MyMpn
The Mycoplasma pneumoniae database
 
e.g Mpn001 or dnaN or polymerase
Gene pdhA (MPN393)
Name 
pdhA
Stable ID 
MPN393
Location 
470379 - 471455 -
Sequence 
    1  ATGGCAATTT TGATTAAAAA CAAAGTCCCT ACTACACTTT ACCAAGTGTA TGACAATGAG
   61  GGTAAGTTAA TGGACCCTAA TCACAAGATT ACACTTAGCA ACGAACAGTT AAAGCACGCT
  121  TTTTACCTCA TGAATCTTTC CCGAATCATG GACAAGAAGA TGCTTGTTTG ACAACGTGCT
  181  GGTAAGATGT TGAACTTTGC GCCTAACTTA GGTGAGGAAG CACTGCAAGT TGGTATGGGC
  241  ATGGGTTTAA ATGAAAATGA CTGGTTCTGC CCTACCTTCC GTTCCGGTGC GTTAATGTTG
  301  TACCGTGGTG TTAAACCAGA ACAGCTTTTA CTTTACTGAA ACGGTAACGA AAACGGTAGT
  361  AAGATCGAAG CTAAATACAA AACGCTGCCC ATTAACATTA CCATTGGTGC ACAGTACTCT
  421  CATGCTGCTG GACTTGGTTA CATGTTGCAC TACAAGAAAC TCCCTAACGT AGCCGTTACG
  481  ATGATTGGGG ATGGTGGTAC AGCTGAAGGT GAGTTTTATG AAGCGATGAA CATTGCTTCC
  541  ATTCACAAGT GAAACTCGGT CTTTTGTATT AACAACAACC AGTTTGCCAT TTCCACCAGA
  601  ACTAAATTAG AGTCCGCTGT AAGTGACCTT TCCACCAAGG CTATTGCGGT TAACATTCCT
  661  CGTATTCGCG TTGACGGTAA TGACTTAATT GCGAGTTACG AAGCAATGCA CGAAGCAGCT
  721  AACTATGCGA GAAGCGGTAA TGGACCAGTG TTAATTGAGT TCTTCTCTTG ACGTCAAGGT
  781  CCCCACACCA CTTCCGATGA CCCTTCCATT TACCGTACTA AAGAAGAGGA AGCGGAAGCG
  841  ATGAAGAGTG ACCCTGTGAA GCGGTTACGT AACTTCTTGT TTGACCGTGG TATTCTAACC
  901  CCACAACAAG AAGAGGAAAT GGTAGCTAAG ATTGAACAAG AAGTGCAAGC TGCATATGAG
  961  GTAATGGTTA GCAAAACGCC AGTTACCTTG GATGAAGTGT TTGATTATAA CTATGAAAAG
 1021  TTGACTCCTG ATCTAGCGCG CCAAAAGGCT GAAGCTAAAA AATACTTTAA AGACTAA
Download Sequence
Operon 
OP437
Operon location 
469365 - 472927
Protein (mpn393)
Name 
Pyruvate dehydrogenase E1 component subunit alpha (EC 1.2.4.1)
Stable ID 
Mpn393
Molecular Weight 
39380
Isoelectric Point 
7
Localization 
Cytoplasm
Comment -
Sequence 
MAILIKNKVPTTLYQVYDNEGKLMDPNHKITLSNEQLKHAFYLMNLSRIMDKKMLVWQRAGKMLNFAPNLGEEALQVGMG
MGLNENDWFCPTFRSGALMLYRGVKPEQLLLYWNGNENGSKIEAKYKTLPINITIGAQYSHAAGLGYMLHYKKLPNVAVT
MIGDGGTAEGEFYEAMNIASIHKWNSVFCINNNQFAISTRTKLESAVSDLSTKAIAVNIPRIRVDGNDLIASYEAMHEAA
NYARSGNGPVLIEFFSWRQGPHTTSDDPSIYRTKEEEAEAMKSDPVKRLRNFLFDRGILTPQQEEEMVAKIEQEVQAAYE
VMVSKTPVTLDEVFDYNYEKLTPDLARQKAEAKKYFKD
Post translational modifications
Modification Modified sequence Relative start Relative end Amino acid
Oxidation NkVPTTLYQVYDNEGKLmDPNHk 7 30 M
Oxidation NKVPTTLYQVYDNEGKLmDPNHK 7 30 M
Oxidation NKVPTTLYQVYDNEGKLmDPNHKITLSNEQLK 7 39 M
Oxidation LmDPNHK 23 30 M
Oxidation LmDPNHk 23 30 M
Oxidation LmDPNHKITLSNEQLK 23 39 M
Oxidation LmDPNHKITLSNEQLKHAFYLmNLSR 23 49 M
Oxidation LmDPNHKITLSNEQLKHAFYLMNLSR 23 49 M
Oxidation ITLSNEQLKHAFYLmNLSR 30 49 M
Oxidation HAFYLmNLSR 39 49 M
Oxidation HAFYLmNLSr 39 49 M
Oxidation ImDKKmLVWQR 49 60 M
Oxidation KmLVWQR 53 60 M
Oxidation mLVWQR 54 60 M
Oxidation mLVWQr 54 60 M
Oxidation MLNFAPNLGEEALQVGmGMGLNENDWFcPTFR 63 95 M
Oxidation mLNFAPNLGEEALQVGMGMGLNENDWFcPTFR 63 95 M
Oxidation mLNFAPNLGEEALQVGMGmGLNENDWFcPTFR 63 95 M
Oxidation mLNFAPNLGEEALQVGmGMGLNENDWFcPTFR 63 95 M
