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Conserved domains on  [gi|1331381824|ref|WP_102605804|]
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MULTISPECIES: alpha-ketoglutarate dehydrogenase [unclassified Pseudomonas]

Protein Classification

pyruvate dehydrogenase E1 component( domain architecture ID 11486350)

E1 component of the acetyl-transferring homodimeric-type pyruvate dehydrogenase multienzyme complex

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PRK13012 PRK13012
2-oxoacid dehydrogenase subunit E1; Provisional
14-891 0e+00

2-oxoacid dehydrogenase subunit E1; Provisional


:

Pssm-ID: 237267 [Multi-domain]  Cd Length: 896  Bit Score: 1698.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824  14 DQEELAEWRDALASLVANAGAARAREILDMLADAGGAPHIAWKPRHGTPYINSIAVEQQPPFPGDLATEERLASVVRWNA 93
Cdd:PRK13012   21 DPQETAEWLEALDAVVAHAGPERARYLLDRLLERAAARGIALPGLLTTPYVNTIPVDQQPPYPGDLALEERLAAIIRWNA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824  94 LAMVVRANQAYGELGGHIASYASAADLFEVGFNHFFRARSDSFGGDLVFYQPHSAPGIYARAFLEGRLSEADLAHYRQEI 173
Cdd:PRK13012  101 LAMVVRANRAYGELGGHIASYASAADLFEVGFNHFFRGRDDAGGGDLVYFQPHSAPGIYARAFLEGRLSEEQLDHFRQEI 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 174 GAGkagarGLSSYPHPWLMPDFWQFPTGSMGIGPISSIFQARFMRYLQHRGLQDSTDRHVWGVFGDGEMDEPESMSALTL 253
Cdd:PRK13012  181 GGP-----GLSSYPHPWLMPDFWQFPTGSMGIGPINAIYQARFMRYLQHRGLKDTSGRKVWGFFGDGEMDEPESIAALSL 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 254 AAREGLDNLTWVVNCNLQRLDGPVRGNGRIIDELEALFAGAGWNVIKLVWGSDWDALLAKDTDGELARTLSQTVDGQFQT 333
Cdd:PRK13012  256 AAREGLDNLVFVINCNLQRLDGPVRGNGRIIQELEALFRGAGWNVIKVLWGSDWDALFARDTTGALVRRFAETVDGQFQT 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 334 FAAKDGAYNREHFFGQSEALSKLVEGLSDEQIDRLKRGGHDMVKIHAAYHAARRVAGKPTVILAQTKKGFGMGEAGQGKM 413
Cdd:PRK13012  336 FKANDGAYNREHFFGQDPELAALVAHLSDEDIDRLKRGGHDPRKVYAAYAAAVRHKGQPTVILAKTKKGYGMGEAGEGRM 415
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 414 TTHQQKKLDREALIAFRNRFQLPLSDEQAESLSFYKPAEGSLEMRYLHQRRATLGGYVPSRGQQAPSVSVPPVSGYGAFA 493
Cdd:PRK13012  416 TTHQQKKLDVEALKAFRDRFRLPLSDEQLEQLPFYKPAEDSPEMRYLHARRAALGGYLPRRRTAAPPLPVPPLSAFAQFA 495
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 494 TQAEGKEMSTTMAFVRMLTNLLKDKALGPRIVPIVADEARTFGMANLFKQIGIYSSVGQRYEPEDIGSILSYREATDGQI 573
Cdd:PRK13012  496 LGAGGKEMSTTMAFVRMLGNLLKDKALGPRIVPIVADEARTFGMANLFRQVGIYSPLGQLYEPEDAGSLLYYREAKDGQI 575
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 574 LEEGISEASAISSWVAAATSYSVHGLRMLPFYIYYSMFGFQRVGDLIWAAADQRARGFLLGATAGRTTLGGEGLQHQDGS 653
Cdd:PRK13012  576 LEEGITEAGAISSWIAAATSYSVHGLPMLPFYIYYSMFGFQRVGDLIWAAADQRARGFLLGATAGRTTLGGEGLQHQDGH 655
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 654 SHLMAATVPNCRAYDPAFAGEFAVILDHGMRQMLEHDVDEFYYVTLMNENYPQPSLPEGVEAAIIKGMYRLSGQPGG-KV 732
Cdd:PRK13012  656 SHLLASTIPNCRAYDPAFAYELAVIVDDGMRRMLEEQEDVFYYLTVMNENYAQPALPEGAEEGILKGMYRLAAAAEApRV 735
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 733 RLLGSGTLVREAQAAAQLLAEDWQVDAEVFSVTSFSELARDARDVERWNRLHPQQPARRSHLAECLPKG-APVVAVSDYV 811
Cdd:PRK13012  736 QLLGSGAILREVLAAARLLADDWGVDADVWSVTSFTELRRDGLAAERANLLGPAEEARVPYVTQCLAGTrGPVVAATDYV 815
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 812 RAVPQMLGSYVDSAYTVLGTDGFGRSDTRAALRDFFEVDRHHIVLAALTALVEQGSLDRQVCQQAIKRYGVQTDREPSWT 891
Cdd:PRK13012  816 RAVPEQIRAFVPARYVTLGTDGFGRSDTRAALRRFFEVDRHSIVLAALKALADDGEVERTVVAEAIERYGIDDDKTPPWE 895
 
Name Accession Description Interval E-value
PRK13012 PRK13012
2-oxoacid dehydrogenase subunit E1; Provisional
14-891 0e+00

2-oxoacid dehydrogenase subunit E1; Provisional


Pssm-ID: 237267 [Multi-domain]  Cd Length: 896  Bit Score: 1698.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824  14 DQEELAEWRDALASLVANAGAARAREILDMLADAGGAPHIAWKPRHGTPYINSIAVEQQPPFPGDLATEERLASVVRWNA 93
Cdd:PRK13012   21 DPQETAEWLEALDAVVAHAGPERARYLLDRLLERAAARGIALPGLLTTPYVNTIPVDQQPPYPGDLALEERLAAIIRWNA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824  94 LAMVVRANQAYGELGGHIASYASAADLFEVGFNHFFRARSDSFGGDLVFYQPHSAPGIYARAFLEGRLSEADLAHYRQEI 173
Cdd:PRK13012  101 LAMVVRANRAYGELGGHIASYASAADLFEVGFNHFFRGRDDAGGGDLVYFQPHSAPGIYARAFLEGRLSEEQLDHFRQEI 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 174 GAGkagarGLSSYPHPWLMPDFWQFPTGSMGIGPISSIFQARFMRYLQHRGLQDSTDRHVWGVFGDGEMDEPESMSALTL 253
Cdd:PRK13012  181 GGP-----GLSSYPHPWLMPDFWQFPTGSMGIGPINAIYQARFMRYLQHRGLKDTSGRKVWGFFGDGEMDEPESIAALSL 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 254 AAREGLDNLTWVVNCNLQRLDGPVRGNGRIIDELEALFAGAGWNVIKLVWGSDWDALLAKDTDGELARTLSQTVDGQFQT 333
Cdd:PRK13012  256 AAREGLDNLVFVINCNLQRLDGPVRGNGRIIQELEALFRGAGWNVIKVLWGSDWDALFARDTTGALVRRFAETVDGQFQT 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 334 FAAKDGAYNREHFFGQSEALSKLVEGLSDEQIDRLKRGGHDMVKIHAAYHAARRVAGKPTVILAQTKKGFGMGEAGQGKM 413
Cdd:PRK13012  336 FKANDGAYNREHFFGQDPELAALVAHLSDEDIDRLKRGGHDPRKVYAAYAAAVRHKGQPTVILAKTKKGYGMGEAGEGRM 415
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 414 TTHQQKKLDREALIAFRNRFQLPLSDEQAESLSFYKPAEGSLEMRYLHQRRATLGGYVPSRGQQAPSVSVPPVSGYGAFA 493
Cdd:PRK13012  416 TTHQQKKLDVEALKAFRDRFRLPLSDEQLEQLPFYKPAEDSPEMRYLHARRAALGGYLPRRRTAAPPLPVPPLSAFAQFA 495
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 494 TQAEGKEMSTTMAFVRMLTNLLKDKALGPRIVPIVADEARTFGMANLFKQIGIYSSVGQRYEPEDIGSILSYREATDGQI 573
Cdd:PRK13012  496 LGAGGKEMSTTMAFVRMLGNLLKDKALGPRIVPIVADEARTFGMANLFRQVGIYSPLGQLYEPEDAGSLLYYREAKDGQI 575
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 574 LEEGISEASAISSWVAAATSYSVHGLRMLPFYIYYSMFGFQRVGDLIWAAADQRARGFLLGATAGRTTLGGEGLQHQDGS 653
Cdd:PRK13012  576 LEEGITEAGAISSWIAAATSYSVHGLPMLPFYIYYSMFGFQRVGDLIWAAADQRARGFLLGATAGRTTLGGEGLQHQDGH 655
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 654 SHLMAATVPNCRAYDPAFAGEFAVILDHGMRQMLEHDVDEFYYVTLMNENYPQPSLPEGVEAAIIKGMYRLSGQPGG-KV 732
Cdd:PRK13012  656 SHLLASTIPNCRAYDPAFAYELAVIVDDGMRRMLEEQEDVFYYLTVMNENYAQPALPEGAEEGILKGMYRLAAAAEApRV 735
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 733 RLLGSGTLVREAQAAAQLLAEDWQVDAEVFSVTSFSELARDARDVERWNRLHPQQPARRSHLAECLPKG-APVVAVSDYV 811
Cdd:PRK13012  736 QLLGSGAILREVLAAARLLADDWGVDADVWSVTSFTELRRDGLAAERANLLGPAEEARVPYVTQCLAGTrGPVVAATDYV 815
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 812 RAVPQMLGSYVDSAYTVLGTDGFGRSDTRAALRDFFEVDRHHIVLAALTALVEQGSLDRQVCQQAIKRYGVQTDREPSWT 891
Cdd:PRK13012  816 RAVPEQIRAFVPARYVTLGTDGFGRSDTRAALRRFFEVDRHSIVLAALKALADDGEVERTVVAEAIERYGIDDDKTPPWE 895
AceE COG2609
Pyruvate dehydrogenase complex, dehydrogenase (E1) component [Energy production and conversion] ...
1-892 0e+00

