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Conserved domains on  [gi|45551847|ref|NP_731263|]
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uncharacterized protein Dmel_CG8036, isoform C [Drosophila melanogaster]

Protein Classification

transketolase family protein( domain architecture ID 11481869)

transketolase family protein such as transketolase, which catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK05899 PRK05899
transketolase; Reviewed
8-624 0e+00

transketolase; Reviewed


:

Pssm-ID: 235639 [Multi-domain]  Cd Length: 586  Bit Score: 558.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847    8 AKTVQDLKDLAQKLRIHSINATQASKSGHPTSCASIAEIMSVLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAE 87
Cdd:PRK05899   2 MMDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLHL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   88 AGL-FPIADLNNLRKIDSDLEGHPTPR-LNFIDVGTGSLGQGVAVGAGMA----YVGKNFDKA-----DYRTYVVVGDGE 156
Cdd:PRK05899  82 AGYdLSIDDLKNFRQLGSKTPGHPEYGhTPGVETTTGPLGQGLANAVGMAlaekYLAALFNRPgldivDHYTYVLCGDGD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  157 SAEGSIWESLHFAGHYKLDNLCVIFDVNRLGQSEATSLqHKLDVYRDRLEAFGFNAVVVDGHDVEELSKAFhCAAITKNK 236
Cdd:PRK05899 162 LMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEG-WFTEDVKKRFEAYGWHVIEVDGHDVEAIDAAI-EEAKASTK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  237 PTAIIAKTFKGRDFPNIEDLDNWHGKPLGdkAAEVVKHLEGLivnknvkltpkpvpktgaapdvDINNiklssppayklg 316
Cdd:PRK05899 240 PTLIIAKTIIGKGAPNKEGTHKVHGAPLG--AEEIAAAKKEL----------------------GWDY------------ 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  317 dsiatRLAYGTALAKIGQNNLRVVALDGDTKNSTFSDK------LKNLDPQRYIECFIAEQNLVGVAVGAACRRRTVAFV 390
Cdd:PRK05899 284 -----RKASGKALNALAKALPELVGGSADLAGSNNTKIkgskdfAPEDYSGRYIHYGVREFAMAAIANGLALHGGFIPFG 358
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  391 STFATFFTRAFDQIRMGAISQTNVNFVGSHCGCSIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAA-NTK 469
Cdd:PRK05899 359 GTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALeRKD 438
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  470 GVCFIRTSRPNTCVIYD--NEEPFTIGrGKVVRqkSSDEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAE 547
Cdd:PRK05899 439 GPSALVLTRQNLPVLERtaQEEGVAKG-GYVLR--DDPDVILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQ 515
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  548 liiehgkqcggrvvvvEDHYQQGGLGEAVLSALAGE-------RNFV---VKHLYVPTVPRSGPPSVLIDMFGISARHVV 617
Cdd:PRK05899 516 ----------------DAAYKESVLPAAVTARVAVEagvadgwYKYVgldGKVLGIDTFGASAPADELFKEFGFTVENIV 579

                 ....*..
gi 45551847  618 NAVNEIL 624
Cdd:PRK05899 580 AAAKELL 586
 
Name Accession Description Interval E-value
PRK05899 PRK05899
transketolase; Reviewed
8-624 0e+00

transketolase; Reviewed


Pssm-ID: 235639 [Multi-domain]  Cd Length: 586  Bit Score: 558.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847    8 AKTVQDLKDLAQKLRIHSINATQASKSGHPTSCASIAEIMSVLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAE 87
Cdd:PRK05899   2 MMDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLHL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   88 AGL-FPIADLNNLRKIDSDLEGHPTPR-LNFIDVGTGSLGQGVAVGAGMA----YVGKNFDKA-----DYRTYVVVGDGE 156
Cdd:PRK05899  82 AGYdLSIDDLKNFRQLGSKTPGHPEYGhTPGVETTTGPLGQGLANAVGMAlaekYLAALFNRPgldivDHYTYVLCGDGD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  157 SAEGSIWESLHFAGHYKLDNLCVIFDVNRLGQSEATSLqHKLDVYRDRLEAFGFNAVVVDGHDVEELSKAFhCAAITKNK 236
Cdd:PRK05899 162 LMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEG-WFTEDVKKRFEAYGWHVIEVDGHDVEAIDAAI-EEAKASTK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  237 PTAIIAKTFKGRDFPNIEDLDNWHGKPLGdkAAEVVKHLEGLivnknvkltpkpvpktgaapdvDINNiklssppayklg 316
Cdd:PRK05899 240 PTLIIAKTIIGKGAPNKEGTHKVHGAPLG--AEEIAAAKKEL----------------------GWDY------------ 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  317 dsiatRLAYGTALAKIGQNNLRVVALDGDTKNSTFSDK------LKNLDPQRYIECFIAEQNLVGVAVGAACRRRTVAFV 390
Cdd:PRK05899 284 -----RKASGKALNALAKALPELVGGSADLAGSNNTKIkgskdfAPEDYSGRYIHYGVREFAMAAIANGLALHGGFIPFG 358
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  391 STFATFFTRAFDQIRMGAISQTNVNFVGSHCGCSIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAA-NTK 469
Cdd:PRK05899 359 GTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALeRKD 438
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  470 GVCFIRTSRPNTCVIYD--NEEPFTIGrGKVVRqkSSDEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAE 547
Cdd:PRK05899 439 GPSALVLTRQNLPVLERtaQEEGVAKG-GYVLR--DDPDVILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQ 515
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  548 liiehgkqcggrvvvvEDHYQQGGLGEAVLSALAGE-------RNFV---VKHLYVPTVPRSGPPSVLIDMFGISARHVV 617
Cdd:PRK05899 516 ----------------DAAYKESVLPAAVTARVAVEagvadgwYKYVgldGKVLGIDTFGASAPADELFKEFGFTVENIV 579

                 ....*..
gi 45551847  618 NAVNEIL 624
Cdd:PRK05899 580 AAAKELL 586
TPP_TK cd02012
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ...
19-270 1.04e-130

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: 383.78  E-value: 1.04e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  19 QKLRIHSINATQASKSGHPTSCASIAEIMSVLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAEAGLFPIADLNN 98
Cdd:cd02012   1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYLPEEDLKT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  99 LRKIDSDLEGHPTPRLN-FIDVGTGSLGQGVAVGAGMAYVGKnFDKADYRTYVVVGDGESAEGSIWESLHFAGHYKLDNL 177
Cdd:cd02012  81 FRQLGSRLPGHPEYGLTpGVEVTTGSLGQGLSVAVGMALAEK-LLGFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDNL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 178 CVIFDVNRLGQSEATSLQHKLDVYRDRLEAFGFNAVVVDGHDVEELSKAFHCAAITKNKPTAIIAKTFKGRDFPNIEDLD 257
Cdd:cd02012 160 IAIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKSKGKPTLIIAKTIKGKGVPFMENTA 239
                       250
                ....*....|...
gi 45551847 258 NWHGKPLGDKAAE 270
Cdd:cd02012 240 KWHGKPLGEEEVE 252
TktA2 COG3958
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
317-624 2.83e-107

Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];


Pssm-ID: 443158 [Multi-domain]  Cd Length: 308  Bit Score: 325.89  E-value: 2.83e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 317 DSIATRLAYGTALAKIGQNNLRVVALDGDTKNSTFSDKLKNLDPQRYIECFIAEQNLVGVAVG-AACRRRtvAFVSTFAT 395
Cdd:COG3958   2 EKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGlALAGKI--PFVSTFAP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 396 FFT-RAFDQIRM-GAISQTNVNFVGSHCGCSIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAANTKGVCF 473
Cdd:COG3958  80 FLTgRAYEQIRNdIAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 474 IRTSRPNTCVIYDNEEPFTIGRGKVVRQksSDEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHG 553
Cdd:COG3958 160 LRLGRGAVPVVYDEDYEFEIGKARVLRE--GKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAA 237
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45551847 554 KQCgGRVVVVEDHYQQGGLGEAVLSALAGERNFVVKHLYVP-TVPRSGPPSVLIDMFGISARHVVNAVNEIL 624
Cdd:COG3958 238 RKT-GAVVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPdRFGESGSPEELLEKYGLDAEGIVAAAKELL 308
tktlase_bact TIGR00232
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ...
15-536 2.89e-75

transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial transketolases. The group includes two from the yeast Saccharomyces cerevisiae but excludes dihydroxyactetone synthases (formaldehyde transketolases) from various yeasts and the even more distant mammalian transketolases. Among the family of thiamine diphosphate-dependent enzymes that includes transketolases, dihydroxyacetone synthases, pyruvate dehydrogenase E1-beta subunits, and deoxyxylulose-5-phosphate synthases, mammalian and bacterial transketolases seem not to be orthologous. [Energy metabolism, Pentose phosphate pathway]