Oxidation mLNFAPNLGEEALQVGmGmGLNENDWFcPTFR 63 95 M
Oxidation MLNFAPNLGEEALQVGmGmGLNENDWFcPTFR 63 95 M
Oxidation SGALmLYr 95 103 M
Oxidation SGALmLYR 95 103 M
Oxidation YKTLPINITIGAQYSHAAGLGYmLHYK 126 153 M
Oxidation TLPINITIGAQYSHAAGLGYmLHYk 128 153 M
Oxidation TLPINITIGAQYSHAAGLGYmLHYK 128 153 M
Oxidation kLPNVAVTmIGDGGTAEGEFYEAMNIASIHk 153 184 M
Oxidation KLPNVAVTmIGDGGTAEGEFYEAmNIASIHK 153 184 M
Oxidation KLPNVAVTmIGDGGTAEGEFYEAMNIASIHK 153 184 M
Oxidation kLPNVAVTMIGDGGTAEGEFYEAmNIASIHk 153 184 M
Oxidation KLPNVAVTMIGDGGTAEGEFYEAmNIASIHK 153 184 M
Oxidation LPNVAVTMIGDGGTAEGEFYEAmNIASIHK 154 184 M
Oxidation LPNVAVTmIGDGGTAEGEFYEAmNIASIHK 154 184 M
Oxidation LPNVAVTmIGDGGTAEGEFYEAMNIASIHK 154 184 M
Oxidation IRVDGNDLIASYEAmHEAANYAr 222 245 M
Oxidation IrVDGNDLIASYEAmHEAANYAr 222 245 M
Oxidation IRVDGNDLIASYEAmHEAANYAR 222 245 M
Oxidation IrVDGNDLIASYEAmHEAANYAR 222 245 M
Oxidation VDGNDLIASYEAmHEAANYAr 224 245 M
Oxidation VDGNDLIASYEAmHEAANYAR 224 245 M
Oxidation TkEEEAEAmk 273 283 M
Oxidation TKEEEAEAmK 273 283 M
Oxidation TKEEEAEAmk 273 283 M
Oxidation TkEEEAEAmK 273 283 M
Oxidation TKEEEAEAmKSDPVK 273 288 M
Oxidation TkEEEAEAmKSDPVk 273 288 M
Oxidation TkEEEAEAmkSDPVk 273 288 M
Oxidation TkEEEAEAmKSDPVkr 273 289 M
Oxidation TKEEEAEAmkSDPVkr 273 289 M
Oxidation TkEEEAEAmkSDPVkr 273 289 M
Oxidation TKEEEAEAmKSDPVKR 273 289 M
Oxidation TkEEEAEAmkSDPVKr 273 289 M
Oxidation EEEAEAmK 275 283 M
Oxidation EEEAEAmKSDPVKR 275 289 M
Oxidation eEEAEAmKSDPVKR 275 289 M
Formylation eEEAEAmKSDPVKR 275 289 N
Oxidation LRNFLFDRGILTPQQEEEmVAK 289 311 M
Oxidation NFLFDRGILTPQQEEEmVAK 291 311 M
Oxidation GILTPQQEEEmVAK 297 311 M
Oxidation GILTPQQEEEmVAk 297 311 M
Oxidation GILTPQQEEEMVAKIEQEVQAAYEVmVSK 297 326 M
Oxidation GILTPQQEEEmVAKIEQEVQAAYEVmVSK 297 326 M
Oxidation GILTPQQEEEmVAKIEQEVQAAYEVMVSK 297 326 M
Oxidation IEQEVQAAYEVmVSk 311 326 M
Oxidation IEQEVQAAYEVmVSK 311 326 M
GENE/PROTEIN pdhA (Domains Overview)
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Domains (InterProScan)
Location (aa) Name (InterPro ID) Description GO terms Sequence Evalue
7-351 G3DSA:3.40.50.970 (n.a.) NULL 0
7-358 SSF52518 (n.a.) NULL 0
12-352 TIGR03181 (IPR017596) Pyruvate dehydrogenase (acetyl-transferring) E1 co 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';:0006096'>'glycolysis' == '' ? '': 'glycolysis'; ('GO' == '' ? '': 'GO';:0006096) <'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';:0004739'>'pyruvate' == '' ? '': 'pyruvate'; 'dehydrogenase' == '' ? '': 'dehydrogenase'; ('acetyl' == '' ? '': 'acetyl';-'transferring' == '' ? '': 'transferring';) 'activity' == '' ? '': 'activity'; ('GO' == '' ? '': 'GO';:0004739) <'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';:0030976'>'thiamin' == '' ? '': 'thiamin'; 'pyrophosphate' == '' ? '': 'pyrophosphate'; 'binding' == '' ? '': 'binding'; ('GO' == '' ? '': 'GO';:0030976)

