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P16544 (ACT3_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. 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:
Putative ketoacyl reductase

EC=1.3.1.-
Gene names
Name:actIII
Ordered Locus Names:SCO5086
ORF Names:SCBAC28G1.12c
OrganismStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]
Taxonomic identifier100226 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length261 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Pathway

Antibiotic biosynthesis; actinorhodin biosynthesis.

Subunit structure

Homotetramer. Ref.4

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords
   Biological processAntibiotic biosynthesis
   LigandNADP
   Molecular functionOxidoreductase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processantibiotic biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionoxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 261261Putative ketoacyl reductase
PRO_0000054447

Regions

Nucleotide binding11 – 3929NADP

Sites

Active site1571Proton acceptor By similarity
Binding site631NADP
Binding site1441Substrate By similarity
Binding site1611NADP

Secondary structure

........................................... 261
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16544 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: B87C83F45A88B7A9

FASTA26127,265
        10         20         30         40         50         60 
MATQDSEVAL VTGATSGIGL EIARRLGKEG LRVFVCARGE EGLRTTLKEL REAGVEADGR 

        70         80         90        100        110        120 
TCDVRSVPEI EALVAAVVER YGPVDVLVNN AGRPGGGATA ELADELWLDV VETNLTGVFR 

       130        140        150        160        170        180 
VTKQVLKAGG MLERGTGRIV NIASTGGKQG VVHAAPYSAS KHGVVGFTKA LGLELARTGI 

       190        200        210        220        230        240 
TVNAVCPGFV ETPMAASVRE HYSDIWEVST EEAFDRITAR VPIGRYVQPS EVAEMVAYLI 

       250        260 
GPGAAAVTAQ ALNVCGGLGN Y 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence, transcription and deduced function of a gene involved in polyketide antibiotic synthesis in Streptomyces coelicolor."
Hallam S., Malpartida F., Hopwood D.
Gene 74:305-320(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-471 / A3(2) / M145.
[3]"Structural analysis of actinorhodin polyketide ketoreductase: cofactor binding and substrate specificity."
Korman T.P., Hill J.A., Vu T.N., Tsai S.C.
Biochemistry 43:14529-14538(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH NADPH.
[4]"The crystal structure of the actIII actinorhodin polyketide reductase: proposed mechanism for ACP and polyketide binding."
Hadfield A.T., Limpkin C., Teartasin W., Simpson T.J., Crosby J., Crump M.P.
Structure 12:1865-1875(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NADPH, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M19536 Genomic DNA. Translation: AAA26688.1.
AL939122 Genomic DNA. Translation: CAC44199.1.
PIRA28788. JS0108.
RefSeqNP_629236.1. NC_003888.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1W4ZX-ray2.50A/B1-261[»]
1X7GX-ray2.30A/B1-261[»]
1X7HX-ray2.30A/B1-261[»]
1XR3X-ray2.71A/B1-261[»]
2RH4X-ray2.30A/B1-261[»]
2RHCX-ray2.10A/B1-261[»]
2RHRX-ray2.50A/B1-261[»]
3CSDX-ray2.29A/B1-261[»]
3QRWX-ray2.79A/B1-261[»]
3RI3X-ray2.29A/B1-261[»]
4DBZX-ray2.64A/B1-261[»]
4DC0X-ray2.81A/B1-261[»]
4DC1X-ray2.82A/B1-261[»]
ProteinModelPortalP16544.
SMRP16544. Positions 1-261.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING100226.SCO5086.

Proteomic databases

PRIDEP16544.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC44199; CAC44199; CAC44199.
GeneID1100527.
KEGGsco:SCO5086.
PATRIC23740012. VBIStrCoe124346_5166.

Phylogenomic databases

eggNOGCOG1028.
KOK12420.
OMAGRACAIR.
OrthoDBEOG6N3CR8.
PhylomeDBP16544.
ProtClustDBCLSK636083.

Enzyme and pathway databases

UniPathwayUPA00173.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PfamPF00106. adh_short. 1 hit.
[Graphical view]
PIRSFPIRSF000126. 11-beta-HSD1. 1 hit.
PRINTSPR00081. GDHRDH.
PR00080. SDRFAMILY.
PROSITEPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP16544.

Entry information

Entry nameACT3_STRCO
AccessionPrimary (citable) accession number: P16544
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: April 16, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways