|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
31-355 |
0e+00 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 554.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 31 VQLTVREAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEF 110
Cdd:PRK11892 140 VTMTVREALRDAMAEEMRRDEDVFVMGEEVAEYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGAAFAGLKPIVEF 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 111 MTFNFSMQAIDQVINSAAKTYYMSAGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSA 190
Cdd:PRK11892 220 MTFNFAMQAIDQIINSAAKTLYMSGGQMGCPIVFRGPNGAAARVAAQHSQDYAAWYSHIPGLKVVAPYSAADAKGLLKAA 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 191 IRDDNPVVMLENELMYGVAFELPteaQSKDFLIPIGKAKIERQGTHITVVAHSRPVGHCLEAAAVLSKEGIECEVINLRT 270
Cdd:PRK11892 300 IRDPNPVIFLENEILYGQSFDVP---KLDDFVLPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 271 IRPMDIEAIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEgPAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDII 350
Cdd:PRK11892 377 IRPMDTETIVESVKKTNRLVTVEEGWPQSGVGAEIAARVME-QAFDYLDAPVLRVTGKDVPMPYAANLEKLALPSVAEVV 455
|
....*
gi 56090293 351 FAIKK 355
Cdd:PRK11892 456 EAVKA 460
|
|
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
32-358 |
6.48e-180 |
|
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: 501.47 E-value: 6.48e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 32 QLTVREAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFM 111
Cdd:COG0022 3 ELTYREAINEALREEMERDPRVFVMGEDVGKYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAALAGLRPVVEIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 112 TFNFSMQAIDQVINSAAKTYYMSAGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAI 191
Cdd:COG0022 83 FADFIYPAFDQIVNQAAKLRYMSGGQFKVPMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 192 RDDNPVVMLENELMYGVAFELPTEaqskDFLIPIGKAKIERQGTHITVVAHSRPVGHCLEAAAVLSKEGIECEVINLRTI 271
Cdd:COG0022 163 RDDDPVIFLEHKRLYRLKGEVPEE----DYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 272 RPMDIEAIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEGpAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDIIF 351
Cdd:COG0022 239 SPLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAEE-AFDYLDAPVKRVTGPDTPIPYAPALEKAYLPSADRIVA 317
|
....*..
gi 56090293 352 AIKKTLN 358
Cdd:COG0022 318 AVRELLA 324
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
37-203 |
1.67e-108 |
|
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 [Multi-domain] Cd Length: 167 Bit Score: 314.42 E-value: 1.67e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 37 EAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFS 116
Cdd:cd07036 1 QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 117 MQAIDQVINSAAKTYYMSAGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDDNP 196
Cdd:cd07036 81 LPAFDQIVNEAAKLRYMSGGQFKVPIVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160
|
....*..
gi 56090293 197 VVMLENE 203
Cdd:cd07036 161 VIFLEHK 167
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
32-208 |
1.31e-45 |
|
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: 153.86 E-value: 1.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 32 QLTVREAINQGMDEELERDEKVFLLGEEVAQydGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAG-LRPICEF 110
Cdd:pfam02779 2 KIATRKASGEALAELAKRDPRVVGGGADLAG--GTFTVTKGLLHPQGAGRVIDTGIAEQAMVGFANGMALHGpLLPPVEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 111 MTFNFSMqaidqvINSAAKTYYMSAGLQPVP-IVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKS 189
Cdd:pfam02779 80 TFSDFLN------RADDAIRHGAALGKLPVPfVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRA 153
|
170 180
....*....|....*....|.
