NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|291084858|ref|NP_001166939|]
View 

pyruvate dehydrogenase E1 component subunit beta, mitochondrial isoform 2 precursor [Homo sapiens]

Graphical summary

show options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
TPP_PYR_E1-PDHc-beta_like cd07036
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ...
37-185 4.88e-94

Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate dehydrogenase complex (E1- PDHc) and related proteins; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain of the beta subunits of the E1 components of: human pyruvate dehydrogenase complex (E1- PDHc), the acetoin dehydrogenase complex (ADC), and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC), 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. E1-PDHc is an alpha2beta2 dimer-of-heterodimers having two active sites lying between PYR and PP domains of separate subunits, the PYR domains are arranged on the beta subunit, the PP domains on the alpha subunits. PDHc 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. 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: 132919  Cd Length: 167  Bit Score: 279.75  E-value: 4.88e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  37 DAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFS 116
Cdd:cd07036    1 QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 117 MQAIDQVINSAAKTYYMSG------------------VAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDNNP 178
Cdd:cd07036   81 LPAFDQIVNEAAKLRYMSGgqfkvpivirgpngggigGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160

                 ....*..
gi 291084858 179 VVVLENE 185
Cdd:cd07036  161 VIFLEHK 167
Transketolase_C pfam02780
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ...
208-330 6.97e-43

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


:

Pssm-ID: 251527  Cd Length: 124  Bit Score: 146.21  E-value: 6.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  208 GKAKIERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEI 287
Cdd:pfam02780   1 GKAEILREGDDVTIVAYGSMVHEALEAAEELAKEGISAEVIDLRTVKPLDEDTILESVKKTGRLVVVEEAVKRGGFGSEV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 291084858  288 CARIMEGpAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKD 330
Cdd:pfam02780  81 AAALAEE-GFDYLDAPVLRVGGPDTPIPHGPALELAYLGLTAE 122
PLN02683 PLN02683
pyruvate dehydrogenase E1 component subunit beta
6-338 0e+00

pyruvate dehydrogenase E1 component subunit beta


:

Pssm-ID: 215368 [Multi-domain]  Cd Length: 356  Bit Score: 513.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858   6 GLVRRPLREVSGLLKRRFhwtAPAALQVTVRDAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDT 85
Cdd:PLN02683   3 GQLLRRTRPAAAAAARGY---ASAAKEMTVRDALNSALDEEMSADPKVFIMGEEVGEYQGAYKITKGLLQKYGPDRVLDT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  86 PISEMGFAGIAVGAAMAGLRPICEFMTFNFSMQAIDQVINSAAKTYYMS------------------GVAAQHSQCFAAW 147
Cdd:PLN02683  80 PITEAGFTGIGVGAAYAGLKPVVEFMTFNFSMQAIDHIINSAAKTNYMSagqisvpivfrgpngaaaGVGAQHSQCFAAW 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 148 YGHCPGLKVVSPWNSEDAKGLIKSAIRDNNPVVVLENELMYGVPFEFPPEAQSKDFLIPIGKAKIERQGTHITVVSHSRP 227
Cdd:PLN02683 160 YSSVPGLKVLAPYSSEDARGLLKAAIRDPDPVVFLENELLYGESFPVSAEVLDSSFVLPIGKAKIEREGKDVTIVAFSKM 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 228 VGHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEgPAFNFLDAPAVRV 307
Cdd:PLN02683 240 VGYALKAAEILAKEGISAEVINLRSIRPLDRDTINASVRKTNRLVTVEEGWPQHGVGAEICASVVE-ESFDYLDAPVERI 318
                        330       340       350
                 ....*....|....*....|....*....|.
gi 291084858 308 TGADVPMPYAKILEDNSIPQVKDIIFAIKKT 338
Cdd:PLN02683 319 AGADVPMPYAANLERLALPQVEDIVRAAKRA 349
 
Name Accession Description Interval E-value
TPP_PYR_E1-PDHc-beta_like cd07036
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ...
37-185 4.88e-94

Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate dehydrogenase complex (E1- PDHc) and related proteins; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain of the beta subunits of the E1 components of: human pyruvate dehydrogenase complex (E1- PDHc), the acetoin dehydrogenase complex (ADC), and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC), 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. E1-PDHc is an alpha2beta2 dimer-of-heterodimers having two active sites lying between PYR and PP domains of separate subunits, the PYR domains are arranged on the beta subunit, the PP domains on the alpha subunits. PDHc 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. 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: 132919  Cd Length: 167  Bit Score: 279.75  E-value: 4.88e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  37 DAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFS 116
Cdd:cd07036    1 QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 117 MQAIDQVINSAAKTYYMSG------------------VAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDNNP 178
Cdd:cd07036   81 LPAFDQIVNEAAKLRYMSGgqfkvpivirgpngggigGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160

                 ....*..
gi 291084858 179 VVVLENE 185
Cdd:cd07036  161 VIFLEHK 167
Transket_pyr pfam02779
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ...
32-191 3.47e-43

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


Pssm-ID: 251526  Cd Length: 172  Bit Score: 148.44  E-value: 3.47e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858   32 QVTVRDAINQGMDEELERDEKVFLLGEEVAQydGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFM 111
Cdd:pfam02779   2 KIATRKASGEALAELAKRDPRVVGGGADVAG--GTFTVTKGLLHPQGDGRVIDTGIAEQAMVGIANGMALHGLLPPVEAT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  112 TFNFSMQAIDQVINSAAKTYYMSGV-------------AAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDNNP 178
Cdd:pfam02779  80 FGDFANRADDAIRHYAALGKLPVPFvvtrdpigvgedgPTHQSQEDLAFLRAIPNLKVVRPSDAAETKGLLRAAIEDDGP 159
                         170
                  ....*....|...
gi 291084858  179 VVVLENELMYGVP 191
Cdd:pfam02779 160 VVLRLPRQLLRHK 172
Transketolase_C pfam02780
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ...
208-330 6.97e-43

