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CDS information : A4793_00310


close this sectionLocation

Organism
StrainNRRL 15009
Entry nameA47934
Contig
Start / Stop / Direction64,874 / 65,866 / + [in whole cluster]
64,874 / 65,866 / + [in contig]
Location64874..65866 [in whole cluster]
64874..65866 [in contig]
TypeCDS
Length993 bp (330 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category4.4 resistance
ProductD-lactate dehydrogenase
Product (GenBank)D-lactate dehydrogenase
GenevanHst
ORF3
Gene (GenBank)DLDHStoy
EC number
Keyword
Note
Note (GenBank)
  • VanHst
Reference
ACC
PmId
[10387095] Molecular mechanism of VanHst, an alpha-ketoacid dehydrogenase required for glycopeptide antibiotic resistance from a glycopeptide producing organism. (Biochemistry. , 1999)
[12060705] Assembling the glycopeptide antibiotic scaffold: The biosynthesis of A47934 from Streptomyces toyocaensis NRRL15009. (Proc Natl Acad Sci U S A. , 2002)
Related Reference
ACC
Q05709
PmId
[1931965] Molecular basis for vancomycin resistance in Enterococcus faecium BM4147: biosynthesis of a depsipeptide peptidoglycan precursor by vancomycin resistance proteins VanH and VanA. (Biochemistry. , 1991)
[1503450] Evidence for in vivo incorporation of D-lactate into peptidoglycan precursors of vancomycin-resistant enterococci. (Antimicrob Agents Chemother. , 1992)
[9605319] A thioredoxin fusion protein of VanH, a D-lactate dehydrogenase from Enterococcus faecium: cloning, expression, purification, kinetic analysis, and crystallization. (Protein Sci. , 1998)

close this sectionSequence

selected fasta
>D-lactate dehydrogenase [D-lactate dehydrogenase]
MTHSEKAHIAVYGCGPDEAVLFRELAPGLGVQPVITDAPVSEANSELALGSRCVSISHKT
PVTHATLRALGRVGVGYISTRSIGYNHIDVEYADSIGIVVENVSYSPDSVADYTLMLMLM
VLRDAKAIVRRTDMHDYRLSEVRGKELRDLTVGVVGTGRIGTAVLDRLRGFGCRVLAHDN
HPADRPGVAEYVPLDELLRRSDVVTLHAPLTTATHHLLDQQRLARMKDGALVINTGRGGL
IDTEALVHELESGRLGGAALDVVEGEEGIFYADCRDRPMESKALLRLQELPNALITPHTA
YYTDHALRDTVENSLTNCLTFRKQESAWPD
selected fasta
>D-lactate dehydrogenase [D-lactate dehydrogenase]
ATGACCCACAGCGAGAAGGCCCATATCGCCGTATACGGGTGTGGTCCGGACGAAGCCGTT
CTGTTCCGCGAGCTGGCGCCCGGCCTCGGTGTGCAGCCGGTCATCACCGACGCCCCGGTG
TCCGAGGCCAACAGTGAACTGGCCTTGGGCAGCCGGTGCGTCAGCATCAGCCACAAGACG
CCCGTCACCCATGCCACGCTGCGTGCGCTCGGCAGGGTCGGCGTCGGCTACATCTCCACC
CGGAGCATCGGGTACAACCACATCGACGTGGAATACGCGGACAGCATCGGCATCGTTGTG
GAGAACGTCTCCTACTCGCCGGACAGCGTGGCCGACTACACCCTGATGCTCATGTTGATG
GTGCTGCGGGACGCGAAAGCCATCGTCCGTCGCACCGACATGCACGACTACCGGCTGAGT
GAGGTGCGCGGGAAGGAACTGCGCGATCTGACGGTCGGAGTGGTCGGGACGGGGCGTATC
GGCACGGCGGTCCTGGACCGGTTGCGAGGTTTCGGCTGCCGCGTTCTGGCCCATGACAAC
CATCCGGCGGACCGCCCCGGTGTCGCCGAGTACGTTCCGCTCGACGAACTGCTGCGGCGG
AGCGACGTGGTCACGCTGCATGCGCCGCTCACCACGGCCACGCACCATCTGCTCGATCAG
CAGCGCCTGGCGCGGATGAAGGACGGCGCGCTGGTCATCAACACCGGACGTGGTGGGCTC
ATCGACACCGAGGCCCTGGTGCACGAATTGGAAAGCGGCAGGCTGGGCGGCGCGGCGCTG
GATGTCGTCGAAGGCGAGGAGGGCATCTTCTACGCCGACTGCCGGGACAGACCCATGGAA
AGCAAGGCACTGTTGCGGCTTCAGGAGCTGCCGAATGCGCTCATCACTCCGCACACCGCC
TACTACACGGATCACGCCCTGCGCGACACCGTGGAGAACTCTCTCACCAACTGCCTGACA
TTTCGAAAGCAGGAATCAGCATGGCCAGACTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09
show BLAST table
InterPro
Database:interpro:38.0
IPR006139 D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain (Domain)
 [16-325]  1.69999999999999e-19 PF00389
PF00389   2-Hacid_dh
IPR006140 D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding (Domain)
 [115-300]  2.19999999999997e-54 PF02826
PF02826   2-Hacid_dh_C
 [152-179]  PS00065
PS00065   D_2_HYDROXYACID_DH_1
 [197-219]  PS00670
PS00670   D_2_HYDROXYACID_DH_2
 [226-242]  PS00671
PS00671   D_2_HYDROXYACID_DH_3
IPR016040 NAD(P)-binding domain (Domain)
 [9-122]  1.69999999999999e-24 G3DSA:3.40.50.720 [123-300]  5.79999999999997e-59 G3DSA:3.40.50.720
G3DSA:3.40.50.720   NAD(P)-bd
SignalP No significant hit
TMHMM No significant hit