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CDS information : Gelda_00060


close this sectionLocation

Organism
Strain17997
Entry nameGeldanamycin
Contig
Start / Stop / Direction25,819 / 24,707 / - [in whole cluster]
16,419 / 15,307 / - [in contig]
Locationcomplement(24707..25819) [in whole cluster]
complement(15307..16419) [in contig]
TypeCDS
Length1,113 bp (370 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category2.1 modification addition of extender units
Productputative oxidoreductase
Product (GenBank)GdmI
Gene
Gene (GenBank)gdmI
EC number
Keyword
  • methoxymalonyl-ACP
Note
Note (GenBank)
  • biosynthesis pathway protein methoxymalonyl-ACP; fkbI
Reference
ACC
PmId
[18214443] The LuxR family members GdmRI and GdmRII are positive regulators of geldanamycin biosynthesis in Streptomyces hygroscopicus 17997. (Arch Microbiol. , 2008)
Related Reference
ACC
Q9KIE5
NITE
Asco_00090
PmId
[14623185] Crystal structure of an Acyl-ACP dehydrogenase from the FK520 polyketide biosynthetic pathway: insights into extender unit biosynthesis. (J Mol Biol. , 2003)
[15179529] Engineered biosynthesis of 16-membered macrolides that require methoxymalonyl-ACP precursors in Streptomyces fradiae. (Appl Microbiol Biotechnol. , 2004)
ACC
Q8KUG3
NITE
Ansam_00170
PmId
[11960423] Identification of a set of genes involved in the formation of the substrate for the incorporation of the unusual "glycolate" chain extension unit in ansamitocin biosynthesis. (J Am Chem Soc. , 2002)
[11996558] Functional expression of genes involved in the biosynthesis of the novel polyketide chain extension unit, methoxymalonyl-acyl carrier protein, and engineered biosynthesis of 2-desmethyl-2-methoxy-6-deoxyerythronolide B. (J Am Chem Soc. , 2002)
ACC
Q84G17
NITE
Gelda2_00150
PmId
[12586396] Cloning and characterization of a gene cluster for geldanamycin production in Streptomyces hygroscopicus NRRL 3602. (FEMS Microbiol Lett. , 2003)

close this sectionSequence

selected fasta
>putative oxidoreductase [GdmI]
MTDAATDHAELVSGLIGDRADAWDLAGELPRDLLVKLGASGVLCAQVGPEHGGTGLDSHA
NGELTARVGARCSSLRSVMTSQGMAAWTVRRLGGTEQWDTFLPRLTSGDLAAVGFSEPGA
GSDLSAMETEIADDGAEVVVTGRKVWITAAHYADLLLVFGKYRGGATAVVVPARTPGVRI
TRVENPLGCRAAGHANITLDAVRVPAGHVLGGTGLPLSLATTAALTYGRMSVAWGCVGIL
RACLDAAATHTATREQSGRALAEHQLVARHLAELYVAERHATRACEHASASWDTGSPDMA
VDAVHAKYVASREAAQGAARAVQLLASAGASDGHVVARAYRDAKLMEVIEGTSEICQLVL
ARHMRKKVRP
selected fasta
>putative oxidoreductase [GdmI]
GTGACCGACGCCGCCACCGACCACGCGGAGCTGGTCAGCGGGTTGATCGGGGACCGGGCC
GACGCCTGGGACCTGGCCGGGGAACTGCCCCGCGACCTCCTGGTCAAACTCGGCGCCTCC
GGTGTGCTGTGCGCACAGGTCGGCCCCGAGCACGGCGGCACCGGACTGGACAGCCATGCC
AACGGGGAGCTCACCGCGCGGGTCGGCGCCCGGTGCAGCTCCCTGCGCAGCGTGATGACC
TCGCAGGGCATGGCGGCGTGGACGGTGCGCAGGCTCGGCGGCACCGAGCAGTGGGACACC
TTTCTGCCCCGGCTGACCTCCGGTGACCTGGCGGCGGTCGGATTCAGCGAACCCGGCGCC
GGCAGCGACCTGTCGGCGATGGAGACCGAGATCGCCGACGACGGCGCCGAGGTGGTCGTC
ACCGGACGGAAGGTGTGGATCACCGCCGCCCACTACGCCGATCTGCTGCTGGTGTTCGGG
AAGTACCGGGGCGGCGCCACGGCCGTGGTCGTGCCCGCCCGGACACCCGGAGTGCGCATC
ACACGGGTGGAGAACCCCCTGGGCTGCCGCGCCGCCGGTCATGCGAACATCACCCTGGAC
GCGGTCCGGGTGCCCGCCGGGCATGTACTCGGCGGCACCGGGCTGCCGCTTTCCCTGGCG
ACCACCGCCGCGCTCACCTACGGGCGCATGTCCGTGGCCTGGGGGTGCGTCGGCATCCTG
CGCGCGTGCCTGGACGCCGCCGCCACGCACACCGCCACCCGGGAGCAGTCCGGCCGGGCG
CTCGCCGAGCACCAGTTGGTGGCCCGGCACCTGGCCGAGCTGTACGTCGCGGAGCGGCAC
GCCACCCGGGCCTGTGAACACGCCAGCGCCTCCTGGGACACCGGCTCGCCCGACATGGCC
GTCGACGCGGTGCACGCGAAGTACGTCGCCTCGCGCGAGGCGGCACAGGGCGCGGCACGC
GCCGTACAGCTCCTGGCGTCGGCCGGGGCGTCCGACGGCCATGTGGTGGCCCGTGCCTAC
CGCGACGCGAAGCTGATGGAAGTCATCGAGGGCACCAGCGAGATCTGCCAGCTCGTGCTC
GCCCGGCACATGCGGAAGAAGGTGCGACCATGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR006090 Acyl-CoA oxidase/dehydrogenase, type 1 (Domain)
 [222-364]  1e-29 PF00441
PF00441   Acyl-CoA_dh_1
IPR006091 Acyl-CoA oxidase/dehydrogenase, central domain (Domain)
 [112-161]  7.20000000000001e-15 PF02770
PF02770   Acyl-CoA_dh_M
 [112-203]  1.8e-28 G3DSA:2.40.110.10
G3DSA:2.40.110.10   Acyl_CoA_DH/ox_M
IPR006092 Acyl-CoA dehydrogenase, N-terminal (Domain)
 [18-109]  2.4e-11 PF02771
PF02771   Acyl-CoA_dh_N
IPR009075 Acyl-CoA dehydrogenase/oxidase C-terminal (Domain)
 [204-367]  9.9e-38 G3DSA:1.20.140.10
G3DSA:1.20.140.10   AcylCoA_DH_1/2_C
 [213-368]  2.39999798157265e-31 SSF47203
SSF47203   AcylCoADH_C_like
IPR009100 Acyl-CoA dehydrogenase/oxidase (Domain)
 [8-214]  1e-51 SSF56645
SSF56645   AcylCoA_dehyd_NM
IPR013786 Acyl-CoA dehydrogenase/oxidase, N-terminal (Domain)
 [14-109]  4.5e-22 G3DSA:1.10.540.10
G3DSA:1.10.540.10   AcylCoA_DH/ox_N
SignalP
 [1-45]  0.057 Signal
Bacteria, Gram-negative   
 [1-22]  0.144 Signal
Bacteria, Gram-positive   
TMHMM No significant hit