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


Pssm-ID: 251527  Cd Length: 124  Bit Score: 146.21  E-value: 6.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  208 GKAKIERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEI 287
Cdd:pfam02780   1 GKAEILREGDDVTIVAYGSMVHEALEAAEELAKEGISAEVIDLRTVKPLDEDTILESVKKTGRLVVVEEAVKRGGFGSEV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 291084858  288 CARIMEGpAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKD 330
Cdd:pfam02780  81 AAALAEE-GFDYLDAPVLRVGGPDTPIPHGPALELAYLGLTAE 122
Transket_pyr smart00861
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
83-189 4.62e-27

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  Cd Length: 136  Bit Score: 104.11  E-value: 4.62e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858    83 IDTPISEMGFAGIAVGAAMAGLRPICEFMtFNFSMQAIDQVINSAAKT------------YYMSGVAAQHSQCFAAWYGH 150
Cdd:smart00861  18 IDTGIAEQAMVGFAAGLALHGLRPVVEIF-FTFFDRAKDQIRSAGASGnvpvvfrhdgggGVGEDGPTHHSIEDEALLRA 96
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 291084858   151 CPGLKVVSPWNSEDAKGLIKSAIRDNNPVVV-LENELMYG 189
Cdd:smart00861  97 IPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIrLERKSLYR 136
PLN02683 PLN02683
pyruvate dehydrogenase E1 component subunit beta
6-338 0e+00

pyruvate dehydrogenase E1 component subunit beta


Pssm-ID: 215368 [Multi-domain]  Cd Length: 356  Bit Score: 513.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858   6 GLVRRPLREVSGLLKRRFhwtAPAALQVTVRDAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDT 85
Cdd:PLN02683   3 GQLLRRTRPAAAAAARGY---ASAAKEMTVRDALNSALDEEMSADPKVFIMGEEVGEYQGAYKITKGLLQKYGPDRVLDT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  86 PISEMGFAGIAVGAAMAGLRPICEFMTFNFSMQAIDQVINSAAKTYYMS------------------GVAAQHSQCFAAW 147
Cdd:PLN02683  80 PITEAGFTGIGVGAAYAGLKPVVEFMTFNFSMQAIDHIINSAAKTNYMSagqisvpivfrgpngaaaGVGAQHSQCFAAW 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 148 YGHCPGLKVVSPWNSEDAKGLIKSAIRDNNPVVVLENELMYGVPFEFPPEAQSKDFLIPIGKAKIERQGTHITVVSHSRP 227
Cdd:PLN02683 160 YSSVPGLKVLAPYSSEDARGLLKAAIRDPDPVVFLENELLYGESFPVSAEVLDSSFVLPIGKAKIEREGKDVTIVAFSKM 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 228 VGHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEgPAFNFLDAPAVRV 307
Cdd:PLN02683 240 VGYALKAAEILAKEGISAEVINLRSIRPLDRDTINASVRKTNRLVTVEEGWPQHGVGAEICASVVE-ESFDYLDAPVERI 318
                        330       340       350
                 ....*....|....*....|....*....|.
gi 291084858 308 TGADVPMPYAKILEDNSIPQVKDIIFAIKKT 338
Cdd:PLN02683 319 AGADVPMPYAANLERLALPQVEDIVRAAKRA 349
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
32-337 0e+00

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 517.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  32 QVTVRDAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFM 111
Cdd:PRK11892 141 TMTVREALRDAMAEEMRRDEDVFVMGEEVAEYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGAAFAGLKPIVEFM 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 112 TFNFSMQAIDQVINSAAKTYYMSG------------------VAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAI 173
Cdd:PRK11892 221 TFNFAMQAIDQIINSAAKTLYMSGgqmgcpivfrgpngaaarVAAQHSQDYAAWYSHIPGLKVVAPYSAADAKGLLKAAI 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 174 RDNNPVVVLENELMYGVPFEFPpeaQSKDFLIPIGKAKIERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRTI 253
Cdd:PRK11892 301 RDPNPVIFLENEILYGQSFDVP---KLDDFVLPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTI 377
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 254 RPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEgPAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDIIF 333
Cdd:PRK11892 378 RPMDTETIVESVKKTNRLVTVEEGWPQSGVGAEIAARVME-QAFDYLDAPVLRVTGKDVPMPYAANLEKLALPSVAEVVE 456

                 ....
gi 291084858 334 AIKK 337
Cdd:PRK11892 457 AVKA 460
PTZ00182 PTZ00182
3-methyl-2-oxobutanate dehydrogenase; Provisional
19-339 1.34e-175

