Enter_00030 Enter_00030   Enter_00050 Enter_00050

Enter_00040 : CDS information

close this sectionLocation

Organism
Strain
Entry nameEnterocin
Contig
Start / Stop / Direction3,330 / 4,937 / + [in whole cluster]
3,330 / 4,937 / + [in contig]
Location3330..4937 [in whole cluster]
3330..4937 [in contig]
TypeCDS
Length1,608 bp (535 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category2.2 modification addition of starter unit
Productcinnamic acid--CoA ligase
cinnamoyl-CoA synthetase
Product (GenBank)putative acyl-CoA ligase EncH
Gene
Gene (GenBank)encH
EC number6.2.1.-
Keyword
Note
Note (GenBank)
Reference
ACC
PmId
[11137817] Cloning, sequencing and analysis of the enterocin biosynthesis gene cluster from the marine isolate 'Streptomyces maritimus': evidence for the derailment of an aromatic polyketide synthase. (Chem Biol. , 2000)
[12511484] Characterization of benzoyl coenzyme A biosynthesis genes in the enterocin-producing bacterium "Streptomyces maritimus". (J Bacteriol. , 2003)
comment
[PMID: 11137817](2000)
enterocin と wailupemycinsの生合成をコードするgene clusterの同定。

EncH: Acyl-CoA ligase

配列解析のみ。long-chain fatty acid-CoA ligasesと相同性がある。
PKS starter unitであるbenzoic acidの生合成経路(Figure 3)で、2番目の反応として
cinnamic acid → cinnamoyl-CoAを触媒すると考えられている。


---
同じ著者らの続報。
[PMID: 12511484](2003)
benzoyl-CoA生合成遺伝子についての報告。

EncH: Cinnamate-CoA ligase

encH, encI, encJの破壊mutantは、benzoyl-CoA-primed enterocinの収量がwildより下がった。
完全に抑制されないのは、一次代謝酵素が代替しているのかもしれない。

encH mutantは翻訳共役なencI の不活化の影響を受けているのかもしれず、EncHの機能が不明瞭なので、EncHをoctahistidyl-tagged recombinant proteinとして発現、精製し、実際にin virtoでtrans-cinnamic acidのCoA活性化を触媒することを確認した(unpublished observations)。
Related Reference
ACC
Q9EY88
PmId
[11152072] Identification of Amycolatopsis sp. strain HR167 genes, involved in the bioconversion of ferulic acid to vanillin. (Appl Microbiol Biotechnol. , 2000)
comment
Blast 126th, id34%, 4e-58
Amycolatopsis sp. HR167_fcs
Feruloyl-CoA synthetase

Amycolatopsis sp. strain HR167からech (encoding enoyl-CoA hydratase/aldolase), fcs (encoding an unusual feruloyl-CoA synthetase)を含む4 kb断片をクローニングしてシークエンス。
この断片をE. coliに導入するとferulic acid → vanillinへ変換できるようになり、feruloyl-CoA synthetase活性、enoyl-CoA hydratase/aldolase活性が検出された。

