Actino_00210 Actino_00210   Actino_00230 Actino_00230

Actino_00220 : CDS information

close this sectionLocation

Organism
StrainA3(2) (=NBRC 15146)
Entry nameActinorhodin
Contig
Start / Stop / Direction21,835 / 22,728 / + [in whole cluster]
3,830 / 4,723 / + [in contig]
Location21835..22728 [in whole cluster]
3830..4723 [in contig]
TypeCDS
Length894 bp (297 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category3.4 other modification
Productcyclase/dehydratase
Product (GenBank)Dehydrase
GeneactIV
Gene (GenBank)actIORF5
EC number
Keyword
  • 2nd ring
Note
Note (GenBank)
Reference
ACC
PmId
[1527048] Nucleotide sequence and deduced functions of a set of cotranscribed genes of Streptomyces coelicolor A3(2) including the polyketide synthase for the antibiotic actinorhodin. (J Biol Chem. , 1992)
[11851466] Genetic Contributions to Understanding Polyketide Synthases. (Chem Rev. , 1997)
comment
cluster論文の登録があるのは(Q02057)だが、entry Acc_numは新しい全ゲノム解析(2002)のものを採用。

---
[PMID: 1527048](1992)
actinorhodin biosynthetic gene clusterのactI領域の配列解析。

dehydrase (ORF5)

--
[Pubmed登録なし]Engineered Biosynthesis of Novel Polyketides: actVII and actIV Genes Encode Aromatase and Cyclase Enzymes, Respectively. J. Am. Chem. Soc., 1994, 116 (24), pp 10855-10859

act minimal PKS, KR(actIII ), actVII, actIV の様々な組み合わせのrecombinantsによって産生されたpolyketides構造を測定。

minimal PKS = SEK4
minimal PKS + act KR = mutactin
minimal PKS + act KR + actVII = SEK34
minimal PKS + act KR + actVII + actIV = DMAC

ActVII は1st carbocyclic ringの2つのdehydrationsを触媒することを担うaromataseとして機能する。
AcyIV は2つめのringを形成するための分子内aldol縮合を触媒するcyclase(aldolase)である。

ActVII homologsは、gra, fren, tcm, gris生合成clusterにある。
ActIV homologsは、gra, fren, gris生合成clusterにある。

--
[PMID:11851466](1997)
上記PMIDなし論文がRef採用されているレビュー。
Conflict
Sequence
E (279..279)
Comment
conflict with Q93IZ0 (A)

close this sectionSequence

selected fasta
>cyclase/dehydratase [Dehydrase]
MTVEVREVAEGVYAYEQAPGGWCVSNAGIVVGGDGALVVDTLSTIPRARRLAEWVDKLAA
GPGRTVVNTHFHGDHAFGNQVFAPGTRIIAHEDMRSAMVTTGLALTGLWPRVDWGEIELR
PPNVTFRDRLTLHVGERQVELICVGPAHTDHDVVVWLPEERVLFAGDVVMSGVTPFALFG
SVAGTLAALDRLAELEPEVVVGGHGPVAGPEVIDANRDYLRWVQRLAADAVDRRLTPLQA
ARRADLGAFAGLLDAERLVANLHRAHEELLGGHVRDAMEIFAELVAYNGGQLPTCLA
selected fasta
>cyclase/dehydratase [Dehydrase]
ATGACGGTCGAGGTCCGTGAGGTCGCCGAGGGTGTCTACGCCTACGAGCAGGCCCCCGGC
GGCTGGTGCGTCAGCAACGCGGGCATCGTGGTGGGCGGCGACGGCGCGCTCGTCGTCGAC
ACGCTGTCGACGATCCCGAGGGCGCGGCGGCTGGCGGAGTGGGTCGACAAGCTCGCCGCG
GGCCCCGGCCGTACCGTGGTCAACACCCACTTCCACGGCGACCACGCCTTCGGCAACCAG
GTCTTCGCGCCGGGGACGCGGATCATCGCGCACGAGGACATGCGGTCCGCCATGGTGACG
ACCGGCCTGGCCCTCACCGGGCTCTGGCCGCGGGTCGACTGGGGCGAGATCGAGCTGAGG
CCGCCGAACGTGACCTTCCGCGACCGGTTGACCCTGCACGTCGGCGAGCGACAGGTCGAA
CTGATCTGCGTCGGCCCCGCGCACACCGATCACGACGTGGTGGTCTGGCTGCCCGAGGAG
CGGGTGCTGTTCGCGGGGGACGTCGTCATGTCGGGCGTCACTCCGTTCGCCCTCTTCGGT
TCGGTGGCCGGCACGCTGGCCGCGCTCGACCGGCTGGCGGAGCTGGAGCCCGAGGTGGTC
GTCGGCGGGCACGGCCCGGTGGCGGGACCCGAGGTGATCGACGCCAACCGGGACTATCTG
CGCTGGGTCCAGCGCCTCGCCGCCGATGCGGTCGACCGCCGGCTGACACCGTTGCAGGCC
GCGCGCCGGGCGGACCTCGGCGCCTTCGCCGGGCTGCTGGACGCGGAGCGCCTCGTCGCG
AACCTGCACCGGGCCCACGAGGAGCTGCTGGGCGGGCACGTGCGTGACGCCATGGAGATC
TTCGCGGAGCTGGTCGCCTACAACGGTGGGCAGCTGCCCACCTGCCTCGCCTAG

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR001279 Beta-lactamase-like (Domain)
[21-204] 9.8e-24 PF00753
PF00753   Lactamase_B
[24-204] 2.1e-31 SM00849
SM00849   Metallo-beta-lactamase superfamily
SignalP No significant hit
TMHMM No significant hit
Actino_00210 Actino_00210   Actino_00230 Actino_00230
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