Spino_00040 Spino_00040   Spino_00060 Spino_00060

Spino_00050 : CDS information

close this sectionLocation

Organism
StrainNRRL 18538
Entry nameSpinosyn
Contig
Start / Stop / Direction6,751 / 5,363 / - [in whole cluster]
6,751 / 5,363 / - [in contig]
Locationcomplement(5363..6751) [in whole cluster]
complement(5363..6751) [in contig]
TypeCDS
Length1,389 bp (462 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category2.3 modification addition of sugar moiety
Productpyridoxamine 5'-monophosphate-dependent NDP-hexose C-3 dehydratase
Product (GenBank)probable NDP-hexose-3,4-dehydratase
Gene
Gene (GenBank)spnQ
EC number
Keyword
  • D-forosamine
Note
Note (GenBank)
  • probably involved in forosamine biosynthesis
Reference
ACC
PmId
[11358695] Cloning and analysis of the spinosad biosynthetic gene cluster of Saccharopolyspora spinosa. (Chem Biol. , 2001)
[11386361] A cluster of genes for the biosynthesis of spinosyns, novel macrolide insect control agents produced by Saccharopolyspora spinosa. (Antonie Van Leeuwenhoek. , 2000)
[17076492] Characterization of SpnQ from the spinosyn biosynthetic pathway of Saccharopolyspora spinosa: mechanistic and evolutionary implications for C-3 deoxygenation in deoxysugar biosynthesis. (J Am Chem Soc. , 2006)
[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
[PMID:11358695](2001)
spinosad biosynthetic gene clusterの報告。

spnQ(463aa): forosamine; 3,4-dehydratase

NDP-ferosamine合成過程において3,4位のdehydratase活性を担うと考えられる。脱水して3,4-enolを形成する。

--
[PMID:11386361](2000)
同じ著者らの先行論文。
spnQ: Forosamine synthesis

---
forosamine生合成におけるC-3 deoxygenationに関与したPMP-dependent 3-dehydrataseであるという続報あり。

[PMID: 17076492](2006)
SpnQをクローニング、過剰発現、精製して、"ColD-like" conditions と "E1-like" conditionsの両方で触媒活性をテスト。
E3のような特異的reductaseを必要とせず、一般的なferredoxin/ferredoxin reductase またはflavodoxin/flavodoxin reductaseと効率的に働く。

[PMID: 18345667](2008)
dTDP-D-forosamine形成に関連する5つの酵素SpnO, N, Q, R, and Sの生化学的機能解明。
使用している株はNRRL 18537.
SpnQのsteady-state kinetic parameters、基質特異性を調査。

