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CDS information : Lasal2_00140


close this sectionLocation

Organism
StrainATCC 31180
Entry nameLasalocid
Contig
Start / Stop / Direction15,965 / 17,329 / + [in whole cluster]
15,965 / 17,329 / + [in contig]
Location15965..17329 [in whole cluster]
15965..17329 [in contig]
TypeCDS
Length1,365 bp (454 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category2.1 modification addition of extender units
Productputative crotonyl-CoA reductase
Product (GenBank)crotonyl-CoA reductase
Gene
Gene (GenBank)las5
EC number1.3.1.-
Keyword
  • ethylmalonyl-CoA
Note
Note (GenBank)
  • NADPH:quinone reductase and related Zn-dependent oxidoreductases
Reference
ACC
PmId
[19025863] Analysis of specific mutants in the lasalocid gene cluster: evidence for enzymatic catalysis of a disfavoured polyether ring closure. (Chembiochem. , 2008)
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)
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)
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)
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)

close this sectionSequence

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

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR010085 Crotonyl-CoA reductase (Family)
 [32-428]  TIGR01751
TIGR01751   Crot-CoA-red
IPR011032 GroES-like (Domain)
 [44-239]  5.10001002358244e-32 SSF50129
SSF50129   GroES_like
IPR013149 Alcohol dehydrogenase, C-terminal (Domain)
 [236-380]  3.2e-36 PF00107
PF00107   ADH_zinc_N
IPR013154 Alcohol dehydrogenase GroES-like (Domain)
 [68-191]  5.3e-08 PF08240
PF08240   ADH_N
IPR016040 NAD(P)-binding domain (Domain)
 [232-345]  1.4e-20 G3DSA:3.40.50.720
G3DSA:3.40.50.720   NAD(P)-bd
SignalP No significant hit
TMHMM No significant hit