Aver_00150 Aver_00150   Aver_00170 Aver_00170

Aver_00160 : CDS information

close this sectionLocation

Organism
StrainATCC 31267 (=NBRC 14893)
Entry nameAvermectin
Contig
Start / Stop / Direction78,352 / 76,943 / - [in whole cluster]
7,397 / 5,988 / - [in contig]
Locationcomplement(76943..78352) [in whole cluster]
complement(5988..7397) [in contig]
TypeCDS
Length1,410 bp (469 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category2.3 modification addition of sugar moiety
Productputative NDP-hexose 2,3-dehydratase
Product (GenBank)dTDP-4-keto-6-deoxy-L-hexose2,3-dehydratase
Gene
Gene (GenBank)aveBVI
EC number
Keyword
  • L-oleandrose
Note
Note (GenBank)
  • function in oleandrose biosynthesis
Reference
ACC
PmId
[10449723] Organization of the biosynthetic gene cluster for the polyketide anthelmintic macrolide avermectin in Streptomyces avermitilis. (Proc Natl Acad Sci U S A. , 1999)
[11451669] Insights about the biosynthesis of the avermectin deoxysugar L-oleandrose through heterologous expression of Streptomyces avermitilis deoxysugar genes in Streptomyces lividans. (Chem Biol. , 2001)
comment
[PMID:10449723](1999)
avermectin生合成gene clusterの報告。

AveBVI: dTDP-4-keto-6-deoxy-L-hexose 2,3-dehydratase
この論文で実験確認しているわけではない。

---
[PMID: 11451669](2001)
avrG/aveBVI: dTDP-4-keto-6-deoxyglucose 2,3-dehydratase

oleandroseとmycaroseの生合成を参照して、6-deoxyhexoses形成共通2stepsの後は、avrG/aveBVI(encoding a C-2,3-dehydratase) and avrI/aveBVIII (encoding a C-3-ketoreductase)が関連するC-2 deoxygenationが起こると言っている。

S.lividansでS.avermitilis avrBCDEFGHIを発現させて外因性aglyconeと反応させて産物解析。
delta-avrGな発現は実験していない。
Related Reference
ACC
Q845B8
PmId
[12889805] Functional identification of rub52 gene involved in the biosynthesis of rubradirin. (Biotechnol Lett. , 2003)
comment
16th(Q845B8) 60%, 1e-144
Streptomyces achromogenes_rub52
DTDP-glucose-2,3-dehydratase

Streptomyces achromogenes var. nibradiris NRRL3061のrub52を、E.coliで可溶性His-tagged fusion proteinとして発現。in vitro enzyme assayからthymidine diphospho-4-keto-6-deoxyglucoseのC-2 deoxygenation機能性が割り当てられた。
ACC
Q9ALN6
NITE
Spino_00070
PmId
[18345667] In vitro characterization of the enzymes involved in TDP-D-forosamine biosynthesis in the spinosyn pathway of Saccharopolyspora spinosa. (J Am Chem Soc. , 2008)
comment
53rd(Q9ALN6) 49%, 1e-109
Saccharopolyspora spinosa_spnO
[Spino_00070]dTDP-4-keto-6-deoxyglucose 2,3-dehydratase

dTDP-4-keto-6-deoxy-D-glucose 2,3-dehydratase_SpnO

dTDP-D-glucose, RfbB(dTDP-D-glucose→dTDP-4-keto-6-deoxy-D-glucose), and either NADH or NADPHと一緒にSpnO and SpnNをインキュベートし、NAD(P)Hの消費量をフォローしてtandem reactionを測定。SpnO or SpnNのどちらかを欠いた場合、消費が見られなかった。
dTDP-3,4-diketo-2,6-dideoxy-D-glucoseは不安定で急速にdTDP and maltolに分解してしまうため、SpnOのみの触媒効率は定量できていない。