Pssm-ID: 272974 [Multi-domain]  Cd Length: 653  Bit Score: 253.10  E-value: 2.89e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847    15 KDLAQKLRIHSINATQASKSGHPTSCASIAEIMSVLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAEAGL-FPI 93
Cdd:TIGR00232   1 KKLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKFNPTNPKWINRDRFVLSNGHGSMLLYSLLHLTGYdLSI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847    94 ADLNNLRKIDSDLEGHPT-PRLNFIDVGTGSLGQGVAVGAGMAYVGKN---------FDKADYRTYVVVGDGESAEGSIW 163
Cdd:TIGR00232  81 EDLKQFRQLHSKTPGHPEyGHTAGVEATTGPLGQGIANAVGMAIAEKTlaatfnkpgFEIVDHYTYVFVGDGCLQEGISY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   164 ESLHFAGHYKLDNLCVIFDVNRLGQSEATSLQHKLDVyRDRLEAFGFNAV-VVDGHDVEELSKAFHCAAITKNKPTAIIA 242
Cdd:TIGR00232 161 EVASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDV-AKRFEAYGWEVLeVEDGHDLAAIDAAIEEAKASTDKPTLIEV 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   243 KTFKGRDFPNIEDLDNWHGKPLGDkaaEVVKHLeglivNKNVKLTPKP--VPKT------------GAAPDVDINNI--- 305
Cdd:TIGR00232 240 KTTIGFGSPNKAGTHGVHGAPLGD---EEVALT-----KKNLGWNYNPfeIPQEvydhfkktvkerGAKAEQEWNELfaa 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   306 -KLSSP----------------------PAYKL-GDSIATRLAYGTALAKIGQNNLRVVALDGDTKNSTFS----DKLKN 357
Cdd:TIGR00232 312 yKKKYPelaaeftrrlsgelpadwdkqlPEFKVkLQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTkwkgSGDLH 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   358 LDP-QRYIECFIAEQNLVGVAVGAACRRRTVAFVSTFATFFTRAFDQIRMGAISQTNVNFVGSHCGCSIGEDGPSQMGLE 436
Cdd:TIGR00232 392 ENPlGNYIHYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIE 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   437 DIAMFRTIPGSTIFYPSDAVSTERAVELA-ANTKGVCFIRTSRPNTCVIyDNEEPFTIGRGKVVRQKSSD-EVLLIGAGI 514
Cdd:TIGR00232 472 QLASLRAIPNLSVWRPCDGNETAAAWKYAlESQDGPTALILSRQNLPQL-EESSLEKVLKGGYVLKDSKGpDLILIATGS 550
                         570       580
                  ....*....|....*....|..
gi 45551847   515 TLYECLAAADQLEKNCITVRVI 536
Cdd:TIGR00232 551 EVQLAVEAAKKLAAENIKVRVV 572
Transket_pyr pfam02779
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ...
317-483 3.73e-52

Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate dehydrogenases, and branched chain alpha-keto acid decarboxylases.


Pssm-ID: 460692 [Multi-domain]  Cd Length: 174  Bit Score: 176.97  E-value: 3.73e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   317 DSIATRLAYGTALAKIGQNNLRVVALDGDTKNSTFSDKLKNLDPQ---RYIECFIAEQNLVGVAVGAACR-RRTVAFVST 392
Cdd:pfam02779   1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHgPLLPPVEAT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   393 FATFFTRAFDQIRMG-AISQTNVNFVGSHCGCSIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAANTKG- 470
Cdd:pfam02779  81 FSDFLNRADDAIRHGaALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGr 160
                         170
                  ....*....|....
gi 45551847   471 -VCFIRTSRPNTCV 483
Cdd:pfam02779 161 kPVVLRLPRQLLRP 174
Transket_pyr smart00861
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
364-480 1.06e-32

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: 122.59  E-value: 1.06e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847    364 IECFIAEQNLVGVAVGAACRRRtVAFVSTFATFFTRAFDQIRMGAISQtNVNFVGSHCGC-SIGEDGPSQMGLEDIAMFR 442
Cdd:smart00861  18 IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFFDRAKDQIRSAGASG-NVPVVFRHDGGgGVGEDGPTHHSIEDEALLR 95
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 45551847    443 TIPGSTIFYPSDAVSTERAVELAANTKGVCFIRTSRPN 480
Cdd:smart00861  96 AIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLERKS 133
 
Name Accession Description Interval E-value
PRK05899 PRK05899
transketolase; Reviewed
8-624 0e+00

transketolase; Reviewed


Pssm-ID: 235639 [Multi-domain]  Cd Length: 586  Bit Score: 558.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847    8 AKTVQDLKDLAQKLRIHSINATQASKSGHPTSCASIAEIMSVLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAE 87
Cdd:PRK05899   2 MMDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLHL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   88 AGL-FPIADLNNLRKIDSDLEGHPTPR-LNFIDVGTGSLGQGVAVGAGMA----YVGKNFDKA-----DYRTYVVVGDGE 156
Cdd:PRK05899  82 AGYdLSIDDLKNFRQLGSKTPGHPEYGhTPGVETTTGPLGQGLANAVGMAlaekYLAALFNRPgldivDHYTYVLCGDGD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  157 SAEGSIWESLHFAGHYKLDNLCVIFDVNRLGQSEATSLqHKLDVYRDRLEAFGFNAVVVDGHDVEELSKAFhCAAITKNK 236
Cdd:PRK05899 162 LMEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEG-WFTEDVKKRFEAYGWHVIEVDGHDVEAIDAAI-EEAKASTK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  237 PTAIIAKTFKGRDFPNIEDLDNWHGKPLGdkAAEVVKHLEGLivnknvkltpkpvpktgaapdvDINNiklssppayklg 316
Cdd:PRK05899 240 PTLIIAKTIIGKGAPNKEGTHKVHGAPLG--AEEIAAAKKEL----------------------GWDY------------ 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  317 dsiatRLAYGTALAKIGQNNLRVVALDGDTKNSTFSDK------LKNLDPQRYIECFIAEQNLVGVAVGAACRRRTVAFV 390
Cdd:PRK05899 284 -----RKASGKALNALAKALPELVGGSADLAGSNNTKIkgskdfAPEDYSGRYIHYGVREFAMAAIANGLALHGGFIPFG 358
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  391 STFATFFTRAFDQIRMGAISQTNVNFVGSHCGCSIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAA-NTK 469
Cdd:PRK05899 359 GTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAIPNLTVIRPADANETAAAWKYALeRKD 438
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  470 GVCFIRTSRPNTCVIYD--NEEPFTIGrGKVVRqkSSDEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAE 547
Cdd:PRK05899 439 GPSALVLTRQNLPVLERtaQEEGVAKG-GYVLR--DDPDVILIATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQ 515
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  548 liiehgkqcggrvvvvEDHYQQGGLGEAVLSALAGE-------RNFV---VKHLYVPTVPRSGPPSVLIDMFGISARHVV 617
Cdd:PRK05899 516 ----------------DAAYKESVLPAAVTARVAVEagvadgwYKYVgldGKVLGIDTFGASAPADELFKEFGFTVENIV 579

                 ....*..
gi 45551847  618 NAVNEIL 624
Cdd:PRK05899 580 AAAKELL 586
TPP_TK cd02012
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ...
19-270 1.04e-130

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: 383.78  E-value: 1.04e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  19 QKLRIHSINATQASKSGHPTSCASIAEIMSVLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAEAGLFPIADLNN 98
Cdd:cd02012   1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYLPEEDLKT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  99 LRKIDSDLEGHPTPRLN-FIDVGTGSLGQGVAVGAGMAYVGKnFDKADYRTYVVVGDGESAEGSIWESLHFAGHYKLDNL 177
Cdd:cd02012  81 FRQLGSRLPGHPEYGLTpGVEVTTGSLGQGLSVAVGMALAEK-LLGFDYRVYVLLGDGELQEGSVWEAASFAGHYKLDNL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 178 CVIFDVNRLGQSEATSLQHKLDVYRDRLEAFGFNAVVVDGHDVEELSKAFHCAAITKNKPTAIIAKTFKGRDFPNIEDLD 257
Cdd:cd02012 160 IAIVDSNRIQIDGPTDDILFTEDLAKKFEAFGWNVIEVDGHDVEEILAALEEAKKSKGKPTLIIAKTIKGKGVPFMENTA 239
                       250
                ....*....|...
gi 45551847 258 NWHGKPLGDKAAE 270
Cdd:cd02012 240 KWHGKPLGEEEVE 252
TktA2 COG3958
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
317-624 2.83e-107

Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];


Pssm-ID: 443158 [Multi-domain]  Cd Length: 308  Bit Score: 325.89  E-value: 2.83e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 317 DSIATRLAYGTALAKIGQNNLRVVALDGDTKNSTFSDKLKNLDPQRYIECFIAEQNLVGVAVG-AACRRRtvAFVSTFAT 395
Cdd:COG3958   2 EKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAKAFPDRFFNVGIAEQNMVGVAAGlALAGKI--PFVSTFAP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 396 FFT-RAFDQIRM-GAISQTNVNFVGSHCGCSIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAANTKGVCF 473
Cdd:COG3958  80 FLTgRAYEQIRNdIAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHDGPVY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 474 IRTSRPNTCVIYDNEEPFTIGRGKVVRQksSDEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHG 553
Cdd:COG3958 160 LRLGRGAVPVVYDEDYEFEIGKARVLRE--GKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTIKPLDEEAILKAA 237
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45551847 554 KQCgGRVVVVEDHYQQGGLGEAVLSALAGERNFVVKHLYVP-TVPRSGPPSVLIDMFGISARHVVNAVNEIL 624
Cdd:COG3958 238 RKT-GAVVTAEEHSIIGGLGSAVAEVLAENYPVPLRRIGVPdRFGESGSPEELLEKYGLDAEGIVAAAKELL 308
TktA1 COG3959
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
7-277 2.49e-106

Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];


Pssm-ID: 443159 [Multi-domain]  Cd Length: 277  Bit Score: 322.03  E-value: 2.49e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   7 EAKTVQDLKDLAQKLRIHSINATQASKSGHPTSCASIAEIMSVLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWA 86
Cdd:COG3959   1 TKEDIKELEEKARQIRRDILRMIYAAGSGHPGGSLSAADILAALYFKVMNIDPKNPDWPDRDRFILSKGHAAPALYAVLA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  87 EAGLFPIADLNNLRKIDSDLEGHPTP-RLNFIDVGTGSLGQGVAVGAGMAYVGKnFDKADYRTYVVVGDGESAEGSIWES 165
Cdd:COG3959  81 EKGYFPKEELATFRKLGSRLQGHPDMkKTPGVEMSTGSLGQGLSVAVGMALAAK-LDGKDYRVYVLLGDGELQEGQVWEA 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 166 LHFAGHYKLDNLCVIFDVNRLGQSEATSLQHKLDVYRDRLEAFGFNAVVVDGHDVEELSKAFHCAAITKNKPTAIIAKTF 245
Cdd:COG3959 160 AMAAAHYKLDNLIAIVDRNGLQIDGPTEDVMSLEPLAEKWEAFGWHVIEVDGHDIEALLAALDEAKAVKGKPTVIIAHTV 239
                       250       260       270
                ....*....|....*....|....*....|...
gi 45551847 246 KGRDFPNIEDLDNWHGKPL-GDKAAEVVKHLEG 277
Cdd:COG3959 240 KGKGVSFMENRPKWHGKAPnDEELEQALAELEA 272
tktlase_bact TIGR00232
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ...
15-536 2.89e-75

transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial transketolases. The group includes two from the yeast Saccharomyces cerevisiae but excludes dihydroxyactetone synthases (formaldehyde transketolases) from various yeasts and the even more distant mammalian transketolases. Among the family of thiamine diphosphate-dependent enzymes that includes transketolases, dihydroxyacetone synthases, pyruvate dehydrogenase E1-beta subunits, and deoxyxylulose-5-phosphate synthases, mammalian and bacterial transketolases seem not to be orthologous. [Energy metabolism, Pentose phosphate pathway]


