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CDS information : Chlor_00320


close this sectionLocation

Organism
StrainA82846UV37B
Entry nameChloroeremomycin
Contig
Start / Stop / Direction59,813 / 60,901 / + [in whole cluster]
25,569 / 26,657 / + [in contig]
Location59813..60901 [in whole cluster]
25569..26657 [in contig]
TypeCDS
Length1,089 bp (362 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)PCZA361.10
Gene
Gene (GenBank)
EC number2.5.1.54
Keyword
  • Bht
  • Hpg
  • Dpg
Note
Note (GenBank)
  • similar to phospho-2-dehydro-3-deoxyheptonate aldolase
Reference
ACC
PmId
[9545426] Sequencing and analysis of genes involved in the biosynthesis of a vancomycin group antibiotic. (Chem Biol. , 1998)
Related Reference
ACC
Q799B0
NITE
Balhi_00360
PmId
[20570618] Increased glycopeptide production after overexpression of shikimate pathway genes being part of the balhimycin biosynthetic gene cluster. (Metab Eng. , 2010)
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 [PCZA361.10]
MTTSTPAAAVDLDNQRIDRIVPLVTPALLHHELPLSAKAADTVRRGRENVLRVLDGTDDR
LLVITGPCSIHDPAAALDYADHLATMAGRFTDDLLIVMRVYFEKPRTVGGWKGLINDPHL
DGTGDVNHGLRIARHLLLELAERGLPVACEWLDTTIPAYLADTVSWGAIGARTVESQNHR
MLASGLSMPVGFKNRRDGDITVAIDAIRAAAARHVVPGVDPGGLPAILHTAGNPDCHLVL
RGGNSAPNHDASSVHTALTALQDAGLPRRVVIDASHDNSRKDHHRQPVVAGQIADQVKGG
QRGIVGVMLESNLRAGRQDLRPGQPLTYGQSITDACIDIPTTQTVLQTLATATAARRRLS
QN
selected fasta
>putative phospho-2-dehydro-3-deoxyheptonate aldolase [PCZA361.10]
ATGACAACATCTACTCCCGCCGCCGCGGTCGACCTCGACAACCAGAGGATCGACCGCATA
GTCCCATTGGTGACACCGGCCCTGCTGCACCATGAACTGCCGCTCAGCGCCAAGGCAGCC
GACACCGTGCGACGAGGTCGTGAGAACGTCCTTCGCGTCCTCGACGGTACGGATGACCGG
CTGCTCGTGATCACTGGACCGTGCTCCATCCACGACCCGGCCGCGGCCCTCGACTACGCC
GACCACCTCGCCACGATGGCCGGCCGGTTCACTGACGACCTCCTGATCGTCATGCGCGTG
TACTTCGAGAAACCGCGAACGGTCGGTGGCTGGAAAGGGCTCATCAACGACCCCCACCTC
GACGGCACCGGCGACGTGAACCACGGCCTGCGAATCGCCCGGCACCTGTTGCTGGAGCTC
GCCGAACGCGGCCTGCCCGTCGCGTGCGAGTGGCTGGACACGACCATCCCGGCCTACCTC
GCCGACACCGTTTCCTGGGGCGCGATCGGTGCCCGCACCGTGGAAAGCCAAAACCACCGC
ATGCTCGCCAGCGGTCTGTCCATGCCGGTCGGCTTCAAGAACCGCCGCGACGGCGACATC
ACCGTGGCCATCGACGCGATCCGCGCTGCGGCGGCCCGTCACGTCGTTCCTGGCGTCGAC
CCCGGCGGCTTGCCCGCCATCCTGCACACCGCCGGCAACCCCGACTGCCATCTTGTTCTG
CGCGGCGGCAATTCCGCGCCCAACCACGACGCCTCGTCTGTCCACACAGCACTCACCGCG
CTGCAGGACGCCGGTCTTCCCCGCCGGGTCGTGATCGATGCCAGCCATGACAACAGCCGC
AAGGACCACCACCGGCAACCTGTTGTCGCCGGGCAGATCGCCGACCAGGTCAAGGGCGGC
CAACGCGGCATTGTTGGCGTGATGCTCGAATCCAACCTCCGCGCCGGCCGCCAGGACCTC
CGCCCCGGCCAGCCTCTGACCTACGGCCAGTCCATCACGGACGCCTGCATCGACATCCCC
ACGACGCAGACCGTTCTGCAGACCCTCGCCACGGCAACCGCGGCTCGGCGGCGTCTCAGC
CAGAACTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR006218 DAHP synthetase I/KDSA (Domain)
 [52-346]  2.20000000000002e-84 PF00793
PF00793   DAHP_synth_1
IPR006219 DHAP synthase, class 1 (Family)
 [1-361]  PIRSF001361
PIRSF001361   DAHP_synthase
 [13-357]  TIGR00034
TIGR00034   AroFGH
IPR013785 Aldolase-type TIM barrel (Domain)
 [16-358]  G3DSA:3.20.20.70
G3DSA:3.20.20.70   Aldolase_TIM
SignalP No significant hit
TMHMM No significant hit