Pyruvate dehydrogenase complex, dehydrogenase (E1) component [Energy production and conversion]; Pyruvate dehydrogenase complex, dehydrogenase (E1) component is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 442021 [Multi-domain]  Cd Length: 891  Bit Score: 1647.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824   1 MNGFASAVSQTAMDQEELAEWRDALASLVANAGAARAREILDMLADAGGAPHIAWKPRHGTPYINSIAVEQQPPFPGDLA 80
Cdd:COG2609     1 MSMDGLPSQLPDIDPQETQEWLESLDAVIEEEGPERARYLLERLLERARRSGVGLPFSATTPYINTIPVEQEPPYPGDEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824  81 TEERLASVVRWNALAMVVRANQAYGELGGHIASYASAADLFEVGFNHFFRARSDSFGGDLVFYQPHSAPGIYARAFLEGR 160
Cdd:COG2609    81 LERRIRSIIRWNAMAMVVRANRKGGGLGGHISSFASAATLYEVGFNHFFRGPDHPGGGDLVYFQGHASPGIYARAFLEGR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 161 LSEADLAHYRQEIGAGkagarGLSSYPHPWLMPDFWQFPTGSMGIGPISSIFQARFMRYLQHRGLQDSTDRHVWGVFGDG 240
Cdd:COG2609   161 LTEEQLDNFRQEVDGK-----GLSSYPHPWLMPDFWQFPTVSMGLGPINAIYQARFMKYLHNRGLKDTSDRKVWAFLGDG 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 241 EMDEPESMSALTLAAREGLDNLTWVVNCNLQRLDGPVRGNGRIIDELEALFAGAGWNVIKLVWGSDWDALLAKDTDGELA 320
Cdd:COG2609   236 EMDEPESLGAISLAAREKLDNLIFVINCNLQRLDGPVRGNGKIIQELEGVFRGAGWNVIKVIWGSEWDPLLAKDTDGALV 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 321 RTLSQTVDGQFQTFAAKDGAYNREHFFGQSEALSKLVEGLSDEQIDRLKRGGHDMVKIHAAYHAARRVAGKPTVILAQTK 400
Cdd:COG2609   316 KRMNETVDGDYQTYKAKDGAYVREHFFGKYPELKALVADMSDEDIWRLNRGGHDPRKVYAAYKAAVEHKGQPTVILAKTI 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 401 KGFGMGEAGQGKMTTHQQKKLDREALIAFRNRFQLPLSDEQAESLSFYKPAEGSLEMRYLHQRRATLGGYVPSRGQQAPS 480
Cdd:COG2609   396 KGYGMGEAGEGRNITHQQKKLDLDDLKAFRDRFNIPISDEQLEELPYYKPAEDSPEMKYLHERRKALGGYLPQRRTKAEP 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 481 VSVPPVSGYGAFATQAEGKEMSTTMAFVRMLTNLLKDKALGPRIVPIVADEARTFGMANLFKQIGIYSSVGQRYEPEDIG 560
Cdd:COG2609   476 LEVPELSAFAALLKGSGKREISTTMAFVRILNDLLKDKEIGKRIVPIVPDEARTFGMEGLFRQIGIYSPVGQLYTPVDAD 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 561 SILSYREATDGQILEEGISEASAISSWVAAATSYSVHGLRMLPFYIYYSMFGFQRVGDLIWAAADQRARGFLLGATAGRT 640
Cdd:COG2609   556 QLLYYKESKDGQILQEGINEAGAMSSWIAAGTSYSTHGVPMIPFYIYYSMFGFQRVGDLAWAAGDQRARGFLIGATAGRT 635
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 641 TLGGEGLQHQDGSSHLMAATVPNCRAYDPAFAGEFAVILDHGMRQMLEHDVDEFYYVTLMNENYPQPSLPEGVEAAIIKG 720
Cdd:COG2609   636 TLNGEGLQHQDGHSHLLASTIPNCVSYDPAFAYELAVIVQDGLRRMYGEQENVFYYITVMNENYAQPAMPEGVEEGILKG 715
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 721 MYRLS---GQPGGKVRLLGSGTLVREAQAAAQLLAEDWQVDAEVFSVTSFSELARDARDVERWNRLHPQQPARRSHLAEC 797
Cdd:COG2609   716 MYLLKegeGKGKPRVQLLGSGTILREVLAAAELLAEDWGVAADVWSVTSFNELRRDGLDVERWNLLHPEEEPRVPYVTQC 795
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 798 LPKG-APVVAVSDYVRAVPQMLGSYVDSAYTVLGTDGFGRSDTRAALRDFFEVDRHHIVLAALTALVEQGSLDRQVCQQA 876
Cdd:COG2609   796 LAGAeGPVVAATDYMRAVPDQIRPWVPGRYTVLGTDGFGRSDTREALRRFFEVDRYSIVVAALKALADEGKIDASVVAEA 875
                         890
                  ....*....|....*.
gi 1331381824 877 IKRYGVQTDREPSWTS 892
Cdd:COG2609   876 IKKYGIDPDKPNPLTA 891
AKGDH_not_PDH TIGR03186
alpha-ketoglutarate dehydrogenase; Several bacterial species have a paralog to homodimeric ...
14-892 0e+00

alpha-ketoglutarate dehydrogenase; Several bacterial species have a paralog to homodimeric form of the pyruvate dehydrogenase E1 component (see model TIGR00759), often encoded next to L-methionine gamma-lyase gene (mdeA). The member from a strain of Pseudomonas putida was shown to act on alpha-ketobutyrate, which is produced by MdeA.This model serves as an exception model to TIGR00759, as other proteins hitting TIGR00759 should be identified as the pyruvate dehydrogenase E1 component.