3-methyl-2-oxobutanate dehydrogenase; Provisional


Pssm-ID: 185502 [Multi-domain]  Cd Length: 355  Bit Score: 494.50  E-value: 1.34e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  19 LKRRFHWTAP--AALQVTVRDAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIA 96
Cdd:PTZ00182  19 SASRSSSTESkgATVKMNVREAINSALDEELARDPKVFVLGEDVAQYGGVYKCTKGLLDKYGPDRVFDTPITEQGFAGFA 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  97 VGAAMAGLRPICEFMTFNFSMQAIDQVINSAAKTYYMSG------------------VAAQHSQCFAAWYGHCPGLKVVS 158
Cdd:PTZ00182  99 IGAAMNGLRPIAEFMFADFIFPAFDQIVNEAAKYRYMSGgqfdcpivirgpngavghGGAYHSQSFEAYFAHVPGLKVVA 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 159 PWNSEDAKGLIKSAIRDNNPVVVLENELMYGVPFEFPPEAqskDFLIPIGKAKIERQGTHITVVSHSRPVGHCLEAAAVL 238
Cdd:PTZ00182 179 PSDPEDAKGLLKAAIRDPNPVVFFEPKLLYRESVEVVPEA---DYTLPLGKAKVVREGKDVTIVGYGSQVHVALKAAEEL 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 239 SKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEGpAFNFLDAPAVRVTGADVPMPYAK 318
Cdd:PTZ00182 256 AKEGISCEVIDLRSLRPWDRETIVKSVKKTGRCVIVHEAPPTCGIGAEIAAQIMED-CFLYLEAPIKRVCGADTPFPYAK 334
                        330       340
                 ....*....|....*....|.
gi 291084858 319 ILEDNSIPQVKDIIFAIKKTL 339
Cdd:PTZ00182 335 NLEPAYLPDKEKVVEAAKRVL 355
AcoB COG0022
Pyruvate/2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, eukaryotic type, ...
32-340 5.87e-163

Pyruvate/2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, eukaryotic type, beta subunit [Energy production and conversion]


Pssm-ID: 223101 [Multi-domain]  Cd Length: 324  Bit Score: 461.23  E-value: 5.87e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  32 QVTVRDAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFM 111
Cdd:COG0022    1 QMTMIEAINEAMDEEMERDERVVVLGEDVGVYGGVFRVTKGLQEKFGEERVIDTPIAESGIAGIAVGAALTGLRPIVEIQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 112 TFNFSMQAIDQVINSAAKTYYMSG------------------VAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAI 173
Cdd:COG0022   81 FADFIYPAFDQIVNQAAKIRYRSGgqftvpivirtpngggigGGAQHSQSLEALFAHIPGLKVVMPSTPYDAKGLLKAAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 174 RDNNPVVVLENELMYGVP-FEFPpeaqSKDFLIPIGKAKIERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRT 252
Cdd:COG0022  161 RDPDPVIFLEHKRLYRSFkGEVP----EEDYTIPLGKAKIVREGSDVTIVTYGAMVHTALEAAEELEKEGISAEVIDLRT 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 253 IRPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEgPAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDII 332
Cdd:COG0022  237 LSPLDKETIIASVKKTGRLVIVHEAPKTGGIGAEIAALIAE-EAFDYLDAPILRVAGPDTPVPYSAALEKAYLPNPERIV 315

                 ....*...
gi 291084858 333 FAIKKTLN 340
Cdd:COG0022  316 AAVKKVLE 323
odpB CHL00144
pyruvate dehydrogenase E1 component beta subunit; Validated
37-340 3.05e-94

pyruvate dehydrogenase E1 component beta subunit; Validated


Pssm-ID: 177066 [Multi-domain]  Cd Length: 327  Bit Score: 286.25  E-value: 3.05e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  37 DAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFS 116
Cdd:CHL00144   8 EALREAIDEEMARDPRVFVIGEDVGHYGGSYKVTKGLHEKYGDLRVLDTPIAENSFTGMAIGAAMTGLRPIVEGMNMGFL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 117 MQAIDQVINSAAKTYYMSG------------------VAAQHSQCFAAWYGHCPGLKVV---SPWNsedAKGLIKSAIRD 175
Cdd:CHL00144  88 LLAFNQISNNAGMLHYTSGgnftipivirgpggvgrqLGAEHSQRLESYFQSVPGLQIVacsTPYN---AKGLLKSAIRS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 176 NNPVVVLENELMYGVPFEFPPEaqskDFLIPIGKAKIERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRTIRP 255
Cdd:CHL00144 165 NNPVIFFEHVLLYNLKEEIPDN----EYLLPLEKAEVVRPGNDITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 256 MDMETIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEGpAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDIIFAI 335
Cdd:CHL00144 241 LDLGTISKSVKKTHKVLIVEECMKTGGIGAELIAQINEH-LFDELDAPIVRLSSQDVPTPYNGPLEEATVIQPAQIIEAV 319

                 ....*
gi 291084858 336 KKTLN 340
Cdd:CHL00144 320 EQIIT 324
dxs TIGR00204
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ...
80-293 7.03e-14

1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent enzyme related to transketolase and the pyruvate dehydrogenase E1-beta subunit. By an acyloin condensation of pyruvate with glyceraldehyde 3-phosphate, it produces 1-deoxy-D-xylulose 5-phosphate, a precursor of thiamine diphosphate (TPP), pyridoxal phosphate, and the isoprenoid building block isopentenyl diphosphate (IPP) [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine, Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine].