0
16-358 PTHR11516:SF1 (n.a.) NULL 0
16-358 PTHR11516 (n.a.) NULL 0
43-328 PF00676 (IPR001017) Dehydrogenase, E1 component 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';:'oxidoreductase' == '' ? '': 'oxidoreductase';'>'oxidoreductase' == '' ? '': 'oxidoreductase'; 'activity' == '' ? '': 'activity';

0
Protein Homology (BLASTP results)
Protein Start Protein End Hit Size Orthologous Organism Orthologous Start Orthologous End Evalue Identity Score Alignment
10 357 347 - MAG0930 Mycoplasma agalactiae 15 362 <1e-50 40.1709 644
21 356 335 - MCJ_000670 Mycoplasma conjunctivae 36 371 <1e-50 53.1157 903
16 357 341 - MCAP_0225 Mycoplasma capricolum subsp. capricolum 17 359 <1e-50 38.1924 574
1 358 357 - MYCGA4850 Mycoplasma gallisepticum 1 358 <1e-50 61.4525 1240
1 358 357 - MG274 Mycoplasma genitalium 1 358 <1e-50 88.2682 1733
24 357 333 - MHP7448_0115 Mycoplasma hyopneumoniae 7448 38 371 <1e-50 52.3952 890
12 357 345 - MMOB5840 Mycoplasma mobile 19 366 <1e-50 49.7126 912
16 357 341 - MSC_0265 Mycoplasma mycoides subsp. mycoides SC 17 359 <1e-50 37.9009 576
11 356 345 - MYPE5080 Mycoplasma penetrans 10 355 <1e-50 47.6879 893
13 353 340 - Lactococcus lactis subsp. lactis KF147 23 374 <1e-50 34.2697 475
61 294 233 - LIC_11897 Leptospira interrogans serovar Copenhage 38 280 1e-26 31.7073 283
10 357 347 - MS53_0272 Mycoplasma synoviae 21 369 <1e-50 50.1433 855
32 353 321 - MT2572 Mycobacterium tuberculosis 39 360 <1e-50 35.0932 543
35 317 282 - MT0865 Mycobacterium tuberculosis 14 303 0.00000000005 24.1497 149
70 298 228 - Caulobacter crescentus NA1000 62 299 5e-27 30.9623 287
14 348 334 - Bacillus subtilis subsp. subtilis 26 361 <1e-50 32.4405 511
14 348 334 - Bacillus subtilis subsp. subtilis 26 361 <1e-50 32.4405 511
27 340 313 - Bacillus subtilis subsp. subtilis 6 330 6e-38 30.1538 384
44 340 296 - Bacillus subtilis subsp. subtilis 1 308 5e-37 31.4935 376
71 324 253 - Bacillus subtilis subsp. subtilis 51 307 3e-28 29.434 300
71 324 253 - Bacillus subtilis subsp. subtilis 51 307 8e-28 29.434 297
156 327 171 - Bacillus subtilis subsp. subtilis 355 526 0.0000001 26.9663 123
156 327 171 - Bacillus subtilis subsp. subtilis 346 517 0.0000001 26.9663 122
13 357 344 - Mycoplasma pulmonis 20 363 <1e-50 51.5942 921
External IDs
COG 
COG1071C
EC number 
1.2.4.1
Gene ID 
877083
GI 
13508132
GO 
Energy production and conversion
Home COG 
C
InterPro 
IPR001017|Dehydrogenase, E1 component
Old MP number 
MP445
Pathway 
Metabolism energy
PDB homologs 
1olx_A
PDB homologs 
1ols_A
PDB homologs 
1dtw_A
PDB homologs 
1AYO-A
Pfam 
PF00676
PID 
g1674133
RefSeq 
NP_110081.1
Swiss-Prot protein ID 
ODPA_MYCPN
phylomeDB tree 
ODPA_MYCPN
UniProt 
P75390
Transcription
IMAGE BROWSERS

OPERON OP437 (Genomic Overview)
Region:469365-472927

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STRING image

STRING of Mpn393STRING legend

PDB image(s)

1olx

PDB 1olx

1ols

PDB 1ols

1dtw

PDB 1dtw

1AYO

PDB 1AYO
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All data provided for download in the MyMpn database is free to use. Upon doing so, please cite the original data source and the MyMpn database
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