Pssm-ID: 132230 [Multi-domain]  Cd Length: 889  Bit Score: 1393.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824  14 DQEELAEWRDALASLVANAGAARAREILDMLADAGGAPHIAWKPRHGTPYINSIAVEQQPPFPGDLATEERLASVVRWNA 93
Cdd:TIGR03186   7 DPQETAEWLDALDGVVAHAGAERAQYLLAQLAAHAARLGLAPPAAGATPYVNTIAVDQEPPYPGDLQLEERLAAILRWNA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824  94 LAMVVRANQAYGELGGHIASYASAADLFEVGFNHFFRARSDSFGGDLVFYQPHSAPGIYARAFLEGRLSEADLAHYRQEI 173
Cdd:TIGR03186  87 LAMVVRANRAYGELGGHIASYASAADLFEVGFNHFFRAAGDASGGDLVYFQPHSAPGVYARAFLEGFLSDAQLAHYRQEI 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 174 GAgkagaRGLSSYPHPWLMPDFWQFPTGSMGIGPISSIFQARFMRYLQHRGLQDSTDRHVWGVFGDGEMDEPESMSALTL 253
Cdd:TIGR03186 167 AG-----PGLCSYPHPWLMPDFWQFPTGSMGIGPINAIYQARFMRYLQNRGLARTEGRKVWGFFGDGEMDEPESIGALSL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 254 AAREGLDNLTWVVNCNLQRLDGPVRGNGRIIDELEALFAGAGWNVIKLVWGSDWDALLAKDTDGELARTLSQTVDGQFQT 333
Cdd:TIGR03186 242 AARERLDNLVFVINCNLQRLDGPVRGNGRIIDELESQFAGAGWNVIKVLWGSDWDALFARDATGALARAFAHTVDGQFQT 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 334 FAAKDGAYNREHFFGQSEALSKLVEGLSDEQIDRLKRGGHDMVKIHAAYHAARRVAGKPTVILAQTKKGFGMGEAGQGKM 413
Cdd:TIGR03186 322 FSANDGAYNRARFFGQDPALAALVAHLSDEDIDRLRRGGHDARKLYAAYDRAVRHEGRPTVILAKTMKGFGMGAIGQGRM 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 414 TTHQQKKLDREALIAFRNRFQLPLSDEQAESLSFYKPAEGSLEMRYLHQRRATLGGYVPSRGQQAP-SVSVPPVSGYGAF 492
Cdd:TIGR03186 402 TTHQQKKLDVEALLAFRDRFRLPLSDADVEQLKFYKPDEDSAEMRYLHARRAALGGYLPRRRTAAThALAVPALPSWGRF 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 493 ATQAEGKEMSTTMAFVRMLTNLLKDKALGPRIVPIVADEARTFGMANLFKQIGIYSSVGQRYEPEDIGSILSYREATDGQ 572
Cdd:TIGR03186 482 ALDAEGKEMSTTMAIVRMLGALLKDAELGPRIVPIVADEARTFGMANLFRQVGIYSPLGQRYEPEDLGSMLYYREDTDGQ 561
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 573 ILEEGISEASAISSWVAAATSYSVHGLRMLPFYIYYSMFGFQRVGDLIWAAADQRARGFLLGATAGRTTLGGEGLQHQDG 652
Cdd:TIGR03186 562 ILEEGISEAGAISSWIAAATSYSVHDLPMLPFYIYYSMFGFQRIGDLIWAAADQRARGFLIGATSGKTTLGGEGLQHQDG 641
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 653 SSHLMAATVPNCRAYDPAFAGEFAVILDHGMRQMLEHDVDEFYYVTLMNENYPQPSLPEG----VEAAIIKGMYRL--SG 726
Cdd:TIGR03186 642 TSHLAASTVPNCRAWDPAFAYEVAVIVDEGMREMLERQRDEFYYLTVTNENYAQPSLPEDrldaVRRGILKGMYPLdpAA 721
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 727 QPGGKVRLLGSGTLVREAQAAAQLLAEDWQVDAEVFSVTSFSELARDARDVERWNRLHPQQPARRSHLAECL-PKGAPVV 805
Cdd:TIGR03186 722 LAAARVQLLGSGAILGEVQAAARLLRDDWGIDAAVWSVTSFTELARDGRAAERAQRLGDAERPPSPHVAQALgATQGPVI 801
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 806 AVSDYVRAVPQMLGSYVDSAYTVLGTDGFGRSDTRAALRDFFEVDRHHIVLAALTALVEQGSLDRQVCQQAIKRYGVQ-T 884
Cdd:TIGR03186 802 AATDYVRAVPELIRAYVPRRYVTLGTDGFGRSDTRAALRAFFEVDRASIVIAALQALADDGLVARDVVRQAIARYGKAaT 881

                  ....*...
gi 1331381824 885 DREPSWTS 892
Cdd:TIGR03186 882 SRAPPWER 889
TPP_E1_EcPDC_like cd02017
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ...
82-469 0e+00

Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; composed of proteins similar to the E1 component of the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDC). PDC catalyzes the oxidative decarboxylation of pyruvate and the subsequent acetylation of coenzyme A to acetyl-CoA. The E1 component of PDC catalyzes the first step of the multistep process, using TPP and a divalent cation as cofactors. E. coli PDC is a homodimeric enzyme.


Pssm-ID: 238975 [Multi-domain]  Cd Length: 386  Bit Score: 626.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824  82 EERLASVVRWNALAMVVRANQAYGELGGHIASYASAADLFEVGFNHFFRARSDSFGGDLVFYQPHSAPGIYARAFLEGRL 161
Cdd:cd02017     4 ERRIRSLIRWNAMAMVHRANKKDLGIGGHIATFASAATLYEVGFNHFFRARGEGGGGDLVYFQGHASPGIYARAFLEGRL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 162 SEADLAHYRQEIGAGkagarGLSSYPHPWLMPDFWQFPTGSMGIGPISSIFQARFMRYLQHRGLQDSTDRHVWGVFGDGE 241
Cdd:cd02017    84 TEEQLDNFRQEVGGG-----GLSSYPHPWLMPDFWEFPTVSMGLGPIQAIYQARFNRYLEDRGLKDTSDQKVWAFLGDGE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 242 MDEPESMSALTLAAREGLDNLTWVVNCNLQRLDGPVRGNGRIIDELEALFAGAGWNVIKLVWGSDWDALLAKDTDGELAR 321
Cdd:cd02017   159 MDEPESLGAIGLAAREKLDNLIFVVNCNLQRLDGPVRGNGKIIQELEGIFRGAGWNVIKVIWGSKWDELLAKDGGGALRQ 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 322 TLSQTVDGQFQTFAAKDGAYNREHFFGQSEALSKLVEGLSDEQIDRLKRGGHDMVKIHAAYHAARRVAGKPTVILAQTKK 401
Cdd:cd02017   239 RMEETVDGDYQTLKAKDGAYVREHFFGKYPELKALVTDLSDEDLWALNRGGHDPRKVYAAYKKAVEHKGKPTVILAKTIK 318
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331381824 402 GFGMGEAGQGKMTTHQQKKLDREALIAFRNRFQLPLSDEQAESLSFYKPAEGSLEMRYLHQRRATLGG 469
Cdd:cd02017   319 GYGLGAAGEGRNHAHQVKKMTEDELKALRDRFGIPVSDEQLEEGPYYKPPEGSEEIKYLHERRHALGG 386
PDH_E1_M pfam17831
Pyruvate dehydrogenase E1 component middle domain; This entry represents one of the thiamin ...
492-707 2.70e-100

Pyruvate dehydrogenase E1 component middle domain; This entry represents one of the thiamin diphosphate-binding domains found in pyruvate dehydrogenase E1 component.


