Borre_00120 Borre_00120   Borre_00140 Borre_00140

Borre_00130 : CDS information

close this sectionLocation

Organism
StrainTü4055
Entry nameBorrelidin
Contig
Start / Stop / Direction13,611 / 11,992 / - [in whole cluster]
13,611 / 11,992 / - [in contig]
Locationcomplement(11992..13611) [in whole cluster]
complement(11992..13611) [in contig]
TypeCDS
Length1,620 bp (539 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category2.2 modification addition of starter unit
Productputative acyltransferase
Product (GenBank)putative acetolactate synthase
Gene
Gene (GenBank)borG
EC number
Keyword
  • trans-1,2-CPDA
Note
Note (GenBank)
Reference
ACC
PmId
[15112998] Biosynthesis of the angiogenesis inhibitor borrelidin by Streptomyces parvulus Tu4055: cluster analysis and assignment of functions. (Chem Biol. , 2004)
comment
Borrelidin生合成gene clusterのクローニング。
borG: starter unit biosynthesis
closest similar to Acetolactate synthase, large subunit

borG productは、starter unit(trans-1,2-CPDA)生合成において定義される役割を示唆するタンパクとの明らかな類似が見られない。

borG insertional inactivation mutantはborrelidin産生が1/10に減る。
このmutant株にtrans-1,2-CPDAを加えるとborrelidin産生レベルは増加し、wildより約15倍(wild+trans-1,2-CPDA添加の5倍)も多くなる。

よって、BorGはtrans-1,2-CPDA生合成の調節に関与しているかもしれない。
Related Reference
ACC
Q84H44
PmId
[12358600] Sulphoacetaldehyde acetyltransferase yields acetyl phosphate: purification from Alcaligenes defragrans and gene clusters in taurine degradation. (Biochem J. , 2003)
comment
50th(Q84H44) 29%, 5e-46
Alcaligenes defragrans_xsc
Sulfoacetaldehyde acetyltransferase(EC 2.3.3.15)

taurine (2-aminoethanesulphonate)からtransaminateされた2-sulphoacetaldehydeは、phosphate、thiamin diphosphate and Mg(2+) ionsの存在下でsulphite + acetyl phosphateへ変換されることを同定。
これを担う酵素をsulphoacetaldehyde acetyltransferase (Xsc; EC 2.3.1.-)とした。

