close all open/close all

CDS information : Balhi_00360


close this sectionLocation

Organism
StrainDSM 5908
Entry nameBalhimycin
Contig
Start / Stop / Direction64,162 / 65,259 / + [in whole cluster]
64,162 / 65,259 / + [in contig]
Location64162..65259 [in whole cluster]
64162..65259 [in contig]
TypeCDS
Length1,098 bp (365 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category2.1 modification addition of extender units
Productputative phospho-2-dehydro-3-deoxyheptonate aldolase
putative 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase
putative DAHP synthase
Product (GenBank)putative alodlase
Genedahp
Gene (GenBank)ald
EC number2.5.1.54
Keyword
  • Bht
  • Hpg
  • Dpg
Note
Note (GenBank)
Reference
ACC
PmId
[17693715] The border sequence of the balhimycin biosynthesis gene cluster from Amycolatopsis balhimycina contains bbr, encoding a StrR-like pathway-specific regulator. (J Mol Microbiol Biotechnol. , 2007)
[20570618] Increased glycopeptide production after overexpression of shikimate pathway genes being part of the balhimycin biosynthetic gene cluster. (Metab Eng. , 2010)
Related Reference
ACC
Q6TZ04
PmId
[14600244] (De)regulation of key enzyme steps in the shikimate pathway and phenylalanine-specific pathway of the actinomycete Amycolatopsis methanolica. (Microbiology. , 2003)
ACC
P0AB91
PmId
[1682314] Analysis of the metal requirement of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli. (J Biol Chem. , 1991)
[8778789] Purification, crystallization, and preliminary crystallographic analysis of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli. (Proteins. , 1996)
[12126632] Allosteric inhibition of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase alters the coordination of both substrates. (J Mol Biol. , 2002)

close this sectionSequence

selected fasta
>putative phospho-2-dehydro-3-deoxyheptonate aldolase [putative alodlase]
MAAMTHTVATTDLDNQRIERIVPLVTPALLHHELPLSATAAETVRKGRESVVRVLDGTDD
RLLVITGPCSIHDPAAALDYAGHLAAIAGEVAGDLLVVMRVYFEKPRTIGGWKGLINDPH
LDGTGDVNHGLRTARHLLLELAERGLPAACEWLDTTIPAYFADTVSWGAIGARTVESQNH
RMLASGLSMPVGFKNRRDGDITVAIDAIRAAAVRHVVPGVDPGGLPAILHTAGNPDCHVV
LRGGDGAPNHDSASVHKTLTALEAAGLPGRVVIDASHDNSGKDHHRQPLVAAEIAGQVEN
GRNGIVGVMLESNLRAGRQDLQPGRPPAYGQSITDACIDVPTTRTVLHGLAAAAAARRKL
GKQAS
selected fasta
>putative phospho-2-dehydro-3-deoxyheptonate aldolase [putative alodlase]
GTGGCCGCGATGACCCACACCGTCGCCACGACCGACCTCGACAACCAGCGCATCGAGCGG
ATCGTCCCCCTGGTCACCCCCGCCCTGCTGCATCACGAACTGCCGCTCAGCGCCACCGCG
GCCGAGACGGTGCGAAAGGGCCGCGAGAGCGTCGTCCGCGTCCTCGACGGCACGGACGAC
CGGCTGCTCGTGATCACCGGGCCGTGCTCCATCCACGACCCCGCCGCGGCGCTCGACTAC
GCCGGCCACCTCGCCGCCATCGCCGGCGAGGTCGCCGGCGACCTGCTCGTCGTCATGCGC
GTGTACTTCGAGAAACCCCGGACGATCGGCGGCTGGAAGGGGCTCATCAACGACCCCCAC
CTCGACGGCACCGGCGACGTCAACCACGGGCTGCGCACGGCCCGGCACCTCCTGCTGGAG
CTCGCCGAACGCGGCCTGCCCGCCGCGTGCGAATGGCTGGACACCACCATTCCCGCGTAC
TTCGCGGACACGGTCTCGTGGGGCGCCATCGGCGCCCGCACCGTGGAAAGCCAGAACCAC
CGCATGCTCGCCAGCGGCCTGTCCATGCCCGTCGGCTTCAAGAACCGCCGCGACGGCGAC
ATCACCGTCGCCATCGACGCGATCCGGGCCGCCGCGGTCCGCCACGTGGTCCCCGGCGTC
GACCCCGGCGGGTTGCCCGCCATCCTGCACACGGCGGGCAACCCGGACTGCCACGTCGTC
CTGCGCGGTGGTGACGGCGCGCCCAACCACGACTCCGCGTCCGTCCACAAGACACTGACC
GCGCTGGAGGCCGCGGGCCTGCCCGGCCGGGTGGTGATCGACGCCAGCCACGACAACAGC
GGCAAGGACCACCACCGCCAGCCCCTCGTCGCGGCCGAGATCGCGGGCCAGGTCGAGAAC
GGGCGGAACGGCATCGTCGGGGTGATGCTCGAGTCCAACCTCCGCGCCGGCCGCCAGGAC
CTCCAGCCGGGCCGTCCGCCGGCATACGGCCAGTCCATCACCGACGCCTGCATCGACGTC
CCCACCACCCGGACGGTCCTCCACGGCCTCGCCGCGGCGGCCGCGGCCCGGCGAAAGCTC
GGCAAGCAAGCAAGCTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR006218 DAHP synthetase I/KDSA (Domain)
 [53-346]  1.29999999999998e-79 PF00793
PF00793   DAHP_synth_1
IPR006219 DHAP synthase, class 1 (Family)
 [1-362]  PIRSF001361
PIRSF001361   DAHP_synthase
 [14-358]  TIGR00034
TIGR00034   AroFGH
IPR013785 Aldolase-type TIM barrel (Domain)
 [17-361]  4.89999999999985e-129 G3DSA:3.20.20.70
G3DSA:3.20.20.70   Aldolase_TIM
SignalP No significant hit
TMHMM No significant hit