Lando_00140 : CDS information

close this sectionLocation

Organism
StrainS136
Entry nameLandomycin
Contig
Start / Stop / Direction14,216 / 15,520 / + [in whole cluster]
14,216 / 15,520 / + [in contig]
Location14216..15520 [in whole cluster]
14216..15520 [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 homolog
Gene
Gene (GenBank)lanQ
EC number
Keyword
  • L-rhodinose
Note
Note (GenBank)
  • LanQ
Reference
ACC
PmId
[9933932] Cloning and characterization of a gene cluster from Streptomyces cyanogenus S136 probably involved in landomycin biosynthesis. (FEMS Microbiol Lett. , 1999)
comment
landomycin生合成gene clusterの同定論文。

lanQ: NDP-hexose 3,4-dehydratase

配列解析のみ。
Yersinia pseudotuberculosisのAscCや、SMAT (secondary metabolic aminotransferase) familyのタンパクに似ている。AscCはC-3 dehydroxylationに関連する。L-rhodinoseの生合成はposition C-3でのdehydroxylationを必要とするので、LanQはこの反応に関連するかもしれない。
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-161
Saccharopolyspora spinosa_spnQ
probable NDP-hexose-3,4-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 homolog]
MSVHRKLVLDEVRKYHQDTQGDGVFVPGTTEIWPSGAVLDEDDRIALVEAALEMRIAAGR
SSRKFESSFARKMKRRKAHLTNSGSSANLLATTALTSHLLEDRRLRPGDEVITVAAGFPT
TVNPILQNGLIPVFVDVELGTYKTTADRVAQAIGPKTRAIIIAHTLGNPFEVAEIAQLAV
DHDLFLIEDNCDAVGSTYDGKLTGTFGELTTVSFYPAHHLTMGEGGCVLTADLALARIVE
SLRDWGRDCWCEPGESDKCLKRFKYQMGTLPAGYDHKYIFSHVGYNLKATDLQAALGLTQ
LAKLDDFVEARKRNWRRLRDGLDGVPHLLLPEATPRRHPSWFGFVLTVSPDAPFKRAELV
DFLEGRKIGTRRLFAGNLTRHPAYIDQPHRVVGNLDNSDIITEQTFWVGVYPGLTDEMLD
YVISSVKEFVEARG
selected fasta
>putative pyridoxamine 5'-monophosphate-dependent NDP-hexose C-3 dehydratase [NDP-hexose 3,4-dehydratase homolog]
ATGAGCGTGCACAGGAAACTTGTGCTCGACGAGGTCCGCAAGTACCACCAGGACACCCAG
GGCGACGGCGTGTTCGTTCCCGGCACCACGGAGATCTGGCCGTCCGGAGCGGTGCTCGAC
GAGGACGACCGGATCGCTCTCGTCGAGGCAGCCCTGGAGATGCGCATCGCGGCCGGCCGC
AGCTCTCGCAAGTTCGAGTCGTCCTTCGCCCGCAAGATGAAACGGCGCAAGGCCCACCTC
ACCAACTCCGGCTCCTCGGCGAACCTGCTCGCGACGACGGCTCTGACCTCACACCTCCTG
GAGGACCGCAGGCTGCGGCCCGGCGACGAGGTCATCACCGTGGCGGCGGGCTTCCCCACC
ACGGTCAACCCGATCCTGCAGAACGGCCTCATTCCGGTTTTCGTCGACGTCGAACTCGGC
ACCTACAAAACGACAGCGGACCGCGTCGCCCAGGCCATCGGTCCGAAGACCCGGGCGATA
ATTATTGCGCACACGCTCGGCAACCCCTTCGAAGTCGCCGAGATCGCCCAACTCGCCGTC
GACCACGACCTGTTCCTCATCGAGGACAACTGCGACGCGGTCGGTTCGACGTACGACGGC
AAACTCACCGGTACCTTCGGTGAGCTGACCACCGTCAGCTTCTACCCGGCCCACCACCTC
ACGATGGGCGAGGGCGGCTGCGTCCTGACGGCGGACCTGGCACTCGCCCGGATCGTCGAG
TCCCTGCGTGACTGGGGTCGCGACTGCTGGTGCGAGCCCGGTGAGAGCGACAAGTGCCTC
AAGCGGTTCAAGTACCAGATGGGCACCCTGCCGGCCGGCTACGACCACAAGTACATCTTC
TCGCACGTCGGTTACAACCTGAAGGCCACCGATCTGCAGGCGGCGCTCGGCCTCACCCAG
CTCGCCAAGCTCGACGACTTCGTCGAGGCACGCAAGCGCAACTGGCGGCGGCTGCGCGAC
GGCCTGGACGGCGTCCCGCACCTCCTGCTGCCCGAGGCCACACCGCGCAGGCACCCGAGT
TGGTTCGGCTTCGTGCTCACCGTCAGTCCGGACGCCCCCTTCAAGCGCGCGGAGCTGGTG
GACTTCCTGGAGGGCCGCAAGATCGGCACCCGGCGTCTCTTCGCCGGCAACCTCACCCGG
CACCCCGCCTACATCGACCAGCCCCACCGGGTCGTCGGCAACCTCGACAACAGCGACATC
ATCACCGAGCAGACCTTCTGGGTGGGCGTCTACCCGGGCCTGACCGACGAGATGCTCGAC
TACGTGATCTCCTCGGTGAAGGAATTCGTGGAGGCCCGCGGATGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR000653 DegT/DnrJ/EryC1/StrS aminotransferase (Family)
 [2-434]  1.09999184471405e-109 PIRSF000390
PIRSF000390   PLP_StrS
 [41-426]  8.70000000000003e-97 PF01041
PF01041   DegT_DnrJ_EryC1
IPR015421 Pyridoxal phosphate-dependent transferase, major region, subdomain 1 (Domain)
 [32-302]  2.30000000000004e-67 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]  1.6e-49 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]  6.10002656149838e-92 SSF53383
SSF53383   PyrdxlP-dep_Trfase_major
SignalP No significant hit
TMHMM No significant hit
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