gi 56090293 190 AIR--DDNPVVMLENELMYGV 208
Cdd:pfam02779 154 AIRrdGRKPVVLRLPRQLLRP 174
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
83-207 |
7.65e-31 |
|
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: 113.74 E-value: 7.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 83 IDTPISEMGFAGIAVGAAMAGLRPICEFMtFNFSMQAIDQVINSAAktyymsagLQPVPIVFRGPNGASAGV--AAQHSQ 160
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGLRPVVEIF-FTFFDRAKDQIRSAGA--------SGNVPVVFRHDGGGGVGEdgPTHHSI 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 56090293 161 CFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDDNPVVM-LENELMYG 207
Cdd:smart00861 89 EDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIrLERKSLYR 136
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
31-355 |
0e+00 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 554.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 31 VQLTVREAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEF 110
Cdd:PRK11892 140 VTMTVREALRDAMAEEMRRDEDVFVMGEEVAEYQGAYKVTQGLLQEFGARRVIDTPITEHGFAGIGVGAAFAGLKPIVEF 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 111 MTFNFSMQAIDQVINSAAKTYYMSAGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSA 190
Cdd:PRK11892 220 MTFNFAMQAIDQIINSAAKTLYMSGGQMGCPIVFRGPNGAAARVAAQHSQDYAAWYSHIPGLKVVAPYSAADAKGLLKAA 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 191 IRDDNPVVMLENELMYGVAFELPteaQSKDFLIPIGKAKIERQGTHITVVAHSRPVGHCLEAAAVLSKEGIECEVINLRT 270
Cdd:PRK11892 300 IRDPNPVIFLENEILYGQSFDVP---KLDDFVLPIGKARIHREGKDVTIVSFSIGMTYALKAAEELAKEGIDAEVIDLRT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 271 IRPMDIEAIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEgPAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDII 350
Cdd:PRK11892 377 IRPMDTETIVESVKKTNRLVTVEEGWPQSGVGAEIAARVME-QAFDYLDAPVLRVTGKDVPMPYAANLEKLALPSVAEVV 455
|
....*
gi 56090293 351 FAIKK 355
Cdd:PRK11892 456 EAVKA 460
|
|
| PLN02683 |
PLN02683 |
pyruvate dehydrogenase E1 component subunit beta |
6-356 |
0e+00 |
|
pyruvate dehydrogenase E1 component subunit beta
Pssm-ID: 215368 [Multi-domain] Cd Length: 356 Bit Score: 550.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 6 GLVRGPLRQASGLLKRRFhrsAPAAVQLTVREAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDT 85
Cdd:PLN02683 3 GQLLRRTRPAAAAAARGY---ASAAKEMTVRDALNSALDEEMSADPKVFIMGEEVGEYQGAYKITKGLLQKYGPDRVLDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 86 PISEMGFAGIAVGAAMAGLRPICEFMTFNFSMQAIDQVINSAAKTYYMSAGLQPVPIVFRGPNGASAGVAAQHSQCFAAW 165
Cdd:PLN02683 80 PITEAGFTGIGVGAAYAGLKPVVEFMTFNFSMQAIDHIINSAAKTNYMSAGQISVPIVFRGPNGAAAGVGAQHSQCFAAW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 166 YGHCPGLKVVSPWNSEDAKGLIKSAIRDDNPVVMLENELMYGVAFELPTEAQSKDFLIPIGKAKIERQGTHITVVAHSRP 245
Cdd:PLN02683 160 YSSVPGLKVLAPYSSEDARGLLKAAIRDPDPVVFLENELLYGESFPVSAEVLDSSFVLPIGKAKIEREGKDVTIVAFSKM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 246 VGHCLEAAAVLSKEGIECEVINLRTIRPMDIEAIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEgPAFNFLDAPAVRV 325
Cdd:PLN02683 240 VGYALKAAEILAKEGISAEVINLRSIRPLDRDTINASVRKTNRLVTVEEGWPQHGVGAEICASVVE-ESFDYLDAPVERI 318
|
330 340 350
....*....|....*....|....*....|.
gi 56090293 326 TGADVPMPYAKILEDNSIPQVKDIIFAIKKT 356
Cdd:PLN02683 319 AGADVPMPYAANLERLALPQVEDIVRAAKRA 349
|
|
| PTZ00182 |
PTZ00182 |
3-methyl-2-oxobutanate dehydrogenase; Provisional |
1-357 |
0e+00 |
|
3-methyl-2-oxobutanate dehydrogenase; Provisional
Pssm-ID: 185502 [Multi-domain] Cd Length: 355 Bit Score: 533.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 1 MAAVAGLVRGPLRQASGLLKRRFHRSAP--AAVQLTVREAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYG 78
Cdd:PTZ00182 1 ASSFSSTLLGSRLPNSFSSASRSSSTESkgATVKMNVREAINSALDEELARDPKVFVLGEDVAQYGGVYKCTKGLLDKYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 79 DKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFSMQAIDQVINSAAKTYYMSAGLQPVPIVFRGPNGASAGVAAQH 158
Cdd:PTZ00182 81 PDRVFDTPITEQGFAGFAIGAAMNGLRPIAEFMFADFIFPAFDQIVNEAAKYRYMSGGQFDCPIVIRGPNGAVGHGGAYH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 159 SQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDDNPVVMLENELMYGVAFELPTEAqskDFLIPIGKAKIERQGTHIT 238
Cdd:PTZ00182 161 SQSFEAYFAHVPGLKVVAPSDPEDAKGLLKAAIRDPNPVVFFEPKLLYRESVEVVPEA---DYTLPLGKAKVVREGKDVT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 239 VVAHSRPVGHCLEAAAVLSKEGIECEVINLRTIRPMDIEAIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEGpAFNFL 318
Cdd:PTZ00182 238 IVGYGSQVHVALKAAEELAKEGISCEVIDLRSLRPWDRETIVKSVKKTGRCVIVHEAPPTCGIGAEIAAQIMED-CFLYL 316
|
330 340 350
....*....|....*....|....*....|....*....
gi 56090293 319 DAPAVRVTGADVPMPYAKILEDNSIPQVKDIIFAIKKTL 357
Cdd:PTZ00182 317 EAPIKRVCGADTPFPYAKNLEPAYLPDKEKVVEAAKRVL 355
|
|
| PRK09212 |
PRK09212 |
pyruvate dehydrogenase subunit beta; Validated |
32-358 |
0e+00 |
|
pyruvate dehydrogenase subunit beta; Validated
Pssm-ID: 169719 [Multi-domain] Cd Length: 327 Bit Score: 520.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 32 QLTVREAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFM 111
Cdd:PRK09212 3 QLTVREALRDAMQEEMERDPKVFLMGEEVGEYQGAYKVTQGLLEQFGPKRVIDTPITEHGFAGLAVGAAFAGLRPIVEFM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 112 TFNFSMQAIDQVINSAAKTYYMSAGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAI 191
Cdd:PRK09212 83 TFNFSMQAIDQIVNSAAKTNYMSGGQLKCPIVFRGPNGAAARVAAQHSQCYAAWYSHIPGLKVVAPYFAADCKGLLKTAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 192 RDDNPVVMLENELMYGVAFELPTEAQSkdflIPIGKAKIERQGTHITVVAHSRPVGHCLEAAAVLSKEGIECEVINLRTI 271
Cdd:PRK09212 163 RDPNPVIFLENEILYGHSHEVPEEEES----IPIGKAAILREGSDVTIVTFSIQVKLALEAAELLEKEGISVEVIDLRTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 272 RPMDIEAIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEgPAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDIIF 351
Cdd:PRK09212 239 RPLDTETIIESVKKTNRLVVVEEGWPFAGVGAEIAALIMK-EAFDYLDAPVERVTGKDVPLPYAANLEKLALPSEEDIIE 317
|
....*..
gi 56090293 352 AIKKTLN 358
Cdd:PRK09212 318 AVKKVCY 324
|
|
| AcoB |
COG0022 |
Pyruvate/2-oxoglutarate/acetoin dehydrogenase complex, dehydrogenase (E1) component, beta ... |
32-358 |
6.48e-180 |
|
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: 501.47 E-value: 6.48e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 32 QLTVREAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFM 111
Cdd:COG0022 3 ELTYREAINEALREEMERDPRVFVMGEDVGKYGGVFGVTKGLQEKFGPDRVFDTPISEAGIVGAAIGAALAGLRPVVEIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 112 TFNFSMQAIDQVINSAAKTYYMSAGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAI 191
Cdd:COG0022 83 FADFIYPAFDQIVNQAAKLRYMSGGQFKVPMVIRTPYGGGIGAGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 192 RDDNPVVMLENELMYGVAFELPTEaqskDFLIPIGKAKIERQGTHITVVAHSRPVGHCLEAAAVLSKEGIECEVINLRTI 271
Cdd:COG0022 163 RDDDPVIFLEHKRLYRLKGEVPEE----DYTVPLGKARVVREGTDVTIVTYGAMVHRALEAAEELAEEGISAEVIDLRTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 272 RPMDIEAIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEGpAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDIIF 351
Cdd:COG0022 239 SPLDEETILESVKKTGRLVVVDEAPRTGGFGAEIAARIAEE-AFDYLDAPVKRVTGPDTPIPYAPALEKAYLPSADRIVA 317
|
....*..
