Madu_00080 Madu_00080   Madu_00100 Madu_00100

Madu_00090 : CDS information

close this sectionLocation

Organism
StrainATCC 39144
Entry nameMaduropeptin
Contig
Start / Stop / Direction16,169 / 17,389 / + [in whole cluster]
16,169 / 17,389 / + [in contig]
Location16169..17389 [in whole cluster]
16169..17389 [in contig]
TypeCDS
Length1,221 bp (406 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category2.3 modification addition of sugar moiety
Productputative NDP-hexose C-3 C-methyltransferase
Product (GenBank)C-methyltransferase
Gene
Gene (GenBank)mdpA4
EC number2.1.1.-
Keyword
  • madurose
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

mdpA4: C-Methyltransferase

mdpA4はD-glucose-1-phosphateから始まる5つの酵素反応で形成されるaminosugarの生合成に関与するとしている。McmC and TylC3を含むC-methyltransferase familyに相同性を示す。

MdpA4はthymidyl 5'-3-methyl-α-D-erythro-pentapyranosyl-4''-ulose diphosphateを形成するために付随するhydroxyl epimerizationとともにS-adenosylmethionine(SAM)からメチル基を取り込む触媒をする、と配列から推測している。
Related Reference
ACC
P96561
NITE
Chlor_00150
PmId
[11035791] Deoxysugars in glycopeptide antibiotics: enzymatic synthesis of TDP-L-epivancosamine in chloroeremomycin biosynthesis. (Proc Natl Acad Sci U S A. , 2000)
comment
Amycolatopsis orientalis
PCZA361.22

[PMID: 11035791]
EvaC(ORF14)を含むdTDP-L-epivancosamine合成に関連する5つのタンパクをE.coliで発現、精製。
これらと基質を組み合わせて反応させ、産物のmass spectrometry and NMRによって各酵素活性、dTDP-L-epivancosamine生合成経路を同定している。
EvaC(ORF14)は、dTDP-3-amino-2,3,6-trideoxy-D-threo-hexopyranos-4-uloseのC-3にequatorialなmethyl基を形成する。
C-3 methyl基をaxialにするのは、この後の反応が関連している。

close this sectionSequence

selected fasta
>putative NDP-hexose C-3 C-methyltransferase [C-methyltransferase]
MSDGCKICGGAVRQVLDLGRQPRANAFIPPEEAEREFTFRLALDMCDVCTMVQLHEVVPQ
EMRYHGSYRYHASGSAGHRKHFEGVARDLLRTELAGADPFIVEIGCNDGVMLSTVAESGV
RHLGVDPSANVTALAAERGVRVRTAFFDEGLAEEIRAADGPADVLYGANTVCHIAHLESL
FRGAVRLLKPDGIFVFEEPYLGTILDRTAFDQIYDEHCYYFTARSVQAAAELFGLELVDV
APTPLHGGEIRYTLSPAGARRPSPAVQRMLDAEAVRRLADPATLTQFAHTIAGVRDDLLG
LLREITAAGHTVAGYGAPGKAATATAFFGIGPELVPFVSDSTPAKQGLLVPGSHIPVRPP
EEFRRARPDYALLFAWNHADEIMAKEREFRNAGGRWIRYVPDVHVV
selected fasta
>putative NDP-hexose C-3 C-methyltransferase [C-methyltransferase]
ATGAGCGATGGATGCAAGATATGCGGGGGCGCCGTCCGGCAGGTCCTGGATCTCGGCCGG
CAGCCGAGAGCCAATGCCTTCATCCCGCCCGAAGAGGCCGAACGCGAATTCACCTTCCGG
CTCGCACTGGACATGTGCGACGTCTGCACGATGGTGCAACTGCACGAAGTGGTCCCGCAG
GAAATGCGCTACCACGGCTCGTACCGGTACCACGCGTCGGGCTCGGCCGGGCACCGCAAG
CATTTCGAGGGGGTCGCGCGGGACCTGCTGCGCACGGAACTGGCCGGCGCGGACCCGTTC
ATCGTCGAGATCGGCTGCAACGACGGGGTCATGCTCTCGACGGTCGCCGAGTCCGGCGTC
CGGCATCTCGGCGTCGACCCGTCCGCGAACGTCACCGCGCTGGCGGCGGAGCGCGGCGTG
CGGGTGCGCACCGCCTTCTTCGACGAGGGGCTGGCCGAGGAGATCCGCGCGGCCGACGGT
CCGGCCGACGTCCTCTACGGCGCGAACACCGTCTGCCACATCGCGCACCTGGAGTCGCTC
TTCCGCGGCGCGGTGCGGCTGCTGAAGCCGGACGGGATCTTCGTGTTCGAGGAGCCCTAC
CTCGGGACGATCCTCGACCGGACGGCGTTCGACCAGATCTACGACGAGCACTGCTACTAC
TTCACGGCGAGGTCCGTCCAGGCGGCGGCGGAGCTGTTCGGGCTGGAGCTGGTCGACGTC
GCCCCCACTCCCCTGCACGGCGGCGAGATCCGCTACACGCTGAGCCCGGCCGGGGCACGC
CGCCCGTCCCCCGCCGTGCAGCGGATGCTGGACGCCGAGGCGGTCCGCCGGCTCGCCGAC
CCCGCGACGCTGACGCAGTTCGCCCACACCATCGCCGGGGTGCGCGACGACCTGCTCGGG
CTGCTGCGGGAGATCACCGCCGCCGGGCACACCGTCGCGGGCTACGGGGCGCCCGGCAAG
GCCGCCACCGCGACCGCCTTCTTCGGCATCGGGCCGGAGCTGGTGCCGTTCGTGAGCGAC
TCCACCCCCGCCAAGCAGGGGCTCCTCGTCCCCGGATCGCACATCCCGGTCCGGCCGCCC
GAGGAGTTCAGGCGGGCCCGCCCCGACTACGCGCTGCTGTTCGCGTGGAACCACGCCGAC
GAGATCATGGCGAAGGAGCGCGAGTTCCGGAACGCCGGCGGCCGGTGGATCCGCTACGTG
CCGGACGTCCACGTCGTGTAA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR013630 Methyltransferase putative zinc binding domain (Domain)
[5-62] 3.3e-16 PF08421
PF08421   Methyltransf_13
IPR013691 C-methyltransferase (Domain)
[244-401] 1.40000000000001e-49 PF08484
PF08484   Methyltransf_14
SignalP No significant hit
TMHMM No significant hit
Madu_00080 Madu_00080   Madu_00100 Madu_00100
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