Conca_00270 : CDS information

close this sectionLocation

Organism
StrainATCC 27449 (=NBRC 13477)
Entry nameConcanamycin A
Contig
Start / Stop / Direction97,026 / 98,438 / + [in whole cluster]
97,026 / 98,438 / + [in contig]
Location97026..98438 [in whole cluster]
97026..98438 [in contig]
TypeCDS
Length1,413 bp (470 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)
EC number1.3.1.-
Keyword
  • ethylmalonyl-CoA
Note
Note (GenBank)
  • ORF 18*; ethylmalonate biosynthesis
Reference
ACC
PmId
[16207901] Organization of the biosynthetic gene cluster for the macrolide concanamycin A in Streptomyces neyagawaensis ATCC 27449. (Microbiology. , 2005)
comment
ORF18* ethylmalonate biosynthesis (crotonyl CoA reductase)

配列解析から機能推定。
ORF18*とORF19*は、module 10のbutyrate extender unitの合成に関与しそう。
Related Reference
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
48th(Q53865) 48%, 1e-111
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
58th(Q9RNU6) 49%, 1e-109
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
71st(B8XVS5) 40%, 3e-71
Rhodobacter sphaeroides_ccr
Crotonyl-CoA carboxylase/reductase

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+

close this sectionSequence

selected fasta
>putative crotonyl-CoA reductase [crotonyl CoA reductase]
MDPLAEAVLAGAPPDRLAKEPLPTEYTAAHLRAEDVDVFGDAADRDVRRTLRVGPVPMPE
LAVDEVLIAVMASSINYNTVWSATFEPVPTFTFLRRLGRQGGSAARHDRPQHVVGSDAAG
VIVRTGAGVRRWQVGEHVVVSCVQVDDQEPATHADGMLGAEQRIWGFETNFGGLAHYAVV
RASQLLPKPGHLTWEEAASTMLCAATSYRMLVSDRGARIKQGDIVLIWGATGGLGAYAVQ
LVKNAGGIAVGVVSTEEKSRRARALGCDVVINRADIGLDGDLADDPDATIEAGKRLGRII
RAETGEDPHVVFDYIGRATFGISVFVVALSVALVVRRGGTVVTCGSSTGYQHRFDNRCWW
MHLKRIVGSHAANLQEQAECNRLFRLGHLVPVLSAVHPLAEVAEAARLVQTNRHTGKVGV
LCLAPRPGLGVTDQALRDRVGEDRLNLLRDAAPATPGPEPVVTGREGTGR
selected fasta
>putative crotonyl-CoA reductase [crotonyl CoA reductase]
ATGGACCCCTTGGCCGAAGCCGTGCTTGCCGGCGCGCCCCCCGACCGGCTGGCGAAGGAA
CCCCTGCCCACCGAGTACACCGCCGCGCATCTGCGCGCCGAGGACGTGGACGTGTTCGGC
GACGCCGCCGACCGGGACGTACGCCGCACCCTCCGGGTCGGTCCCGTACCCATGCCCGAA
CTGGCCGTGGACGAAGTACTGATCGCCGTGATGGCCAGCTCCATCAACTACAACACCGTC
TGGTCGGCGACCTTCGAACCCGTACCGACCTTCACCTTCCTGCGCAGACTGGGCCGCCAG
GGCGGATCCGCCGCCCGGCACGACCGGCCCCAGCACGTCGTCGGATCGGACGCCGCCGGG
GTCATCGTCCGGACGGGTGCCGGGGTACGGCGCTGGCAGGTGGGCGAGCACGTCGTCGTC
AGCTGCGTCCAGGTGGACGACCAGGAACCCGCCACCCACGCCGACGGCATGCTCGGTGCC
GAGCAGCGCATCTGGGGTTTCGAGACGAACTTCGGCGGACTGGCCCACTACGCGGTGGTG
CGGGCCAGCCAACTGCTCCCCAAGCCGGGCCACCTCACCTGGGAGGAAGCCGCCTCGACG
ATGCTGTGCGCGGCCACCTCCTACCGGATGCTCGTCAGCGACCGGGGCGCCCGGATCAAA
CAGGGCGACATCGTGCTGATCTGGGGCGCCACCGGCGGACTCGGCGCCTACGCCGTCCAG
CTGGTGAAGAACGCCGGCGGCATCGCCGTGGGTGTCGTCAGCACGGAGGAGAAGAGCCGA
CGGGCGCGGGCGCTCGGCTGCGACGTCGTCATCAACCGCGCCGACATCGGCCTGGACGGC
GATCTCGCCGACGACCCGGACGCGACCATAGAGGCCGGCAAACGCCTCGGCAGGATCATC
CGCGCCGAGACCGGCGAGGACCCGCACGTCGTGTTCGACTACATAGGCAGGGCCACGTTC
GGTATCTCGGTCTTCGTCGTCGCGCTCTCGGTCGCCTTGGTCGTGCGCCGCGGCGGCACC
GTGGTCACCTGCGGATCCAGCACCGGGTATCAACACCGGTTCGACAACCGGTGCTGGTGG
ATGCACCTCAAACGGATCGTGGGCAGCCACGCCGCGAACCTCCAGGAACAGGCCGAGTGC
AACCGTCTGTTCCGCCTCGGCCACCTCGTTCCGGTGCTCTCCGCCGTCCACCCGCTCGCC
GAGGTGGCGGAGGCCGCCCGGCTCGTACAGACCAACCGGCACACCGGCAAGGTCGGCGTC
CTGTGTCTTGCGCCCCGGCCCGGGCTCGGGGTGACCGATCAGGCCCTGCGGGACCGTGTG
GGCGAGGACCGGCTGAACCTGCTGCGCGACGCCGCTCCGGCGACCCCCGGGCCCGAGCCG
GTCGTCACCGGACGAGAAGGGACCGGTCGATGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR010085 Crotonyl-CoA reductase (Family)
 [35-433]  TIGR01751
TIGR01751   Crot-CoA-red
IPR011032 GroES-like (Domain)
 [50-236]  1.20000117458134e-26 SSF50129
SSF50129   GroES_like
IPR013149 Alcohol dehydrogenase, C-terminal (Domain)
 [233-382]  9.8e-22 PF00107
PF00107   ADH_zinc_N
IPR013154 Alcohol dehydrogenase GroES-like (Domain)
 [65-187]  4.1e-08 PF08240
PF08240   ADH_N
IPR016040 NAD(P)-binding domain (Domain)
 [229-368]  1.5e-16 G3DSA:3.40.50.720
G3DSA:3.40.50.720   NAD(P)-bd
SignalP
 [1-18]  0.076 Signal
Eukaryota   
 [1-33]  0.039 Signal
Bacteria, Gram-negative   
TMHMM No significant hit
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