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Q02062 (KASB_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Actinorhodin polyketide putative beta-ketoacyl synthase 2

EC=2.3.1.-
Alternative name(s):
actI ORF2
Gene names
Ordered Locus Names:SCO5088
ORF Names:SCBAC28G1.14
OrganismStreptomyces coelicolor
Taxonomic identifier1902 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length407 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Miscellaneous

This putative ketoacyl synthase lacks the active site cysteine.

Sequence similarities

Belongs to the beta-ketoacyl-ACP synthases family.

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 – 407407Actinorhodin polyketide putative beta-ketoacyl synthase 2
PRO_0000180349

Secondary structure

........................................................................ 407
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q02062 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 59FC75A5A0D94632

FASTA40742,550
        10         20         30         40         50         60 
MSVLITGVGV VAPNGLGLAP YWSAVLDGRH GLGPVTRFDV SRYPATLAGQ IDDFHAPDHI 

        70         80         90        100        110        120 
PGRLLPQTDP STRLALTAAD WALQDAKADP ESLTDYDMGV VTANACGGFD FTHREFRKLW 

       130        140        150        160        170        180 
SEGPKSVSVY ESFAWFYAVN TGQISIRHGM RGPSSALVAE QAGGLDALGH ARRTIRRGTP 

       190        200        210        220        230        240 
LVVSGGVDSA LDPWGWVSQI ASGRISTATD PDRAYLPFDE RAAGYVPGEG GAILVLEDSA 

       250        260        270        280        290        300 
AAEARGRHDA YGELAGCAST FDPAPGSGRP AGLERAIRLA LNDAGTGPED VDVVFADGAG 

       310        320        330        340        350        360 
VPELDAAEAR AIGRVFGREG VPVTVPKTTT GRLYSGGGPL DVVTALMSLR EGVIAPTAGV 

       370        380        390        400 
TSVPREYGID LVLGEPRSTA PRTALVLARG RWGFNSAAVL RRFAPTP 

« Hide

References

« Hide 'large scale' references
[1]"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].
Strain: ATCC BAA-471 / A3(2) / M145.
[2]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X63449 Genomic DNA. Translation: CAA45044.1.
AL939122 Genomic DNA. Translation: CAC44201.1.
PIRS25841.
RefSeqNP_629238.1. NC_003888.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QXGmodel-B1-404[»]
1TQYX-ray2.00B/D/F/H2-407[»]
ProteinModelPortalQ02062.
SMRQ02062. Positions 2-403.
ModBaseSearch...

Protein-protein interaction databases

IntActQ02062. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1100529.
GenomeReviewsGene locus SCO5088 in contig AL645882_GR.
KEGGsco:SCO5088.
NMPDRfig|100226.1.peg.5043.
PATRIC23740016. VBIStrCoe124346_5168.

Phylogenomic databases

HOGENOMHBG757733.
OMAPKTMTGR.
PhylomeDBQ02062.
ProtClustDBCLSK902851.

Family and domain databases

InterProIPR000794. Beta-ketoacyl_synthase.
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.
KOK05552.
PANTHERPTHR11712. Ketoacyl_synth. 1 hit.
PfamPF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
[Graphical view]
SUPFAMSSF53901. Thiolase-like. 2 hits.
ProtoNetSearch...

Entry information

Entry nameKASB_STRCO
AccessionPrimary (citable) accession number: Q02062
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: January 25, 2012
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families