MyMpn
The Mycoplasma pneumoniae database
 
e.g Mpn001 or dnaN or polymerase
Gene adh (MPN564)
Name 
adh
Stable ID 
MPN564
Location 
684729 - 685784 -
Sequence 
    1  ATGAAAGCAT ATGCAATGTT AAAAATTGGC GCTACTGGTT GAATCGAAAA ACCAAGACCA
   61  GTTTGTGGGC CCAATGATGC GATAATTCGA CCACTGGCCG TAGCACCATG TACTTCAGAC
  121  GTCCACACCG TTTGGGAAGG TGGCATTGGT GAACGTCACA ACATGGTTTT AGGCCATGAG
  181  GGCTGTGGTG TTGTGGATGA AGTGGGGTCT GAGGTCAAAA GCTTTAAGGT TGGTGATCGC
  241  GTTTTAGTGG CAGCCATTAC ACCAGAATGA AATTCGGTTA ATGCTCAAGC TGGATACCCT
  301  ATGCACTCCG GTGGCATGCT GGGTGGTTGG AAGTTTTCCA ACGTTAAAGA TGGCATGTTT
  361  GCTGAATACT TTCACGTCAA TGATGCTGAG GGTAACTTAG CATTGATGCC AGAAGGGATG
  421  GATTTAGCTG ATGCATGTAT GTTGTCAGAC ATGATTCCCA CAGGCTTTCA CGCCAATGAA
  481  CTAGCTGACA TCCAATACGG TGTCGCGTTG TCGTTTTTTT GTGCTGGTCC AGTTGGTTTA
  541  ATGGCGATCG CTGGTGCAGC CTTAAAGGGT GCTGGACGCA TTATTGTGGT GGATTCTAGA
  601  CCAGATATTG TGGAAATTGC CAAAGCATAC GGTGCGACTG ATTACATTGA TTTCAAAAAG
  661  GTTTCAGTTG TGGATGAAAT CTTGAAGTGA ACCAACAATG AAGGAGTGGA AAAGGTGTTA
  721  ATTTCTGGTG GTGGTTCGAC TATCTTAGAA ACAGCGATTA AGGTTTTAAG ACCAGGAGGC
  781  AAAATTGGTA ACGTTAATTA CTTTGGCGCT GGTGAGTTTT TAACTATTCC TAGAGTTGAA
  841  TGGGGCGTTG GTATGGCTCA CAAGGCCATT CATGGTGGTC TTATGCTTGG TGGTCGGTTA
  901  AGGTTAGAAA AATTAGCACG TTTAATTATG ACCAAAAAAC TCGATCCTTC CAAAATGATT
  961  ACCCATCGCT TTAAGGGTTT TGAACACATT GAAGAAGCCC TGTTTTTAAT GAAAGATAAA
 1021  CCGAAGGACT TAATTAAATC CGTGGTTATT TTTTAA
Download Sequence
Operon 
OP349
Operon location 
682000 - 685822
Protein (mpn564)
Name 
Probable NADP-dependent alcohol dehydrogenase (EC 1.1.1.2)
Stable ID 
Mpn564
Molecular Weight 
38610
Isoelectric Point 
7
Localization 
Cytoplasm
Comment Alcohol dehydrogenase (NADP+), acetaldehyde dehydrogenase
Sequence 
MKAYAMLKIGATGWIEKPRPVCGPNDAIIRPLAVAPCTSDVHTVWEGGIGERHNMVLGHEGCGVVDEVGSEVKSFKVGDR
VLVAAITPEWNSVNAQAGYPMHSGGMLGGWKFSNVKDGMFAEYFHVNDAEGNLALMPEGMDLADACMLSDMIPTGFHANE
LADIQYGVALSFFCAGPVGLMAIAGAALKGAGRIIVVDSRPDIVEIAKAYGATDYIDFKKVSVVDEILKWTNNEGVEKVL
ISGGGSTILETAIKVLRPGGKIGNVNYFGAGEFLTIPRVEWGVGMAHKAIHGGLMLGGRLRLEKLARLIMTKKLDPSKMI
THRFKGFEHIEEALFLMKDKPKDLIKSVVIF
Post translational modifications
Modification Modified sequence Relative start Relative end Amino acid
Oxidation HNmVLGHEGcGVVDEVGSEVK 53 74 M
GENE/PROTEIN adh (Domains Overview)
Click on the features to jump to domain info