--
SpnNはdTDP-3,4-diketo-2,6-dideoxy-D-glucose 3-ketoreductaseであることが他で報告されている。

close this sectionSequence

selected fasta
>putative NDP-hexose 2,3-dehydratase [dTDP-4-keto-6-deoxy-L-hexose2,3-dehydratase]
MSVRADADHTEPSTAHRAARRRPARVPRPLRRRGRHRRRTSLDAFTGWWTRRSGAHRFRV
ERIPFHGMDAWSFHPGTGNLAHRSGRFFSVEGLHVRGGEQPFPEWQQPIIHQPEIGILGI
LAKKFDGVLHFLMQAKMEPGNINLVQLSPTVQATRSNYTKVHGGAAVKYLEYFTQPRRAT
VVVDVLQSEHGAWFHRKFNRNIVVETDEDVPLDDDFRWLTLGQIGELMHRDNLVNMDART
VLACLPTPFDEPAALHSDAELLSWYAAERSRHSVHARRVPLAGIPGWTTGAESIAHHADR
YFRVVAVRVEASNREVAAWTQPLIEPCGHGITAFLTRRIGGVPHLLAHGRVEGGFLDTIE
LGPTVQYTPRNYAHLTGPARPRFLDLVLEAAPDRIRYAAVHSEEGGRFLHAQARYLFVEA
DESQAPNDPPPGYRWCTPGQLTQLLRYGRYVNVQARTLLSLLTTRAVEL
selected fasta
>putative NDP-hexose 2,3-dehydratase [dTDP-4-keto-6-deoxy-L-hexose2,3-dehydratase]
ATGAGCGTACGAGCCGATGCCGACCACACCGAGCCCAGCACCGCTCACCGCGCGGCACGA
CGCCGCCCTGCCCGCGTGCCTCGCCCGCTCCGCCGCCGTGGGCGACACCGGCGCCGGACG
TCCCTCGACGCGTTCACCGGCTGGTGGACGCGGCGGTCCGGGGCCCACCGGTTCCGGGTC
GAGCGCATCCCCTTCCACGGGATGGACGCCTGGTCGTTTCACCCCGGAACCGGCAATCTG
GCCCACCGCAGCGGCCGGTTCTTCTCCGTGGAGGGACTGCACGTCCGAGGCGGTGAACAG
CCCTTCCCGGAATGGCAGCAGCCCATCATCCACCAGCCCGAGATCGGCATCCTCGGCATC
CTCGCCAAGAAGTTCGACGGGGTCCTGCACTTCCTGATGCAGGCCAAGATGGAGCCCGGC
AACATCAACCTGGTCCAGCTGTCGCCCACCGTGCAGGCCACGCGCAGCAACTACACCAAG
GTCCACGGGGGCGCCGCCGTGAAGTACCTCGAGTACTTCACACAGCCCCGGCGCGCCACC
GTGGTGGTCGACGTCCTCCAGTCCGAGCACGGAGCCTGGTTCCACCGGAAGTTCAACCGC
AACATCGTGGTGGAGACCGACGAGGACGTACCACTGGACGACGACTTCCGCTGGCTGACA
CTGGGGCAGATCGGCGAACTGATGCACCGGGACAACCTGGTGAACATGGACGCACGCACG
GTCCTCGCCTGCCTTCCCACCCCGTTCGACGAGCCCGCGGCCCTGCACAGCGACGCCGAA
CTGCTCTCCTGGTACGCCGCCGAACGCTCCCGGCACTCCGTGCACGCCCGCCGCGTGCCC
CTGGCCGGCATCCCCGGCTGGACCACGGGCGCGGAGTCCATCGCCCACCACGCGGACCGG
TACTTCCGTGTGGTCGCGGTCCGTGTCGAGGCCTCCAACCGGGAGGTCGCCGCCTGGACC
CAGCCCCTGATCGAACCGTGCGGCCACGGCATCACCGCCTTCCTGACCCGGCGGATCGGC
GGCGTACCGCACCTGCTCGCCCACGGCAGGGTCGAGGGCGGCTTCCTCGACACGATCGAA
CTCGGCCCGACGGTCCAGTACACCCCGCGCAACTACGCCCACCTCACGGGACCGGCCAGG
CCGCGCTTCCTCGACCTGGTGCTGGAGGCCGCGCCCGACCGCATCCGCTACGCGGCGGTC
CACTCGGAGGAGGGCGGTCGCTTTCTGCACGCACAGGCGCGCTACCTGTTCGTCGAGGCC
GACGAGAGCCAGGCGCCGAACGACCCGCCCCCGGGGTACCGCTGGTGCACCCCGGGCCAG
CTGACCCAGCTGCTGCGGTACGGCCGTTACGTGAACGTGCAGGCCCGCACCCTGCTGTCC
CTGCTCACCACCCGCGCCGTCGAGCTGTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR005212 NDP-hexose 2,3-dehydratase (Domain)
[41-245] 1e-87 PF03559 [256-462] 2.99999999999998e-80 PF03559
PF03559   Hexose_dehydrat
SignalP No significant hit
TMHMM No significant hit
Aver_00150 Aver_00150   Aver_00170 Aver_00170
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