L., Hopwood D.A., Malpartida F.
J. Biol. Chem. 267:19278-19290(1992) [PubMed: 1527048] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-467.
Strain: ATCC BAA-471 / A3(2) / M145.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL939122 Genomic DNA. Translation: CAC44200.1.
X63449 Genomic DNA. Translation: CAA45043.1. Different initiation.
PIRS25840.
RefSeqNP_629237.1. NC_003888.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QXGmodel-A45-461[»]
1TQYX-ray2.00A/C/E/G45-467[»]
ProteinModelPortalQ02059.
SMRQ02059. Positions 46-466.
ModBaseSearch...

Protein-protein interaction databases

IntActQ02059. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1100528.
GenomeReviewsGene locus SCO5087 in contig AL645882_GR.
KEGGsco:SCO5087.
NMPDRfig|100226.1.peg.5042.
PATRIC23740014. VBIStrCoe124346_5167.

Phylogenomic databases

HOGENOMHBG757733.
OMAPITSACF.
PhylomeDBQ02059.
ProtClustDBCLSK902850.

Family and domain databases

InterProIPR000794. Beta-ketoacyl_synthase.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
Gene3DG3DSA:3.40.47.10. Thiolase-like_subgr. 2 hits.
KOK05551.
PANTHERPTHR11712. Ketoacyl_synth. 1 hit.
PfamPF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]
SUPFAMSSF53901. Thiolase-like. 1 hit.
PROSITEPS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKASA_STRCO
AccessionPrimary (citable) accession number: Q02059
Secondary accession number(s): Q93IZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 17, 2003
Last modified: January 25, 2012
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families