Pssm-ID: 465525 [Multi-domain]  Cd Length: 229  Bit Score: 312.05  E-value: 2.70e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 492 FATQ---AEGKEMSTTMAFVRMLTNLLKDKALGPRIVPIVADEARTFGMANLFKQIGIYSSVGQRYEPEDIGSILSYREA 568
Cdd:pfam17831  11 FASQtggSKGREISTTMAFVRILNGLVKDKKIGKQVVPIIPDEARTFGMEGMFRQLGIYTSEGQKYEPVDKGQIMFYRED 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 569 TDGQILEEGISEASAISSWVAAATSYSVHGLRMLPFYIYYSMFGFQRVGDLIWAAADQRARGFLLGATAGRTTLGGEGLQ 648
Cdd:pfam17831  91 KQGQILEEGISEAGAMSAWIAAATSYSNHNTTLLPFYVYYSMFGFQRIGDLAWAAGDMQARGFLVGGTAGRTTLNGEGLQ 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1331381824 649 HQDGSSHLMAATVPNCRAYDPAFAGEFAVILDHGMRQMLEHDVDEFYYVTLMNENYPQP 707
Cdd:pfam17831 171 HQDGHSHIQASTIPNCRSYDPTYAHEVAVIVQDGLKRMFADKENCFYYLTVMNENYEHP 229
Transket_pyr smart00861
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
563-685 1.05e-05

Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.


Pssm-ID: 214865 [Multi-domain]  Cd Length: 136  Bit Score: 45.94  E-value: 1.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824  563 LSYREATdGQILEE-----GISEASAisswVAAATSYSVHGLRmlPFYIYYSMFgFQRVGD-LIWAAADQRArgFLLGAT 636
Cdd:smart00861   3 IATRKAF-GEALAElaidtGIAEQAM----VGFAAGLALHGLR--PVVEIFFTF-FDRAKDqIRSAGASGNV--PVVFRH 72
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1331381824  637 AGRTTLGGEGLQHQDGSSHLMAATVPNCRAYDPAFAGEFAVILDHGMRQ 685
Cdd:smart00861  73 DGGGGVGEDGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRD 121
 
Name Accession Description Interval E-value
PRK13012 PRK13012
2-oxoacid dehydrogenase subunit E1; Provisional
14-891 0e+00

2-oxoacid dehydrogenase subunit E1; Provisional


Pssm-ID: 237267 [Multi-domain]  Cd Length: 896  Bit Score: 1698.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824  14 DQEELAEWRDALASLVANAGAARAREILDMLADAGGAPHIAWKPRHGTPYINSIAVEQQPPFPGDLATEERLASVVRWNA 93
Cdd:PRK13012   21 DPQETAEWLEALDAVVAHAGPERARYLLDRLLERAAARGIALPGLLTTPYVNTIPVDQQPPYPGDLALEERLAAIIRWNA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824  94 LAMVVRANQAYGELGGHIASYASAADLFEVGFNHFFRARSDSFGGDLVFYQPHSAPGIYARAFLEGRLSEADLAHYRQEI 173
Cdd:PRK13012  101 LAMVVRANRAYGELGGHIASYASAADLFEVGFNHFFRGRDDAGGGDLVYFQPHSAPGIYARAFLEGRLSEEQLDHFRQEI 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 174 GAGkagarGLSSYPHPWLMPDFWQFPTGSMGIGPISSIFQARFMRYLQHRGLQDSTDRHVWGVFGDGEMDEPESMSALTL 253
Cdd:PRK13012  181 GGP-----GLSSYPHPWLMPDFWQFPTGSMGIGPINAIYQARFMRYLQHRGLKDTSGRKVWGFFGDGEMDEPESIAALSL 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 254 AAREGLDNLTWVVNCNLQRLDGPVRGNGRIIDELEALFAGAGWNVIKLVWGSDWDALLAKDTDGELARTLSQTVDGQFQT 333
Cdd:PRK13012  256 AAREGLDNLVFVINCNLQRLDGPVRGNGRIIQELEALFRGAGWNVIKVLWGSDWDALFARDTTGALVRRFAETVDGQFQT 335
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 334 FAAKDGAYNREHFFGQSEALSKLVEGLSDEQIDRLKRGGHDMVKIHAAYHAARRVAGKPTVILAQTKKGFGMGEAGQGKM 413
Cdd:PRK13012  336 FKANDGAYNREHFFGQDPELAALVAHLSDEDIDRLKRGGHDPRKVYAAYAAAVRHKGQPTVILAKTKKGYGMGEAGEGRM 415
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 414 TTHQQKKLDREALIAFRNRFQLPLSDEQAESLSFYKPAEGSLEMRYLHQRRATLGGYVPSRGQQAPSVSVPPVSGYGAFA 493
Cdd:PRK13012  416 TTHQQKKLDVEALKAFRDRFRLPLSDEQLEQLPFYKPAEDSPEMRYLHARRAALGGYLPRRRTAAPPLPVPPLSAFAQFA 495
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 494 TQAEGKEMSTTMAFVRMLTNLLKDKALGPRIVPIVADEARTFGMANLFKQIGIYSSVGQRYEPEDIGSILSYREATDGQI 573
Cdd:PRK13012  496 LGAGGKEMSTTMAFVRMLGNLLKDKALGPRIVPIVADEARTFGMANLFRQVGIYSPLGQLYEPEDAGSLLYYREAKDGQI 575
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 574 LEEGISEASAISSWVAAATSYSVHGLRMLPFYIYYSMFGFQRVGDLIWAAADQRARGFLLGATAGRTTLGGEGLQHQDGS 653
Cdd:PRK13012  576 LEEGITEAGAISSWIAAATSYSVHGLPMLPFYIYYSMFGFQRVGDLIWAAADQRARGFLLGATAGRTTLGGEGLQHQDGH 655
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 654 SHLMAATVPNCRAYDPAFAGEFAVILDHGMRQMLEHDVDEFYYVTLMNENYPQPSLPEGVEAAIIKGMYRLSGQPGG-KV 732
Cdd:PRK13012  656 SHLLASTIPNCRAYDPAFAYELAVIVDDGMRRMLEEQEDVFYYLTVMNENYAQPALPEGAEEGILKGMYRLAAAAEApRV 735
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 733 RLLGSGTLVREAQAAAQLLAEDWQVDAEVFSVTSFSELARDARDVERWNRLHPQQPARRSHLAECLPKG-APVVAVSDYV 811
Cdd:PRK13012  736 QLLGSGAILREVLAAARLLADDWGVDADVWSVTSFTELRRDGLAAERANLLGPAEEARVPYVTQCLAGTrGPVVAATDYV 815
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 812 RAVPQMLGSYVDSAYTVLGTDGFGRSDTRAALRDFFEVDRHHIVLAALTALVEQGSLDRQVCQQAIKRYGVQTDREPSWT 891
Cdd:PRK13012  816 RAVPEQIRAFVPARYVTLGTDGFGRSDTRAALRRFFEVDRHSIVLAALKALADDGEVERTVVAEAIERYGIDDDKTPPWE 895
AceE COG2609
Pyruvate dehydrogenase complex, dehydrogenase (E1) component [Energy production and conversion] ...
1-892 0e+00