gi 56090293 352 AIKKTLN 358
Cdd:COG0022 318 AVRELLA 324
|
|
| TPP_PYR_E1-PDHc-beta_like |
cd07036 |
Pyrimidine (PYR) binding domain of the beta subunits of the E1 components of human pyruvate ... |
37-203 |
1.67e-108 |
|
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 [Multi-domain] Cd Length: 167 Bit Score: 314.42 E-value: 1.67e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 37 EAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFS 116
Cdd:cd07036 1 QAINEALDEEMERDPRVVVLGEDVGDYGGVFKVTKGLLDKFGPDRVIDTPIAEAGIVGLAVGAAMNGLRPIVEIMFADFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 117 MQAIDQVINSAAKTYYMSAGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDDNP 196
Cdd:cd07036 81 LPAFDQIVNEAAKLRYMSGGQFKVPIVIRGPNGGGIGGGAQHSQSLEAWFAHIPGLKVVAPSTPYDAKGLLKAAIRDDDP 160
|
....*..
gi 56090293 197 VVMLENE 203
Cdd:cd07036 161 VIFLEHK 167
|
|
| odpB |
CHL00144 |
pyruvate dehydrogenase E1 component beta subunit; Validated |
37-358 |
2.46e-103 |
|
pyruvate dehydrogenase E1 component beta subunit; Validated
Pssm-ID: 177066 [Multi-domain] Cd Length: 327 Bit Score: 307.05 E-value: 2.46e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 37 EAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFS 116
Cdd:CHL00144 8 EALREAIDEEMARDPRVFVIGEDVGHYGGSYKVTKGLHEKYGDLRVLDTPIAENSFTGMAIGAAMTGLRPIVEGMNMGFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 117 MQAIDQVINSAAKTYYMSAGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVV---SPWNsedAKGLIKSAIRD 193
Cdd:CHL00144 88 LLAFNQISNNAGMLHYTSGGNFTIPIVIRGPGGVGRQLGAEHSQRLESYFQSVPGLQIVacsTPYN---AKGLLKSAIRS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 194 DNPVVMLENELMYGVAFELPTEaqskDFLIPIGKAKIERQGTHITVVAHSRPVGHCLEAAAVLSKEGIECEVINLRTIRP 273
Cdd:CHL00144 165 NNPVIFFEHVLLYNLKEEIPDN----EYLLPLEKAEVVRPGNDITILTYSRMRHHVLQAVKVLVEKGYDPEIIDLISLKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 274 MDIEAIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEGpAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDIIFAI 353
Cdd:CHL00144 241 LDLGTISKSVKKTHKVLIVEECMKTGGIGAELIAQINEH-LFDELDAPIVRLSSQDVPTPYNGPLEEATVIQPAQIIEAV 319
|
....*
gi 56090293 354 KKTLN 358
Cdd:CHL00144 320 EQIIT 324
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
32-208 |
1.31e-45 |
|
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: 153.86 E-value: 1.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 32 QLTVREAINQGMDEELERDEKVFLLGEEVAQydGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAG-LRPICEF 110
Cdd:pfam02779 2 KIATRKASGEALAELAKRDPRVVGGGADLAG--GTFTVTKGLLHPQGAGRVIDTGIAEQAMVGFANGMALHGpLLPPVEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 111 MTFNFSMqaidqvINSAAKTYYMSAGLQPVP-IVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKS 189
Cdd:pfam02779 80 TFSDFLN------RADDAIRHGAALGKLPVPfVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRA 153
|
170 180
....*....|....*....|.
gi 56090293 190 AIR--DDNPVVMLENELMYGV 208
Cdd:pfam02779 154 AIRrdGRKPVVLRLPRQLLRP 174
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
226-349 |
6.51e-45 |
|
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: 150.44 E-value: 6.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 226 GKAKIERQGTHITVVAHSRPVGHCLEAAAVLSKEGIECEVINLRTIRPMDIEAIEASVMKTNHLVTVEGGWPQFGVGAEI 305
Cdd:pfam02780 1 GKAEILREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETILESVKKTGRLVTVEEAVPRGGFGSEV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 56090293 306 CARIMEgPAFNFLDAPAVRVTGADVPMPY-AKILEDNSIPQVKDI 349
Cdd:pfam02780 81 AAALAE-EAFDGLDAPVLRVGGPDFPEPGsADELEKLYGLTPEKI 124
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
38-203 |
1.00e-31 |
|
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: 117.06 E-value: 1.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 38 AINQGMDEELerdeKVFLLGEEVAQYdgayKVSRGLWKKyGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFSM 117
Cdd:cd06586 2 AFAEVLTAWG----VRHVFGYPGDEI----SSLLDALRE-GDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTSGTGLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 118 QAIDQVInsaaktyymSAGLQPVPIVFR-GPNGASAGV-AAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDDN 195
Cdd:cd06586 73 NAINGLA---------DAAAEHLPVVFLiGARGISAQAkQTFQSMFDLGMYRSIPEANISSPSPAELPAGIDHAIRTAYA 143
|
170
....*....|.
gi 56090293 196 ---PVVMLENE 203
Cdd:cd06586 144 sqgPVVVRLPR 154
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
83-207 |
7.65e-31 |
|
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: 113.74 E-value: 7.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 83 IDTPISEMGFAGIAVGAAMAGLRPICEFMtFNFSMQAIDQVINSAAktyymsagLQPVPIVFRGPNGASAGV--AAQHSQ 160
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGLRPVVEIF-FTFFDRAKDQIRSAGA--------SGNVPVVFRHDGGGGVGEdgPTHHSI 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 56090293 161 CFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDDNPVVM-LENELMYG 207
Cdd:smart00861 89 EDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDDGPVVIrLERKSLYR 136
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
32-293 |
4.73e-29 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 114.03 E-value: 4.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 32 QLTVREAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSrglwKKYGDkRIIDTPISEMGFAGIAVGAAMAGLRPICefM 111
Cdd:COG3958 3 KKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFA----KAFPD-RFFNVGIAEQNMVGVAAGLALAGKIPFV--S 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 112 TF-NF-SMQAIDQVINSAAktyYMSAglqPVPIVfrgpnGASAGVAAQHS----QCFA--AWYGHCPGLKVVSPWNSEDA 183
Cdd:COG3958 76 TFaPFlTGRAYEQIRNDIA---YPNL---NVKIV-----GSHAGLSYGEDgathQALEdiALMRALPNMTVIVPADAVET 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 184 KGLIKSAIRDDNPVVMlenELMYGVAFELPTEaqskDFLIPIGKAKIERQGTHITVVAHSRPVGHCLEAAAVLSKEGIEC 263
Cdd:COG3958 145 EAAVRAAAEHDGPVYL---RLGRGAVPVVYDE----DYEFEIGKARVLREGKDVTIIATGIMVAEALEAAELLAKEGISA 217
|
250 260 270
....*....|....*....|....*....|
gi 56090293 264 EVINLRTIRPMDIEAIEASVMKTNHLVTVE 293
Cdd:COG3958 218 RVINMHTIKPLDEEAILKAARKTGAVVTAE 247
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
37-199 |
3.54e-22 |
|
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: 91.35 E-value: 3.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 37 EAINQGMDEELERDEKVFLLGEEVAQYDGAYKvsrgLWKKYGDkRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFnFS 116
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDK----FAKKFPD-RFIDVGIAEQNMVGIAAGLALHGLKPFVSTFSF-FL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 117 MQAIDQVINSAAktyymsagLQPVPIVFRGpNGASAGVAA----QHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIR 192
Cdd:cd07033 75 QRAYDQIRHDVA--------LQNLPVKFVG-THAGISVGEdgptHQGIEDIALLRAIPNMTVLRPADANETAAALEAALE 145
|
....*..
gi 56090293 193 DDNPVVM 199
Cdd:cd07033 146 YDGPVYI 152
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
75-311 |
7.24e-21 |
|
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: 93.92 E-value: 7.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 75 KKYGDkRIIDTPISE---MGFAGiavGAAMAGLRPICE-FMTFnfsMQ-AIDQVInsaaktyyMSAGLQPVPIVF---R- 145
Cdd:COG1154 355 ERFPD-RFFDVGIAEqhaVTFAA---GLATEGLKPVVAiYSTF---LQrAYDQVI--------HDVALQNLPVTFaidRa 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 146 ---GPNGAS-AGVaaqhsqcF-AAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDDNPVVmleneLMY----GVAFELPTEA 216
Cdd:COG1154 420 glvGADGPThHGV-------FdLSYLRCIPNMVIMAPKDENELRHMLYTALAYDGPTA-----IRYprgnGPGVELPAEL 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 217 QSkdflIPIGKAKIERQGTHITVVAHSRPVGHCLEAAAVLSKEGIECEVINLRTIRPMDIEAIEASVMKTNHLVTVEGGW 296
Cdd:COG1154 488 EP----LPIGKGEVLREGKDVAILAFGTMVAEALEAAERLAAEGISATVVDARFVKPLDEELILELAREHDLVVTVEEGV 563
|
250
....*....|....*
gi 56090293 297 PQFGVGAEICARIME 311
Cdd:COG1154 564 LAGGFGSAVLEFLAD 578
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
73-311 |
1.22e-16 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 80.90 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 73 LWKKYGDkRIIDTPISE---MGFAGiavGAAMAGLRPICE-FMTFnfsMQ-AIDQVInsaaktyyMSAGLQPVPIVF--- 144
Cdd:PRK05444 315 FSKRFPD-RYFDVGIAEqhaVTFAA---GLATEGLKPVVAiYSTF---LQrAYDQVI--------HDVALQNLPVTFaid 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 145 R----GPNGASagvaaqHSQCF-AAWYGHCPGLKVVSPWNSEDAKGLIKSAIR-DDNPVVMlenelMY----GVAFELPT 214
Cdd:PRK05444 380 RaglvGADGPT------HQGAFdLSYLRCIPNMVIMAPSDENELRQMLYTALAyDDGPIAI-----RYprgnGVGVELPE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 215 EAQskdflIPIGKAKIERQGTHITVVAHSRPVGHCLEAAAVLSkegiECEVINLRTIRPMDIEAIEASVMKTNHLVTVEG 294
Cdd:PRK05444 449 LEP-----LPIGKGEVLREGEDVAILAFGTMLAEALKAAERLA----SATVVDARFVKPLDEELLLELAAKHDLVVTVEE 519
|
250
....*....|....*..
gi 56090293 295 GWPQFGVGAEICARIME 311
Cdd:PRK05444 520 GAIMGGFGSAVLEFLAD 536
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
81-295 |
2.54e-15 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 77.06 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 81 RIIDTPISEMGFAGIAVGAAMAGLRPICEFMTfNFSMQAIDQVINSAaktyymsaGLQPVPIVFRGPNGASAGV-AAQHS 159
Cdd:PLN02234 400 RCFDVGIAEQHAVTFAAGLACEGLKPFCTIYS-SFMQRAYDQVVHDV--------DLQKLPVRFAIDRAGLMGAdGPTHC 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 160 QCFAAWYGHC-PGLKVVSPWNSEDAKGLIKSAIRDDNPVVMLENELMYGVAFELPteAQSKDFLIPIGKAKIERQGTHIT 238
Cdd:PLN02234 471 GAFDVTFMAClPNMIVMAPSDEAELFNMVATAAAIDDRPSCFRYHRGNGIGVSLP--PGNKGVPLQIGRGRILRDGERVA 548
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 56090293 239 VVAHSRPVGHCLEAAAVLSKEGIECEVINLRTIRPMDIEAIEASVMKTNHLVTVEGG 295
Cdd:PLN02234 549 LLGYGSAVQRCLEAASMLSERGLKITVADARFCKPLDVALIRSLAKSHEVLITVEEG 605
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
80-305 |
2.92e-13 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 70.91 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 80 KRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTfNFSMQAIDQVInsaaktyyMSAGLQPVPIVF-------RGPNGASa 152
Cdd:PRK12571 361 NRVFDVGIAEQHAVTFAAGLAAAGLKPFCAVYS-TFLQRGYDQLL--------HDVALQNLPVRFvldraglVGADGAT- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 153 gvaaqHSQCF-AAWYGHCPGLKVVSPWNSEDAKGLIKSAI-RDDNPVVmleneLMY----GVAFELPTEAQskdfLIPIG 226
Cdd:PRK12571 431 -----HAGAFdLAFLTNLPNMTVMAPRDEAELRHMLRTAAaHDDGPIA-----VRFprgeGVGVEIPAEGT----ILGIG 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 227 KAKIERQGTHITVV---AHSRPvghCLEAAAVLSKEGIECEVINLRTIRPMDiEAIEASVMKTNHLVTVEGGWPQFGVGA 303
Cdd:PRK12571 497 KGRVPREGPDVAILsvgAHLHE---CLDAADLLEAEGISVTVADPRFVKPLD-EALTDLLVRHHIVVIVEEQGAMGGFGA 572
|
..
gi 56090293 304 EI 305
Cdd:PRK12571 573 HV 574
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
81-295 |
2.66e-12 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 68.00 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 81 RIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFnFSMQAIDQVINSAaktyymsaGLQPVPIVFRGPNGASAGV-AAQHS 159
Cdd:PLN02582 399 RCFDVGIAEQHAVTFAAGLACEGLKPFCAIYSS-FLQRGYDQVVHDV--------DLQKLPVRFAMDRAGLVGAdGPTHC 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 160 QCFAAWYGHC-PGLKVVSPWNSEDAKGLIKSAIRDDNPVVMLENELMYGVAFELPteAQSKDFLIPIGKAKIERQGTHIT 238
Cdd:PLN02582 470 GAFDVTYMAClPNMVVMAPSDEAELFHMVATAAAIDDRPSCFRYPRGNGIGVQLP--PNNKGIPIEVGKGRILLEGERVA 547
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 56090293 239 VVAHSRPVGHCLEAAAVLSKEGIECEVINLRTIRPMDIEAIEASVMKTNHLVTVEGG 295
Cdd:PLN02582 548 LLGYGTAVQSCLAAASLLERHGLSATVADARFCKPLDRALIRSLAKSHEVLITVEEG 604
|
|
| PLN02225 |
PLN02225 |
1-deoxy-D-xylulose-5-phosphate synthase |
81-295 |
4.29e-08 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177870 [Multi-domain] Cd Length: 701 Bit Score: 54.72 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 81 RIIDTPISEMGFAGIAVGAAMAGLRPICeFMTFNFSMQAIDQVIN------SAAKTYYMSAGLQpvpivfrGPNGASagv 154
Cdd:PLN02225 424 RFFNVGMAEQHAVTFSAGLSSGGLKPFC-IIPSAFLQRAYDQVVHdvdrqrKAVRFVITSAGLV-------GSDGPV--- 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 155 aaqhsQCFA---AWYGHCPGLKVVSPWNSEDAKGLIKSAIR-DDNPVvmlenelmygvAFELPTEA-QSKDFLIP----- 224
Cdd:PLN02225 493 -----QCGAfdiAFMSSLPNMIAMAPADEDELVNMVATAAYvTDRPV-----------CFRFPRGSiVNMNYLVPtglpi 556
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56090293 225 -IGKAKIERQGTHITVVAHSRPVGHCLEAAAVLSKEGIECEVINLRTIRPMDIEAIEASVMKTNHLVTVEGG 295
Cdd:PLN02225 557 eIGRGRVLVEGQDVALLGYGAMVQNCLHAHSLLSKLGLNVTVADARFCKPLDIKLVRDLCQNHKFLITVEEG 628
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
20-305 |
2.44e-07 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 52.32 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 20 KRRFHRSAP----------AAVQLTVREAINQGMDEELERDEKVFLLGeevAQYDGAYKVSRgLWKKYGDkRIIDTPISE 89
Cdd:PRK12315 255 KEAFHWHMPfdletgqskvPASGESYSSVTLDYLLKKIKEGKPVVAIN---AAIPGVFGLKE-FRKKYPD-QYVDVGIAE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 90 MGFAGIAVGAAMAGLRPICeFMTFNFSMQAIDQVINSaaktyyMSAGLQPVPIVFRGpnGASAGVAAQHSQCFA-AWYGH 168
Cdd:PRK12315 330 QESVAFASGIAANGARPVI-FVNSTFLQRAYDQLSHD------LAINNNPAVMIVFG--GSISGNDVTHLGIFDiPMISN 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56090293 169 CPGLKVVSPWNSEDAKGLIKSAIRD-DNPVV--MLENELMYGvafelptEAQSKDFLIPigKAKIERQGTHITVVAHSRP 245
Cdd:PRK12315 401 IPNLVYLAPTTKEELIAMLEWALTQhEHPVAirVPEHGVESG-------PTVDTDYSTL--KYEVTKAGEKVAILALGDF 471
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56090293 246 VGHCLEAAAVLSKE-GIECEVINLRTIRPMDIEAIEAsvMKTNH--LVTVEGGWPQFGVGAEI 305
Cdd:PRK12315 472 YELGEKVAKKLKEElGIDATLINPKFITGLDEELLEK--LKEDHelVVTLEDGILDGGFGEKI 532
|
|
| |