Pssm-ID: 272974 [Multi-domain]  Cd Length: 653  Bit Score: 253.10  E-value: 2.89e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847    15 KDLAQKLRIHSINATQASKSGHPTSCASIAEIMSVLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAEAGL-FPI 93
Cdd:TIGR00232   1 KKLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKFNPTNPKWINRDRFVLSNGHGSMLLYSLLHLTGYdLSI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847    94 ADLNNLRKIDSDLEGHPT-PRLNFIDVGTGSLGQGVAVGAGMAYVGKN---------FDKADYRTYVVVGDGESAEGSIW 163
Cdd:TIGR00232  81 EDLKQFRQLHSKTPGHPEyGHTAGVEATTGPLGQGIANAVGMAIAEKTlaatfnkpgFEIVDHYTYVFVGDGCLQEGISY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   164 ESLHFAGHYKLDNLCVIFDVNRLGQSEATSLQHKLDVyRDRLEAFGFNAV-VVDGHDVEELSKAFHCAAITKNKPTAIIA 242
Cdd:TIGR00232 161 EVASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDV-AKRFEAYGWEVLeVEDGHDLAAIDAAIEEAKASTDKPTLIEV 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   243 KTFKGRDFPNIEDLDNWHGKPLGDkaaEVVKHLeglivNKNVKLTPKP--VPKT------------GAAPDVDINNI--- 305
Cdd:TIGR00232 240 KTTIGFGSPNKAGTHGVHGAPLGD---EEVALT-----KKNLGWNYNPfeIPQEvydhfkktvkerGAKAEQEWNELfaa 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   306 -KLSSP----------------------PAYKL-GDSIATRLAYGTALAKIGQNNLRVVALDGDTKNSTFS----DKLKN 357
Cdd:TIGR00232 312 yKKKYPelaaeftrrlsgelpadwdkqlPEFKVkLQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTkwkgSGDLH 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   358 LDP-QRYIECFIAEQNLVGVAVGAACRRRTVAFVSTFATFFTRAFDQIRMGAISQTNVNFVGSHCGCSIGEDGPSQMGLE 436
Cdd:TIGR00232 392 ENPlGNYIHYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIE 471
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   437 DIAMFRTIPGSTIFYPSDAVSTERAVELA-ANTKGVCFIRTSRPNTCVIyDNEEPFTIGRGKVVRQKSSD-EVLLIGAGI 514
Cdd:TIGR00232 472 QLASLRAIPNLSVWRPCDGNETAAAWKYAlESQDGPTALILSRQNLPQL-EESSLEKVLKGGYVLKDSKGpDLILIATGS 550
                         570       580
                  ....*....|....*....|..
gi 45551847   515 TLYECLAAADQLEKNCITVRVI 536
Cdd:TIGR00232 551 EVQLAVEAAKKLAAENIKVRVV 572
TPP_PYR_DXS_TK_like cd07033
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ...
324-478 2.20e-64

Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), transketolase (TK), and related proteins; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), transketolase (TK), and the beta subunits of the E1 component of the human pyruvate dehydrogenase complex (E1- PDHc), subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Like many TPP-dependent enzymes DXS and TK are homodimers having a PYR and a PP domain on the same subunit. TK has two active sites per dimer which lie between PYR and PP domains of different subunits. For DXS each active site is located at the interface of a PYR and a PP domain from the same subunit. E1-PDHc is an alpha2beta2 dimer-of-heterodimers having two active sites but having the PYR and PP domains arranged on separate subunits, the PYR domains on the beta subunits, the PP domains on the alpha subunits. DXS is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis, it catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. 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. TK also plays a central role in the Calvin cycle in plants. PDHc catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. This subfamily includes the beta subunits of the E1 component of the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). ADC participates in the breakdown of acetoin. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate during the breakdown of branched chain amino acids.


Pssm-ID: 132916 [Multi-domain]  Cd Length: 156  Bit Score: 208.84  E-value: 2.20e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 324 AYGTALAKIGQNNLRVVALDGDTKNSTFSDKLKNLDPQRYIECFIAEQNLVGVAVGAACRRrTVAFVSTFATFFTRAFDQ 403
Cdd:cd07033   2 AFGEALLELAKKDPRIVALSADLGGSTGLDKFAKKFPDRFIDVGIAEQNMVGIAAGLALHG-LKPFVSTFSFFLQRAYDQ 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45551847 404 IR-MGAISQTNVNFVGSHCGCSIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAANTKGVCFIRTSR 478
Cdd:cd07033  81 IRhDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVYIRLPR 156
PTZ00089 PTZ00089
transketolase; Provisional
18-625 5.46e-61

transketolase; Provisional


Pssm-ID: 173383 [Multi-domain]  Cd Length: 661  Bit Score: 214.92  E-value: 5.46e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   18 AQKLRIHSINATQASKSGHPTSCASIAEIMSVLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAEAGL-FPIADL 96
Cdd:PTZ00089  10 ANEIRCLSADLVQKANSGHPGAPMGMAPIAHILWSEVMKYNPKDPRWINRDRFVLSNGHASALLYSMLHLTGYdLSMEDL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   97 NNLRKIDSDLEGHP----TPRlnfIDVGTGSLGQGVAVGAGMAYVGKN---------FDKADYRTYVVVGDGESAEGSIW 163
Cdd:PTZ00089  90 KNFRQLGSRTPGHPerhiTPG---VEVTTGPLGQGIANAVGLAIAEKHlaakfnrpgHPIFDNYVYVICGDGCLQEGVSQ 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  164 ESLHFAGHYKLDNLCVIFDVNRLGQSEATSLQHKLDVYRdRLEAFGFNAVVVD--GHDVEELSKAFHCAAITKNKPTAII 241
Cdd:PTZ00089 167 EALSLAGHLGLEKLIVLYDDNKITIDGNTDLSFTEDVEK-KYEAYGWHVIEVDngNTDFDGLRKAIEEAKKSKGKPKLII 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  242 AKTFKGRDfPNIEDLDNWHGKPLGDKAAEVVKHLEGL--------------IVNKNVKLTPKPVPK--------TGAAPD 299
Cdd:PTZ00089 246 VKTTIGYG-SSKAGTEKVHGAPLGDEDIAQVKELFGLdpekkfhvseevrqFFEQHVEKKKENYEAwkkrfakyTAAFPK 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  300 V----------DINNIKLSSPPAYKLGDS-IATRLAYGTALAKIGQNNLRVVALDGD------TKNSTFSDKLKNLDPQR 362
Cdd:PTZ00089 325 EaqaierrfkgELPPGWEKKLPKYTTNDKaIATRKASENVLNPLFQILPELIGGSADltpsnlTRPKEANDFTKASPEGR 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  363 YIECFIAEQNLVGVAVGAACRRRTVAFVSTFATFFTRAFDQIRMGAISQTNVNFVGSHCGCSIGEDGPSQMGLEDIAMFR 442
Cdd:PTZ00089 405 YIRFGVREHAMCAIMNGIAAHGGFIPFGATFLNFYGYALGAVRLAALSHHPVIYVATHDSIGLGEDGPTHQPVETLALLR 484
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  443 TIPGSTIFYPSDAVSTERAVELA-ANTKGVCFIRTSRPNTCVIyDNEEPFTIGRGK--VVRQKSSDEVLLIGAGITLYEC 519
Cdd:PTZ00089 485 ATPNLLVIRPADGTETSGAYALAlANAKTPTILCLSRQNTPPL-PGSSIEGVLKGAyiVVDFTNSPQLILVASGSEVSLC 563
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  520 LAAADQLEKNcITVRVID-P----FTVKPLDaeliiehgkqcggrvvvvedhYQQGGL---GEAVLSALAGERNFVVK-- 589
Cdd:PTZ00089 564 VEAAKALSKE-LNVRVVSmPcwelFDQQSEE---------------------YQQSVLpsgGVPVLSVEAYVSFGWEKys 621
                        650       660       670
                 ....*....|....*....|....*....|....*...
gi 45551847  590 HLYV--PTVPRSGPPSVLIDMFGISARHVVNAVNEILK 625
Cdd:PTZ00089 622 HVHVgiSGFGASAPANALYKHFGFTVENVVEKARALAA 659
PLN02790 PLN02790
transketolase
22-624 5.08e-59