Pyruvate dehydrogenase complex, dehydrogenase (E1) component [Energy production and conversion]; Pyruvate dehydrogenase complex, dehydrogenase (E1) component is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 442021 [Multi-domain]  Cd Length: 891  Bit Score: 1647.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824   1 MNGFASAVSQTAMDQEELAEWRDALASLVANAGAARAREILDMLADAGGAPHIAWKPRHGTPYINSIAVEQQPPFPGDLA 80
Cdd:COG2609     1 MSMDGLPSQLPDIDPQETQEWLESLDAVIEEEGPERARYLLERLLERARRSGVGLPFSATTPYINTIPVEQEPPYPGDEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824  81 TEERLASVVRWNALAMVVRANQAYGELGGHIASYASAADLFEVGFNHFFRARSDSFGGDLVFYQPHSAPGIYARAFLEGR 160
Cdd:COG2609    81 LERRIRSIIRWNAMAMVVRANRKGGGLGGHISSFASAATLYEVGFNHFFRGPDHPGGGDLVYFQGHASPGIYARAFLEGR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 161 LSEADLAHYRQEIGAGkagarGLSSYPHPWLMPDFWQFPTGSMGIGPISSIFQARFMRYLQHRGLQDSTDRHVWGVFGDG 240
Cdd:COG2609   161 LTEEQLDNFRQEVDGK-----GLSSYPHPWLMPDFWQFPTVSMGLGPINAIYQARFMKYLHNRGLKDTSDRKVWAFLGDG 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 241 EMDEPESMSALTLAAREGLDNLTWVVNCNLQRLDGPVRGNGRIIDELEALFAGAGWNVIKLVWGSDWDALLAKDTDGELA 320
Cdd:COG2609   236 EMDEPESLGAISLAAREKLDNLIFVINCNLQRLDGPVRGNGKIIQELEGVFRGAGWNVIKVIWGSEWDPLLAKDTDGALV 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 321 RTLSQTVDGQFQTFAAKDGAYNREHFFGQSEALSKLVEGLSDEQIDRLKRGGHDMVKIHAAYHAARRVAGKPTVILAQTK 400
Cdd:COG2609   316 KRMNETVDGDYQTYKAKDGAYVREHFFGKYPELKALVADMSDEDIWRLNRGGHDPRKVYAAYKAAVEHKGQPTVILAKTI 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 401 KGFGMGEAGQGKMTTHQQKKLDREALIAFRNRFQLPLSDEQAESLSFYKPAEGSLEMRYLHQRRATLGGYVPSRGQQAPS 480
Cdd:COG2609   396 KGYGMGEAGEGRNITHQQKKLDLDDLKAFRDRFNIPISDEQLEELPYYKPAEDSPEMKYLHERRKALGGYLPQRRTKAEP 475
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 481 VSVPPVSGYGAFATQAEGKEMSTTMAFVRMLTNLLKDKALGPRIVPIVADEARTFGMANLFKQIGIYSSVGQRYEPEDIG 560
Cdd:COG2609   476 LEVPELSAFAALLKGSGKREISTTMAFVRILNDLLKDKEIGKRIVPIVPDEARTFGMEGLFRQIGIYSPVGQLYTPVDAD 555
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 561 SILSYREATDGQILEEGISEASAISSWVAAATSYSVHGLRMLPFYIYYSMFGFQRVGDLIWAAADQRARGFLLGATAGRT 640
Cdd:COG2609   556 QLLYYKESKDGQILQEGINEAGAMSSWIAAGTSYSTHGVPMIPFYIYYSMFGFQRVGDLAWAAGDQRARGFLIGATAGRT 635
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 641 TLGGEGLQHQDGSSHLMAATVPNCRAYDPAFAGEFAVILDHGMRQMLEHDVDEFYYVTLMNENYPQPSLPEGVEAAIIKG 720
Cdd:COG2609   636 TLNGEGLQHQDGHSHLLASTIPNCVSYDPAFAYELAVIVQDGLRRMYGEQENVFYYITVMNENYAQPAMPEGVEEGILKG 715
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 721 MYRLS---GQPGGKVRLLGSGTLVREAQAAAQLLAEDWQVDAEVFSVTSFSELARDARDVERWNRLHPQQPARRSHLAEC 797
Cdd:COG2609   716 MYLLKegeGKGKPRVQLLGSGTILREVLAAAELLAEDWGVAADVWSVTSFNELRRDGLDVERWNLLHPEEEPRVPYVTQC 795
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 798 LPKG-APVVAVSDYVRAVPQMLGSYVDSAYTVLGTDGFGRSDTRAALRDFFEVDRHHIVLAALTALVEQGSLDRQVCQQA 876
Cdd:COG2609   796 LAGAeGPVVAATDYMRAVPDQIRPWVPGRYTVLGTDGFGRSDTREALRRFFEVDRYSIVVAALKALADEGKIDASVVAEA 875
                         890
                  ....*....|....*.
gi 1331381824 877 IKRYGVQTDREPSWTS 892
Cdd:COG2609   876 IKKYGIDPDKPNPLTA 891
aceE PRK09405
pyruvate dehydrogenase subunit E1; Reviewed
14-892 0e+00

pyruvate dehydrogenase subunit E1; Reviewed


Pssm-ID: 236500 [Multi-domain]  Cd Length: 891  Bit Score: 1556.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824  14 DQEELAEWRDALASLVANAGAARAREILDMLADAGGAPHIAWKPRHGTPYINSIAVEQQPPFPGDLATEERLASVVRWNA 93
Cdd:PRK09405   13 DPIETQEWLEALDSVIREEGPERAHYLLEQLLERAREKGVSLPASATTPYINTIPVEEEPEYPGDLELERRIRSYIRWNA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824  94 LAMVVRANQAYGELGGHIASYASAADLFEVGFNHFFRARSDSFGGDLVFYQPHSAPGIYARAFLEGRLSEADLAHYRQEI 173
Cdd:PRK09405   93 AAMVLRANKKDLGLGGHISSFASSATLYEVGFNHFFRAPNEPHGGDLVFFQGHASPGIYARAFLEGRLTEEQLDNFRQEV 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 174 GaGKagarGLSSYPHPWLMPDFWQFPTGSMGIGPISSIFQARFMRYLQHRGLQDSTDRHVWGVFGDGEMDEPESMSALTL 253
Cdd:PRK09405  173 D-GK----GLSSYPHPWLMPDFWQFPTVSMGLGPIMAIYQARFLKYLENRGLKDTSDQKVWAFLGDGEMDEPESLGAISL 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 254 AAREGLDNLTWVVNCNLQRLDGPVRGNGRIIDELEALFAGAGWNVIKLVWGSDWDALLAKDTDGELARTLSQTVDGQFQT 333
Cdd:PRK09405  248 AAREKLDNLIFVINCNLQRLDGPVRGNGKIIQELEGIFRGAGWNVIKVIWGSRWDPLLAKDTSGKLVQLMNETVDGDYQT 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 334 FAAKDGAYNREHFFGQSEALSKLVEGLSDEQIDRLKRGGHDMVKIHAAYHAARRVAGKPTVILAQTKKGFGMGEAGQGKM 413
Cdd:PRK09405  328 YKAKDGAYVREHFFGKYPETKALVADMSDDDIWALNRGGHDPRKVYAAYKAAVEHKGQPTVILAKTIKGYGMGEAGEGKN 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 414 TTHQQKKLDREALIAFRNRFQLPLSDEQAESLSFYKPAEGSLEMRYLHQRRATLGGYVPSRGQQAPSVSVPPVSGYGAFA 493
Cdd:PRK09405  408 IAHQVKKLDLDDLKHFRDRFNIPISDEQLEKLPYYKPGEDSPEIKYLHERRKALGGYLPARRPKFEPLEVPALSAFEALL 487
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 494 TQAEGKEMSTTMAFVRMLTNLLKDKALGPRIVPIVADEARTFGMANLFKQIGIYSSVGQRYEPEDIGSILSYREATDGQI 573
Cdd:PRK09405  488 KGSGEREISTTMAFVRILNILLKDKEIGKRIVPIIPDEARTFGMEGLFRQIGIYNPHGQLYTPVDRDQLMYYKESKDGQI 567
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 574 LEEGISEASAISSWVAAATSYSVHGLRMLPFYIYYSMFGFQRVGDLIWAAADQRARGFLLGATAGRTTLGGEGLQHQDGS 653
Cdd:PRK09405  568 LQEGINEAGAMASWIAAATSYSTHGEPMIPFYIYYSMFGFQRIGDLAWAAGDQRARGFLLGGTAGRTTLNGEGLQHEDGH 647
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 654 SHLMAATVPNCRAYDPAFAGEFAVILDHGMRQMLEHDVDEFYYVTLMNENYPQPSLPEGVEAAIIKGMYRLS----GQPG 729
Cdd:PRK09405  648 SHILASTIPNCVSYDPAFAYEVAVIVQDGLRRMYGEQENVFYYITVMNENYHQPAMPEGAEEGILKGMYKLEtaegKKGK 727
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 730 GKVRLLGSGTLVREAQAAAQLLAEDWQVDAEVFSVTSFSELARDARDVERWNRLHPQQPARRSHLAECLpKGA--PVVAV 807
Cdd:PRK09405  728 PKVQLLGSGTILREVLEAAEILAEDYGVAADVWSVTSFNELARDGQDVERWNMLHPTEEPRVPYVTQVL-KGAegPVVAA 806
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 808 SDYVRAVPQMLGSYVDSAYTVLGTDGFGRSDTRAALRDFFEVDRHHIVLAALTALVEQGSLDRQVCQQAIKRYGVQTDRE 887
Cdd:PRK09405  807 TDYMKLFAEQIRAFVPGDYVVLGTDGFGRSDTREALRRFFEVDAEYVVVAALKALADEGEIDASVVAEAIKKYGIDPDKA 886

