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Alip_00220 : CDS information

close this sectionLocation

Organism
StrainTü117
Entry nameAlpha-lipomycin
Contig
Start / Stop / Direction66,871 / 65,411 / - [in whole cluster]
66,871 / 65,411 / - [in contig]
Locationcomplement(65411..66871) [in whole cluster]
complement(65411..66871) [in contig]
TypeCDS
Length1,461 bp (486 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)LipDig5
Gene
Gene (GenBank)lipDig5
EC number
Keyword
  • D-digitoxose
Note
Note (GenBank)
  • putative 2,3-dehydratase
Reference
ACC
PmId
[16723573] Biosynthetic gene cluster for the polyenoyltetramic acid alpha-lipomycin. (Antimicrob Agents Chemother. , 2006)
comment
alpha-lipomycin生合成遺伝子クラスターに関する文献。

lipDig5(486 aa): 2,3-Dehydratase

lipDig2 自体の機能実験は行われていないが相同性より、D-digitoxose moietyを生産する際の
NDP-4-keto-6-deoxy-D-glucose → NDP-3,4-diketo-2,6-dideoxy-D-glucose
へと変換するNDP-4-keto-6-deoxy-D-glucose 2,3-dehydrataseであると予想している。
Related Reference
ACC
Q845B8
PmId
[12889805] Functional identification of rub52 gene involved in the biosynthesis of rubradirin. (Biotechnol Lett. , 2003)
comment
19th, 54%, 1e-122
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
30th, 51%, 1e-113
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 [LipDig5]
MSEVTTRAATTDSTAQKPGGGTRGRPADRPATGPRWDRRTTDLLARSALVTERGAGPATA
SSPTGSPTRGREHAFRVRRIDFAELKGWHFRQPTGNLAHQSGRFFTVEGLRVRTSAGSFP
EWHQPIIRQPEVGILGILAKEIDGVLHFLMQAKMEPGNPNLLQLSPTVQATRSNYTRVHR
GAPVRYVEYFAGPRQGRILADVLQSEHGSWFYRKHNRNMIVETRDEVPPHPDFCWLTLGQ
LYELLRRDNTVNMDSRTVLSSLPPLAELPDSRLALTPDAEVLSWLTEHRSTQDWTIELCP
LTGLPGWARTEREISREDGRFFDVVAVAVEAGNREVPSWTQPLIEPHGEGVAAFLLHEFD
GVPHVLAHARMEGGLPLVVEVAPTVQCVPANYPEDRRPRYLDEVLAAPPARIRYNAVHAE
EGGRFRNAVSRYLIVESDGALAAEPLPPGYAWLSVRQLERLTSAGLSVNVQARTLLACLR
SVARPS
selected fasta
>putative NDP-hexose 2,3-dehydratase [LipDig5]
GTGTCGGAAGTGACGACACGTGCAGCGACGACGGACTCCACCGCGCAGAAACCGGGCGGT
GGCACTCGCGGGCGACCTGCGGACCGGCCCGCGACCGGTCCGCGCTGGGACCGGCGGACC
ACGGATCTTCTGGCCCGGTCGGCCCTGGTGACCGAGCGGGGCGCAGGGCCGGCCACCGCG
AGTTCGCCGACTGGCTCGCCGACCCGCGGACGCGAACACGCCTTCCGGGTGCGGCGGATC
GATTTCGCCGAACTGAAAGGTTGGCATTTCCGTCAGCCGACCGGAAACCTGGCCCACCAG
TCCGGCAGGTTCTTCACCGTGGAAGGACTGCGGGTCCGCACCTCGGCCGGGTCCTTCCCT
GAATGGCATCAACCGATCATCCGGCAACCCGAGGTCGGCATTCTCGGAATCCTGGCGAAG
GAAATCGACGGTGTTCTGCATTTTCTGATGCAGGCGAAGATGGAGCCCGGGAACCCGAAC
CTGCTGCAGCTGTCGCCGACCGTGCAGGCGACCCGCAGCAACTACACGCGTGTGCACCGA
GGTGCGCCCGTCAGATACGTGGAGTACTTCGCCGGGCCGCGCCAGGGCCGGATCCTGGCG
GACGTGCTGCAGTCCGAGCACGGCTCCTGGTTCTACCGCAAGCACAACCGCAACATGATC
GTCGAGACCCGCGACGAGGTGCCCCCGCACCCCGACTTCTGCTGGCTCACCCTCGGTCAG
CTCTACGAACTGCTCCGCCGGGACAACACGGTCAACATGGACTCCCGCACCGTGCTGTCC
AGCTTGCCCCCTCTCGCGGAGCTGCCGGACAGCCGACTGGCGCTCACCCCGGACGCGGAA
GTCCTGAGCTGGCTCACCGAGCACCGCTCCACGCAGGACTGGACGATCGAGCTGTGCCCG
CTGACCGGGCTGCCCGGCTGGGCGCGCACCGAGCGCGAGATCAGCCGCGAGGACGGGCGC
TTCTTCGATGTCGTCGCGGTCGCCGTGGAGGCCGGCAACCGTGAGGTGCCGAGCTGGACG
CAGCCGCTGATCGAACCGCACGGCGAGGGCGTGGCCGCGTTTTTGCTGCACGAATTCGAC
GGCGTACCCCACGTCCTGGCGCACGCCCGCATGGAGGGCGGCCTGCCCCTGGTGGTCGAG
GTGGCGCCCACGGTCCAGTGCGTCCCCGCCAACTACCCCGAGGACAGGCGTCCCCGCTAC
CTCGACGAGGTGCTGGCCGCGCCGCCCGCCCGGATCCGGTACAACGCCGTGCACGCCGAG
GAGGGCGGCCGTTTCCGCAACGCCGTCAGCCGTTACCTCATCGTCGAGTCCGACGGCGCC
CTCGCCGCCGAGCCGCTGCCGCCCGGGTACGCCTGGCTGAGCGTGCGTCAGCTGGAACGG
CTCACCAGCGCCGGGCTGAGCGTCAACGTCCAGGCGCGGACCCTGCTCGCGTGCCTGCGT
TCCGTGGCGCGGCCGTCATGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR005212 NDP-hexose 2,3-dehydratase (Domain)
[70-262] 1e-83 PF03559 [278-479] 1.9e-74 PF03559
PF03559   Hexose_dehydrat
SignalP No significant hit
TMHMM No significant hit
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