Borre_00110 : CDS information

Location

Organism	Streptomyces parvulus
Strain	Tü4055
Entry name	Borrelidin
Contig	AJ580915
Start / Stop / Direction	11,165 / 9,993 / - [in whole cluster] 11,165 / 9,993 / - [in contig]
Location	complement(9993..11165) [in whole cluster] complement(9993..11165) [in contig]
Type	CDS
Length	1,173 bp (390 aa)

Annotation

Category	2.2 modification addition of starter unit
Product	putative cyclase
Product (GenBank)	putative muconate cyclo-isomerase/lactamase
Gene
Gene (GenBank)	borE
EC number
Keyword	trans-1,2-CPDA
Note
Note (GenBank)
Reference	ACC Q70I06 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。 borE: starter unit biosynthesis closest similar to O-succinylbenzoate-CoA synthase borE 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、BorEはtrans-1,2-CPDA生合成に必須である。 borE productはO-succinylbenzoyl-CoA synthaseとchloromuconate cycloisomerasesに似ている。これらはenolase superfamilyに属する酵素で、carboxylate基に隣接するCのanion形成を安定化する能力がある。よってBorEは、trans-1,2-CPDA生合成においてputative intermediate(2-phospho-hepta-1,7-dioic acid)のcyclizationのために必要であると考えられている。
Related Reference	ACC O34508 PmId [11747447] Evolution of enzymatic activities in the enolase superfamily: functional assignment of unknown proteins in Bacillus subtilis and Escherichia coli as L-Ala-D/L-Glu epimerases. (Biochemistry. , 2001) [11747448] Evolution of enzymatic activities in the enolase superfamily: crystal structures of the L-Ala-D/L-Glu epimerases from Escherichia coli and Bacillus subtilis. (Biochemistry. , 2001) comment 126th(O34508) 26%, 1e-17 B.subtilis_ykfB L-Ala-D/L-Glu epimerase(EC 5.1.1.-) L-Ala-D/L-Glu epimerases活性測定あり。その他dipeptidesのepimerizationもできる。
Related Reference	ACC Q44244 PmId [14705949] Evolution of enzymatic activity in the enolase superfamily: functional studies of the promiscuous o-succinylbenzoate synthase from Amycolatopsis. (Biochemistry. , 2004) [15134446] Evolution of enzymatic activity in the enolase superfamily: structural studies of the promiscuous o-succinylbenzoate synthase from Amycolatopsis. (Biochemistry. , 2004) comment 365th(Q44244) 26%, 5e-09 Amycolatopsis sp_Aaar N-acylamino acid racemase -- [PMID: 14705949](2004)abstract Amycolatopsis sp_N-acylamino acid racemaseがむしろmenaquinone biosynthesisに関与するO-Succinylbenzoate synthaseであることを示した論文。 kcat/Km O-Succinylbenzoate synthase: 2.5 x 10(5) M-1 s-1 N-acylamino acid racemase (substrate N-acetylmethinine): 3.1 x 10(2) M-1 s-1 N-acylamino acid racemase (substrate N-acetylphenylglycine): 2.0 x 10(5) M-1 s-1 -- [PMID: 15134446](2004)abstract Amycolatopsis sp.のO-succinylbenzoate synthaseが　N-acylamino acid racemase活性も同時に持つに至った経緯を、タンパクの構造上から考察ている模様。

Sequence

>putative cyclase [putative muconate cyclo-isomerase/lactamase]
MIRRVRLHTAVVPMAAAFDHATRSRRSAASLLVEIELAGTRGWGEGAPRDYVTGETLDGA
VRAVQACDPGELAERIEWRDFESAVASIAQLPLTGLVDGSSAAAAVEIALLDAVCRHFAR
PLADVLRVLAPPARSRRDGPTSVSLVIHLSRDVATVLDALTPRALAALRHVKIKVADPAG
AVDRLTAAQDRLPADTRVSLDVNGAWTAEEAEKVAGELDGVGWVEEPLPPRSWPELGRLR
RATGLPVMLDESCTGPADLHAAATSGAASHINVRLSKCGGFLAAARLALRADELGVGCQL
GVHVAEVGPLWAAGRTLATAWDLWQTVEAGRADEWFPVPLTTPAFTVDRSLHRVEPLTGP
GTGIEPTEELLRHTRCAATWESGGGWRRNT

>putative cyclase [putative muconate cyclo-isomerase/lactamase]
GTGATCCGTCGCGTACGGCTGCACACCGCCGTCGTGCCCATGGCCGCGGCCTTCGACCAC
GCCACGCGCTCCCGTCGCAGCGCGGCGTCCCTGCTGGTCGAGATCGAGCTGGCGGGCACC
CGCGGATGGGGAGAGGGAGCGCCCCGCGACTACGTCACCGGTGAGACCCTGGACGGCGCG
GTGCGAGCCGTCCAGGCCTGCGATCCCGGGGAGCTGGCCGAGCGCATCGAGTGGCGGGAC
TTCGAGAGCGCCGTCGCCTCGATCGCACAGCTGCCGCTGACCGGGCTCGTCGACGGCTCG
TCGGCGGCGGCCGCCGTGGAGATCGCCCTGCTCGACGCGGTGTGCCGGCATTTCGCCCGG
CCGCTCGCCGACGTCCTGCGGGTCCTGGCCCCGCCTGCCCGATCACGGCGGGACGGACCG
ACGTCCGTCAGCCTCGTGATCCACCTCTCGCGCGACGTCGCGACCGTCCTGGACGCACTC
ACGCCGCGGGCGCTGGCGGCGTTGCGGCACGTGAAGATCAAGGTGGCGGACCCGGCCGGG
GCGGTGGACCGGCTGACGGCGGCCCAGGACCGCCTCCCCGCCGACACCCGTGTCTCACTG
GACGTCAACGGCGCCTGGACGGCCGAGGAAGCGGAGAAGGTCGCGGGCGAACTGGACGGC
GTGGGGTGGGTGGAGGAGCCGCTCCCGCCGCGGTCCTGGCCCGAGTTGGGCCGGCTGCGG
CGGGCCACCGGTCTGCCCGTCATGCTCGACGAGTCCTGTACCGGACCGGCCGACCTCCAC
GCCGCCGCCACCAGCGGCGCCGCCAGCCACATCAACGTACGGCTGTCGAAGTGCGGCGGG
TTCCTCGCCGCGGCACGCCTGGCACTGCGCGCCGACGAGCTCGGCGTCGGTTGCCAGCTC
GGCGTTCACGTGGCCGAGGTGGGGCCGCTGTGGGCGGCCGGGCGCACCCTGGCCACCGCA
TGGGACCTGTGGCAGACGGTCGAGGCGGGCCGGGCCGACGAGTGGTTCCCCGTGCCACTG
ACCACGCCGGCGTTCACCGTCGACCGGTCACTGCACCGGGTCGAACCCTTGACCGGTCCG
GGCACGGGCATCGAACCGACCGAAGAACTACTGCGACACACCCGGTGCGCGGCCACCTGG
GAATCCGGCGGCGGCTGGCGGAGGAACACATGA

Feature

BLASTP Database:UniProtKB:2011_09	show BLAST table
InterPro Database:interpro:38.0	IPR013342 Mandelate racemase/muconate lactonizing enzyme, C-terminal (Domain) PF01188 MR_MLE SM00922 MR_MLE
SignalP	Eukaryota Bacteria, Gram-positive
TMHMM	No significant hit

Borre_00100 Borre_00120