Pssm-ID: 129308 [Multi-domain]  Cd Length: 617  Bit Score: 70.96  E-value: 7.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858   80 KRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTfNFSMQAIDQVINSAAKTYY-------MSGV----AAQHSQCFAAWY 148
Cdd:TIGR00204 352 DRYFDVAIAEQHAVTFAAGMAIEGYKPFVAIYS-TFLQRAYDQVVHDVCIQKLpvlfaidRAGIvgadGETHQGAFDISY 430
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  149 GHC-PGLKVVSPWNSEDAKGLIKSAIR-DNNPVVVL---ENELmyGVPFEFPPEAqskdflIPIGKAKIERQGTHITVVS 223
Cdd:TIGR00204 431 LRCiPNMVIMAPSDENELRQMLYTGYHyDDGPIAVRyprGNAV--GVELTPEPEK------LPIGKSEVLRKGEKILILG 502
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  224 HSRPVGHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEICARIME 293
Cdd:TIGR00204 503 FGTLVPEALEVAESLNEKGIEATVVDARFVKPLDEELILEIAASHEKLVTVEENAIMGGAGSAVLEFLMD 572
 
Name Accession Description Interval E-value
TPP_PYR_E1-PDHc-beta_like cd07036
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ...
37-185 4.88e-94

Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate dehydrogenase complex (E1- PDHc) and related proteins; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain of the beta subunits of the E1 components of: human pyruvate dehydrogenase complex (E1- PDHc), the acetoin dehydrogenase complex (ADC), and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC), 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. E1-PDHc is an alpha2beta2 dimer-of-heterodimers having two active sites lying between PYR and PP domains of separate subunits, the PYR domains are arranged on the beta subunit, the PP domains on the alpha subunits. PDHc 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. 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: 132919  Cd Length: 167  Bit Score: 279.75  E-value: 4.88e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  37 DAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFS 116
Cdd:cd07036    1 QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 117 MQAIDQVINSAAKTYYMSG------------------VAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDNNP 178
Cdd:cd07036   81 LPAFDQIVNEAAKLRYMSGgqfkvpivirgpngggigGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160

                 ....*..
gi 291084858 179 VVVLENE 185
Cdd:cd07036  161 VIFLEHK 167
Transket_pyr pfam02779
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ...
32-191 3.47e-43

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


Pssm-ID: 251526  Cd Length: 172  Bit Score: 148.44  E-value: 3.47e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858   32 QVTVRDAINQGMDEELERDEKVFLLGEEVAQydGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFM 111
Cdd:pfam02779   2 KIATRKASGEALAELAKRDPRVVGGGADVAG--GTFTVTKGLLHPQGDGRVIDTGIAEQAMVGIANGMALHGLLPPVEAT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  112 TFNFSMQAIDQVINSAAKTYYMSGV-------------AAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDNNP 178
Cdd:pfam02779  80 FGDFANRADDAIRHYAALGKLPVPFvvtrdpigvgedgPTHQSQEDLAFLRAIPNLKVVRPSDAAETKGLLRAAIEDDGP 159
                         170
                  ....*....|...
gi 291084858  179 VVVLENELMYGVP 191
Cdd:pfam02779 160 VVLRLPRQLLRHK 172
Transketolase_C pfam02780
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ...
208-330 6.97e-43

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


Pssm-ID: 251527  Cd Length: 124  Bit Score: 146.21  E-value: 6.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  208 GKAKIERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEI 287
Cdd:pfam02780   1 GKAEILREGDDVTIVAYGSMVHEALEAAEELAKEGISAEVIDLRTVKPLDEDTILESVKKTGRLVVVEEAVKRGGFGSEV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 291084858  288 CARIMEGpAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKD 330
Cdd:pfam02780  81 AAALAEE-GFDYLDAPVLRVGGPDTPIPHGPALELAYLGLTAE 122
TPP_enzyme_PYR cd06586
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ...
37-185 1.30e-29

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  Cd Length: 154  Bit Score: 111.67  E-value: 1.30e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  37 DAINQGMDEELerdeKVFLLGEEVAQYdgayKVSRGLWKKyGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFS 116
Cdd:cd06586    1 AAFAEVLTAWG----VRHVFGYPGDEI----SSLLDALRE-GDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSGTGL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 117 MQAIDQVInSAAKTY----YMSGV--------AAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDNN---PVVV 181
Cdd:cd06586   72 LNAINGLA-DAAAEHlpvvFLIGArgisaqakQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYAsqgPVVV 150

                 ....
gi 291084858 182 LENE 185
Cdd:cd06586  151 RLPR 154
Transket_pyr smart00861
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ...
83-189 4.62e-27

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  Cd Length: 136  Bit Score: 104.11  E-value: 4.62e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858    83 IDTPISEMGFAGIAVGAAMAGLRPICEFMtFNFSMQAIDQVINSAAKT------------YYMSGVAAQHSQCFAAWYGH 150
Cdd:smart00861  18 IDTGIAEQAMVGFAAGLALHGLRPVVEIF-FTFFDRAKDQIRSAGASGnvpvvfrhdgggGVGEDGPTHHSIEDEALLRA 96
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 291084858   151 CPGLKVVSPWNSEDAKGLIKSAIRDNNPVVV-LENELMYG 189
Cdd:smart00861  97 IPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIrLERKSLYR 136
TPP_PYR_DXS_TK_like cd07033
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ...
37-181 2.42e-20

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  Cd Length: 156  Bit Score: 85.57  E-value: 2.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  37 DAINQGMDEELERDEKVFLLGEEVAQYDGAYKvsrgLWKKYGDkRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFnFS 116
Cdd:cd07033    1 KAFGEALLELAKKDPRIVALSADLGGSTGLDK----FAKKFPD-RFIDVGIAEQNMVGIAAGLALHGLKPFVSTFSF-FL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 117 MQAIDQVINSAAktyYM----------SGVAA------QHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDNNPVV 180
Cdd:cd07033   75 QRAYDQIRHDVA---LQnlpvkfvgthAGISVgedgptHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYDGPVY 151

