Urd_00230 Urd_00230   Urd_00250 Urd_00250

Urd_00240 : CDS information

close this sectionLocation

Organism
StrainTü2717
Entry nameUrdamycin
Contig
Start / Stop / Direction26,577 / 27,881 / + [in whole cluster]
1,069 / 2,373 / + [in contig]
Location26577..27881 [in whole cluster]
1069..2373 [in contig]
TypeCDS
Length1,305 bp (434 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category2.3 modification addition of sugar moiety
Productputative pyridoxamine 5'-monophosphate-dependent NDP-hexose C-3 dehydratase
Product (GenBank)NDP-hexose 3,4-dehydratase UrdQ
Gene
Gene (GenBank)urdQ
EC number
Keyword
  • L-rhodinose
Note
Note (GenBank)
Reference
ACC
PmId
[11094336] The NDP-sugar co-substrate concentration and the enzyme expression level influence the substrate specificity of glycosyltransferases: cloning and characterization of deoxysugar biosynthetic genes of the urdamycin biosynthetic gene cluster. (Chem Biol. , 2000)
[17434221] Surprising production of a new urdamycin derivative by S. fradiae Delta urdQ/R. (J Biotechnol. , 2007)
comment
[PMID: 11094336](2000)
urdZ3, urdQ and urdZ1をそれぞれ不活化するとL-rhodinoseを産生できない株となり、主にurdamycinone Bを蓄積。
各genesで相補され、urdamycin A産生回復。
よってこれらのgenesはNDP-L-rhodinose生合成に関与する。

urdamycin deoxysugar(NDP-D-olivose, NDP-L-rhodinose)生合成経路のFigあり。
UrdQ = NDP-4-keto-2,6-dideoxy-D-glucose → NDP-D-cinerulose
この機能的割り当てを確認するにはさらなる研究が必要。

---
[PMID: 17434221](2007)
urdQ/R double mutantの相補実験あり。

S. cyanogenus S136に由来するlandomycin生合成gene clusterの
dTDP-hexose-3,4-dehydrataseをコードするlanQと、
dTDP-hexose-4-ketoreductaseをコードするlanRでの相補は、
urdamycin A and urdamycin Bの産生をもたらした。

ただ、lanQ, lanR自体が実験的に機能確認されていないので微妙。
Related Reference
ACC
Q9ALN8
NITE
Spino_00050
PmId
[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
Blast 21st, id69%, 1e-162
Saccharopolyspora spinosa_spnQ
probable NDP-hexose-3,4-dehydratase
[DoBISCUIT]pyridoxamine 5'-phosphate-dependent NDP-hexose C-3 dehydratase

--
[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。
SpnQのsteady-state kinetic parameters、基質特異性を調査。

