Madu_00070 Madu_00070   Madu_00090 Madu_00090

Madu_00080 : CDS information

close this sectionLocation

Organism
StrainATCC 39144
Entry nameMaduropeptin
Contig
Start / Stop / Direction15,953 / 14,931 / - [in whole cluster]
15,953 / 14,931 / - [in contig]
Locationcomplement(14931..15953) [in whole cluster]
complement(14931..15953) [in contig]
TypeCDS
Length1,023 bp (340 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category5.1 general function
Productputative alcohol dehydrogenase
Product (GenBank)Zn-dependent alcohol dehydrogenase
Gene
Gene (GenBank)mdpC8
EC number1.1.1.1
Keyword
Note
Note (GenBank)
Reference
ACC
PmId
[17918933] Characterization of the maduropeptin biosynthetic gene cluster from Actinomadura madurae ATCC 39144 supporting a unifying paradigm for enediyne biosynthesis. (J Am Chem Soc. , 2007)
comment
Maduropeptin生合成遺伝子クラスターの報告

mdpC8: Zn-dependent alcohol dehydrgosenase

Eight genes (mdpC to mdpC8 excluding mdpC5)は、L-alpha-tyrosineからの(S)-3-(2-chloro-3-hydroxy-4-methoxyphenyl)-3-hydroxypropionic acid moietyの生合成に関与するとしている。

(S)-beta-hydroxy functionalityはbeta-carbonyl groupの立体特異的な還元によって形成される。この反応の候補としてmdpC8をあげているが機能解析はされていない。
Related Reference
ACC
P42328
PmId
[8020473] A few amino acid substitutions are responsible for the higher thermostability of a novel NAD(+)-dependent bacillar alcohol dehydrogenase. (Eur J Biochem. , 1994)
comment
Bacillus stearothermophilus
Alcohol dehydrogenase

Alcohol dehydrogenase adh-hTをクローニング、シークエンス。E.coliで発現、精製、ADH活性測定。

close this sectionSequence

selected fasta
>putative alcohol dehydrogenase [Zn-dependent alcohol dehydrogenase]
MKAAVIPKPDATWELREVETPRPGPGEVLIRVRACGVCHNDVLATRGAIPFPSISPAITG
HEPAGEVVELGSGVVRRRVGDRVGTTWVRAGCGTCAYCRRDLPVTGQTAMNCPNPVTTGF
TVQGGHAEYMAVREEETVLLPDELPFELAAPVLCAGYTAWSALRTAEPAPHERVAVLGIG
GLGHLALQFSRACGFETIAITSSPDKYDLARELGADIVVRDGAQLCAAGGADVVIATVPS
HPAAAAGLQGLRAGGRMVLAGIDAAEPFTIPPAMTFPFFAQGQRIMGATHGGPVLLREAL
DLVAERKVTPMVETFPKEQVAEAVEKTAKGELRFRAVVTY
selected fasta
>putative alcohol dehydrogenase [Zn-dependent alcohol dehydrogenase]
ATGAAGGCGGCCGTGATCCCCAAGCCCGACGCGACGTGGGAACTCCGCGAGGTCGAGACC
CCGCGTCCCGGGCCCGGGGAGGTGCTGATCAGGGTGCGTGCGTGCGGCGTGTGCCACAAC
GACGTGCTGGCCACCCGCGGGGCGATCCCGTTCCCCTCGATCAGTCCCGCGATCACCGGG
CACGAGCCGGCGGGGGAGGTCGTCGAGCTCGGCTCGGGCGTCGTCCGGCGCCGGGTGGGC
GACCGGGTCGGCACCACCTGGGTGCGGGCCGGGTGCGGCACGTGCGCCTACTGCCGCCGC
GACCTTCCGGTGACGGGGCAGACGGCGATGAACTGCCCGAACCCGGTCACGACGGGGTTC
ACCGTGCAGGGCGGCCACGCCGAGTACATGGCGGTGCGGGAGGAGGAGACGGTCCTCCTG
CCGGACGAGCTGCCGTTCGAGCTGGCCGCGCCCGTGCTGTGCGCCGGGTACACCGCCTGG
TCCGCGCTGCGGACGGCCGAGCCCGCGCCGCACGAGCGGGTGGCGGTGCTGGGCATCGGC
GGCCTGGGCCACCTGGCCCTCCAGTTCTCCCGGGCCTGCGGGTTCGAGACCATCGCGATC
ACCTCGTCGCCGGACAAGTACGACCTGGCCCGCGAGCTGGGCGCGGACATCGTCGTGCGC
GACGGCGCGCAGCTGTGCGCGGCGGGCGGCGCCGACGTCGTCATCGCGACCGTCCCGTCC
CATCCGGCCGCGGCGGCGGGCCTCCAGGGGCTGCGGGCCGGGGGGCGGATGGTGCTGGCC
GGGATCGACGCGGCCGAGCCGTTCACCATTCCCCCGGCGATGACGTTCCCGTTCTTCGCG
CAGGGGCAGCGCATCATGGGCGCCACCCACGGCGGCCCCGTCCTGCTCCGGGAGGCCCTC
GACCTGGTCGCCGAGCGGAAGGTGACCCCGATGGTGGAGACCTTCCCCAAGGAGCAGGTG
GCCGAGGCGGTGGAGAAGACCGCCAAGGGGGAACTCCGGTTCCGCGCCGTCGTGACCTAC
TGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR002328 Alcohol dehydrogenase, zinc-type, conserved site (Conserved_site)
[60-74] PS00059
PS00059   ADH_ZINC
IPR011032 GroES-like (Domain)
[1-188] 5.09998762524166e-53 SSF50129
SSF50129   GroES_like
IPR013149 Alcohol dehydrogenase, C-terminal (Domain)
[181-304] 5.5e-17 PF00107
PF00107   ADH_zinc_N
IPR013154 Alcohol dehydrogenase GroES-like (Domain)
[25-138] 2.5e-25 PF08240
PF08240   ADH_N
IPR016040 NAD(P)-binding domain (Domain)
[178-288] 1.69999999999999e-18 G3DSA:3.40.50.720
G3DSA:3.40.50.720   NAD(P)-bd
SignalP No significant hit
TMHMM No significant hit
Madu_00070 Madu_00070   Madu_00090 Madu_00090
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