                 .
gi 291084858 181 V 181
Cdd:cd07033  152 I 152
PLN02683 PLN02683
pyruvate dehydrogenase E1 component subunit beta
6-338 0e+00

pyruvate dehydrogenase E1 component subunit beta


Pssm-ID: 215368 [Multi-domain]  Cd Length: 356  Bit Score: 513.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858   6 GLVRRPLREVSGLLKRRFhwtAPAALQVTVRDAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDT 85
Cdd:PLN02683   3 GQLLRRTRPAAAAAARGY---ASAAKEMTVRDALNSALDEEMSADPKVFIMGEEVGEYQGAYKITKGLLQKYGPDRVLDT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  86 PISEMGFAGIAVGAAMAGLRPICEFMTFNFSMQAIDQVINSAAKTYYMS------------------GVAAQHSQCFAAW 147
Cdd:PLN02683  80 PITEAGFTGIGVGAAYAGLKPVVEFMTFNFSMQAIDHIINSAAKTNYMSagqisvpivfrgpngaaaGVGAQHSQCFAAW 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 148 YGHCPGLKVVSPWNSEDAKGLIKSAIRDNNPVVVLENELMYGVPFEFPPEAQSKDFLIPIGKAKIERQGTHITVVSHSRP 227
Cdd:PLN02683 160 YSSVPGLKVLAPYSSEDARGLLKAAIRDPDPVVFLENELLYGESFPVSAEVLDSSFVLPIGKAKIEREGKDVTIVAFSKM 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 228 VGHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEgPAFNFLDAPAVRV 307
Cdd:PLN02683 240 VGYALKAAEILAKEGISAEVINLRSIRPLDRDTINASVRKTNRLVTVEEGWPQHGVGAEICASVVE-ESFDYLDAPVERI 318
                        330       340       350
                 ....*....|....*....|....*....|.
gi 291084858 308 TGADVPMPYAKILEDNSIPQVKDIIFAIKKT 338
Cdd:PLN02683 319 AGADVPMPYAANLERLALPQVEDIVRAAKRA 349
PRK11892 PRK11892
pyruvate dehydrogenase subunit beta; Provisional
32-337 0e+00

pyruvate dehydrogenase subunit beta; Provisional


Pssm-ID: 237011 [Multi-domain]  Cd Length: 464  Bit Score: 517.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  32 QVTVRDAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFM 111
Cdd:PRK11892 141 TMTVREALRDAMAEEMRRDEDVFVMGEEVAEYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGAAFAGLKPIVEFM 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 112 TFNFSMQAIDQVINSAAKTYYMSG------------------VAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAI 173
Cdd:PRK11892 221 TFNFAMQAIDQIINSAAKTLYMSGgqmgcpivfrgpngaaarVAAQHSQDYAAWYSHIPGLKVVAPYSAADAKGLLKAAI 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 174 RDNNPVVVLENELMYGVPFEFPpeaQSKDFLIPIGKAKIERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRTI 253
Cdd:PRK11892 301 RDPNPVIFLENEILYGQSFDVP---KLDDFVLPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRTI 377
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 254 RPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEgPAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDIIF 333
Cdd:PRK11892 378 RPMDTETIVESVKKTNRLVTVEEGWPQSGVGAEIAARVME-QAFDYLDAPVLRVTGKDVPMPYAANLEKLALPSVAEVVE 456

                 ....
gi 291084858 334 AIKK 337
Cdd:PRK11892 457 AVKA 460
PTZ00182 PTZ00182
3-methyl-2-oxobutanate dehydrogenase; Provisional
19-339 1.34e-175

3-methyl-2-oxobutanate dehydrogenase; Provisional


Pssm-ID: 185502 [Multi-domain]  Cd Length: 355  Bit Score: 494.50  E-value: 1.34e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  19 LKRRFHWTAP--AALQVTVRDAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIA 96
Cdd:PTZ00182  19 SASRSSSTESkgATVKMNVREAINSALDEELARDPKVFVLGEDVAQYGGVYKCTKGLLDKYGPDRVFDTPITEQGFAGFA 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  97 VGAAMAGLRPICEFMTFNFSMQAIDQVINSAAKTYYMSG------------------VAAQHSQCFAAWYGHCPGLKVVS 158
Cdd:PTZ00182  99 IGAAMNGLRPIAEFMFADFIFPAFDQIVNEAAKYRYMSGgqfdcpivirgpngavghGGAYHSQSFEAYFAHVPGLKVVA 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 159 PWNSEDAKGLIKSAIRDNNPVVVLENELMYGVPFEFPPEAqskDFLIPIGKAKIERQGTHITVVSHSRPVGHCLEAAAVL 238
Cdd:PTZ00182 179 PSDPEDAKGLLKAAIRDPNPVVFFEPKLLYRESVEVVPEA---DYTLPLGKAKVVREGKDVTIVGYGSQVHVALKAAEEL 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 239 SKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEGpAFNFLDAPAVRVTGADVPMPYAK 318
Cdd:PTZ00182 256 AKEGISCEVIDLRSLRPWDRETIVKSVKKTGRCVIVHEAPPTCGIGAEIAAQIMED-CFLYLEAPIKRVCGADTPFPYAK 334
                        330       340
                 ....*....|....*....|.
gi 291084858 319 ILEDNSIPQVKDIIFAIKKTL 339
Cdd:PTZ00182 335 NLEPAYLPDKEKVVEAAKRVL 355
PRK09212 PRK09212
pyruvate dehydrogenase subunit beta; Validated
32-340 4.82e-169