                  ....*
gi 1331381824 888 PSWTS 892
Cdd:PRK09405  887 NPRTA 891
AKGDH_not_PDH TIGR03186
alpha-ketoglutarate dehydrogenase; Several bacterial species have a paralog to homodimeric ...
14-892 0e+00

alpha-ketoglutarate dehydrogenase; Several bacterial species have a paralog to homodimeric form of the pyruvate dehydrogenase E1 component (see model TIGR00759), often encoded next to L-methionine gamma-lyase gene (mdeA). The member from a strain of Pseudomonas putida was shown to act on alpha-ketobutyrate, which is produced by MdeA.This model serves as an exception model to TIGR00759, as other proteins hitting TIGR00759 should be identified as the pyruvate dehydrogenase E1 component.


Pssm-ID: 132230 [Multi-domain]  Cd Length: 889  Bit Score: 1393.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824  14 DQEELAEWRDALASLVANAGAARAREILDMLADAGGAPHIAWKPRHGTPYINSIAVEQQPPFPGDLATEERLASVVRWNA 93
Cdd:TIGR03186   7 DPQETAEWLDALDGVVAHAGAERAQYLLAQLAAHAARLGLAPPAAGATPYVNTIAVDQEPPYPGDLQLEERLAAILRWNA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824  94 LAMVVRANQAYGELGGHIASYASAADLFEVGFNHFFRARSDSFGGDLVFYQPHSAPGIYARAFLEGRLSEADLAHYRQEI 173
Cdd:TIGR03186  87 LAMVVRANRAYGELGGHIASYASAADLFEVGFNHFFRAAGDASGGDLVYFQPHSAPGVYARAFLEGFLSDAQLAHYRQEI 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 174 GAgkagaRGLSSYPHPWLMPDFWQFPTGSMGIGPISSIFQARFMRYLQHRGLQDSTDRHVWGVFGDGEMDEPESMSALTL 253
Cdd:TIGR03186 167 AG-----PGLCSYPHPWLMPDFWQFPTGSMGIGPINAIYQARFMRYLQNRGLARTEGRKVWGFFGDGEMDEPESIGALSL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 254 AAREGLDNLTWVVNCNLQRLDGPVRGNGRIIDELEALFAGAGWNVIKLVWGSDWDALLAKDTDGELARTLSQTVDGQFQT 333
Cdd:TIGR03186 242 AARERLDNLVFVINCNLQRLDGPVRGNGRIIDELESQFAGAGWNVIKVLWGSDWDALFARDATGALARAFAHTVDGQFQT 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 334 FAAKDGAYNREHFFGQSEALSKLVEGLSDEQIDRLKRGGHDMVKIHAAYHAARRVAGKPTVILAQTKKGFGMGEAGQGKM 413
Cdd:TIGR03186 322 FSANDGAYNRARFFGQDPALAALVAHLSDEDIDRLRRGGHDARKLYAAYDRAVRHEGRPTVILAKTMKGFGMGAIGQGRM 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 414 TTHQQKKLDREALIAFRNRFQLPLSDEQAESLSFYKPAEGSLEMRYLHQRRATLGGYVPSRGQQAP-SVSVPPVSGYGAF 492
Cdd:TIGR03186 402 TTHQQKKLDVEALLAFRDRFRLPLSDADVEQLKFYKPDEDSAEMRYLHARRAALGGYLPRRRTAAThALAVPALPSWGRF 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 493 ATQAEGKEMSTTMAFVRMLTNLLKDKALGPRIVPIVADEARTFGMANLFKQIGIYSSVGQRYEPEDIGSILSYREATDGQ 572
Cdd:TIGR03186 482 ALDAEGKEMSTTMAIVRMLGALLKDAELGPRIVPIVADEARTFGMANLFRQVGIYSPLGQRYEPEDLGSMLYYREDTDGQ 561
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 573 ILEEGISEASAISSWVAAATSYSVHGLRMLPFYIYYSMFGFQRVGDLIWAAADQRARGFLLGATAGRTTLGGEGLQHQDG 652
Cdd:TIGR03186 562 ILEEGISEAGAISSWIAAATSYSVHDLPMLPFYIYYSMFGFQRIGDLIWAAADQRARGFLIGATSGKTTLGGEGLQHQDG 641
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 653 SSHLMAATVPNCRAYDPAFAGEFAVILDHGMRQMLEHDVDEFYYVTLMNENYPQPSLPEG----VEAAIIKGMYRL--SG 726
Cdd:TIGR03186 642 TSHLAASTVPNCRAWDPAFAYEVAVIVDEGMREMLERQRDEFYYLTVTNENYAQPSLPEDrldaVRRGILKGMYPLdpAA 721
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 727 QPGGKVRLLGSGTLVREAQAAAQLLAEDWQVDAEVFSVTSFSELARDARDVERWNRLHPQQPARRSHLAECL-PKGAPVV 805
Cdd:TIGR03186 722 LAAARVQLLGSGAILGEVQAAARLLRDDWGIDAAVWSVTSFTELARDGRAAERAQRLGDAERPPSPHVAQALgATQGPVI 801
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 806 AVSDYVRAVPQMLGSYVDSAYTVLGTDGFGRSDTRAALRDFFEVDRHHIVLAALTALVEQGSLDRQVCQQAIKRYGVQ-T 884
Cdd:TIGR03186 802 AATDYVRAVPELIRAYVPRRYVTLGTDGFGRSDTRAALRAFFEVDRASIVIAALQALADDGLVARDVVRQAIARYGKAaT 881

                  ....*...
gi 1331381824 885 DREPSWTS 892
Cdd:TIGR03186 882 SRAPPWER 889
aceE TIGR00759
pyruvate dehydrogenase E1 component, homodimeric type; Most members of this family are ...
14-890 0e+00

pyruvate dehydrogenase E1 component, homodimeric type; Most members of this family are pyruvate dehydrogenase complex, E1 component. Note: this family was classified as subfamily rather than equivalog because it includes a counterexample from Pseudomonas putida, MdeB, that is active as an E1 component of an alpha-ketoglutarate dehydrogenase complex rather than a pyruvate dehydrogase complex. The second pyruvate dehydrogenase complex E1 protein from Alcaligenes eutrophus, PdhE, complements an aceE mutant of E. coli but is not part of a pyruvate dehydrogenase complex operon, is more similar to the Pseudomonas putida MdeB than to E. coli AceE, and may have also have a different primary specificity.