close this sectionSequence

selected fasta
>pyridoxamine 5'-monophosphate-dependent NDP-hexose C-3 dehydratase [probable NDP-hexose-3,4-dehydratase]
MQSRKTRALGKGRARVTSCDDTCATATEMVPDAKDRILASVRDYHREQESPTFVAGSTPI
RPSGAVLDEDDRVALVEAALELRIAAGGNARRFESEFARFFGLRKAHLVNSGSSANLLAL
SSLTSPKLGEARLRPGDEVITAAVGFPTTINPAVQNGLVPVFVDVELGTYNATPDRIKAA
VTERTRAIMLAHTLGNPFAADEIAEIAKEHELFLVEDNCDAVGSTYRGRLTGTFGDLTTV
SFYPAHHITSGEGGCVLTGSLELARIIESLRDWGRDCWCEPGVDNTCRKRFDYHLGTLPP
GYDHKYTFSHVGYNLKTTDLQAALALSQLSKISAFGSARRRNWRRLREGLSGLPGLLLPV
ATPHSDPSWFGFAITISADAGFTRAALVNFLESRNIGTRLLFGGNITRHPAFEQVRYRIA
DALTNSDIVTDRTFWVGVYPGITDQMIDYVVESIAEFVAKSS
selected fasta
>pyridoxamine 5'-monophosphate-dependent NDP-hexose C-3 dehydratase [probable NDP-hexose-3,4-dehydratase]
ATGCAGAGCCGGAAAACCAGAGCGCTGGGGAAAGGGCGCGCCAGAGTGACTTCGTGTGAC
GACACTTGCGCTACCGCTACTGAGATGGTGCCGGATGCCAAGGACCGGATATTGGCATCC
GTACGCGATTACCACCGCGAACAGGAATCCCCGACCTTCGTGGCTGGATCGACGCCGATC
CGGCCATCGGGCGCCGTGCTCGACGAGGACGACCGGGTGGCACTGGTGGAAGCCGCGCTG
GAGCTCCGGATCGCCGCGGGCGGGAATGCACGGCGATTCGAGAGCGAGTTCGCCCGCTTC
TTCGGCCTCCGCAAGGCTCATCTCGTCAACTCCGGTTCGTCGGCCAATCTCCTGGCACTG
AGTTCGCTTACCTCCCCCAAACTCGGCGAGGCACGACTGCGGCCCGGCGACGAAGTGATC
ACTGCGGCGGTCGGCTTCCCCACGACGATCAATCCGGCGGTCCAAAACGGACTCGTCCCG
GTATTCGTCGACGTGGAACTGGGCACCTACAACGCAACGCCAGACCGCATCAAGGCCGCC
GTCACGGAACGGACGCGAGCCATCATGCTGGCGCACACCCTGGGCAACCCCTTCGCCGCT
GACGAAATCGCGGAGATCGCAAAAGAACACGAGCTGTTCCTCGTCGAAGACAACTGTGAT
GCGGTGGGATCCACCTACCGGGGACGGCTGACCGGAACCTTCGGCGACCTGACAACGGTC
AGCTTCTATCCTGCCCATCACATCACCAGCGGCGAGGGTGGCTGCGTGTTGACCGGCAGC
CTGGAATTGGCTCGCATCATCGAGTCGCTGCGTGACTGGGGACGGGATTGCTGGTGCGAG
CCCGGCGTGGACAACACCTGCCGCAAGAGGTTCGACTACCACCTCGGTACCCTTCCACCG
GGCTACGACCACAAGTACACGTTCTCCCACGTCGGTTACAACCTCAAGACCACCGACCTG
CAGGCCGCACTTGCGCTGAGCCAGTTGAGCAAGATTTCCGCATTCGGGTCGGCACGCCGC
CGTAACTGGCGACGGTTGCGCGAAGGGCTGTCCGGGTTGCCGGGCCTGCTGCTGCCGGTA
GCCACACCGCACAGCGACCCGAGCTGGTTCGGGTTTGCGATCACCATCAGTGCGGACGCC
GGGTTCACCCGTGCCGCCCTGGTGAACTTCCTGGAATCCCGCAACATCGGCACCCGACTG
CTGTTCGGCGGTAACATCACCCGGCACCCGGCCTTCGAGCAGGTGCGGTACCGGATCGCC
GACGCGCTCACCAACAGCGACATCGTCACCGACCGAACCTTCTGGGTCGGCGTCTACCCA
GGCATAACGGACCAAATGATCGACTACGTCGTCGAATCAATCGCTGAATTCGTGGCCAAG
AGTTCCTAG

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR000653 DegT/DnrJ/EryC1/StrS aminotransferase (Family)
[4-462] 1.90000694315261e-116 PIRSF000390
PIRSF000390   PLP_StrS
[71-454] 1.29999999999998e-100 PF01041
PF01041   DegT_DnrJ_EryC1
IPR015421 Pyridoxal phosphate-dependent transferase, major region, subdomain 1 (Domain)
[62-330] 1.69999999999998e-70 G3DSA:3.40.640.10
G3DSA:3.40.640.10   PyrdxlP-dep_Trfase_major_sub1
IPR015422 Pyridoxal phosphate-dependent transferase, major region, subdomain 2 (Domain)
[331-454] 6.09999999999996e-48 G3DSA:3.90.1150.10
G3DSA:3.90.1150.10   PyrdxlP-dep_Trfase_major_sub2
IPR015424 Pyridoxal phosphate-dependent transferase, major domain (Domain)
[57-461] 3.699978135861e-97 SSF53383
SSF53383   PyrdxlP-dep_Trfase_major
SignalP No significant hit
TMHMM No significant hit
Spino_00040 Spino_00040   Spino_00060 Spino_00060
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