pyruvate dehydrogenase subunit beta; Validated


Pssm-ID: 169719 [Multi-domain]  Cd Length: 327  Bit Score: 476.91  E-value: 4.82e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  32 QVTVRDAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFM 111
Cdd:PRK09212   3 QLTVREALRDAMQEEMERDPKVFLMGEEVGEYQGAYKVTQGLLEQFGPKRVIDTPITEHGFAGLAVGAAFAGLRPIVEFM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 112 TFNFSMQAIDQVINSAAKTYYMSG------------------VAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAI 173
Cdd:PRK09212  83 TFNFAMQAIDQIVNSAAKTNYMSGgqlkcpivfrgpngaaarVAAQHSQCYAAWYSHIPGLKVVAPYFAADCKGLLKTAI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 174 RDNNPVVVLENELMYGVPFEFPPEAQSkdflIPIGKAKIERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRTI 253
Cdd:PRK09212 163 RDNNPVIFLENEILYGHSHEVPEEEES----IPFGKAAILREGSDVTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 254 RPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEgPAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDIIF 333
Cdd:PRK09212 239 RPLDTETIIESVKKTNRLVVVEEGWPFAGVGAEIAALIMK-EAFDYLDAPVERVTGKDVPLPYAANLEKLALPSEEDIIE 317

                 ....*..
gi 291084858 334 AIKKTLN 340
Cdd:PRK09212 318 AVKKVCY 324
AcoB COG0022
Pyruvate/2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, eukaryotic type, ...
32-340 5.87e-163

Pyruvate/2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, eukaryotic type, beta subunit [Energy production and conversion]


Pssm-ID: 223101 [Multi-domain]  Cd Length: 324  Bit Score: 461.23  E-value: 5.87e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  32 QVTVRDAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFM 111
Cdd:COG0022    1 QMTMIEAINEAMDEEMERDERVVVLGEDVGVYGGVFRVTKGLQEKFGEERVIDTPIAESGIAGIAVGAALTGLRPIVEIQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 112 TFNFSMQAIDQVINSAAKTYYMSG------------------VAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAI 173
Cdd:COG0022   81 FADFIYPAFDQIVNQAAKIRYRSGgqftvpivirtpngggigGGAQHSQSLEALFAHIPGLKVVMPSTPYDAKGLLKAAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 174 RDNNPVVVLENELMYGVP-FEFPpeaqSKDFLIPIGKAKIERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRT 252
Cdd:COG0022  161 RDPDPVIFLEHKRLYRSFkGEVP----EEDYTIPLGKAKIVREGSDVTIVTYGAMVHTALEAAEELEKEGISAEVIDLRT 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 253 IRPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEgPAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDII 332
Cdd:COG0022  237 LSPLDKETIIASVKKTGRLVIVHEAPKTGGIGAEIAALIAE-EAFDYLDAPILRVAGPDTPVPYSAALEKAYLPNPERIV 315

                 ....*...
gi 291084858 333 FAIKKTLN 340
Cdd:COG0022  316 AAVKKVLE 323
odpB CHL00144
pyruvate dehydrogenase E1 component beta subunit; Validated
37-340 3.05e-94

pyruvate dehydrogenase E1 component beta subunit; Validated


Pssm-ID: 177066 [Multi-domain]  Cd Length: 327  Bit Score: 286.25  E-value: 3.05e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  37 DAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFS 116
Cdd:CHL00144   8 EALREAIDEEMARDPRVFVIGEDVGHYGGSYKVTKGLHEKYGDLRVLDTPIAENSFTGMAIGAAMTGLRPIVEGMNMGFL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 117 MQAIDQVINSAAKTYYMSG------------------VAAQHSQCFAAWYGHCPGLKVV---SPWNsedAKGLIKSAIRD 175
Cdd:CHL00144  88 LLAFNQISNNAGMLHYTSGgnftipivirgpggvgrqLGAEHSQRLESYFQSVPGLQIVacsTPYN---AKGLLKSAIRS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 176 NNPVVVLENELMYGVPFEFPPEaqskDFLIPIGKAKIERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRTIRP 255
Cdd:CHL00144 165 NNPVIFFEHVLLYNLKEEIPDN----EYLLPLEKAEVVRPGNDITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 256 MDMETIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEGpAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDIIFAI 335
Cdd:CHL00144 241 LDLGTISKSVKKTHKVLIVEECMKTGGIGAELIAQINEH-LFDELDAPIVRLSSQDVPTPYNGPLEEATVIQPAQIIEAV 319

                 ....*
gi 291084858 336 KKTLN 340
Cdd:CHL00144 320 EQIIT 324
COG3958 COG3958
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]
75-275 3.82e-22

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


Pssm-ID: 226467 [Multi-domain]  Cd Length: 312  Bit Score: 93.50  E-value: 3.82e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  75 KKYGDkRIIDTPISEMGFAGIAVGAAMAGLRP-ICEFMTFnFSMQAIDQVINSAAKTYYMSGVAAQHS-----------Q 142
Cdd:COG3958   45 KEFPD-RFFNVGIAEQDMVGTAAGLALAGKKPfVSTFAAF-LSRRAWEQIRNSIAYNNLNVKIVATHAgvtygedgsshQ 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 143 CFA--AWYGHCPGLKVVSPWNSEDAKGLIKSAIRDNNPVVVLenelMYGVPFEFPPEAQSKDFliPIGKAKIERQGTHIT 220
Cdd:COG3958  123 ALEdiAIMRGLPNMTVIAPADAVETRAILDQIADYKGPVYMR----LGRGKVPVVVDEGGYTF--EIGKANVLRDGSDLT 196
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 291084858 221 VVSHSRPVGHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVE 275
Cdd:COG3958  197 IIATGVMVAEALEAAEILKKEGISAAVINMFTIKPIDEQAILKAARETGRIVTAE 251
Dxs COG1154
Deoxyxylulose-5-phosphate synthase [Coenzyme metabolism / Lipid metabolism]
72-293 1.14e-14

