Gene ulaD (MPN493)
Name
ulaD
Stable ID
MPN493
Location
600316 - 600972 -
Sequence
    1  ATGGCTTTAC CTTTAATCCA AATTGCGCTT GATAACCTCA GTTTAGCGAG TGCTTTAAAT
   61  GACCTGGCTA AAGTCGGGGA TGCTGTTGAT GTTATTGAAG TGGGCACTAT CTTACTAACA
  121  GCGGAGGGCG TTAATGCTGT TAAAGAAATT GCCAAACGCT ATCCCCATAA GTTAATAGTG
  181  GCTGATGGCA AGATTGCTGA TACGGGGAAG GTGTTTAACC AAATGTTCTT TGATGCTGGG
  241  GCACACTTTA CCACGGTCAT TTGTGCAGCG GAATTGCCCA CCGTAAAGGA TGTGGTAACT
  301  GTGGGTAACA GTTACACGCC CATAAAAGAA ACCCAGGTGG AAATGACCAG TAACTTCACT
  361  TGGGAGCAGG TAACGCAGTG AAAACAAGTG GGAGTTCAGC AGGTAGTGTG ACACCGTTCC
  421  CGTGATGCCC AAGCAGCGGG AGTCAACTGA TCAGATAAGG ATTTGCAAGC AGTGAAACGC
  481  TTAGCGGATT TGGGCTTTAA GGTCACCGTT ACCGGCGGCA TTACCCTCAA CGACATCCAG
  541  TTATTTAAGG ATATTCCCAT TTATATCTTT ATTGCTGGGC GTACCATTAG GGATGCTAGT
  601  GATCCACTTC AAACCGTACA ACAATTTAAA GATGAGTTTC ACAAGTACTG AAAATAA
Download Sequence
Operon
OP387
Operon location
599500 - 601885
Protein (mpn493)
Name
Probable 3-keto-L-gulonate-6-phosphate decarboxylase (KGPDC) (EC 4.1.1.85) (3-dehydro-L-gulonate-6-phosphate decarboxylase) (L-ascorbate utilization protein D)
Stable ID
Mpn493
Molecular Weight
23980
Isoelectric Point
6
Localization
Cytoplasm
Comment -
Sequence
MALPLIQIALDNLSLASALNDLAKVGDAVDVIEVGTILLTAEGVNAVKEIAKRYPHKLIVADGKIADTGKVFNQMFFDAG
AHFTTVICAAELPTVKDVVTVGNSYTPIKETQVEMTSNFTWEQVTQWKQVGVQQVVWHRSRDAQAAGVNWSDKDLQAVKR
LADLGFKVTVTGGITLNDIQLFKDIPIYIFIAGRTIRDASDPLQTVQQFKDEFHKYWK
Post translational modifications
No post translational modifications were found
GENE/PROTEIN ulaD (Domains Overview)
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Domains (InterProScan)
Location (aa) Name (InterPro ID) Description GO terms Sequence Evalue
1-216 SSF51366 (IPR011060) Ribulose-phosphate binding barrel Biological Process:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0008152'>'metabolic' == '' ? '': 'metabolic'; 'process' == '' ? '': 'process'; ('GO' == '' ? '': 'GO';:0008152)

Molecular Function:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0003824'>'catalytic' == '' ? '': 'catalytic'; 'activity' == '' ? '': 'activity'; ('GO' == '' ? '': 'GO';:0003824)

1.2e-39
3-217 G3DSA:3.20.20.70 (IPR013785) Aldolase-type TIM barrel Biological Process:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0008152'>'metabolic' == '' ? '': 'metabolic'; 'process' == '' ? '': 'process'; ('GO' == '' ? '': 'GO';:0008152)

Molecular Function:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0003824'>'catalytic' == '' ? '': 'catalytic'; 'activity' == '' ? '': 'activity'; ('GO' == '' ? '': 'GO';:0003824)

0
5-209 SM00934 (IPR001754) Orotidine 5'-phosphate decarboxylase domain Biological Process:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0006207'>''de' == '' ? '': 'de'; 'novo' == '' ? '': 'novo';' 'pyrimidine' == '' ? '': 'pyrimidine'; 'base' == '' ? '': 'base'; 'biosynthetic' == '' ? '': 'biosynthetic'; 'process' == '' ? '': 'process'; ('GO' == '' ? '': 'GO';:0006207)

Molecular Function:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0004590'>'orotidine' == '' ? '': 'orotidine';-5'-'phosphate' == '' ? '': 'phosphate'; 'decarboxylase' == '' ? '': 'decarboxylase'; 'activity' == '' ? '': 'activity'; ('GO' == '' ? '': 'GO';:0004590)

1.5e-35
6-208 PF00215 (IPR001754) Orotidine 5'-phosphate decarboxylase domain Biological Process:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0006207'>''de' == '' ? '': 'de'; 'novo' == '' ? '': 'novo';' 'pyrimidine' == '' ? '': 'pyrimidine'; 'base' == '' ? '': 'base'; 'biosynthetic' == '' ? '': 'biosynthetic'; 'process' == '' ? '': 'process'; ('GO' == '' ? '': 'GO';:0006207)

Molecular Function:
<'A' == '' ? '': 'A'; 'class' == '' ? '': 'class';=''result' == '' ? '': 'result';' 'target' == '' ? '': 'target';='_'blank' == '' ? '': 'blank';' 'href' == '' ? '': 'href';=''http' == '' ? '': 'http';://'amigo' == '' ? '': 'amigo';.'geneontology' == '' ? '': 'geneontology';.'org' == '' ? '': 'org';/'cgi' == '' ? '': 'cgi';-'bin' == '' ? '': 'bin';/'amigo' == '' ? '': 'amigo';/'term' == '' ? '': 'term';-'details' == '' ? '': 'details';.'cgi' == '' ? '': 'cgi';?'term' == '' ? '': 'term';='GO' == '' ? '': 'GO';:0004590'>'orotidine' == '' ? '': 'orotidine';-5'-'phosphate' == '' ? '': 'phosphate'; 'decarboxylase' == '' ? '': 'decarboxylase'; 'activity' == '' ? '': 'activity'; ('GO' == '' ? '': 'GO';:0004590)

7.4e-26
Protein Homology (BLASTP results)
Protein Start Protein End Hit Size Orthologous Organism Orthologous Start Orthologous End Evalue Identity Score Alignment
4 217 213 - MAG6350 Mycoplasma agalactiae 3 216 <1e-50 52.8037 626
1 218 217 - MCJ_002590 Mycoplasma conjunctivae 1 220 <1e-50 57.7273 659
29 210 181 - Bacillus subtilis subsp. subtilis 26 204 0.000000002 29.3478 135
29 210 181 - Bacillus subtilis subsp. subtilis 26 204 0.000000005 28.8043 132
1 217 216 - b3581 Escherichia coli 1 215 8e-39 37.3272 387
1 217 216 - b4196 Escherichia coli 1 215 <1e-50 44.7005 528
1 217 216 - MS53_0029 Mycoplasma synoviae 1 217 <1e-50 50.6912 601
1 217 216 - MHP7448_0438 Mycoplasma hyopneumoniae 7448 1 221 <1e-50 54.7511 638
1 217 216 - MYPE7180 Mycoplasma penetrans 1 216 <1e-50 50.6912 586
4 217 213 - Mycoplasma pulmonis 18 231 <1e-50 53.271 631
External IDs
COG
COG0269G
EC number
4.1.1.85
Gene ID
877220
GI
13508232
GO
Carbohydrate transport and metabolism  
Home COG
G
Old MP number
MP349
Pathway
Metabolism energy, sugars
PDB homologs
1rpx_A
PDB homologs
1h1y_A
PDB homologs
1h1z_A
Pfam
PF00215
PID
g1674026
RefSeq
NP_110181.1
Swiss-Prot protein ID
ULAD_MYCPN
phylomeDB tree
ULAD_MYCPN
UniProt
P75293
Transcription
IMAGE BROWSERS

OPERON OP387 (Genomic Overview)
Region:599500-601885

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STRING image

STRING of Mpn493STRING legend

PDB image(s)

1rpx

PDB 1rpx

1h1y

PDB 1h1y

1h1z

PDB 1h1z