 ExportIMG
Domains (InterProScan)
Location (aa) Name (InterPro ID) Description GO terms Sequence Evalue
1-184 G3DSA:3.90.180.10 (n.a.) NULL 6.39973e-42
1-188 SSF50129 (IPR011032) GroES-like 1.4013e-45
14-351 PTHR11695:SF38 (n.a.) NULL 0
14-351 PTHR11695 (IPR002085) Alcohol dehydrogenase superfamily, zinc-containing 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';:0055114'>'oxidation' == '' ? '': 'oxidation'; 'reduction' == '' ? '': 'reduction'; ('GO' == '' ? '': 'GO';:0055114)

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';:0008270'>'zinc' == '' ? '': 'zinc'; 'ion' == '' ? '': 'ion'; 'binding' == '' ? '': 'binding'; ('GO' == '' ? '': 'GO';:0008270) <'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';:0016491'>'oxidoreductase' == '' ? '': 'oxidoreductase'; 'activity' == '' ? '': 'activity'; ('GO' == '' ? '': 'GO';:0016491)

0
24-128 PF08240 (IPR013154) Alcohol dehydrogenase GroES-like 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';:0016491'>'oxidoreductase' == '' ? '': 'oxidoreductase'; 'activity' == '' ? '': 'activity'; ('GO' == '' ? '': 'GO';:0016491)

0.000000000000076
58-72 PS00059 (IPR002328) Alcohol dehydrogenase, zinc-containing, conserved 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';:0055114'>'oxidation' == '' ? '': 'oxidation'; 'reduction' == '' ? '': 'reduction'; ('GO' == '' ? '': 'GO';:0055114)

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';:0008270'>'zinc' == '' ? '': 'zinc'; 'ion' == '' ? '': 'ion'; 'binding' == '' ? '': 'binding'; ('GO' == '' ? '': 'GO';:0008270) <'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';:0016491'>'oxidoreductase' == '' ? '': 'oxidoreductase'; 'activity' == '' ? '': 'activity'; ('GO' == '' ? '': 'GO';:0016491)

0
140-314 SSF51735 (n.a.) NULL 1.7e-35
177-297 PF00107 (IPR013149) Alcohol dehydrogenase, C-terminal 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';:0055114'>'oxidation' == '' ? '': 'oxidation'; 'reduction' == '' ? '': 'reduction'; ('GO' == '' ? '': 'GO';:0055114)

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';:0008270'>'zinc' == '' ? '': 'zinc'; 'ion' == '' ? '': 'ion'; 'binding' == '' ? '': 'binding'; ('GO' == '' ? '': 'GO';:0008270) <'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';:0016491'>'oxidoreductase' == '' ? '': 'oxidoreductase'; 'activity' == '' ? '': 'activity'; ('GO' == '' ? '': 'GO';:0016491)

2.2e-16
185-270 G3DSA:3.40.50.720 (IPR016040) NAD(P)-binding 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';: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) <'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';:0005488'>'binding' == '' ? '': 'binding'; ('GO' == '' ? '': 'GO';:0005488)

