Actino_00020 Actino_00020   Actino_00040 Actino_00040

Actino_00030 : CDS information

close this sectionLocation

Organism
StrainA3(2) (=NBRC 15146)
Entry nameActinorhodin
Contig
Start / Stop / Direction2,083 / 3,006 / + [in whole cluster]
2,083 / 3,006 / + [in contig]
Location2083..3006 [in whole cluster]
2083..3006 [in contig]
TypeCDS
Length924 bp (307 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category3.3 modification reduction
ProductC-3 ketoreductase
Product (GenBank)hydroxylacyl-CoA dehydrogenase
GeneactVI-ORF1
Gene (GenBank)ORF1
EC number
Keyword
  • S-stereochemistry
Note
Note (GenBank)
Reference
ACC
PmId
[7929165] DNA sequence and functions of the actVI region of the actinorhodin biosynthetic gene cluster of Streptomyces coelicolor A3(2). (J Biol Chem. , 1994)
[10091691] Proof that the ACTVI genetic region of Streptomyces coelicolor A3(2) is involved in stereospecific pyran ring formation in the biosynthesis of actinorhodin. (Bioorg Med Chem Lett. , 1999)
[10805574] Chemical characterisation of disruptants of the Streptomyces coelicolor A3(2) actVI genes involved in actinorhodin biosynthesis. (J Antibiot (Tokyo). , 2000)
[15498668] Remarkably different structures and reaction mechanisms of ketoreductases for the opposite stereochemical control in the biosynthesis of BIQ antibiotics. (Bioorg Med Chem. , 2004)
[17579485] Actinorhodin biosynthesis: structural requirements for post-PKS tailoring intermediates revealed by functional analysis of ActVI-ORF1 reductase. (Biochemistry. , 2007)
comment
[PMID: 7929165](1994)
actinorhodin biosynthetic gene clusterのactVI regionに関する報告。

ORF1: 3-Hydroxyacyl-CoA dehydrogenase

これまでにactVI mutantとして分離されているB22, B159株は、actVI-ORF1のC末側に変異があることを相補実験で確認。

--
[PMID: 10091691](1999) abstract
act clusterが削除されたS.coelicolor CH999にact minimal PKS, KR, ARO, CYCとactVI-ORF1を持つpIJ5660を導入したCH999/pIJ5660株で、actinorhodin生合成におけるchiral中間体(S)-DNPAを産生。

--
[PMID: 10805574](2000)
actVI-ORF1破壊株は、3,8-dihydroxy-1-methylanthraquinone-2-carboxylic acid (DMAC)とaloesaponarin II をshunt産物として産生。
actinorhodinの産生は見られない。

--
[PMID: 15498668](2004) abstract
S.coelicolor A3(2)でのactinorhodin生合成におけるketoreductase=RED1→→→(S)-DNPA産生
S.violaceoruber Tu22でのdihydrogranaticin生合成におけるketoreductase=RED2→→→(R)-DNPA産生

RED1とRED2のAA配列類似性なし。familyも異なる。
RED1は不安定な実際の基質の代わりに合成類似体を用いた生体内変換ができ、基質特異性が広い。
Homology modelling研究とsite directed mutagenesisにおいても、RED1とRED2で触媒メカニズムと3次元構造が著しく異なることが示されている。

--
[PMID: 17579485](2007) abstract
actVI-ORF1がコードするRED1をE.coliで発現、精製し酵素実験に使用。
基質としてACPのついていない2環beta-keto acidを認識することを確認。
3-oxo-4-naphthylbutyric acid (ONBA)と高い親和性あり。
ONBAのmethyl esterは、RED1の競合的阻害剤として働く。

close this sectionSequence

selected fasta
>C-3 ketoreductase [hydroxylacyl-CoA dehydrogenase]
MSTVTVIGAGTIGLGWINLFSARGLTVRVNSRRPDVRRVVHEALELFSPGRVDELAARIE
YEPDVGRAVAGADVVSENAPDDLPLKQRLFAEIGAAAPDHALVLSSTSKLLPDELSRDMP
GPGRLVVAHPFNPPHIVPLVEVVRGERTDPEAVERTLAFLASVGRTPVVVRRALPGFAAN
RLQSALLRESIHLVLEGVVTVEELDRIVTDSIGLRWSTIGPFHAFHLGGGPGGLRKWLEH
LGSGLEQGWRGLGQPALTPQAVEALVAQTEAAYGHRPYAELVRDRDDRHLAVLAALERTE
QPQEETK
selected fasta
>C-3 ketoreductase [hydroxylacyl-CoA dehydrogenase]
ATGAGCACCGTGACAGTGATCGGGGCGGGCACGATCGGCCTGGGATGGATCAACCTGTTC
AGCGCCCGCGGGCTGACCGTACGCGTCAACAGCCGTCGGCCCGACGTCCGGCGCGTCGTG
CACGAGGCGCTCGAGCTGTTCTCCCCGGGGCGGGTGGACGAGCTGGCGGCGCGCATCGAG
TACGAGCCGGACGTCGGCCGGGCGGTGGCCGGGGCGGACGTCGTCTCCGAGAACGCCCCC
GACGACCTGCCGCTCAAGCAGCGGTTGTTCGCAGAGATCGGAGCGGCCGCCCCGGACCAC
GCCCTCGTGCTGTCCTCGACGTCGAAGCTGCTTCCCGACGAGCTGAGTCGGGACATGCCG
GGACCGGGCCGGCTGGTCGTCGCGCATCCGTTCAACCCACCGCACATCGTTCCGCTGGTC
GAGGTGGTCCGCGGCGAGCGCACCGACCCGGAGGCCGTCGAACGGACACTGGCCTTCCTG
GCGTCGGTCGGGCGGACCCCCGTCGTGGTGCGCAGGGCGCTGCCCGGCTTCGCGGCCAAC
CGGCTGCAGTCGGCGCTGCTGCGCGAGAGCATCCACCTCGTCCTCGAAGGCGTGGTGACC
GTCGAGGAGCTCGACCGGATCGTCACCGACTCGATCGGCCTGCGCTGGTCCACCATCGGG
CCGTTCCACGCGTTCCACCTGGGCGGCGGTCCCGGCGGCCTGCGCAAGTGGCTCGAGCAC
CTCGGCAGCGGCCTCGAACAGGGCTGGCGTGGGCTCGGACAGCCCGCCCTCACCCCGCAG
GCCGTCGAGGCTCTGGTCGCACAGACCGAAGCCGCCTACGGACACCGGCCCTACGCCGAA
CTGGTCCGGGACCGTGACGACCGGCACCTCGCCGTACTGGCCGCCCTGGAGCGGACCGAG
CAGCCCCAGGAGGAGACCAAGTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR006108 3-hydroxyacyl-CoA dehydrogenase, C-terminal (Domain)
[176-268] 5.2e-13 PF00725
PF00725   3HCDH
IPR006176 3-hydroxyacyl-CoA dehydrogenase, NAD binding (Domain)
[3-171] 1.5e-44 PF02737
PF02737   3HCDH_N
IPR008927 6-phosphogluconate dehydrogenase, C-terminal-like (Domain)
[176-264] 1.6e-11 SSF48179
SSF48179   6-phosphogluconate dehydrogenase C-terminal domain-like
IPR013328 Dehydrogenase, multihelical (Domain)
[178-230] 4.4e-07 G3DSA:1.10.1040.10
G3DSA:1.10.1040.10   no description
IPR016040 NAD(P)-binding domain (Domain)
[3-177] 2e-36 G3DSA:3.40.50.720
G3DSA:3.40.50.720   no description
SignalP
[1-33] 0.167 Signal
Bacteria, Gram-positive   
TMHMM
[5-27] Transmembrane (o-i)
Transmembrane 1   
Actino_00020 Actino_00020   Actino_00040 Actino_00040
Page top