transketolase


Pssm-ID: 215424 [Multi-domain]  Cd Length: 654  Bit Score: 209.11  E-value: 5.08e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   22 RIHSINATQASKSGHPTSCASIAEIMSVLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAEAGL--FPIADLNNL 99
Cdd:PLN02790   2 RFLAIDAVNKANSGHPGLPMGCAPMGHVLYDEVMKYNPKNPYWFNRDRFVLSAGHGCMLQYALLHLAGYdsVQMEDLKQF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  100 RKIDSDLEGHPTprlNF----IDVGTGSLGQGVAVGAGMAYVGKN----FDKADY-----RTYVVVGDGESAEGSIWESL 166
Cdd:PLN02790  82 RQWGSRTPGHPE---NFetpgIEVTTGPLGQGIANAVGLALAEKHlaarFNKPDHkivdhYTYCILGDGCQMEGISNEAA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  167 HFAGHYKLDNLCVIFDVNRLGQSEATSLQHKLDVYRdRLEAFGFNAVVVDG--HDVEELSKAFHCAAITKNKPTAIIAKT 244
Cdd:PLN02790 159 SLAGHWGLGKLIVLYDDNHISIDGDTEIAFTEDVDK-RYEALGWHTIWVKNgnTDYDEIRAAIKEAKAVTDKPTLIKVTT 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  245 FKGRDFPNIEDLDNWHGKPLGDKAAEVVK-----HLEGLIVNKNVKLTPKPVPKTGAAPDVDIN---------------N 304
Cdd:PLN02790 238 TIGYGSPNKANSYSVHGAALGEKEVDATRknlgwPYEPFHVPEDVKSHWSKHTKEGAALEAEWNakfaeykkkypeeaaE 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  305 IK-----------LSSPPAYKLGDSI-ATRLAYGT---ALAK-----IG------QNNLRVVALDGDTKNSTFSdklknl 358
Cdd:PLN02790 318 LKslisgelpsgwEKALPTFTPEDPAdATRNLSQKclnALAKvlpglIGgsadlaSSNMTLLKDFGDFQKDTPE------ 391
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  359 dpQRYIECFIAEQNLVGVAVGAACRRRT-VAFVSTFATFFTRAFDQIRMGAISQTNVNFVGSHCGCSIGEDGPSQMGLED 437
Cdd:PLN02790 392 --ERNVRFGVREHGMGAICNGIALHSSGlIPYCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLGEDGPTHQPIEH 469
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  438 IAMFRTIPGSTIFYPSDAVSTERAVELA-ANTKG---VCFIRTSRPNTCVIYDNEepftIGRGK-VVRQKSSD---EVLL 509
Cdd:PLN02790 470 LASLRAMPNILMLRPADGNETAGAYKVAvTNRKRptvLALSRQKVPNLPGTSIEG----VEKGGyVISDNSSGnkpDLIL 545
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  510 IGAGITLYECLAAADQLEKNCITVRVidpftVKPLDAELIIEHgkqcggrvvvvEDHYQQGGLGEAVLSALA-------G 582
Cdd:PLN02790 546 IGTGSELEIAAKAAKELRKEGKKVRV-----VSMVCWELFEEQ-----------SDEYKESVLPSSVTARVSveagstfG 609
                        650       660       670       680
                 ....*....|....*....|....*....|....*....|....*
gi 45551847  583 ERNFVV---KHLYVPTVPRSGPPSVLIDMFGISARHVVNAVNEIL 624
Cdd:PLN02790 610 WEKYVGskgKVIGVDRFGASAPAGILYKEFGFTVENVVAAAKSLL 654
TktA COG0021
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ...
12-536 3.55e-56

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: 201.39  E-value: 3.55e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  12 QDLKDLAQKLRIHSINATQASKSGHP---TSCASIAEimsVLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAEA 88
Cdd:COG0021   2 PLDQLAANAIRALAMDAVQKANSGHPglpMGMAPIAY---VLWTKFLKHNPANPKWPNRDRFVLSAGHGSMLLYSLLHLT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  89 GL-FPIADLNNLRKIDSDLEGHP----TPrlnFIDVGTGSLGQGVAVGAGMAYVGK----NFDKA-----DYRTYVVVGD 154
Cdd:COG0021  79 GYdLSLDDLKNFRQLGSKTPGHPeyghTP---GVETTTGPLGQGIANAVGMAIAERhlaaRFNRPghdivDHYTYVIAGD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 155 GESAEGSIWESLHFAGHYKLDNLCVIFDVNR--------LGQSEatslqhklDVyRDRLEAFGFNAV-VVDGHDVEELSK 225
Cdd:COG0021 156 GDLMEGISHEAASLAGHLKLGKLIVLYDDNGisidgdtdLAFSE--------DV-AKRFEAYGWHVIrVEDGHDLEAIDA 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 226 AFHCAAITKNKPTAIIAKTFKGRDFPNIEDLDNWHGKPLGDKAAEVVKhleglivnKNVKLTPKP--VP----------- 292
Cdd:COG0021 227 AIEAAKAETDKPTLIICKTIIGYGSPNKQGTAKAHGAPLGAEEIAATK--------EALGWPPEPfeVPdevyahwraag 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 293 KTGAA----------------PD-----VDINNIKL-----SSPPAYKLGD-SIATRLAYGTALAKIGQN--NLrVVA-- 341
Cdd:COG0021 299 ERGAAaeaewnerfaayaaayPElaaelERRLAGELpedwdAALPAFEADAkGVATRKASGKVLNALAPVlpEL-IGGsa 377
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 342 -LDGDTKnsTFSDKLKNLDPQ----RYIECFIAEQnlvgvAVGAAC-----RRRTVAFVSTFATF--FTRAfdQIRMGAI 409
Cdd:COG0021 378 dLAGSNK--TTIKGAGSFSPEdpsgRNIHFGVREH-----AMGAIMngialHGGLRPYGGTFLVFsdYMRP--AIRLAAL 448
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 410 SQTNVNFVGSHcgCSI--GEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELA-ANTKG-VCFIrTSRPNTCVIY 485
Cdd:COG0021 449 MKLPVIYVFTH--DSIglGEDGPTHQPVEQLASLRAIPNLDVIRPADANETAAAWKLAlERKDGpTALI-LSRQNLPTLD 525
                       570       580       590       600       610
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 45551847 486 DNEEPFT-IGRGKVVRQKSSD--EVLLIGAG--ITLyeCLAAADQLEKNCITVRVI 536
Cdd:COG0021 526 RTAAAAEgVAKGAYVLADAEGtpDVILIATGseVSL--AVEAAELLAAEGIKVRVV 579
PRK05444 PRK05444
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
123-624 1.40e-54

1-deoxy-D-xylulose-5-phosphate synthase; Provisional


Pssm-ID: 235470 [Multi-domain]  Cd Length: 580  Bit Score: 195.30  E-value: 1.40e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  123 SLGQGVAVGAGMAyvgknfDKADYRTYVVVGDGESAEGSIWESLHFAGHYKlDNLCVIFDVNRLGQSEAT-SLQHKLDvy 201
Cdd:PRK05444 124 SAALGMAKARDLK------GGEDRKVVAVIGDGALTGGMAFEALNNAGDLK-SDLIVILNDNEMSISPNVgALSNYLA-- 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  202 rdRL------EAFGFNAV-VVDGHDVEELSKAFHcAAITKNKPTAIIAKTFKGRDFPNIE-DLDNWHGkplgdkaaevvk 273
Cdd:PRK05444 195 --RLrsstlfEELGFNYIgPIDGHDLDALIETLK-NAKDLKGPVLLHVVTKKGKGYAPAEaDPIKYHG------------ 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  274 hleglivnknvklTPKPVPKTGAAPdvdinniKLSSPPAYKLGDsiatrlAYGTALAKIGQNNLRVVAL-----DGdTKN 348
Cdd:PRK05444 260 -------------VGKFDPETGEQP-------KSSKPGKPSYTK------VFGETLCELAEKDPKIVAItaampEG-TGL 312
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  349 STFSDKLknldPQRYIECFIAEQNLVGVAVGAACRRRTVaFVSTFATFFTRAFDQIRMG-AISQTNVNFVGSHCGCSiGE 427
Cdd:PRK05444 313 VKFSKRF----PDRYFDVGIAEQHAVTFAAGLATEGLKP-VVAIYSTFLQRAYDQVIHDvALQNLPVTFAIDRAGLV-GA 386
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  428 DGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELA-ANTKGVCFIRTSRPN-TCVIYDNEEPFTIGRGKVVRQksSD 505
Cdd:PRK05444 387 DGPTHQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTAlAYDDGPIAIRYPRGNgVGVELPELEPLPIGKGEVLRE--GE 464
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  506 EVLLIGAGITLYECLAAADQLEKncitVRVIDPFTVKPLDAELIIEHGKQcGGRVVVVEDHYQQGGLGEAVLSALAGERN 585
Cdd:PRK05444 465 DVAILAFGTMLAEALKAAERLAS----ATVVDARFVKPLDEELLLELAAK-HDLVVTVEEGAIMGGFGSAVLEFLADHGL 539
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|..
gi 45551847  586 FV-VKHLYVPT--VPRsGPPSVLIDMFGISARHVVNAVNEIL 624
Cdd:PRK05444 540 DVpVLNLGLPDefIDH-GSREELLAELGLDAEGIARRILELL 580
Transket_pyr pfam02779
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ...
317-483 3.73e-52

Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate dehydrogenases, and branched chain alpha-keto acid decarboxylases.


Pssm-ID: 460692 [Multi-domain]  Cd Length: 174  Bit Score: 176.97  E-value: 3.73e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   317 DSIATRLAYGTALAKIGQNNLRVVALDGDTKNSTFSDKLKNLDPQ---RYIECFIAEQNLVGVAVGAACR-RRTVAFVST 392
Cdd:pfam02779   1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQgagRVIDTGIAEQAMVGFANGMALHgPLLPPVEAT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   393 FATFFTRAFDQIRMG-AISQTNVNFVGSHCGCSIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAANTKG- 470
Cdd:pfam02779  81 FSDFLNRADDAIRHGaALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGr 160
                         170
                  ....*....|....
gi 45551847   471 -VCFIRTSRPNTCV 483
Cdd:pfam02779 161 kPVVLRLPRQLLRP 174
Dxs COG1154
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ...
206-625 1.93e-50

Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and metabolism]; Deoxyxylulose-5-phosphate synthase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 440768 [Multi-domain]  Cd Length: 623  Bit Score: 184.83  E-value: 1.93e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 206 EAFGFNAV-VVDGHDVEELSKAFHcAAITKNKPTAIIAKTFKGRDF-PNIEDLDNWHGkplgdkaaevvkhlegliVNKN 283
Cdd:COG1154 242 EELGFKYIgPIDGHDLDALVETLR-NAKDLKGPVLLHVVTKKGKGYaPAEKDPDKFHG------------------VGPF 302
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 284 VKLTPKPVPKTgaapdvdinniklSSPPAYklgdsiaTRlAYGTALAKIGQNNLRVVA-----LDGdTKNSTFSDKLknl 358
Cdd:COG1154 303 DPETGEPKKSK-------------SSAPSY-------TD-VFGDTLVELAEKDPRIVAitaamPEG-TGLDKFAERF--- 357
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 359 dPQRYIECFIAEQNLVGVAVGAACRRrTVAFVSTFATFFTRAFDQIRMG-AISQTNVNFVgshcgcsI------GEDGPS 431
Cdd:COG1154 358 -PDRFFDVGIAEQHAVTFAAGLATEG-LKPVVAIYSTFLQRAYDQVIHDvALQNLPVTFA-------IdraglvGADGPT 428
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 432 QMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAANTKGVCFIRTSRPNTC-VIYDNE-EPFTIGRGKVVRQksSDEVLL 509
Cdd:COG1154 429 HHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAYDGPTAIRYPRGNGPgVELPAElEPLPIGKGEVLRE--GKDVAI 506
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 510 IGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQCgGRVVVVEDHYQQGGLGEAVLSALAGERNFV-V 588
Cdd:COG1154 507 LAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELILELAREH-DLVVTVEEGVLAGGFGSAVLEFLADAGLDVpV 585
                       410       420       430
                ....*....|....*....|....*....|....*....
gi 45551847 589 KHLYVPT--VPRsGPPSVLIDMFGISARHVVNAVNEILK 625
Cdd:COG1154 586 LRLGLPDrfIEH-GSRAELLAELGLDAEGIARAILELLG 623
Transketolase_N pfam00456
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ...
15-271 4.84e-49