close this sectionSequence

selected fasta
>putative acyltransferase [putative acetolactate synthase]
MKVFHALADALTAHGVDTVFGLMGNANLLYLPAFADAGGRFVAVAHEAGAVAMADGRARM
CGGIGVASVTHGPAFTNALTPLVEAARSHSQVLLITGDPPPVPTHFHHFDIATVAAAAGA
GYERVHRPASLVADLNRAVQRIVAERRPVVLNVPIDLMQAEAGEQAPVTLPVAPGPLAAP
EAEALDGALGLIGSAKRPLVLAGHGAAVAGAREALVELADRTGAALATTVLGKEMFAGHP
RDVGIFGSLAHSVASTVIAESDCVIAFGASLNMWTVLNGELLRGKRVVHVDTDPARFGSY
SPVDEPVAGDARRTAETMNVLLDQAGVTAANGAWAERVAGQLAGFSPQDDVDDRSGAETV
DIRTAMIRLDRILPAERSVVSDIGRFDVGVWPYLRVADPLHFTVMGGFGSIGLGVAGAIG
AATAGTGRPVVAAVGDGGFMMHLSEFTTAVRYRLPLVVVVLNDGAYGAEHYKLRNHGYDP
AYSAFAWPDLAGLATAMGARALTVRKAEELDAVGDLLSTLEGPLLVDVRLDPDVNLVRY
selected fasta
>putative acyltransferase [putative acetolactate synthase]
ATGAAGGTTTTCCACGCGCTCGCCGACGCTCTGACCGCACACGGCGTCGATACCGTCTTC
GGTCTCATGGGCAACGCCAATCTGCTCTATCTGCCCGCCTTCGCCGACGCGGGCGGACGG
TTCGTGGCGGTCGCCCACGAGGCGGGCGCCGTCGCCATGGCCGACGGCCGCGCACGTATG
TGCGGCGGCATCGGTGTGGCGTCCGTGACGCACGGGCCGGCTTTCACCAACGCCTTGACC
CCTCTTGTGGAAGCGGCTCGTAGCCACAGCCAGGTCCTGCTGATCACAGGTGATCCGCCA
CCGGTGCCCACGCACTTCCACCACTTCGACATCGCGACGGTCGCGGCCGCGGCGGGCGCG
GGGTACGAACGCGTCCACAGACCGGCCTCGCTCGTCGCGGACCTGAACCGGGCCGTCCAG
CGGATCGTGGCCGAGCGGCGGCCCGTCGTACTCAATGTGCCGATCGACCTCATGCAGGCG
GAGGCGGGCGAGCAGGCGCCGGTCACGCTCCCGGTGGCGCCGGGTCCTCTGGCCGCTCCG
GAGGCCGAGGCGCTGGACGGCGCGCTGGGGCTGATCGGCTCGGCCAAGCGGCCGCTGGTC
CTCGCCGGGCACGGTGCGGCCGTCGCCGGTGCGCGAGAGGCCCTGGTGGAGCTGGCGGAC
CGTACCGGAGCAGCGCTGGCCACCACCGTGCTCGGCAAGGAGATGTTCGCCGGTCACCCC
CGCGACGTCGGCATCTTCGGCTCGCTCGCGCACAGCGTGGCGAGCACGGTCATCGCCGAG
TCGGACTGCGTGATCGCGTTCGGGGCGAGCCTGAACATGTGGACCGTGCTCAACGGCGAG
CTGCTCCGCGGCAAGAGAGTCGTGCACGTGGACACCGATCCGGCACGGTTCGGCTCGTAC
AGCCCCGTCGACGAGCCCGTGGCCGGGGATGCCCGCCGCACGGCCGAGACCATGAACGTC
CTGCTGGATCAGGCCGGAGTCACCGCGGCCAACGGCGCCTGGGCGGAGCGCGTCGCCGGG
CAACTGGCCGGGTTCTCGCCGCAGGACGACGTCGACGACCGCAGTGGAGCGGAGACCGTC
GACATCCGGACGGCCATGATCCGGCTGGACCGGATACTGCCCGCCGAGCGCAGTGTCGTC
AGCGATATCGGCCGCTTCGACGTGGGTGTCTGGCCGTATCTGCGCGTGGCGGACCCGCTG
CACTTCACCGTCATGGGCGGCTTCGGCTCGATCGGGCTCGGCGTCGCCGGGGCGATCGGC
GCGGCGACGGCCGGGACCGGCCGGCCCGTGGTCGCCGCCGTGGGGGACGGCGGCTTCATG
ATGCACCTGTCGGAGTTCACGACGGCGGTACGGTACCGGCTGCCGCTCGTCGTGGTCGTA
CTCAACGACGGGGCGTACGGAGCCGAGCACTACAAACTCAGGAACCACGGCTACGACCCG
GCGTACTCGGCGTTCGCCTGGCCCGACCTCGCCGGGCTGGCCACGGCGATGGGCGCACGT
GCCCTCACCGTCCGCAAGGCGGAAGAACTCGACGCCGTCGGCGACCTGTTGTCGACGCTC
GAAGGACCGCTCCTCGTCGACGTCCGGCTGGACCCCGACGTCAATCTCGTCCGGTACTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR011766 Thiamine pyrophosphate enzyme, C-terminal TPP-binding (Domain)
[382-528] 1.8e-30 PF02775
PF02775   TPP_enzyme_C
IPR012000 Thiamine pyrophosphate enzyme, central domain (Domain)
[186-316] 2.7e-28 PF00205
PF00205   TPP_enzyme_M
IPR012001 Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain (Domain)
[1-164] 1.99999999999999e-36 PF02776
PF02776   TPP_enzyme_N
SignalP No significant hit
TMHMM No significant hit
Borre_00120 Borre_00120   Borre_00140 Borre_00140
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