Pssm-ID: 273255 [Multi-domain]  Cd Length: 885  Bit Score: 1339.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824  14 DQEELAEWRDALASLVANAGAARAREILDMLADAGGAPHIAWKPRHGTPYINSIAVEQQPPFPGDLATEERLASVVRWNA 93
Cdd:TIGR00759   7 DPIETQEWLESLDSVLAEEGPARARYLLEQLLEYAREHGVPIPAGTTTDYINTIPVEEQPAYPGDLELERRIRSIIRWNA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824  94 LAMVVRANQAYGELGGHIASYASAADLFEVGFNHFFRARSDSFGGDLVFYQPHSAPGIYARAFLEGRLSEADLAHYRQEI 173
Cdd:TIGR00759  87 IAMVLRANKKDLGLGGHISTYASAATLYEVGFNHFFRGHSEGGGGDLVFFQGHAAPGIYARAFLEGRLTEEQLDNFRQEV 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 174 GAGkagarGLSSYPHPWLMPDFWQFPTGSMGIGPISSIFQARFMRYLQHRGLQDSTDRHVWGVFGDGEMDEPESMSALTL 253
Cdd:TIGR00759 167 QGD-----GLSSYPHPWLMPDFWQFPTVSMGLGPINAIYQARFMKYLENRGLKDTGDQKVWAFLGDGEMDEPESKGAITF 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 254 AAREGLDNLTWVVNCNLQRLDGPVRGNGRIIDELEALFAGAGWNVIKLVWGSDWDALLAKDTDGELARTLSQTVDGQFQT 333
Cdd:TIGR00759 242 AAREKLDNLTFVINCNLQRLDGPVRGNGKIIQELESLFRGAGWNVIKVLWGSEWDALLARDTSGVLVKLMNETVDGDYQT 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 334 FAAKDGAYNREHFFGQSEALSKLVEGLSDEQIDRLKRGGHDMVKIHAAYHAARRVAGKPTVILAQTKKGFGMGEAGQGKM 413
Cdd:TIGR00759 322 YKAKDGAYVREHFFNRTPELKALVADMSDADIWALNRGGHDPRKVYAAYAAAQEHKGQPTVILAKTIKGYGMGDAAESRN 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 414 TTHQQKKLDREALIAFRNRFQLPLSDEQAESLSFYKPAEGSLEMRYLHQRRATLGGYVPSRGQQAPSVSVPPVSGYGAFA 493
Cdd:TIGR00759 402 TAHQVKKLEVDALKNFRDRFELPLSDAQVEELPYYHPGEGSPEVRYLLARRQALGGYLPARRTFAEHLTVPALEFFGALL 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 494 TQAEGKEMSTTMAFVRMLTNLLKDKALGPRIVPIVADEARTFGMANLFKQIGIYSSVGQRYEPEDIGSILSYREATDGQI 573
Cdd:TIGR00759 482 KGSGEREVSTTMAFVRILNKLLKDKEIGKRIVPIVPDEARTFGMEGLFRQIGIYSPHGQTYTPVDADSLLAYKESKDGQI 561
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 574 LEEGISEASAISSWVAAATSYSVHGLRMLPFYIYYSMFGFQRVGDLIWAAADQRARGFLLGATAGRTTLGGEGLQHQDGS 653
Cdd:TIGR00759 562 LQEGINEAGAMASWIAAATSYATHGEPMIPFYIYYSMFGFQRIGDLCWAAADQRARGFLLGATAGRTTLNGEGLQHEDGH 641
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 654 SHLMAATVPNCRAYDPAFAGEFAVILDHGMRQMLEHDVDEFYYVTLMNENYPQPSLPEGVEAAIIKGMYRLSGQPG---- 729
Cdd:TIGR00759 642 SLLQAATIPNCIAYDPAFAYEVAVIMEDGLRRMYGEQEDVFYYVTVMNENYVQPPMPEGAEEGILKGLYRFETSTEekak 721
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 730 GKVRLLGSGTLVREAQAAAQLLAEDWQVDAEVFSVTSFSELARDARDVERWNRLHPQQPARRSHLAECLPKG-APVVAVS 808
Cdd:TIGR00759 722 GHVQLLGSGAIMRAVIEAAQLLAADWGVASDVWSVTSFTELARDGHDVERWNLLHPTETPRVSYVAQVLNEAdAPVIAST 801
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 809 DYVRAVPQMLGSYVDSAYTVLGTDGFGRSDTRAALRDFFEVDRHHIVLAALTALVEQGSLDRQVCQQAIKRYGVQTDREP 888
Cdd:TIGR00759 802 DYVRAFAEQIRPYVPRKYVTLGTDGFGRSDTRENLRHFFEVDAKSVVLAALYALADDGEIDGDVVADAIAKYGIDPDKAN 881

                  ..
gi 1331381824 889 SW 890
Cdd:TIGR00759 882 PV 883
TPP_E1_EcPDC_like cd02017
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ...
82-469 0e+00

Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; composed of proteins similar to the E1 component of the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDC). PDC catalyzes the oxidative decarboxylation of pyruvate and the subsequent acetylation of coenzyme A to acetyl-CoA. The E1 component of PDC catalyzes the first step of the multistep process, using TPP and a divalent cation as cofactors. E. coli PDC is a homodimeric enzyme.


Pssm-ID: 238975 [Multi-domain]  Cd Length: 386  Bit Score: 626.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824  82 EERLASVVRWNALAMVVRANQAYGELGGHIASYASAADLFEVGFNHFFRARSDSFGGDLVFYQPHSAPGIYARAFLEGRL 161
Cdd:cd02017     4 ERRIRSLIRWNAMAMVHRANKKDLGIGGHIATFASAATLYEVGFNHFFRARGEGGGGDLVYFQGHASPGIYARAFLEGRL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 162 SEADLAHYRQEIGAGkagarGLSSYPHPWLMPDFWQFPTGSMGIGPISSIFQARFMRYLQHRGLQDSTDRHVWGVFGDGE 241
Cdd:cd02017    84 TEEQLDNFRQEVGGG-----GLSSYPHPWLMPDFWEFPTVSMGLGPIQAIYQARFNRYLEDRGLKDTSDQKVWAFLGDGE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 242 MDEPESMSALTLAAREGLDNLTWVVNCNLQRLDGPVRGNGRIIDELEALFAGAGWNVIKLVWGSDWDALLAKDTDGELAR 321
Cdd:cd02017   159 MDEPESLGAIGLAAREKLDNLIFVVNCNLQRLDGPVRGNGKIIQELEGIFRGAGWNVIKVIWGSKWDELLAKDGGGALRQ 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 322 TLSQTVDGQFQTFAAKDGAYNREHFFGQSEALSKLVEGLSDEQIDRLKRGGHDMVKIHAAYHAARRVAGKPTVILAQTKK 401
Cdd:cd02017   239 RMEETVDGDYQTLKAKDGAYVREHFFGKYPELKALVTDLSDEDLWALNRGGHDPRKVYAAYKKAVEHKGKPTVILAKTIK 318
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331381824 402 GFGMGEAGQGKMTTHQQKKLDREALIAFRNRFQLPLSDEQAESLSFYKPAEGSLEMRYLHQRRATLGG 469
Cdd:cd02017   319 GYGLGAAGEGRNHAHQVKKMTEDELKALRDRFGIPVSDEQLEEGPYYKPPEGSEEIKYLHERRHALGG 386
PDH_E1_M pfam17831
Pyruvate dehydrogenase E1 component middle domain; This entry represents one of the thiamin ...
492-707 2.70e-100

Pyruvate dehydrogenase E1 component middle domain; This entry represents one of the thiamin diphosphate-binding domains found in pyruvate dehydrogenase E1 component.


Pssm-ID: 465525 [Multi-domain]  Cd Length: 229  Bit Score: 312.05  E-value: 2.70e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 492 FATQ---AEGKEMSTTMAFVRMLTNLLKDKALGPRIVPIVADEARTFGMANLFKQIGIYSSVGQRYEPEDIGSILSYREA 568
Cdd:pfam17831  11 FASQtggSKGREISTTMAFVRILNGLVKDKKIGKQVVPIIPDEARTFGMEGMFRQLGIYTSEGQKYEPVDKGQIMFYRED 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 569 TDGQILEEGISEASAISSWVAAATSYSVHGLRMLPFYIYYSMFGFQRVGDLIWAAADQRARGFLLGATAGRTTLGGEGLQ 648
Cdd:pfam17831  91 KQGQILEEGISEAGAMSAWIAAATSYSNHNTTLLPFYVYYSMFGFQRIGDLAWAAGDMQARGFLVGGTAGRTTLNGEGLQ 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1331381824 649 HQDGSSHLMAATVPNCRAYDPAFAGEFAVILDHGMRQMLEHDVDEFYYVTLMNENYPQP 707
Cdd:pfam17831 171 HQDGHSHIQASTIPNCRSYDPTYAHEVAVIVQDGLKRMFADKENCFYYLTVMNENYEHP 229
TPP_TK cd02012
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ...
89-404 1.91e-22

Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.