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: 174.11  E-value: 4.84e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847    15 KDLAQKLRIHSINATQASKSGHPTSCASIAEIMSVLFFQQLRLNLKHPRDPSSDRFILSKGHAAPILYAAWAEAGL-FPI 93
Cdd:pfam00456   3 KRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYdLSM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847    94 ADLNNLRKIDSDLEGHP----TPRlnfIDVGTGSLGQGVAVGAGMAYVGKN---------FDKADYRTYVVVGDGESAEG 160
Cdd:pfam00456  83 EDLKSFRQLGSKTPGHPefghTAG---VEVTTGPLGQGIANAVGMAIAERNlaatynrpgFDIVDHYTYVFLGDGCLMEG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   161 SIWESLHFAGHYKLDNLCVIFDVNRLGQSEATSLQHKLDVyRDRLEAFGFNAV-VVDGHDVEELSKAFHCAAITKNKPTA 239
Cdd:pfam00456 160 VSSEASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDT-AARFEAYGWHVIeVEDGHDVEAIAAAIEEAKAEKDKPTL 238
                         250       260       270
                  ....*....|....*....|....*....|..
gi 45551847   240 IIAKTFKGRDFPNIEDLDNWHGKPLGdkAAEV 271
Cdd:pfam00456 239 IKCRTVIGYGSPNKQGTHDVHGAPLG--ADEV 268
Transketolase_C pfam02780
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ...
496-616 1.61e-37

Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as a regulatory molecule binding site.


Pssm-ID: 460693 [Multi-domain]  Cd Length: 124  Bit Score: 135.42  E-value: 1.61e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   496 GKVVRQKSSDEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEhGKQCGGRVVVVEDHYQQGGLGEA 575
Cdd:pfam02780   1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILE-SVKKTGRLVTVEEAVPRGGFGSE 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 45551847   576 VLSALAGE----RNFVVKHLYVPTVPRSGPPSVLIDMFGISARHV 616
Cdd:pfam02780  80 VAAALAEEafdgLDAPVLRVGGPDFPEPGSADELEKLYGLTPEKI 124
PRK12571 PRK12571
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
124-625 6.70e-34

1-deoxy-D-xylulose-5-phosphate synthase; Provisional


Pssm-ID: 183601 [Multi-domain]  Cd Length: 641  Bit Score: 137.16  E-value: 6.70e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  124 LGQGvAVGAGMAYVG-KNFDKADYRTYVVVGDGE-------SAEGSIWESLHFAGHYKLDNLCVIFDVNRLGQSEATSLQ 195
Cdd:PRK12571 148 IGDG-SLTAGMAYEAlNNAGAADRRLIVILNDNEmsiappvGALAAYLSTLRSSDPFARLRAIAKGVEERLPGPLRDGAR 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  196 HKLDVYRDR------LEAFGFNAV-VVDGHDVEELSKAFHCAAITKNKPTAIIAKTFKGRDFPNIE-DLDNWHGkplgdk 267
Cdd:PRK12571 227 RARELVTGMigggtlFEELGFTYVgPIDGHDMEALLSVLRAARARADGPVLVHVVTEKGRGYAPAEaDEDKYHA------ 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  268 aaevvkhlegliVNKNVKLTPKPvpkTGAAPdvdinniklsSPPAYklgdsiaTRLaYGTALAKIGQNNLRVVALDGDTK 347
Cdd:PRK12571 301 ------------VGKFDVVTGLQ---KKSAP----------SAPSY-------TSV-FGEELTKEAAEDSDIVAITAAMP 347
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  348 NSTFSDKLKNLDPQRYIECFIAEQNLVGVAVGAACRRrTVAFVSTFATFFTRAFDQIRMG-AISQTNVNFVGSHCGCsIG 426
Cdd:PRK12571 348 LGTGLDKLQKRFPNRVFDVGIAEQHAVTFAAGLAAAG-LKPFCAVYSTFLQRGYDQLLHDvALQNLPVRFVLDRAGL-VG 425
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  427 EDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAV-ELAANTKGVCFIRTSRPNTC--VIYDNEEPFTIGRGKVVRQKS 503
Cdd:PRK12571 426 ADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLrTAAAHDDGPIAVRFPRGEGVgvEIPAEGTILGIGKGRVPREGP 505
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  504 sdEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELI---IEHGKqcggrVVVVEDHYQQGGLGEAVLSAL 580
Cdd:PRK12571 506 --DVAILSVGAHLHECLDAADLLEAEGISVTVADPRFVKPLDEALTdllVRHHI-----VVIVEEQGAMGGFGAHVLHHL 578
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|..
gi 45551847  581 A--GERNFVVKhLYVPTVPR-----SGPPSVLIDMfGISARHVVNAVNEILK 625
Cdd:PRK12571 579 AdtGLLDGGLK-LRTLGLPDrfidhASREEMYAEA-GLTAPDIAAAVTGALA 628
Transket_pyr smart00861
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
364-480 1.06e-32

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: 122.59  E-value: 1.06e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847    364 IECFIAEQNLVGVAVGAACRRRtVAFVSTFATFFTRAFDQIRMGAISQtNVNFVGSHCGC-SIGEDGPSQMGLEDIAMFR 442
Cdd:smart00861  18 IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFFDRAKDQIRSAGASG-NVPVVFRHDGGgGVGEDGPTHHSIEDEALLR 95
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 45551847    443 TIPGSTIFYPSDAVSTERAVELAANTKGVCFIRTSRPN 480
Cdd:smart00861  96 AIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIRLERKS 133
AcoB COG0022
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ...
368-625 1.12e-24

Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta subunit [Energy production and conversion]; Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 439793 [Multi-domain]  Cd Length: 325  Bit Score: 105.10  E-value: 1.12e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 368 IAEQNLVGVAVGAACR-RRTVAFVsTFATFFTRAFDQI-----RMGAIS--QTNVNFV-----GSHcgcsIGEdGP--SQ 432
Cdd:COG0022  58 ISEAGIVGAAIGAALAgLRPVVEI-QFADFIYPAFDQIvnqaaKLRYMSggQFKVPMVirtpyGGG----IGA-GAqhSQ 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 433 MgLEdiAMFRTIPGSTIFYPSDAvstERAVEL--AAntkgvcfIRTSRPntcVIY--------------DNEEPFTIGRG 496
Cdd:COG0022 132 S-LE--AWFAHIPGLKVVAPSTP---YDAKGLlkAA-------IRDDDP---VIFlehkrlyrlkgevpEEDYTVPLGKA 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 497 KVVRQksSDEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQCgGRVVVVEDHYQQGGLGEAV 576
Cdd:COG0022 196 RVVRE--GTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTLSPLDEETILESVKKT-GRLVVVDEAPRTGGFGAEI 272
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 45551847 577 LSALAgERNFvvKHLYVPTVPRSGP------PSVLIDMFGISARHVVNAVNEILK 625
Cdd:COG0022 273 AARIA-EEAF--DYLDAPVKRVTGPdtpipyAPALEKAYLPSADRIVAAVRELLA 324
TPP_E1_EcPDC_like cd02017
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ...
22-247 4.14e-24

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: 104.69  E-value: 4.14e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  22 RIHSI---NATQ----ASK-----SGHPTSCASIAEIMSVLFFQQLRlnlKHPRDPSSDRfILSKGHAAPILYA-AWAEa 88
Cdd:cd02017   6 RIRSLirwNAMAmvhrANKkdlgiGGHIATFASAATLYEVGFNHFFR---ARGEGGGGDL-VYFQGHASPGIYArAFLE- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  89 GLFPIADLNNLRKIDSD--LEGHPTPRL--NFIDVGTGSLGQGVAVGAGMA----YV---GKNfDKADYRTYVVVGDGES 157
Cdd:cd02017  81 GRLTEEQLDNFRQEVGGggLSSYPHPWLmpDFWEFPTVSMGLGPIQAIYQArfnrYLedrGLK-DTSDQKVWAFLGDGEM 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 158 AEGSIWESLHFAGHYKLDNLCVIFDVNR-------------LGQSEAT--------------SLQHKL------DVYRDR 204
Cdd:cd02017 160 DEPESLGAIGLAAREKLDNLIFVVNCNLqrldgpvrgngkiIQELEGIfrgagwnvikviwgSKWDELlakdggGALRQR 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 205 LEA---------------------FG----FNAVVVD------------GHDVEELSKAFHCAAITKNKPTAIIAKTFKG 247
Cdd:cd02017 240 MEEtvdgdyqtlkakdgayvrehfFGkypeLKALVTDlsdedlwalnrgGHDPRKVYAAYKKAVEHKGKPTVILAKTIKG 319
PLN02234 PLN02234
1-deoxy-D-xylulose-5-phosphate synthase
120-581 8.52e-24