close this sectionSequence

selected fasta
>cinnamic acid--CoA ligase [putative acyl-CoA ligase EncH]
MEPAPQAPTQPVIDARRPEAGPRWETIGELIKDAALLHGDKEFLRCGDKTLSFSETDTRT
DRLAQALIAQGVKPGDRVAVMMDNVADWPLSWFAAIKAGAITVPVNTRFGATDLAHVLKD
SQAVRVLASPGCVPLARDVSGSIGHPCAVRTLRELEADFGDRPVDGPGLSAHADDTVNFQ
YTSGTTGFPKACMLSHDYWLRTAWMIAVHSGLRPDDVVLTAQAFSYMDPQWKAVMCLMGG
VPLVVLPRFSASGFWHSVRQHRATLTYVLGSMPMLLYKQPPHSGDRDHAMRLVLCSGIPR
DLHHAFEDRWGAAWREVYGSTESGLDLIMPPGEEATVGSGAMGYPPSGKEVIVADERQRP
VQPGQIGEILVRGRPMMKGYWNNPDSTERAFRGGWYHTGDLGRAEAAGSVVHAGRLKDMI
RRGGENIAAAEVESVLEAHPAVLAAALAGIPDELFGELPKAFLQLRPGYRPTTATARSVL
AHTRRHLAKFKVPAYVEFVDSFPMTPSARIQKRQLLRPGDDQRTGAFDAAADAWA
selected fasta
>cinnamic acid--CoA ligase [putative acyl-CoA ligase EncH]
ATGGAACCGGCCCCTCAGGCCCCCACACAACCTGTGATCGACGCTCGGCGCCCCGAAGCG
GGACCGCGTTGGGAGACCATCGGCGAGCTCATCAAAGATGCCGCGTTGCTGCACGGCGAC
AAGGAATTCCTCCGATGCGGCGACAAGACGCTCAGCTTCTCCGAGACCGACACCCGCACC
GACCGGTTGGCGCAGGCGCTGATCGCCCAAGGTGTCAAACCGGGTGACCGTGTCGCGGTC
ATGATGGACAACGTGGCGGACTGGCCGTTGAGCTGGTTCGCGGCCATCAAGGCCGGTGCC
ATCACGGTGCCGGTCAACACCCGCTTCGGCGCTACGGACCTCGCGCACGTCCTGAAGGAC
TCTCAGGCCGTGCGGGTCCTGGCCTCCCCAGGCTGCGTGCCTTTGGCCCGTGACGTGAGC
GGCAGCATCGGGCACCCCTGTGCGGTCCGGACGCTACGCGAACTGGAGGCCGACTTCGGC
GACCGGCCGGTGGACGGTCCGGGCCTGTCGGCGCACGCGGACGACACCGTCAACTTCCAG
TACACCTCCGGCACCACAGGCTTTCCGAAAGCCTGCATGCTCAGCCACGACTACTGGCTG
CGCACGGCGTGGATGATCGCTGTCCACTCCGGCCTCCGTCCCGACGACGTCGTGCTGACG
GCCCAGGCGTTCTCCTACATGGATCCCCAGTGGAAAGCCGTGATGTGCCTGATGGGCGGC
GTTCCGCTGGTGGTGCTCCCGCGGTTCTCCGCCTCCGGCTTCTGGCACTCCGTCCGCCAG
CACCGGGCCACGCTGACCTACGTGCTGGGCAGCATGCCCATGCTGCTGTACAAGCAGCCG
CCCCACTCGGGCGACCGCGATCATGCGATGCGGCTGGTCTTGTGCTCGGGCATCCCGCGC
GACTTGCACCATGCGTTCGAGGACCGCTGGGGTGCGGCCTGGCGGGAGGTGTACGGCTCC
ACCGAGAGCGGACTGGACTTGATCATGCCGCCTGGTGAGGAGGCCACCGTGGGCAGCGGC
GCGATGGGGTACCCGCCGTCCGGCAAGGAGGTCATCGTCGCCGACGAGCGCCAACGCCCC
GTCCAGCCAGGGCAGATCGGCGAGATCCTGGTGCGGGGAAGGCCCATGATGAAAGGCTAC
TGGAACAACCCGGACAGTACCGAGCGGGCGTTCCGCGGCGGCTGGTACCACACCGGTGAC
CTCGGACGTGCCGAGGCGGCCGGGAGCGTGGTGCACGCCGGGCGGCTGAAGGACATGATC
CGACGCGGTGGGGAGAACATCGCAGCGGCCGAAGTCGAGAGCGTCCTCGAAGCCCACCCG
GCGGTCCTGGCCGCCGCGCTCGCCGGCATCCCCGACGAGCTCTTCGGTGAGCTGCCCAAA
GCCTTCCTGCAGCTGCGCCCCGGCTACCGGCCCACCACGGCAACGGCTCGCAGCGTCCTC
GCGCACACCCGCCGCCACCTCGCGAAATTCAAGGTCCCTGCCTATGTCGAATTCGTCGAC
TCCTTCCCCATGACCCCCTCCGCCCGTATCCAGAAGCGCCAGCTGCTTCGTCCCGGAGAC
GACCAGCGCACCGGTGCGTTCGACGCCGCAGCGGATGCATGGGCATGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR000873 AMP-dependent synthetase/ligase (Domain)
[52-446] 1.99999999999999e-92 PF00501
PF00501   AMP-binding
IPR020845 AMP-binding, conserved site (Conserved_site)
[179-190] PS00455
PS00455   AMP_BINDING
IPR025110 Domain of unknown function DUF4009 (Domain)
[490-515] 2.1e-05 PF13193
PF13193   DUF4009
SignalP No significant hit
TMHMM No significant hit
Enter_00030 Enter_00030   Enter_00050 Enter_00050
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