Pssm-ID: 238970 [Multi-domain]  Cd Length: 255  Bit Score: 97.57  E-value: 1.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824  89 VRWNALAMVVRANqaygelGGHIASYASAADLFEVGFNHFFR---ARSDSFGGD-LVFYQPHSAPGIYARAFLEGRLSEA 164
Cdd:cd02012     3 IRRLSIDMVQKAG------SGHPGGSLSAADILAVLYFKVLKydpADPKWPNRDrFVLSKGHASPALYAVLALAGYLPEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 165 DLAHYRQeIGagkagarglSSYP-HP-WLMPDFWQFPTGSMGIGPISSIFQARFMRYLQhrglqdsTDRHVWGVFGDGEM 242
Cdd:cd02012    77 DLKTFRQ-LG---------SRLPgHPeYGLTPGVEVTTGSLGQGLSVAVGMALAEKLLG-------FDYRVYVLLGDGEL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 243 DEPESMSALTLAAREGLDNLTWVVNCNLQRLDGPVRG---NGRIIDELEALfagaGWNVIklvwgsdwdallakdtdgel 319
Cdd:cd02012   140 QEGSVWEAASFAGHYKLDNLIAIVDSNRIQIDGPTDDilfTEDLAKKFEAF----GWNVI-------------------- 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 320 artlsqTVDgqfqtfaakdgaynrehffgqsealsklveglsdeqidrlkrgGHDMVKIHAAYHAARRVAGKPTVILAQT 399
Cdd:cd02012   196 ------EVD-------------------------------------------GHDVEEILAALEEAKKSKGKPTLIIAKT 226

                  ....*
gi 1331381824 400 KKGFG 404
Cdd:cd02012   227 IKGKG 231
PRK05899 PRK05899
transketolase; Reviewed
78-404 2.72e-15

transketolase; Reviewed


Pssm-ID: 235639 [Multi-domain]  Cd Length: 586  Bit Score: 80.18  E-value: 2.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824  78 DLATEERLASVVRWNALAMVVRANQaygelgGHIASYASAADLFEVGFNHFFR---ARSDSFGGD-LVFYQPHSAPGIYA 153
Cdd:PRK05899    4 DMELLQLLANAIRVLSIDAVQKANS------GHPGMPMGAADIAYVLWTRFLRhdpKNPKWPNRDrFVLSAGHGSMLLYS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 154 RAFLEG-RLSEADLAHYRQeigagkAGarglSSYP-HPwlmpDFWQFP-----TGSMGIGpISS----IFQARFMRYLQH 222
Cdd:PRK05899   78 LLHLAGyDLSIDDLKNFRQ------LG----SKTPgHP----EYGHTPgvettTGPLGQG-LANavgmALAEKYLAALFN 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 223 RGLQDSTDRHVWGVFGDGEMDEPESMSALTLAAREGLDNLTWVVNCN-LQrLDGPVRGNgrIIDELEALFAGAGWNVIKl 301
Cdd:PRK05899  143 RPGLDIVDHYTYVLCGDGDLMEGISHEACSLAGHLKLGNLIVIYDDNrIS-IDGPTEGW--FTEDVKKRFEAYGWHVIE- 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 302 vwgsdwdallakdtdgelartlsqtVDgqfqtfaakdgaynrehffgqsealsklveglsdeqidrlkrgGHDMVKIHAA 381
Cdd:PRK05899  219 -------------------------VD-------------------------------------------GHDVEAIDAA 230
                         330       340
                  ....*....|....*....|...
gi 1331381824 382 YHAARRVaGKPTVILAQTKKGFG 404
Cdd:PRK05899  231 IEEAKAS-TKPTLIIAKTIIGKG 252
Transketolase_N pfam00456
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ...
81-404 1.28e-06

Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes EC:2.2.1.1. and also partially matches to 2-oxoisovalerate dehydrogenase beta subunit EC:1.2.4.4. Both these enzymes utilize thiamine pyrophosphate as a cofactor, suggesting there may be common aspects in their mechanism of catalysis.


Pssm-ID: 395366 [Multi-domain]  Cd Length: 334  Bit Score: 51.23  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824  81 TEERLASVVRWNALAMVVRANqaygelGGHIASYASAADLFEVGFNHFFR---ARSDSFGGD-LVFYQPHSAPGIYARAF 156
Cdd:pfam00456   1 IDKRAVNAIRALAMDAVEKAN------SGHPGAPMGMAPIAEVLFKRFLKhnpNDPKWINRDrFVLSNGHGSMLLYSLLH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 157 LEG-RLSEADLAHYRQeIGAGKAGarglssypHPwlmpDFWQFP-----TGSMGIGPISSIFQARFMRYLQ---HRGLQD 227
Cdd:pfam00456  75 LTGyDLSMEDLKSFRQ-LGSKTPG--------HP----EFGHTAgvevtTGPLGQGIANAVGMAIAERNLAatyNRPGFD 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 228 STDRHVWGVFGDGEMDEPESMSALTLAAREGLDNLTWVVNCNLQRLDGPVRGNgrIIDELEALFAGAGWNVIKLVwgsdw 307
Cdd:pfam00456 142 IVDHYTYVFLGDGCLMEGVSSEASSLAGHLGLGNLIVFYDDNQISIDGETKIS--FTEDTAARFEAYGWHVIEVE----- 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 308 dallakdtdgelartlsqtvdgqfqtfaakdgaynrehffgqsealsklveglsdeqidrlkrGGHDMVKIHAAYHAARR 387
Cdd:pfam00456 215 ---------------------------------------------------------------DGHDVEAIAAAIEEAKA 231
                         330
                  ....*....|....*..
gi 1331381824 388 VAGKPTVILAQTKKGFG 404
Cdd:pfam00456 232 EKDKPTLIKCRTVIGYG 248
Transket_pyr smart00861
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
563-685 1.05e-05

Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 Kd subunits. TK sequences from a variety of eukaryotic and prokaryotic sources show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Hansenula polymorpha, there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.


Pssm-ID: 214865 [Multi-domain]  Cd Length: 136  Bit Score: 45.94  E-value: 1.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824  563 LSYREATdGQILEE-----GISEASAisswVAAATSYSVHGLRmlPFYIYYSMFgFQRVGD-LIWAAADQRArgFLLGAT 636
Cdd:smart00861   3 IATRKAF-GEALAElaidtGIAEQAM----VGFAAGLALHGLR--PVVEIFFTF-FDRAKDqIRSAGASGNV--PVVFRH 72
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1331381824  637 AGRTTLGGEGLQHQDGSSHLMAATVPNCRAYDPAFAGEFAVILDHGMRQ 685
Cdd:smart00861  73 DGGGGVGEDGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRD 121
TktA COG0021
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ...
230-404 4.19e-03

Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway/BioSystem: Pentose phosphate pathway


Pssm-ID: 439792 [Multi-domain]  Cd Length: 661  Bit Score: 40.76  E-value: 4.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 230 DRHVWGVFGDGEMDEPESMSALTLAAREGLDNLTWVVNCNLQRLDGPVrgNGRIIDELEALFAGAGWNVIKLVWGsdwda 309
Cdd:COG0021   146 DHYTYVIAGDGDLMEGISHEAASLAGHLKLGKLIVLYDDNGISIDGDT--DLAFSEDVAKRFEAYGWHVIRVEDG----- 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331381824 310 llakdtdgelartlsqtvdgqfqtfaakdgaynrehffgqsealsklveglsdeqidrlkrggHDMVKIHAAYHAARRVA 389
Cdd:COG0021   219 ---------------------------------------------------------------HDLEAIDAAIEAAKAET 235
                         170
                  ....*....|....*
gi 1331381824 390 GKPTVILAQTKKGFG 404
Cdd:COG0021   236 DKPTLIICKTIIGYG 250
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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