1-deoxy-D-xylulose-5-phosphate synthase


Pssm-ID: 177878 [Multi-domain]  Cd Length: 641  Bit Score: 106.34  E-value: 8.52e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  120 GTGSLGQGVAVGAGMAyVGKNFDKADYRTYVVVGDGESAEGSIWESLHFAGHYKLDNLCVIFDVNRLGQSEA-------- 191
Cdd:PLN02234 175 GTGHSSTTLSAGLGMA-VGRDLKGMNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMIVILNDNKQVSLPTAnldgptqp 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  192 --------TSLQHKLDVYRDR----LEAFGFNAV-VVDGHDVEELSKAFHCAAITKN-KPTAIIAKTFKGRDFPNIEDLD 257
Cdd:PLN02234 254 vgalscalSRLQSNCGMIRETsstlFEELGFHYVgPVDGHNIDDLVSILETLKSTKTiGPVLIHVVTEKGRGYPYAERAD 333
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  258 nwhgkplgDKAAEVVKHleglivnknvkltpkpVPKTGAapdvDINNIklSSPPAYKLgdsiatrlAYGTALAKIGQNNL 337
Cdd:PLN02234 334 --------DKYHGVLKF----------------DPETGK----QFKNI--SKTQSYTS--------CFVEALIAEAEADK 375
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  338 RVVALDGDTKNSTFSDKLKNLDPQRYIECFIAEQNLVGVAVGAACRRRTvAFVSTFATFFTRAFDQIRMGA-ISQTNVNF 416
Cdd:PLN02234 376 DIVAIHAAMGGGTMLNLFESRFPTRCFDVGIAEQHAVTFAAGLACEGLK-PFCTIYSSFMQRAYDQVVHDVdLQKLPVRF 454
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  417 VGSHCGCsIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAA--NTKGVCFiRTSRPNTCVIY----DNEEP 490
Cdd:PLN02234 455 AIDRAGL-MGADGPTHCGAFDVTFMACLPNMIVMAPSDEAELFNMVATAAaiDDRPSCF-RYHRGNGIGVSlppgNKGVP 532
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  491 FTIGRGKVVRQksSDEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQcgGRVVVVEDHYQQG 570
Cdd:PLN02234 533 LQIGRGRILRD--GERVALLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKS--HEVLITVEEGSIG 608
                        490
                 ....*....|.
gi 45551847  571 GLGEAVLSALA 581
Cdd:PLN02234 609 GFGSHVVQFLA 619
PLN02582 PLN02582
1-deoxy-D-xylulose-5-phosphate synthase
10-624 2.12e-19

1-deoxy-D-xylulose-5-phosphate synthase


Pssm-ID: 178194 [Multi-domain]  Cd Length: 677  Bit Score: 92.27  E-value: 2.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   10 TVQDLKDLAQKLR---IHSINATqaskSGHPTSCASIAEimsvlffqqLRLNLKHPRDPSSDRFILSKGHAA---PILYA 83
Cdd:PLN02582  47 SVKELKQLADELRsdvIFNVSKT----GGHLGSSLGVVE---------LTVALHYVFNAPQDKILWDVGHQSyphKILTG 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   84 AWAEaglfpiadLNNLRKIDSdLEGHPTPRLNFID-VGTGSLGQGVAVGAGMAyVGKNFDKADYRTYVVVGDGESAEGSI 162
Cdd:PLN02582 114 RRDK--------MHTMRQTNG-LSGFTKRAESEYDcFGTGHSSTTISAGLGMA-VGRDLKGKKNNVVAVIGDGAMTAGQA 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  163 WESLHFAGHYKLDNLCVIFDVNRLGQSEAT-------------------------------------------SLQHKLD 199
Cdd:PLN02582 184 YEAMNNAGYLDSDMIVILNDNKQVSLPTATldgpappvgalssalsrlqssrplrelrevakgvtkqiggpmhELAAKVD 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  200 VYRDRL---------EAFGFNAV-VVDGHDVEELSKAFHCAAITKNK-PTAIIAKTFKGRDFPNIEDL-DNWHGkplgdk 267
Cdd:PLN02582 264 EYARGMisgsgstlfEELGLYYIgPVDGHNIDDLVTILREVKSTKTTgPVLIHVVTEKGRGYPYAERAaDKYHG------ 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  268 aaeVVKHleglivnknvkltpkpVPKTGaapdvdinniklssppayKLGDSIATRLAYGT----ALAKIGQNNLRVVALD 343
Cdd:PLN02582 338 ---VVKF----------------DPATG------------------KQFKVKAKTQSYTTyfaeALIAEAEVDKDVVAIH 380
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  344 GDTKNSTFSDKLKNLDPQRYIECFIAEQNLVGVAVGAACRRRTvAFVSTFATFFTRAFDQIRMGA-ISQTNVNFVGSHCG 422
Cdd:PLN02582 381 AAMGGGTGLNLFARRFPTRCFDVGIAEQHAVTFAAGLACEGLK-PFCAIYSSFLQRGYDQVVHDVdLQKLPVRFAMDRAG 459
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  423 CsIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAA--NTKGVCFiRTSRPNTCVIYDNEE----PFTIGRG 496
Cdd:PLN02582 460 L-VGADGPTHCGAFDVTYMACLPNMVVMAPSDEAELFHMVATAAaiDDRPSCF-RYPRGNGIGVQLPPNnkgiPIEVGKG 537
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  497 KVVRQksSDEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQcgGRVVVVEDHYQQGGLGEAV 576
Cdd:PLN02582 538 RILLE--GERVALLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLDRALIRSLAKS--HEVLITVEEGSIGGFGSHV 613
                        650       660       670       680       690
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 45551847  577 LSALAGE---------RNFVVKHLYVptvpRSGPPSVLIDMFGISARHVVNAVNEIL 624
Cdd:PLN02582 614 AQFMALDglldgklkwRPLVLPDRYI----DHGAPADQLAEAGLTPSHIAATVLNVL 666
PTZ00182 PTZ00182
3-methyl-2-oxobutanate dehydrogenase; Provisional
360-624 2.31e-19

3-methyl-2-oxobutanate dehydrogenase; Provisional


Pssm-ID: 185502 [Multi-domain]  Cd Length: 355  Bit Score: 90.04  E-value: 2.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  360 PQRYIECFIAEQNLVGVAVGAACR-RRTVAFVsTFATFFTRAFDQIrmgaisqtnVNFV-------GSHCGCSIGEDGPS 431
Cdd:PTZ00182  81 PDRVFDTPITEQGFAGFAIGAAMNgLRPIAEF-MFADFIFPAFDQI---------VNEAakyrymsGGQFDCPIVIRGPN 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  432 ----QMGLEDI----AMFRTIPGSTIFYPSDAVSTeRAVELAAntkgvcfIRTsrPNTCVIYDNE------------EPF 491
Cdd:PTZ00182 151 gavgHGGAYHSqsfeAYFAHVPGLKVVAPSDPEDA-KGLLKAA-------IRD--PNPVVFFEPKllyresvevvpeADY 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  492 T--IGRGKVVRQKSsdEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQCgGRVVVVEDHYQQ 569
Cdd:PTZ00182 221 TlpLGKAKVVREGK--DVTIVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDRETIVKSVKKT-GRCVIVHEAPPT 297
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45551847  570 GGLGeAVLSALAGERNFvvKHLYVPTVPRSG-----PPSVLIDMFGI-SARHVVNAVNEIL 624
Cdd:PTZ00182 298 CGIG-AEIAAQIMEDCF--LYLEAPIKRVCGadtpfPYAKNLEPAYLpDKEKVVEAAKRVL 355
PRK09212 PRK09212
pyruvate dehydrogenase subunit beta; Validated
355-586 4.80e-17

pyruvate dehydrogenase subunit beta; Validated


Pssm-ID: 169719 [Multi-domain]  Cd Length: 327  Bit Score: 82.46  E-value: 4.80e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  355 LKNLDPQRYIECFIAEQNLVGVAVGAA-CRRRTVAFVSTFaTFFTRAFDQIRMGAiSQTNVnFVGSHCGCSIGEDGP--- 430
Cdd:PRK09212  45 LEQFGPKRVIDTPITEHGFAGLAVGAAfAGLRPIVEFMTF-NFSMQAIDQIVNSA-AKTNY-MSGGQLKCPIVFRGPnga 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  431 -----SQMGLEDIAMFRTIPGSTIFYPSdavsteraveLAANTKGVCFIRTSRPNTCVIYDNE-------------EPFT 492
Cdd:PRK09212 122 aarvaAQHSQCYAAWYSHIPGLKVVAPY----------FAADCKGLLKTAIRDPNPVIFLENEilyghshevpeeeESIP 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  493 IGRGKVVRQKSSdeVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQCgGRVVVVEDHYQQGGL 572
Cdd:PRK09212 192 IGKAAILREGSD--VTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTLRPLDTETIIESVKKT-NRLVVVEEGWPFAGV 268
                        250
                 ....*....|....
gi 45551847  573 GeAVLSALAGERNF 586
Cdd:PRK09212 269 G-AEIAALIMKEAF 281
PRK12315 PRK12315
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
104-625 1.32e-16