Deoxyxylulose-5-phosphate synthase [Coenzyme metabolism / Lipid metabolism]


Pssm-ID: 224076 [Multi-domain]  Cd Length: 627  Bit Score: 73.39  E-value: 1.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  72 GLWK---KYGDkRIIDTPISE---MGFAGiavGAAMAGLRPICE-FMTFnfsMQ-AIDQVIN-------------SAAKT 130
Cdd:COG1154  348 GLVKfskKFPD-RFFDVGIAEqhaVTFAA---GLAAEGMKPVVAiYSTF---LQrAYDQLIHdvaiqnlpvtfaiDRAGI 420
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 131 YYMSGvaAQHSQCFA-AWYGHCPGLKVVSPWNSEDAKGLIKSAIR-DNNPVVV-LENELMYGVPFEFPPEaqskdfLIPI 207
Cdd:COG1154  421 VGADG--PTHQGLFDlSFLRCIPNMVIMAPRDEEELRQMLYTALAqDDGPVAIrYPRGNGVGVILTPELE------PLEI 492
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 208 GKAKIERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEI 287
Cdd:COG1154  493 GKGELLKEGEKVAILAFGTMLPEALKVAEKLNAYGISVTVVDPRFVKPLDEALLLELAKSHDLVVTLEENVVDGGFGSAV 572

                 ....*.
gi 291084858 288 CARIME 293
Cdd:COG1154  573 LEFLAA 578
PRK05444 PRK05444
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
73-293 1.23e-14

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


Pssm-ID: 235470 [Multi-domain]  Cd Length: 580  Bit Score: 73.19  E-value: 1.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  73 LWKKYGDkRIIDTPISE---MGFAGiavGAAMAGLRPICE-FMTFnfsMQ-AIDQVINSaaktyymsgVAAQ-------- 139
Cdd:PRK05444 315 FSKRFPD-RYFDVGIAEqhaVTFAA---GLATEGLKPVVAiYSTF---LQrAYDQVIHD---------VALQnlpvtfai 378
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 140 ------------HSQCF-AAWYGHCPGLKVVSPWNSEDAKGLIKSAIR-DNNPVVVlenelMY----GVPFEFPPEAQsk 201
Cdd:PRK05444 379 draglvgadgptHQGAFdLSYLRCIPNMVIMAPSDENELRQMLYTALAyDDGPIAI-----RYprgnGVGVELPELEP-- 451
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 202 dflIPIGKAKIERQGTHITVVSHSRPVGHCLEAAAVLSkegvECEVINMRTIRPMDMETIEASVMKTNHLVTVEGGWPQF 281
Cdd:PRK05444 452 ---LPIGKGEVLREGEDVAILAFGTMLAEALKAAERLA----SATVVDARFVKPLDEELLLELAAKHDLVVTVEEGAIMG 524
                        250
                 ....*....|..
gi 291084858 282 GVGAEICARIME 293
Cdd:PRK05444 525 GFGSAVLEFLAD 536
PLN02234 PLN02234
1-deoxy-D-xylulose-5-phosphate synthase
81-277 3.13e-14

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


Pssm-ID: 177878 [Multi-domain]  Cd Length: 641  Bit Score: 72.44  E-value: 3.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  81 RIIDTPISEMGFAGIAVGAAMAGLRPICEFMTfNFSMQAIDQVIN-----------SAAKTYYMSGVAAQHSQCFAAWYG 149
Cdd:PLN02234 400 RCFDVGIAEQHAVTFAAGLACEGLKPFCTIYS-SFMQRAYDQVVHdvdlqklpvrfAIDRAGLMGADGPTHCGAFDVTFM 478
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 150 HC-PGLKVVSPWNSEDAKGLIKSAIRDNNPVVVLENELMYGVPFEFPPeaQSKDFLIPIGKAKIERQGTHITVVSHSRPV 228
Cdd:PLN02234 479 AClPNMIVMAPSDEAELFNMVATAAAIDDRPSCFRYHRGNGIGVSLPP--GNKGVPLQIGRGRILRDGERVALLGYGSAV 556
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 291084858 229 GHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGG 277
Cdd:PLN02234 557 QRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKSHEVLITVEEG 605
dxs TIGR00204
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ...
80-293 7.03e-14

1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent enzyme related to transketolase and the pyruvate dehydrogenase E1-beta subunit. By an acyloin condensation of pyruvate with glyceraldehyde 3-phosphate, it produces 1-deoxy-D-xylulose 5-phosphate, a precursor of thiamine diphosphate (TPP), pyridoxal phosphate, and the isoprenoid building block isopentenyl diphosphate (IPP) [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine, Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine].


Pssm-ID: 129308 [Multi-domain]  Cd Length: 617  Bit Score: 70.96  E-value: 7.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858   80 KRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTfNFSMQAIDQVINSAAKTYY-------MSGV----AAQHSQCFAAWY 148
Cdd:TIGR00204 352 DRYFDVAIAEQHAVTFAAGMAIEGYKPFVAIYS-TFLQRAYDQVVHDVCIQKLpvlfaidRAGIvgadGETHQGAFDISY 430
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  149 GHC-PGLKVVSPWNSEDAKGLIKSAIR-DNNPVVVL---ENELmyGVPFEFPPEAqskdflIPIGKAKIERQGTHITVVS 223
Cdd:TIGR00204 431 LRCiPNMVIMAPSDENELRQMLYTGYHyDDGPIAVRyprGNAV--GVELTPEPEK------LPIGKSEVLRKGEKILILG 502
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  224 HSRPVGHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEICARIME 293
Cdd:TIGR00204 503 FGTLVPEALEVAESLNEKGIEATVVDARFVKPLDEELILEIAASHEKLVTVEENAIMGGAGSAVLEFLMD 572
PRK12571 PRK12571
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
80-287 1.35e-10