7.7e-25
Protein Homology (BLASTP results)
Protein Start Protein End Hit Size Orthologous Organism Orthologous Start Orthologous End Evalue Identity Score Alignment
20 337 317 - b2545 Escherichia coli 23 339 1e-19 26.3804 225
1 340 339 - b1776 Escherichia coli 1 345 3e-18 25.3482 212
25 264 239 - b0608 Escherichia coli 26 289 2e-17 31.4607 205
5 349 344 - b1774 Escherichia coli 6 343 1e-16 26.1708 198
1 328 327 - b3616 Escherichia coli 1 326 0.000000000000003 27.7457 187
37 334 297 - b2091 Escherichia coli 38 330 0.0000000000008 24.5161 165
14 351 337 - b4358 Escherichia coli 17 340 0.00000000003 24.5614 151
1 351 350 - b1580 Escherichia coli 1 337 0.000000001 24.4444 137
120 259 139 - b0356 Escherichia coli 141 280 0.000000003 29.8611 135
26 279 253 - b1478 Escherichia coli 26 272 0.00000002 25.7692 128
37 261 224 - MARTH_orf738 Mycoplasma arthritidis 40 259 0.000000000003 26.3158 154
19 324 305 - MAG2740 Mycoplasma agalactiae 19 319 1e-29 30.8917 303
14 261 247 - MAG4280 Mycoplasma agalactiae 16 256 0.0000000000005 29.7619 161
1 349 348 - MYPE4620 Mycoplasma penetrans 10 361 <1e-50 30.618 453
10 279 269 - Lactococcus lactis subsp. lactis KF147 12 276 1e-19 30.292 222
25 349 324 - Lactococcus lactis subsp. lactis KF147 26 343 4e-30 29.912 312
29 262 233 - LIC_10809 Leptospira interrogans serovar Copenhage 35 264 2e-21 31.3559 238
2 157 155 - LIC_11586 Leptospira interrogans serovar Copenhage 3 162 0.000000000004 28.4024 159
16 272 256 - LIC_10958 Leptospira interrogans serovar Copenhage 19 265 0.000000002 25.5639 136
1 333 332 - LIC_11357 Leptospira interrogans serovar Copenhage 1 329 0.0000004 22.5714 116
1 265 264 - Rv1895 Mycobacterium tuberculosis 1 260 9e-21 28.7313 234
20 351 331 - MT2320 Mycobacterium tuberculosis 25 361 0.00000000000001 25.3561 182
23 262 239 - MT3171 Mycobacterium tuberculosis 26 281 0.0000000005 26.5385 141
23 95 72 - Rv3045 Mycobacterium tuberculosis 27 99 0.000006 38.3562 106
37 269 232 - Lactococcus lactis subsp. lactis KF147 37 275 0.000000002 26.506 133
1 351 350 - Caulobacter crescentus NA1000 1 365 5e-23 27.8947 253
25 349 324 - Caulobacter crescentus NA1000 26 343 6e-23 25.4601 252
1 277 276 - Bacillus subtilis subsp. subtilis 9 284 2e-23 32.0423 259
1 277 276 - Bacillus subtilis subsp. subtilis 33 308 7e-23 31.338 254
25 349 324 - Bacillus subtilis subsp. subtilis 26 376 8e-16 24.8634 193
25 349 324 - Bacillus subtilis subsp. subtilis 26 376 0.000000000000007 25.3406 185
28 211 183 - Bacillus subtilis subsp. subtilis 47 240 0.00000000000002 31.8408 181
28 211 183 - Bacillus subtilis subsp. subtilis 52 245 0.00000000000002 31.8408 180
1 351 350 - Bacillus subtilis subsp. subtilis 1 338 0.00000000000003 22.9462 179
1 351 350 - Bacillus subtilis subsp. subtilis 1 338 0.0000000000005 22.6629 168
1 339 338 - Bacillus subtilis subsp. subtilis 6 337 0.000000000008 25.9887 158
6 339 333 - Bacillus subtilis subsp. subtilis 1 328 0.00000000001 25.5014 158
24 81 57 - Bacillus subtilis subsp. subtilis 31 88 0.000009 45.9016 106
External IDs
COG 
COG1063ER
EC number 
1.1.1.1
EC number 
1.2.1.10
Gene ID 
876853
GI 
13508303
GO 
Energy production and conversion
Home COG 
C
InterPro 
IPR002085|Alcohol dehydrogenase superfamily, zinc-containing
InterPro 
IPR013154|Alcohol dehydrogenase GroES-like
InterPro 
IPR013149|Alcohol dehydrogenase, zinc-binding
InterPro 
IPR011032|GroES-like
InterPro 
IPR002328|Alcohol dehydrogenase, zinc-containing
Old MP number 
MP278
Pathway 
Metabolism
PDB homologs 
1m6h_A
PDB homologs 
1m6w_A
PDB homologs 
1mc5_A
PDB homologs 
1YKF
Pfam 
PF00107
Pfam 
PF08240
PID 
g1673949
RefSeq 
NP_110253.1
Swiss-Prot protein ID 
ADH_MYCPN
phylomeDB tree 
ADH_MYCPN
UniProt 
P75214
Transcription
IMAGE BROWSERS

OPERON OP349 (Genomic Overview)
Region:682000-685822

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STRING image

STRING of Mpn564STRING legend

PDB image(s)

1m6h

PDB 1m6h

1m6w

PDB 1m6w

1mc5

PDB 1mc5

1YKF

PDB 1YKF
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