Salino_00890 : CDS information

close this sectionLocation

Organism
StrainDSM 41398
Entry nameSalinomycin
Contig
Start / Stop / Direction101,665 / 99,947 / - [in whole cluster]
101,665 / 99,947 / - [in contig]
Locationcomplement(99947..101665) [in whole cluster]
complement(99947..101665) [in contig]
TypeCDS
Length1,719 bp (572 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category2.1 modification addition of extender units
Productputative 3-hydroxyacyl-CoA dehydrogenase
putative beta-keto-reductase
Product (GenBank)3-hydroxyacyl-CoA dehydrogenase
Gene
Gene (GenBank)salP
EC number1.1.1.35
Keyword
  • ethylmalonyl-CoA
Note
Note (GenBank)
Reference
ACC
PmId
[22076845] A late-stage intermediate in salinomycin biosynthesis is revealed by specific mutation in the biosynthetic gene cluster. (Chembiochem. , 2012)
comment
monC gene-based hybridisation probeを使って、Streptomyces albus DSM 41398からsalinomycin(sal)生合成gene clusterを同定。

salP (572aa) : 3-hydroxybutyryl-CoA dehydrogenase

配列解析のみ。
普通でない伸長unitのethylmalonyl-CoAを導く前駆体経路で働くかもしれない。
Related Reference
ACC
H6D567
NITE
Salino3_00110
PmId
[22156425] Cloning and characterization of the polyether salinomycin biosynthesis gene cluster of Streptomyces albus XM211. (Appl Environ Microbiol. , 2012)
comment
配列は[H1ZZT1]と全く同じ。株違い。

polyetherに特異的なepoxidaseの配列に基づいた縮重プライマーを用いて、Streptomyces albus XM211からsalinomycin(sln)生合成gene clusterを同定。

Orf11 (572aa) : 3-Hydroxybutyryl-CoA dehydrogenase

orf11を置換して不活化するとsalinomycin収量がwildの10%になった。
よってbutyrate伸長unitsの供給を通してsalinomycin生合成に関連すると示唆される。
ACC
P52041
PmId
[8655474] Cloning, sequencing, and expression of clustered genes encoding beta-hydroxybutyryl-coenzyme A (CoA) dehydrogenase, crotonase, and butyryl-CoA dehydrogenase from Clostridium acetobutylicum ATCC 824. (J Bacteriol. , 1996)
comment
Blast 82nd, 2hsp: N末側33%, C末側41%
Clostridium acetobutylicum_hbd
3-hydroxybutyryl-CoA dehydrogenase(EC 1.1.1.157)

BCS (butyryl-CoA synthesis) operon (crt-bcd-etfB-etfA-hbd)のクローニングとシークエンス。
crt geneの上流にあるプロモーターによって制御される。transcriptional unitであることを確認。

BCS operonをE. coliで過剰発現。
crotonase, beta-hydroxybutyryl-CoA dehydrogenase activity確認。

BCS operonをC. acetobutylicum で発現。
crotonase, beta-hydroxybutyryl-CoA dehydrogenase, butyryl-CoA dehydrogenase activity上昇。