1-deoxy-D-xylulose-5-phosphate synthase; Provisional


Pssm-ID: 237053 [Multi-domain]  Cd Length: 581  Bit Score: 83.13  E-value: 1.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  104 SDLEGHPTPRLN---FIDVGTGSlgQGVAVGAGMAyVGKNFDKADYRTYVVVGDGESAEGSIWESLHFAGHYKlDNLCVI 180
Cdd:PRK12315  94 DDVTGYTNPEESehdFFTVGHTS--TSIALATGLA-KARDLKGEKGNIIAVIGDGSLSGGLALEGLNNAAELK-SNLIII 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  181 FDVNRLGQSEATS-LQHKLDVYRDR--------LEAFGFNAVVV-DGHDVEELSKAFHCAAITkNKPTAIIAKTFKGRDF 250
Cdd:PRK12315 170 VNDNQMSIAENHGgLYKNLKELRDTngqsennlFKAMGLDYRYVeDGNDIESLIEAFKEVKDI-DHPIVLHIHTLKGKGY 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  251 -PNIEDLDNWH-GKPLgdkaaevvkHLEglivnknvklTPKP-VPKTGAapdvDINNIKLSSppaykLGDSIAtrlaygt 327
Cdd:PRK12315 249 qPAEENKEAFHwHMPF---------DLE----------TGQSkVPASGE----SYSSVTLDY-----LLKKIK------- 293
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  328 alakigqNNLRVVALDGDTKNSTFSDKLKNLDPQRYIECFIAEQNLVGVAVG-AACRRRTVAFVstFATFFTRAFDQIRM 406
Cdd:PRK12315 294 -------EGKPVVAINAAIPGVFGLKEFRKKYPDQYVDVGIAEQESVAFASGiAANGARPVIFV--NSTFLQRAYDQLSH 364
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  407 G-AISQTNVNFVGShcGCSIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAAN-TKGVCFIRTsrPNTCVI 484
Cdd:PRK12315 365 DlAINNNPAVMIVF--GGSISGNDVTHLGIFDIPMISNIPNLVYLAPTTKEELIAMLEWALTqHEHPVAIRV--PEHGVE 440
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  485 YDNEEP--FTIGRGKVVRQKSsdEVLLIGAGiTLYEC-LAAADQL-EKNCITVRVIDPFTVKPLDAELiIEHGKQCGGRV 560
Cdd:PRK12315 441 SGPTVDtdYSTLKYEVTKAGE--KVAILALG-DFYELgEKVAKKLkEELGIDATLINPKFITGLDEEL-LEKLKEDHELV 516
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45551847  561 VVVEDHYQQGGLGEAVLSALAGER----NFVVKHLYVPTVprsgPPSVLIDMFGISARHVVNAVNEILK 625
Cdd:PRK12315 517 VTLEDGILDGGFGEKIARYYGNSDmkvlNYGAKKEFNDRV----PVEELYKRNHLTPEQIVEDILSVLK 581
TPP_E1_PDC_ADC_BCADC cd02000
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ...
120-245 1.86e-15

Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).


Pssm-ID: 238958 [Multi-domain]  Cd Length: 293  Bit Score: 77.15  E-value: 1.86e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 120 GTGSLGQGVAVGAGMAYVGKnFDKADYRTYVVVGDGESAEGSIWESLHFAGHYKLDNLCVIFDvNRLGQSEATSLQHKLD 199
Cdd:cd02000 102 GNGIVGGQVPLAAGAALALK-YRGEDRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFVCEN-NGYAISTPTSRQTAGT 179
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 45551847 200 VYRDRLEAFGFNAVVVDGHDVEELSKAFHCA---AITKNKPTAIIAKTF 245
Cdd:cd02000 180 SIADRAAAYGIPGIRVDGNDVLAVYEAAKEAverARAGGGPTLIEAVTY 228
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
360-586 2.97e-14

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 75.34  E-value: 2.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  360 PQRYIECFIAEQNLVGVAVGAACR--RRTVAFVsTFaTFFTRAFDQIRMGAiSQTNVnFVGSHCGCSIGEDGPS------ 431
Cdd:PRK11892 188 ARRVIDTPITEHGFAGIGVGAAFAglKPIVEFM-TF-NFAMQAIDQIINSA-AKTLY-MSGGQMGCPIVFRGPNgaaarv 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  432 --QMGLEDIAMFRTIPGSTIFYPSDAvsteravelaANTKGV--CFIRTsrPNTCVIYDNE------------EPFT--I 493
Cdd:PRK11892 264 aaQHSQDYAAWYSHIPGLKVVAPYSA----------ADAKGLlkAAIRD--PNPVIFLENEilygqsfdvpklDDFVlpI 331
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  494 GRGKVVRQKSsdEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQCgGRVVVVEDHYQQGGLG 573
Cdd:PRK11892 332 GKARIHREGK--DVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTIRPMDTETIVESVKKT-NRLVTVEEGWPQSGVG 408
                        250
                 ....*....|...
gi 45551847  574 eAVLSALAGERNF 586
Cdd:PRK11892 409 -AEIAARVMEQAF 420
PLN02225 PLN02225
1-deoxy-D-xylulose-5-phosphate synthase
341-616 3.83e-13

1-deoxy-D-xylulose-5-phosphate synthase


Pssm-ID: 177870 [Multi-domain]  Cd Length: 701  Bit Score: 72.44  E-value: 3.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  341 ALDGDTKNSTFSDKLknldPQRYIECFIAEQNLVGVAVGAACRRRTvAFVSTFATFFTRAFDQIRMGAISQTN-VNFVGS 419
Cdd:PLN02225 407 GMEMDASLITFQERF----PDRFFNVGMAEQHAVTFSAGLSSGGLK-PFCIIPSAFLQRAYDQVVHDVDRQRKaVRFVIT 481
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  420 HCGCsIGEDGPSQMGLEDIAMFRTIPGSTIFYPSDAVSTERAVELAA--NTKGVC--FIRTSRPNTCVIYDNEEPFTIGR 495
Cdd:PLN02225 482 SAGL-VGSDGPVQCGAFDIAFMSSLPNMIAMAPADEDELVNMVATAAyvTDRPVCfrFPRGSIVNMNYLVPTGLPIEIGR 560
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  496 GKVVRQksSDEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQcgGRVVVVEDHYQQGGLGEA 575
Cdd:PLN02225 561 GRVLVE--GQDVALLGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDIKLVRDLCQN--HKFLITVEEGCVGGFGSH 636
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 45551847  576 VLS--ALAGERNFVVKhlYVPTVPRSG-----PPSVLIDMFGISARHV 616
Cdd:PLN02225 637 VAQfiALDGQLDGNIK--WRPIVLPDGyieeaSPREQLALAGLTGHHI 682
E1_dh pfam00676
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ...
108-246 9.78e-11

Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family includes pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase and 2-oxoisovalerate dehydrogenase.


Pssm-ID: 395548 [Multi-domain]  Cd Length: 300  Bit Score: 63.11  E-value: 9.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   108 GHPTPRLNFIDVGTGSLGQGVAVGAGMAYVGKnFDKADYRTYVVVGDGESAEGSIWESLHFAghyKLDNLCVIFDV--NR 185
Cdd:pfam00676  87 GYYGAKGNRFYGGNGILGAQVPLGAGIALAAK-YRGKKEVAITLYGDGAANQGDFFEGLNFA---ALWKLPVIFVCenNQ 162
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45551847   186 LGQSEATSLQHKLDVYRDRLEAFGFNAVVVDGHDVEELSKAFHCA---AITKNKPTAIIAKTFK 246
Cdd:pfam00676 163 YGISTPAERASASTTYADRARGYGIPGLHVDGMDPLAVYQASKFAaerARTGKGPFLIELVTYR 226
TPP_DXS cd02007
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ...
120-250 1.71e-10

Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; 1-Deoxy-D-xylulose-5-phosphate synthase (DXS) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. DXS catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. The formation of DXP leads to the formation of the terpene precursor IPP (isopentyl diphosphate) and to the formation of thiamine (vitamin B1) and pyridoxal (vitamin B6).


Pssm-ID: 238965 [Multi-domain]  Cd Length: 195  Bit Score: 60.64  E-value: 1.71e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 120 GTGSLGQGVAVGAGMAyVGKNFDKADYRTYVVVGDGESAEGSIWESLHFAGHYKlDNLCVIFDVNRLGQSEATSLQHKLd 199
Cdd:cd02007  73 GTGHSSTSISAALGMA-VARDLKGKKRKVIAVIGDGALTGGMAFEALNNAGYLK-SNMIVILNDNEMSISPNVGTPGNL- 149
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 45551847 200 vyrdrLEAFGFNAV-VVDGHDVEELSKAFHCAAITKnKPTAIIAKTFKGRDF 250
Cdd:cd02007 150 -----FEELGFRYIgPVDGHNIEALIKVLKEVKDLK-GPVLLHVVTKKGKGY 195
PLN02683 PLN02683
pyruvate dehydrogenase E1 component subunit beta
355-586 1.82e-09

pyruvate dehydrogenase E1 component subunit beta


Pssm-ID: 215368 [Multi-domain]  Cd Length: 356  Bit Score: 59.83  E-value: 1.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  355 LKNLDPQRYIECFIAEQNLVGVAVGAACR--RRTVAFVsTFaTFFTRAFDQIRMGAISQTNVNfvGSHCGCSIGEDGP-- 430
Cdd:PLN02683  68 LQKYGPDRVLDTPITEAGFTGIGVGAAYAglKPVVEFM-TF-NFSMQAIDHIINSAAKTNYMS--AGQISVPIVFRGPng 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  431 ------SQMGLEDIAMFRTIPGSTIFYPSDAvSTERAVELAAntkgvcfIRTsrPNTCVIYDNE----EPFT-------- 492
Cdd:PLN02683 144 aaagvgAQHSQCFAAWYSSVPGLKVLAPYSS-EDARGLLKAA-------IRD--PDPVVFLENEllygESFPvsaevlds 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  493 -----IGRGKVVRQKSsdEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQCgGRVVVVEDHY 567
Cdd:PLN02683 214 sfvlpIGKAKIEREGK--DVTIVAFSKMVGYALKAAEILAKEGISAEVINLRSIRPLDRDTINASVRKT-NRLVTVEEGW 290
                        250
                 ....*....|....*....
gi 45551847  568 QQGGLGeAVLSALAGERNF 586
Cdd:PLN02683 291 PQHGVG-AEICASVVEESF 308
TPP_enzymes cd00568
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ...
116-244 3.92e-08

Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.


