Borre_00100 : CDS information

close this sectionLocation

Organism
StrainTü4055
Entry nameBorrelidin
Contig
Start / Stop / Direction9,996 / 9,244 / - [in whole cluster]
9,996 / 9,244 / - [in contig]
Locationcomplement(9244..9996) [in whole cluster]
complement(9244..9996) [in contig]
TypeCDS
Length753 bp (250 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category2.2 modification addition of starter unit
Productputative oxidoreductase
Product (GenBank)putative ketoreductase
Gene
Gene (GenBank)borD
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。
borD: starter unit biosynthesis
closest similar to 3-oxoacyl-ACP reductase FabG

borD insertional inactivation mutantはborrelidin産生が消滅。
borrelidin starter unitであるtrans-cyclopentane (1R,2R)-dicarboxylic acid (trans-1,2-CPDA)添加でborrelidin産生は回復し、wildよりも増えたりする。
よって、BorDはtrans-1,2-CPDA生合成に必須である。

trans-1,2-CPDA生合成経路において、BorC or BorDのどちらかがC2でketo基をhydroxyl基に還元すると考えられる。
Related Reference
ACC
P0AEK2
PmId
[1556094] The gene encoding Escherichia coli acyl carrier protein lies within a cluster of fatty acid biosynthetic genes. (J Biol Chem. , 1992)
[11669613] Structure of beta-ketoacyl-[acyl carrier protein] reductase from Escherichia coli: negative cooperativity and its structural basis. (Biochemistry. , 2001)
comment
76th(P0AEK2) 35%, 8e-29
E.coli_fabG
3-oxoacyl-[acyl-carrier-protein] reductase(EC 1.1.1.100)

(3R)-3-hydroxyacyl-[acyl-carrier-protein] + NADP+ = 3-oxoacyl-[acyl-carrier-protein] + NADPH.

--
[PMID: 1556094](1992)
acpP-fabD のクローニングとシークエンス, cotranscriprion確認。

--
[PMID: 11669613](2001)
FabGの結晶構造解析。
FabGはNADPHのnegative cooperative bindingを示す。この効果はACPの存在によって拡大される。

close this sectionSequence

selected fasta
>putative oxidoreductase [putative ketoreductase]
MTARHDVALVTGAGSGICAEVARGLAARGLRVVLLDKDAEAVHRVADGLGDRLARDPLVA
DVTDPHALASAVDSLAPQHRPGVLVNGVGGDTRARSVTELTEADLQEAVTHNLASVFTMT
RLCVPAMVAAGWGRVVNLASVAGRTYTRFSNAAYVAAKAGVIGFTKQCAYELAPHGVTVN
AVAHGVIGTERIRRAWEDKPPQWTADRVSHIPAGRFGSVAEAAGMVCHLCGEDAGYTTGT
VVDVNGGLHI
selected fasta
>putative oxidoreductase [putative ketoreductase]
ATGACGGCACGACACGACGTGGCTCTGGTGACCGGAGCGGGCAGCGGCATCTGCGCGGAG
GTCGCCCGAGGCCTGGCGGCCCGGGGCCTGCGGGTGGTCCTGCTCGACAAGGACGCCGAG
GCGGTGCACCGGGTCGCGGACGGGCTCGGCGACCGGCTGGCCCGGGACCCGCTGGTCGCC
GACGTGACCGACCCTCACGCCCTGGCGTCCGCCGTCGACTCGCTCGCCCCGCAGCACCGG
CCGGGCGTCCTGGTCAACGGCGTCGGTGGCGACACCCGGGCCCGCTCGGTGACCGAACTG
ACCGAGGCCGACCTCCAGGAGGCCGTCACGCACAACCTGGCGAGCGTGTTCACCATGACC
CGGCTGTGCGTCCCGGCGATGGTCGCGGCGGGGTGGGGCAGGGTCGTCAACCTGGCGTCC
GTGGCCGGTCGCACGTACACCCGGTTCAGCAATGCCGCCTACGTCGCCGCCAAGGCCGGC
GTCATCGGGTTCACCAAGCAGTGCGCCTACGAACTGGCCCCGCACGGCGTGACGGTCAAC
GCGGTCGCCCACGGCGTCATCGGCACCGAGCGCATCCGCCGGGCTTGGGAGGACAAGCCC
CCGCAGTGGACCGCCGACCGCGTCAGCCACATCCCCGCCGGCCGCTTCGGCAGCGTCGCC
GAGGCCGCGGGCATGGTCTGCCATCTGTGCGGCGAGGACGCCGGATACACCACCGGCACG
GTCGTCGACGTCAACGGCGGACTGCACATATGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR002198 Short-chain dehydrogenase/reductase SDR (Family)
 [79-90]  2.6999988713206e-08 PR00080 [133-141]  2.6999988713206e-08 PR00080 [154-173]  2.6999988713206e-08 PR00080
PR00080   SDRFAMILY
 [7-172]  1.2e-21 PF00106
PF00106   adh_short
IPR002347 Glucose/ribitol dehydrogenase (Family)
 [7-24]  1.10000150671642e-29 PR00081 [127-143]  1.10000150671642e-29 PR00081 [154-173]  1.10000150671642e-29 PR00081 [175-192]  1.10000150671642e-29 PR00081 [212-232]  1.10000150671642e-29 PR00081
PR00081   GDHRDH
IPR016040 NAD(P)-binding domain (Domain)
 [4-250]  2.50000000000001e-63 G3DSA:3.40.50.720
G3DSA:3.40.50.720   NAD(P)-bd
SignalP
 [1-19]  0.689 Signal
Eukaryota   
TMHMM No significant hit
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