close this sectionSequence

selected fasta
>putative 3-hydroxyacyl-CoA dehydrogenase [3-hydroxyacyl-CoA dehydrogenase]
MTSAPPAFDSVAVFGLGTIGSALTASLLRTGARVTAVEADEASLARGREAVRQAAGEAAE
QVTYTLDPDAVAGSGLVIEAVTEDLALKAAVLRRAGEVCGPATILATTTALSVTQVAAET
GRLPRTIGLHPVGHAPDGGVVEVVATPVTDPEVRERTAELVAQLGRTAVDSTDLPGFTGG
GLLMAYLAGAVAMLERRYASRDDIDAAMTLGCGLPLGPLAHLDLIGLDTALDTLRGLHRL
TGERRFLPPPLLTHMVTAGLLGVKSGRGFYSYPADAPGRPVAASPGLGEPRPVRQVGIVG
SGTMARGIAEVFARSGYATVLTARSEVKAKEAVAGVGRSLDRGVSRGKLSAEVAATALDR
LVPADDFGALADCDLLIEAVAEELPVKRQIFGALDKACRPDAVLSTTTSSLPVVECAMAT
RRPGSVVGMHFFNPAPVMKLVEVVGTVLTAPDALATAHRVCADLGKHPVACADRAGFIVN
ALLFPYLNDAVRLLEEHRAPAEDIDTVMAQGCGYPLGPLALHDVIGLDVSLQIQRSLHAA
FHEESLAPAAHLEHLVGAGYLGRKTGRGFRSH
selected fasta
>putative 3-hydroxyacyl-CoA dehydrogenase [3-hydroxyacyl-CoA dehydrogenase]
ATGACGTCCGCACCGCCCGCCTTCGACTCCGTCGCGGTCTTCGGACTCGGCACCATCGGC
TCCGCCCTCACCGCCTCCCTGCTGCGCACCGGCGCGCGGGTGACCGCCGTGGAGGCCGAC
GAGGCCTCGCTCGCCCGGGGCCGGGAGGCGGTGCGGCAGGCCGCCGGTGAGGCGGCGGAG
CAGGTCACGTACACCCTGGACCCGGACGCCGTCGCGGGCAGCGGGCTGGTCATCGAGGCG
GTGACCGAGGACCTCGCCCTGAAGGCCGCGGTGCTGCGCCGGGCGGGCGAGGTCTGCGGG
CCCGCGACGATCCTCGCGACCACCACCGCGCTCTCCGTCACCCAGGTCGCCGCCGAGACC
GGGCGCCTGCCGCGGACCATCGGCCTGCACCCGGTGGGGCACGCCCCGGACGGCGGCGTG
GTCGAGGTGGTCGCCACCCCGGTCACCGACCCGGAGGTGCGGGAGCGGACCGCGGAGCTG
GTCGCCCAACTCGGCCGTACCGCCGTGGACTCCACCGATCTGCCGGGCTTCACCGGCGGC
GGTCTGCTGATGGCCTACCTCGCGGGCGCCGTCGCGATGCTGGAGCGGCGCTACGCCTCC
CGCGACGACATCGACGCGGCGATGACGCTGGGCTGCGGACTGCCTCTCGGGCCGCTCGCC
CACCTCGACCTGATAGGCCTGGACACCGCGCTCGACACCCTGCGCGGGCTGCACCGCCTC
ACCGGCGAGCGGCGCTTTTTGCCGCCGCCGCTGCTCACCCACATGGTCACCGCGGGCCTG
CTCGGCGTGAAGTCCGGCCGCGGCTTCTACAGTTACCCCGCCGACGCGCCGGGCCGGCCG
GTGGCCGCGAGCCCCGGGCTCGGCGAGCCGCGCCCGGTGCGGCAGGTCGGCATCGTCGGC
TCCGGCACCATGGCGCGGGGCATCGCGGAGGTCTTCGCCCGCAGCGGCTACGCGACGGTG
CTCACCGCCCGCTCCGAGGTCAAGGCGAAGGAGGCGGTCGCCGGGGTCGGCCGCTCCCTG
GACCGCGGGGTGAGCCGCGGCAAGCTCTCCGCGGAGGTCGCCGCGACGGCTCTGGACCGG
CTGGTGCCCGCCGACGACTTCGGCGCGCTCGCCGACTGCGATCTGCTGATCGAGGCGGTC
GCCGAGGAACTCCCGGTCAAGCGGCAGATCTTCGGCGCCCTGGACAAGGCCTGCCGGCCG
GACGCGGTGCTCTCCACCACCACCTCCAGCCTGCCCGTGGTCGAGTGCGCGATGGCCACC
CGGCGGCCCGGCTCGGTGGTCGGCATGCACTTCTTCAACCCGGCGCCGGTGATGAAGCTG
GTCGAGGTGGTCGGCACCGTGCTGACCGCGCCGGACGCGCTGGCCACCGCGCACCGGGTC
TGCGCGGACCTCGGCAAGCACCCGGTGGCCTGCGCGGACCGCGCCGGGTTCATCGTCAAC
GCCCTCCTCTTCCCGTACCTCAACGACGCGGTGCGGCTCCTGGAGGAGCACCGGGCACCG
GCCGAGGACATCGACACGGTGATGGCGCAGGGCTGCGGCTATCCGCTCGGCCCGCTGGCC
CTGCACGACGTCATCGGGCTCGATGTCTCGCTGCAGATCCAGCGCAGCCTGCACGCGGCC
TTCCACGAGGAGTCGCTCGCCCCGGCGGCGCATCTGGAGCACCTGGTCGGCGCGGGCTAT
CTGGGCCGCAAGACGGGCCGCGGCTTCCGCAGCCACTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR006108 3-hydroxyacyl-CoA dehydrogenase, C-terminal (Domain)
 [176-272]  1e-23 PF00725 [476-570]  8.5e-28 PF00725
PF00725   3HCDH
IPR006176 3-hydroxyacyl-CoA dehydrogenase, NAD binding (Domain)
 [10-173]  7.9e-32 PF02737 [295-473]  1.9e-55 PF02737
PF02737   3HCDH_N
IPR008927 6-phosphogluconate dehydrogenase, C-terminal-like (Domain)
 [175-324]  1.4e-27 SSF48179 [476-572]  4.8e-26 SSF48179
SSF48179   6-phosphogluconate dehydrogenase C-terminal domain-like
IPR013328 Dehydrogenase, multihelical (Domain)
 [178-272]  9.8e-24 G3DSA:1.10.1040.10 [478-569]  2.8e-26 G3DSA:1.10.1040.10
G3DSA:1.10.1040.10   no description
IPR016040 NAD(P)-binding domain (Domain)
 [8-177]  2.6e-25 G3DSA:3.40.50.720 [288-477]  8.3e-48 G3DSA:3.40.50.720
G3DSA:3.40.50.720   no description
SignalP
 [1-24]  0.845 Signal
Eukaryota   
 [1-39]  0.783 Signal
Bacteria, Gram-positive   
TMHMM No significant hit
Page top