close this sectionSequence

selected fasta
>putative pyridoxamine 5'-monophosphate-dependent NDP-hexose C-3 dehydratase [NDP-hexose 3,4-dehydratase UrdQ]
MGDRKELVLEEVRTYHRDVSPDQEFIPGTTEIWPSGAVLDESDRVALVEAALDMRIAAGT
SSRKFESAFARRLKRRKAHLTNSGSSANLLAVSALTSHVLEDRRLRPGDEVITVAAGFPT
TVNPILQNGLVPVFVDVDLPTYNATAERVAQAIGPKTRAIIIAHALGNPFEVAEMAQLAE
EHDLFLIEDNCDAVGSTYDGQLTGTFGDLTTVSFYPAHHLTMGEGGCVLTSNLSLARIVE
SLRDWGRDCWCEPGENDRCLKRFKYQMGTLPAGYDHKYIFSHVGYNLKATDIQAALGLTQ
LAKLDDFIEARQRNWRRLREGLDGVPGLLLPEPTPRSQPSWFGFVITVAPDAPFSRAELV
DFLEDRKIGTRRLFAGNLTRHPAYIDQPHRIVGELTNSDLVTEQTFWIGVYPALTDEMLD
YVTASIKEFVAARG
selected fasta
>putative pyridoxamine 5'-monophosphate-dependent NDP-hexose C-3 dehydratase [NDP-hexose 3,4-dehydratase UrdQ]
ATGGGTGACCGCAAGGAACTGGTGCTGGAAGAGGTCCGCACGTATCACCGGGATGTCTCG
CCCGACCAGGAGTTCATCCCGGGAACCACCGAGATCTGGCCGTCCGGCGCGGTGCTGGAC
GAGTCCGACCGCGTGGCCTTGGTCGAGGCCGCCCTCGACATGCGCATCGCCGCGGGAACG
AGTTCCCGGAAGTTCGAATCCGCCTTTGCTCGACGGCTCAAGCGGCGCAAGGCCCATCTC
ACCAACTCCGGTTCGTCCGCGAACCTGCTCGCCGTGTCGGCACTCACCTCGCACGTCCTG
GAGGATCGAAGGCTGAGGCCGGGCGACGAGGTGATCACGGTGGCCGCCGGCTTCCCCACC
ACCGTGAACCCGATCCTGCAGAACGGCCTGGTCCCGGTGTTCGTGGACGTGGACCTTCCC
ACCTACAACGCCACCGCCGAGCGGGTGGCCCAGGCGATCGGCCCCAAGACCCGGGCGATC
ATCATCGCCCATGCGCTGGGCAACCCGTTCGAGGTGGCCGAGATGGCCCAGCTCGCCGAG
GAGCACGACCTGTTCCTGATCGAGGACAACTGCGACGCGGTGGGCTCCACCTACGACGGA
CAGCTCACGGGCACCTTCGGCGACCTGACCACGGTCAGTTTCTATCCGGCGCACCATCTG
ACCATGGGGGAGGGCGGGTGCGTCCTGACCTCCAACCTCAGCCTCGCCCGCATCGTGGAG
TCACTGCGTGACTGGGGCCGGGACTGCTGGTGCGAACCGGGCGAGAACGACAGGTGCCTC
AAGCGCTTCAAGTACCAGATGGGCACCCTCCCCGCCGGATACGACCACAAGTACATTTTC
TCGCACGTCGGTTACAACCTGAAGGCCACCGACATACAGGCGGCCCTCGGCCTGACGCAG
CTCGCCAAGCTGGACGACTTCATCGAAGCCCGTCAGCGCAACTGGCGTCGTCTGCGCGAA
GGGCTCGACGGCGTACCGGGCCTGCTGTTGCCGGAGCCCACGCCGCGTTCCCAGCCGAGC
TGGTTCGGCTTCGTGATCACCGTCGCCCCCGACGCACCCTTCAGCCGGGCCGAGTTGGTC
GACTTCCTGGAGGACCGGAAGATCGGCACTCGACGCTTGTTCGCCGGCAACCTCACCAGG
CACCCGGCCTACATCGACCAGCCGCACCGCATCGTCGGCGAGCTCACCAACAGCGACCTC
GTCACCGAGCAGACCTTCTGGATCGGCGTCTATCCCGCGCTCACCGACGAAATGCTCGAT
TACGTGACCGCCTCGATCAAGGAGTTCGTCGCCGCACGTGGCTAG

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR000653 DegT/DnrJ/EryC1/StrS aminotransferase (Family)
[1-434] 2.39999798157263e-112 PIRSF000390
PIRSF000390   PLP_StrS
[43-426] 1.29999999999998e-99 PF01041
PF01041   DegT_DnrJ_EryC1
IPR015421 Pyridoxal phosphate-dependent transferase, major region, subdomain 1 (Domain)
[32-302] 4.40000000000003e-69 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)
[303-427] 2.29999999999998e-50 G3DSA:3.90.1150.10
G3DSA:3.90.1150.10   PyrdxlP-dep_Trfase_major_sub2
IPR015424 Pyridoxal phosphate-dependent transferase, major domain (Domain)
[29-433] 2.2999842048857e-96 SSF53383
SSF53383   PyrdxlP-dep_Trfase_major
SignalP No significant hit
TMHMM No significant hit
Urd_00230 Urd_00230   Urd_00250 Urd_00250
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