Lasal2_00140 : CDS information

Location

Organism	Streptomyces lasaliensis
Strain	ATCC 31180
Entry name	Lasalocid
Contig	FM173265
Start / Stop / Direction	15,965 / 17,329 / + [in whole cluster] 15,965 / 17,329 / + [in contig]
Location	15965..17329 [in whole cluster] 15965..17329 [in contig]
Type	CDS
Length	1,365 bp (454 aa)

Annotation

Category	2.1 modification addition of extender units
Product	putative crotonyl-CoA reductase
Product (GenBank)	crotonyl-CoA reductase
Gene
Gene (GenBank)	las5
EC number	1.3.1.-
Keyword	ethylmalonyl-CoA
Note
Note (GenBank)	NADPH:quinone reductase and related Zn-dependent oxidoreductases
Reference	ACC B5M9K6 PmId [19025863] Analysis of specific mutants in the lasalocid gene cluster: evidence for enzymatic catalysis of a disfavoured polyether ring closure. (Chembiochem. , 2008) comment GenBank,Uniprotでは、NRRL3382Rと登録されている。 S. lasaliensis ATCC31180におけるLasalocid生合成gene clusterの報告。 las5: ethylmalonyl CoA synthase homolog: PlmT7_Streptomyces sp. HK803 このORFとlas6は、crotonyl-CoA reductaseと3-hydroxyacyl CoA dehydrogenaseをエンコードすると推測。両ORFは、PKSのためのunusual butyrate unitsの原料であるethylmalonyl CoAの供給に関与しそうだと推測している。
Related Reference	ACC B6ZK62 NITE Lasal_00110 PmId [19129623] Identification of a gene cluster of polyether antibiotic lasalocid from Streptomyces lasaliensis. (Biosci Biotechnol Biochem. , 2009) comment GenBank,Uniprotでは、ATCC31180と登録されている。 S.lasaliensis ATCC35851におけるLasalocid生合成gene clusterの報告。 lsd9: ethylmalonyl-CoA biosynthesis homolog: PlmT7_streptomyces sp. HK803 crotonyl-CoA reductaseは、lasalocid poryketide骨格の必須伸張ユニットであるethylmalonyl-CoAを提供するkey酵素。最近の研究では、crotonyl-CoA reductaseは、直接ethylmalonyl-CoA を提供するためにcrotoconyl-CoAの還元とカルボキシル化を行うことがわかっているとの記述有り。
	ACC Q53865 PmId [8521864] Purification of crotonyl-CoA reductase from Streptomyces collinus and cloning, sequencing and expression of the corresponding gene in Escherichia coli. (Eur J Biochem. , 1995) comment Streptomyces collinus_ccr Crotonyl CoA reductase 分子量からおそらくhomodimerで機能していると考えられる。 E.coliでcloning､発現､精製し、活性をみている。crotonyl-CoAとenoyl-CoA（C4）には高い基質特異性を見せるが、enoyl-CoA thioester, acryloyl-CoAのような短鎖(C3)には測定可能な活性はみられなかった。
	ACC Q9RNU6 PmId [10542184] Role of crotonyl coenzyme A reductase in determining the ratio of polyketides monensin A and monensin B produced by Streptomyces cinnamonensis. (J Bacteriol. , 1999) comment Streptomyces cinnamonensis_ccr Crotonyl-CoA reductase S. cinnamonensis_ccr、そのS. cinnamonensisで異種性発現させたS. collinus_ccr、ccr-disrupted mutantなどでCCR activity測定あり。 monensin A/monensin Bの比率は、CCR活性のレベルと、CCRの基質であるcrotonyl-CoAの両方に依存する。
	ACC B8XVS5 PmId [17548827] Synthesis of C5-dicarboxylic acids from C2-units involving crotonyl-CoA carboxylase/reductase: the ethylmalonyl-CoA pathway. (Proc Natl Acad Sci U S A. , 2007) [19458256] Carboxylation mechanism and stereochemistry of crotonyl-CoA carboxylase/reductase, a carboxylating enoyl-thioester reductase. (Proc Natl Acad Sci U S A. , 2009) comment Rhodobacter sphaeroides_Crotonyl-CoA carboxylase/reductase(ccr) この酵素だけでcrotonyl-CoAのreductionとreductive carboxylationが触媒されることを確かめている。 crotonyl-CoA＋NADPH＋CO2 → ethylmalonyl-CoA-＋NADP+

Sequence

>putative crotonyl-CoA reductase [crotonyl-CoA reductase]
MEEIISAVLSEDAVEGDFGALPVPDHYRGAVVLRDETAMFEGLATADKDPGKSLHVQDVP
TPLPAPGEVLVAVMASAINYNTVWSAIFEPLPTFGFLERYARSGPDAARHDQPYHVLGSD
LSGVVLRTGPGVRRWKPGDRVVAHCLSVELESPDGHDDTMLDPEQRIWGFETNFGGLAEL
ALVKANQLMPMPEHLTWEEAACSGLVNSTAYRQLVSRNGAGMKQGDVVLIWGAGGGLGSY
ATQLALNGGAVPVCVVSGPRKAELVRSMGADLVIDRAAEGYRFWKDPQTQDPREWRRFGA
RIRELTGGQDPDIVVEHPGRETFGASVYVTRRGGTVVTCASTAGYQHQYDNRYLWMSLKR
IVGTHFANYREAWEANRLIARGMIHPTLSAVFPLTATGEATREVHANRHSGKVGVLGLAP
AEGLGVRDPETRERHLAALNRFRTPQARPTAAER

>putative crotonyl-CoA reductase [crotonyl-CoA reductase]
GTGGAAGAGATCATCAGTGCCGTACTGTCCGAGGACGCGGTCGAGGGGGACTTCGGCGCC
CTGCCGGTGCCCGACCACTACCGCGGGGCAGTGGTCCTCAGGGACGAGACAGCCATGTTC
GAGGGGCTGGCCACCGCCGACAAGGACCCGGGCAAGTCCCTGCACGTCCAGGACGTGCCG
ACCCCGCTGCCCGCACCGGGCGAGGTGCTCGTCGCCGTCATGGCGAGCGCGATCAATTAC
AACACCGTGTGGAGCGCGATCTTCGAACCGCTGCCCACGTTCGGGTTCCTGGAGCGGTAC
GCGCGCTCCGGCCCGGACGCGGCCCGCCACGACCAGCCGTACCACGTCCTGGGGTCCGAC
CTGTCCGGGGTGGTGCTGCGCACCGGGCCAGGGGTGCGGCGCTGGAAACCGGGCGACCGG
GTGGTGGCGCACTGCCTGTCGGTCGAACTGGAGTCCCCCGACGGCCACGACGACACCATG
CTCGATCCCGAGCAGCGCATCTGGGGCTTCGAGACCAACTTCGGCGGCCTGGCCGAACTG
GCGCTGGTCAAGGCCAACCAGCTGATGCCCATGCCCGAGCACCTCACCTGGGAGGAGGCG
GCGTGCTCCGGGCTGGTCAACTCCACGGCGTACCGCCAGCTCGTCTCCCGCAACGGGGCC
GGGATGAAGCAGGGGGACGTGGTGCTGATCTGGGGCGCCGGCGGCGGCCTCGGCTCCTAC
GCCACCCAACTCGCCCTCAACGGCGGGGCGGTGCCGGTGTGTGTGGTGTCGGGGCCCCGC
AAGGCCGAGCTGGTCCGGTCGATGGGCGCCGACCTGGTCATCGACCGGGCCGCCGAGGGC
TACCGCTTCTGGAAGGACCCGCAGACCCAGGATCCGCGGGAGTGGCGGCGCTTCGGCGCC
CGGATCAGGGAGCTGACCGGCGGCCAGGACCCCGACATCGTCGTGGAGCACCCGGGCCGG
GAGACGTTCGGTGCCAGTGTCTACGTCACGCGCCGCGGCGGCACCGTCGTGACGTGCGCC
TCGACGGCCGGGTACCAGCACCAGTACGACAACCGCTACCTGTGGATGTCGCTGAAGCGG
ATCGTGGGCACCCACTTCGCCAACTACCGCGAGGCGTGGGAGGCCAACCGGCTCATCGCT
CGGGGCATGATCCATCCCACGCTGTCCGCCGTCTTCCCGCTCACGGCTACCGGCGAGGCG
ACGCGCGAGGTGCACGCCAACCGGCACAGCGGGAAGGTCGGTGTCCTCGGCCTGGCCCCG
GCCGAAGGACTGGGCGTGCGCGACCCGGAGACCAGGGAACGCCACCTGGCGGCCCTCAAC
CGGTTCCGGACACCGCAGGCACGACCGACGGCAGCCGAACGCTAG

Feature

BLASTP Database:UniProtKB:2011_09	show BLAST table
InterPro Database:interpro:38.0	IPR010085 Crotonyl-CoA reductase (Family) TIGR01751 Crot-CoA-red IPR011032 GroES-like (Domain) SSF50129 GroES_like IPR013149 Alcohol dehydrogenase, C-terminal (Domain) PF00107 ADH_zinc_N IPR013154 Alcohol dehydrogenase GroES-like (Domain) PF08240 ADH_N IPR016040 NAD(P)-binding domain (Domain) G3DSA:3.40.50.720 NAD(P)-bd
SignalP	No significant hit
TMHMM	No significant hit

Lasal2_00130 Lasal2_00150