NamePutative ketoacyl reductase
Synonyms
  • 1.3.1.-
Gene NameactIII
OrganismStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Amino acid sequence
>lcl|BSEQ0016851|Putative ketoacyl reductase
MATQDSEVALVTGATSGIGLEIARRLGKEGLRVFVCARGEEGLRTTLKELREAGVEADGR
TCDVRSVPEIEALVAAVVERYGPVDVLVNNAGRPGGGATAELADELWLDVVETNLTGVFR
VTKQVLKAGGMLERGTGRIVNIASTGGKQGVVHAAPYSASKHGVVGFTKALGLELARTGI
TVNAVCPGFVETPMAASVREHYSDIWEVSTEEAFDRITARVPIGRYVQPSEVAEMVAYLI
GPGAAAVTAQALNVCGGLGNY
Number of residues261
Molecular Weight27264.88
Theoretical pI5.02
GO Classification
Functions
  • oxidoreductase activity
Processes
  • antibiotic biosynthetic process
General FunctionOxidoreductase activity
Specific FunctionNot Available
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein IDNot Available
UniProtKB IDP16544
UniProtKB Entry NameACT3_STRCO
Cellular LocationNot Available
Gene sequence
>lcl|BSEQ0016852|Putative ketoacyl reductase (actIII)
ATGGCCACGCAGGACTCCGAAGTCGCACTGGTGACGGGTGCGACCAGCGGAATCGGGCTG
GAGATCGCCCGCAGGCTCGGTAAGGAGGGGTTGCGCGTGTTCGTCTGCGCGCGCGGCGAA
GAAGGACTGCGGACGACGCTGAAGGAGTTGCGGGAGGCGGGCGTGGAGGCGGACGGGCGG
ACCTGCGACGTCCGCTCGGTCCCGGAGATCGAGGCTCTCGTGGCGGCGGTGGTCGAGCGT
TACGGTCCGGTCGACGTGCTGGTGAACAACGCGGGCCGGCCCGGCGGCGGCGCCACGGCC
GAACTCGCCGACGAACTCTGGCTCGATGTCGTGGAGACCAACCTCACCGGCGTGTTCCGG
GTGACCAAACAGGTCCTCAAGGCGGGCGGCATGCTCGAACGGGGCACGGGCCGAATCGTC
AACATCGCCTCGACCGGCGGAAAGCAGGGTGTGGTGCACGCCGCGCCCTACTCCGCCTCG
AAGCACGGCGTGGTCGGCTTCACCAAGGCGCTCGGTCTCGAACTGGCGAGGACCGGCATC
ACGGTGAACGCCGTCTGCCCCGGATTCGTCGAGACGCCGATGGCCGCGTCCGTGCGCGAG
CACTACTCGGACATCTGGGAGGTGTCGACCGAGGAGGCCTTCGACCGGATCACCGCGCGC
GTGCCGATCGGCCGGTACGTGCAGCCGTCCGAGGTGGCGGAGATGGTGGCGTACCTGATC
GGGCCCGGTGCGGCCGCGGTCACCGCGCAGGCGCTGAACGTCTGCGGCGGGCTGGGGAAC
TACTGA
GenBank Gene IDM19536
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDNot Available
Chromosome LocationNot Available
LocusNot Available
References
  1. Hallam SE, Malpartida F, Hopwood DA: Nucleotide sequence, transcription and deduced function of a gene involved in polyketide antibiotic synthesis in Streptomyces coelicolor. Gene. 1988 Dec 30;74(2):305-20. 2469622
  2. Bentley SD, Chater KF, Cerdeno-Tarraga AM, Challis GL, Thomson NR, James KD, Harris DE, Quail MA, Kieser H, Harper D, Bateman A, Brown S, Chandra G, Chen CW, Collins M, Cronin A, Fraser A, Goble A, Hidalgo J, Hornsby T, Howarth S, Huang CH, Kieser T, Larke L, Murphy L, Oliver K, O'Neil S, Rabbinowitsch E, Rajandream MA, Rutherford K, Rutter S, Seeger K, Saunders D, Sharp S, Squares R, Squares S, Taylor K, Warren T, Wietzorrek A, Woodward J, Barrell BG, Parkhill J, Hopwood DA: Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2). Nature. 2002 May 9;417(6885):141-7. 12000953
  3. Korman TP, Hill JA, Vu TN, Tsai SC: Structural analysis of actinorhodin polyketide ketoreductase: cofactor binding and substrate specificity. Biochemistry. 2004 Nov 23;43(46):14529-38. 15544323
  4. Hadfield AT, Limpkin C, Teartasin W, Simpson TJ, Crosby J, Crump MP: The crystal structure of the actIII actinorhodin polyketide reductase: proposed mechanism for ACP and polyketide binding. Structure. 2004 Oct;12(10):1865-75. 15458634