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


Pssm-ID: 183601 [Multi-domain]  Cd Length: 641  Bit Score: 61.28  E-value: 1.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  80 KRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTfNFSMQAIDQVINSAA-----KTYYM--SGV----AAQHSQCF-AAW 147
Cdd:PRK12571 361 NRVFDVGIAEQHAVTFAAGLAAAGLKPFCAVYS-TFLQRGYDQLLHDVAlqnlpVRFVLdrAGLvgadGATHAGAFdLAF 439
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 148 YGHCPGLKVVSPWNSEDAKGLIKSAIRDNNPVVVLENELMYGVPFEFPPEAQskdfLIPIGKAKIERQGTHITVVS---H 224
Cdd:PRK12571 440 LTNLPNMTVMAPRDEAELRHMLRTAAAHDDGPIAVRFPRGEGVGVEIPAEGT----ILGIGKGRVPREGPDVAILSvgaH 515
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 291084858 225 SRPvghCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGGwPQFGVGAEI 287
Cdd:PRK12571 516 LHE---CLDAADLLEAEGISVTVADPRFVKPLDEALTDLLVRHHIVVIVEEQG-AMGGFGAHV 574
PLN02582 PLN02582
1-deoxy-D-xylulose-5-phosphate synthase
81-277 2.36e-10

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


Pssm-ID: 178194 [Multi-domain]  Cd Length: 677  Bit Score: 60.30  E-value: 2.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  81 RIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFnFSMQAIDQVIN-----------SAAKTYYMSGVAAQHSQCFAAWYG 149
Cdd:PLN02582 399 RCFDVGIAEQHAVTFAAGLACEGLKPFCAIYSS-FLQRGYDQVVHdvdlqklpvrfAMDRAGLVGADGPTHCGAFDVTYM 477
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 150 HC-PGLKVVSPWNSEDAKGLIKSAIRDNNPVVVLENELMYGVPFEFPPEaqSKDFLIPIGKAKIERQGTHITVVSHSRPV 228
Cdd:PLN02582 478 AClPNMVVMAPSDEAELFHMVATAAAIDDRPSCFRYPRGNGIGVQLPPN--NKGIPIEVGKGRILLEGERVALLGYGTAV 555
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 291084858 229 GHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGG 277
Cdd:PLN02582 556 QSCLAAASLLERHGLSATVADARFCKPLDRALIRSLAKSHEVLITVEEG 604
PRK12315 PRK12315
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
20-287 1.18e-08

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


Pssm-ID: 237053 [Multi-domain]  Cd Length: 581  Bit Score: 55.01  E-value: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  20 KRRFHWTAPAALQV----------TVRDAINQGMDEELERDEKVFLLGeevAQYDGAYKVSRgLWKKYGDkRIIDTPISE 89
Cdd:PRK12315 255 KEAFHWHMPFDLETgqskvpasgeSYSSVTLDYLLKKIKEGKPVVAIN---AAIPGVFGLKE-FRKKYPD-QYVDVGIAE 329
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  90 MGFAGIAVGAAMAGLRPICeFMTFNFSMQAIDQVI-------NSAAKTYYMSGVAAQ---HSQCFA-AWYGHCPGLKVVS 158
Cdd:PRK12315 330 QESVAFASGIAANGARPVI-FVNSTFLQRAYDQLShdlainnNPAVMIVFGGSISGNdvtHLGIFDiPMISNIPNLVYLA 408
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 159 PWNSEDAKGLIKSAIRDNN-PVVVleneLMYGVPFEFPPEAQSkDFLIPigKAKIERQGTHITVVSHSRPVGHCLEAAAV 237
Cdd:PRK12315 409 PTTKEELIAMLEWALTQHEhPVAI----RVPEHGVESGPTVDT-DYSTL--KYEVTKAGEKVAILALGDFYELGEKVAKK 481
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 291084858 238 LSKE-GVECEVINMRTIRPMDMETIEAsvMKTNH--LVTVEGGWPQFGVGAEI 287
Cdd:PRK12315 482 LKEElGIDATLINPKFITGLDEELLEK--LKEDHelVVTLEDGILDGGFGEKI 532
PLN02225 PLN02225
1-deoxy-D-xylulose-5-phosphate synthase
81-277 4.51e-08

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


Pssm-ID: 177870 [Multi-domain]  Cd Length: 701  Bit Score: 53.18  E-value: 4.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858  81 RIIDTPISEMGFAGIAVGAAMAGLRPICeFMTFNFSMQAIDQVINSA-----AKTYYMSGVAAQHS----QCFA---AWY 148
Cdd:PLN02225 424 RFFNVGMAEQHAVTFSAGLSSGGLKPFC-IIPSAFLQRAYDQVVHDVdrqrkAVRFVITSAGLVGSdgpvQCGAfdiAFM 502
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291084858 149 GHCPGLKVVSPWNSEDAKGLIKSAIR-DNNPVVvlenelmygvpFEFPPEA-QSKDFLIP------IGKAKIERQGTHIT 220
Cdd:PLN02225 503 SSLPNMIAMAPADEDELVNMVATAAYvTDRPVC-----------FRFPRGSiVNMNYLVPtglpieIGRGRVLVEGQDVA 571
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 291084858 221 VVSHSRPVGHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGG 277
Cdd:PLN02225 572 LLGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDIKLVRDLCQNHKFLITVEEG 628
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH