Grana_00170 : CDS information

close this sectionLocation

Organism
StrainTü22
Entry nameGranaticin
Contig
Start / Stop / Direction19,615 / 20,916 / + [in whole cluster]
19,615 / 20,916 / + [in contig]
Location19615..20916 [in whole cluster]
19615..20916 [in contig]
TypeCDS
Length1,302 bp (433 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)putative CDP-4-keto-6-deoxyglucose-3-dehydratase (E1)
Gene
Gene (GenBank)gra-orf23
EC number
Keyword
  • L-rhodinose
Note
Note (GenBank)
Reference
ACC
PmId
[9831526] The granaticin biosynthetic gene cluster of Streptomyces violaceoruber Tu22: sequence analysis and expression in a heterologous host. (Chem Biol. , 1998)
[11269719] Identification of four genes from the granaticin biosynthetic gene cluster of Streptomyces violaceoruber Tu22 involved in the biosynthesis of L-rhodinose. (J Antibiot (Tokyo). , 2001)
comment
[PMID: 9831526](1998)
entire granaticin gene cluster(gra cluster)の報告。

ORF23: Yersinia pseudotuberculosis ascC(rfbH)のhomolog.
配列解析のみ。

--
[PMID: 11269719](2001)
ORF22-25の各不活化mutantsは、dihydrogranaticin B産生ができなくなり、granaticinを蓄積する。
dihydrogranaticin Bはgranaticin Bの前駆体。
granaticin BはgranaticinにL-rhodinoseが追加された構造。
よって、ORF22-25はどれもL-rhodinose形成・付着に関連。
pathwayでの割り当ては配列相同性から。

Y.pseudotuberculosisでのenzyme E1(AscC) and E3(AscD)での3-deoxygenation機構を参照しているが、gra clusterはascDのhomologを含んでいない。
Related Reference
ACC
Q9L4S6
NITE
Urd_00240
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
Blast 3rd, id71%, 0.0
Streptomyces fradiae_urdQ
NDP-hexose 3,4-dehydratase UrdQ
[Urd_00240]putative pyridoxamine 5'-monophosphate-dependent NDP-hexose C-3 dehydratase

---
[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 (D-olivoseあり、L-rhodinoseなし)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生合成にのみ関与する。

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自体が機能確認されていないようなので微妙。
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 17th, id70%, 1e-168
Saccharopolyspora spinosa_spnQ
probable NDP-hexose-3,4-dehydratase
[Spino_00050]pyridoxamine 5'-monophosphate-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。
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
>putative pyridoxamine 5'-monophosphate-dependent NDP-hexose C-3 dehydratase [putative CDP-4-keto-6-deoxyglucose-3-dehydratase (E1)]
MDAEKTHILERVREYHQAREQREFVPGVTPVQPSGAALDANDRVALVEAALDLRIAAGPS
TQRFERDFARYFGLRKAHMTNSGSSANLLALTSLTSHTLGDRRLRPGDEVITVAAGFPTT
VNPIIQNGLVPVFVDVELGTYNTTAERVLAAVGPRTKAIMIAHALGNPFPVADVAAIAAE
HGLYLVEDNCDAVGSYHQGRLTGTFGDLTTTSFYPAHHITTGEGGCVLTRNLALARIVEQ
LRDWGRDCWCEPGKDNTCFKRFDYQLGTLPHGYDHKYIFTHLGYNLKATDIQAALGVSQL
SRLDSFGKARRANWQRMYEGLAGVPGLLLPRATEHSDPSWFGFVLTVLPDASFTRRGLED
FLGSRKIGTRRLFGGNLTRHPAYQDRDYRVVGELTNSDVITEHTLWVGVHPSMTDEMVDH
VAGSIREFAISAR
selected fasta
>putative pyridoxamine 5'-monophosphate-dependent NDP-hexose C-3 dehydratase [putative CDP-4-keto-6-deoxyglucose-3-dehydratase (E1)]
ATGGATGCGGAGAAGACGCACATCCTGGAGAGGGTGCGCGAGTACCACCAGGCCAGGGAG
CAGCGGGAGTTCGTGCCGGGCGTGACACCGGTGCAGCCCTCGGGCGCGGCGCTCGACGCG
AACGACCGGGTGGCGCTCGTCGAAGCGGCGCTCGACCTGAGGATCGCCGCCGGGCCGAGC
ACACAGCGCTTCGAGCGCGACTTCGCCCGCTACTTCGGGCTGCGCAAGGCACACATGACC
AACTCGGGTTCCTCCGCCAACCTTCTCGCCCTGACCTCGCTGACCTCGCACACGCTGGGC
GACCGCAGGCTGCGGCCCGGGGACGAGGTGATCACGGTGGCGGCCGGGTTCCCGACGACG
GTCAACCCGATCATCCAGAACGGCCTGGTCCCCGTCTTCGTGGACGTGGAGCTGGGGACG
TACAACACGACCGCCGAGCGGGTCCTCGCCGCGGTCGGCCCGCGCACGAAGGCGATCATG
ATCGCGCACGCGCTTGGCAACCCGTTCCCGGTCGCGGACGTCGCCGCCATCGCCGCCGAA
CACGGCCTGTACCTCGTCGAGGACAACTGCGACGCCGTCGGTTCGTACCACCAGGGCAGG
CTGACCGGCACCTTCGGCGACCTGACGACGACCAGTTTCTATCCGGCGCACCACATCACC
ACGGGCGAGGGCGGCTGTGTCCTCACCCGCAATCTGGCTCTCGCGCGGATCGTGGAGCAA
CTGCGGGACTGGGGCCGGGACTGCTGGTGCGAACCGGGCAAGGACAACACCTGCTTCAAG
CGGTTCGACTACCAGCTGGGGACGCTGCCGCACGGCTACGACCACAAGTACATCTTCACG
CATCTCGGCTACAACCTGAAGGCCACCGACATCCAGGCCGCGCTCGGCGTCAGCCAGCTG
TCGCGGCTCGACTCCTTCGGCAAGGCCCGGCGCGCCAACTGGCAGCGGATGTACGAGGGT
CTGGCGGGCGTTCCGGGGCTGCTGCTGCCCCGGGCGACGGAGCACAGCGACCCGAGCTGG
TTCGGCTTCGTGCTCACCGTGCTGCCCGACGCGTCTTTCACCCGGCGCGGCCTGGAGGAC
TTCCTCGGTTCCCGGAAGATCGGCACCAGGCGGCTGTTCGGCGGCAACCTGACCCGGCAC
CCCGCCTACCAGGACCGCGACTACCGGGTCGTGGGCGAGCTGACCAACTCCGACGTCATC
ACCGAGCACACCCTGTGGGTGGGCGTCCATCCCAGCATGACCGACGAGATGGTCGACCAC
GTGGCCGGAAGCATCCGGGAGTTCGCGATCTCGGCACGCTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR000653 DegT/DnrJ/EryC1/StrS aminotransferase (Family)
 [44-426]  3.90000000000001e-99 PF01041
PF01041   DegT_DnrJ_EryC1
 [3-433]  4.60000044330866e-116 PIRSF000390
PIRSF000390   PLP_StrS
IPR015421 Pyridoxal phosphate-dependent transferase, major region, subdomain 1 (Domain)
 [34-301]  1.9e-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)
 [302-426]  1.09999999999999e-45 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]  8.60006330213929e-93 SSF53383
SSF53383   PyrdxlP-dep_Trfase_major
SignalP No significant hit
TMHMM No significant hit
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