Pssm-ID: 238318 [Multi-domain]  Cd Length: 168  Bit Score: 53.03  E-value: 3.92e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 116 FIDVGTGSLGQGV--AVGAGMAYvgknfdkADYRTYVVVGDGESAEGsiWESLHFAGHYKLDNLCVIFD----------- 182
Cdd:cd00568  40 LTSTGFGAMGYGLpaAIGAALAA-------PDRPVVCIAGDGGFMMT--GQELATAVRYGLPVIVVVFNnggygtirmhq 110
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45551847 183 VNRLGQSEATSLQHKLDvYRDRLEAFGFNAVVVDghDVEELSKAFHcAAITKNKPTAIIAKT 244
Cdd:cd00568 111 EAFYGGRVSGTDLSNPD-FAALAEAYGAKGVRVE--DPEDLEAALA-EALAAGGPALIEVKT 168
aceE PRK09405
pyruvate dehydrogenase subunit E1; Reviewed
22-247 1.57e-06

pyruvate dehydrogenase subunit E1; Reviewed


Pssm-ID: 236500 [Multi-domain]  Cd Length: 891  Bit Score: 51.30  E-value: 1.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   22 RIHSI---NA----TQASKS-----GHPTSCASIAEIMSVLF--FQQLRlNLKHPRDpssdrFILSKGHAAPILYA-AWA 86
Cdd:PRK09405  83 RIRSYirwNAaamvLRANKKdlglgGHISSFASSATLYEVGFnhFFRAP-NEPHGGD-----LVFFQGHASPGIYArAFL 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   87 EaGLFPIADLNNLRK-IDSD-LEGHPTPRL--NFIDVGTGSLGQGvAVGA-------------GMAyvgknfDKADYRTY 149
Cdd:PRK09405 157 E-GRLTEEQLDNFRQeVDGKgLSSYPHPWLmpDFWQFPTVSMGLG-PIMAiyqarflkylenrGLK------DTSDQKVW 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  150 VVVGDGESAEGsiwESL---HFAGHYKLDNLcvIFDVNrlgqseaTSLQhKLD--VyR------DRLEAF----GFNAV- 213
Cdd:PRK09405 229 AFLGDGEMDEP---ESLgaiSLAAREKLDNL--IFVIN-------CNLQ-RLDgpV-RgngkiiQELEGIfrgaGWNVIk 294
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  214 -------------------------VVDG-------------------------------------------HDVEELSK 225
Cdd:PRK09405 295 viwgsrwdpllakdtsgklvqlmneTVDGdyqtykakdgayvrehffgkypetkalvadmsdddiwalnrggHDPRKVYA 374
                        330       340
                 ....*....|....*....|..
gi 45551847  226 AFHCAAITKNKPTAIIAKTFKG 247
Cdd:PRK09405 375 AYKAAVEHKGQPTVILAKTIKG 396
AceE COG2609
Pyruvate dehydrogenase complex, dehydrogenase (E1) component [Energy production and conversion] ...
16-247 1.64e-06

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: 51.23  E-value: 1.64e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  16 DLAQKLRIHSI---NA----TQASKS-----GHPTSCASIAEIMSVLF--FQQLRlNLKHPRDpssdrFILSKGHAAPIL 81
Cdd:COG2609  78 DEELERRIRSIirwNAmamvVRANRKggglgGHISSFASAATLYEVGFnhFFRGP-DHPGGGD-----LVYFQGHASPGI 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  82 YA-AWAEaGLFPIADLNNLRKidsDLEGH-----PTPRL--NFIDVGTGSLGQGvAVGA-------------GMAyvgkn 140
Cdd:COG2609 152 YArAFLE-GRLTEEQLDNFRQ---EVDGKglssyPHPWLmpDFWQFPTVSMGLG-PINAiyqarfmkylhnrGLK----- 221
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 141 fDKADYRTYVVVGDGESAEGsiwESL---HFAGHYKLDNLcvIFDVNrlgqseaTSLQhKLD--VyR------DRLEAF- 208
Cdd:COG2609 222 -DTSDRKVWAFLGDGEMDEP---ESLgaiSLAAREKLDNL--IFVIN-------CNLQ-RLDgpV-RgngkiiQELEGVf 286
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 209 ---GFNAV--------------------------VVDG------------------------------------------ 217
Cdd:COG2609 287 rgaGWNVIkviwgsewdpllakdtdgalvkrmneTVDGdyqtykakdgayvrehffgkypelkalvadmsdediwrlnrg 366
                       330       340       350
                ....*....|....*....|....*....|.
gi 45551847 218 -HDVEELSKAFHCAAITKNKPTAIIAKTFKG 247
Cdd:COG2609 367 gHDPRKVYAAYKAAVEHKGQPTVILAKTIKG 397
PRK13012 PRK13012
2-oxoacid dehydrogenase subunit E1; Provisional
16-247 3.03e-06

2-oxoacid dehydrogenase subunit E1; Provisional


Pssm-ID: 237267 [Multi-domain]  Cd Length: 896  Bit Score: 50.32  E-value: 3.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   16 DLAQKLRIHSI---NA----TQASKS-----GHPTSCASIAEIMSV---LFFqqlrlnlKHPRDPSSDRFILSKGHAAPI 80
Cdd:PRK13012  85 DLALEERLAAIirwNAlamvVRANRAygelgGHIASYASAADLFEVgfnHFF-------RGRDDAGGGDLVYFQPHSAPG 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847   81 LYA-AWAEaGLFPIADLNNLRK-IDSD-LEGHPTPRL--NFIDVGTGSLGQGVAVGA----GMAYVGKN--FDKADYRTY 149
Cdd:PRK13012 158 IYArAFLE-GRLSEEQLDHFRQeIGGPgLSSYPHPWLmpDFWQFPTGSMGIGPINAIyqarFMRYLQHRglKDTSGRKVW 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  150 VVVGDGESAEGSIWESLHFAGHYKLDNLcvIFDVNrlgqseaTSLQhKLD--VyR------DRLEAF----GFN------ 211
Cdd:PRK13012 237 GFFGDGEMDEPESIAALSLAAREGLDNL--VFVIN-------CNLQ-RLDgpV-RgngriiQELEALfrgaGWNvikvlw 305
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  212 --------------------AVVVD-------------------------------------------GHDVEELSKAFH 228
Cdd:PRK13012 306 gsdwdalfardttgalvrrfAETVDgqfqtfkandgaynrehffgqdpelaalvahlsdedidrlkrgGHDPRKVYAAYA 385
                        330
                 ....*....|....*....
gi 45551847  229 CAAITKNKPTAIIAKTFKG 247
Cdd:PRK13012 386 AAVRHKGQPTVILAKTKKG 404
TPP_enzyme_PYR cd06586
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ...
346-455 4.18e-06

Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this group. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. In the case of 2-oxoisovalerate dehydrogenase (2OXO), sulfopyruvate decarboxylase (ComDE), and the E1 component of human pyruvate dehydrogenase complex (E1- PDHc) the PYR and PP domains appear on different subunits. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzymes 1-deoxy-D-xylulose 5-phosphate synthase (DXS) and Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit.


Pssm-ID: 132915 [Multi-domain]  Cd Length: 154  Bit Score: 46.95  E-value: 4.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847 346 TKNSTFSDKLKNLDPQRYIECfIAEQNLVGVAVGAA-CRRRTVAFVsTFATFFTRAFDQIRMGAISQTNVNFVGSHCGCS 424
Cdd:cd06586  21 DEISSLLDALREGDKRIIDTV-IHELGAAGAAAGYArAGGPPVVIV-TSGTGLLNAINGLADAAAEHLPVVFLIGARGIS 98
                        90       100       110
                ....*....|....*....|....*....|.
gi 45551847 425 iGEDGPSQMGLEDIAMFRTIPGSTIFYPSDA 455
Cdd:cd06586  99 -AQAKQTFQSMFDLGMYRSIPEANISSPSPA 128
odpB CHL00144
pyruvate dehydrogenase E1 component beta subunit; Validated
362-625 1.06e-05

pyruvate dehydrogenase E1 component beta subunit; Validated


Pssm-ID: 177066 [Multi-domain]  Cd Length: 327  Bit Score: 47.81  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  362 RYIECFIAEQNLVGVAVGAACRRRTVAFVSTFATFFTRAFDQI--RMGAISQTNvnfvGSHCGCSIGEDGPS----QMGL 435
Cdd:CHL00144  52 RVLDTPIAENSFTGMAIGAAMTGLRPIVEGMNMGFLLLAFNQIsnNAGMLHYTS----GGNFTIPIVIRGPGgvgrQLGA 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  436 EDI----AMFRTIPGSTIFypsdAVSTeravelAANTKGV--CFIRTSRPntcVIY--------------DNEEPFTIGR 495
Cdd:CHL00144 128 EHSqrleSYFQSVPGLQIV----ACST------PYNAKGLlkSAIRSNNP---VIFfehvllynlkeeipDNEYLLPLEK 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  496 GKVVRQKSsdEVLLIGAGITLYECLAAADQLEKNCITVRVIDPFTVKPLDAELIIEHGKQCgGRVVVVEDHYQQGGLGeA 575
Cdd:CHL00144 195 AEVVRPGN--DITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKPLDLGTISKSVKKT-HKVLIVEECMKTGGIG-A 270
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45551847  576 VLSALagernfVVKHLY--------------VPTvPRSGPpsvLIDMFGISARHVVNAVNEILK 625
Cdd:CHL00144 271 ELIAQ------INEHLFdeldapivrlssqdVPT-PYNGP---LEEATVIQPAQIIEAVEQIIT 324
PLN02374 PLN02374
pyruvate dehydrogenase (acetyl-transferring)
120-248 1.99e-03

pyruvate dehydrogenase (acetyl-transferring)


Pssm-ID: 215213 [Multi-domain]  Cd Length: 433  Bit Score: 41.08  E-value: 1.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45551847  120 GTGSLGQGVAVGAGMAYVGK------NFDKADYRTYVVVGDGESAEGSIWESLHFAGHYKLDnlcVIFDV-NRL---GQS 189
Cdd:PLN02374 192 GFAFIGEGIPVATGAAFSSKyrrevlKEESCDDVTLAFFGDGTCNNGQFFECLNMAALWKLP---IVFVVeNNLwaiGMS 268
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45551847  190 EATSLQHKlDVYRdRLEAFGFNAVVVDGHD---VEELSKAFHCAAITKNKPTAIIAKTFKGR 248
Cdd:PLN02374 269 HLRATSDP-EIWK-KGPAFGMPGVHVDGMDvlkVREVAKEAIERARRGEGPTLVECETYRFR 328
PLN02269 PLN02269
Pyruvate dehydrogenase E1 component subunit alpha
120-181 3.21e-03

Pyruvate dehydrogenase E1 component subunit alpha


Pssm-ID: 215152 [Multi-domain]  Cd Length: 362  Bit Score: 40.08  E-value: 3.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45551847  120 GTGSLGQGVAVGAGMAYVGKnFDKADYRTYVVVGDGESAEGSIWESLHFAGhykLDNLCVIF 181
Cdd:PLN02269 136 GHGIVGAQVPLGAGLAFAQK-YNKEENVAFALYGDGAANQGQLFEALNIAA---LWDLPVIF 193
 
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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