|
Name |
Accession |
Description |
Interval |
E-value |
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
7-668 |
0e+00 |
|
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway/BioSystem: Pentose phosphate pathway
Pssm-ID: 439792 [Multi-domain] Cd Length: 661 Bit Score: 1246.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 7 QTMANAIRALAMDAVQKAKSGHPGMPMGMADIATALWTRHLRFNPQDPKWSGRDRFILSNGHGSMLQYALLHLTGFDLSM 86
Cdd:COG0021 5 QLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKHNPANPKWPNRDRFVLSAGHGSMLLYSLLHLTGYDLSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 87 DDLKAFRQLGSRTPGHPEVDITPGVETTTGPLGQGIANGVGMALAEKLLAAEFNRDGFPVVDNRTYVFLGDGCLMEGISH 166
Cdd:COG0021 85 DDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGIANAVGMAIAERHLAARFNRPGHDIVDHYTYVIAGDGDLMEGISH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 167 EVCSLAGVWKLNKLIALYDDNGISIDGDVRGWFRDDTRGRFEAYGWNVIGPVDGHDINAVDQAIAQAKESAEKPTLIICR 246
Cdd:COG0021 165 EAASLAGHLKLGKLIVLYDDNGISIDGDTDLAFSEDVAKRFEAYGWHVIRVEDGHDLEAIDAAIEAAKAETDKPTLIICK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 247 TTIGKGSPNRQGTAKVHGEALGDEEIAATKAALGWTYGPFEIPQDVYAAWDHRAE-GAKVEKEWQQTYAGYKAAYPELAK 325
Cdd:COG0021 245 TIIGYGSPNKQGTAKAHGAPLGAEEIAATKEALGWPPEPFEVPDEVYAHWRAAGErGAAAEAEWNERFAAYAAAYPELAA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 326 ELERRLAGDLPDQWDAAVMDAVcqaaEAAETVATRKASQKALNALAPVLPELLGGSADLTGSNLTNWSGSTSLNTGDFHA 405
Cdd:COG0021 325 ELERRLAGELPEDWDAALPAFE----ADAKGVATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIKGAGSFSPEDPSG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 406 RHISYGVREFGMSAILNGIALYGGFIPYGATFLTFSDYSRNALRMSALMNLRAINVFTHDSIGLGEDGPTHQSVEHIPSL 485
Cdd:COG0021 401 RNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFSDYMRPAIRLAALMKLPVIYVFTHDSIGLGEDGPTHQPVEQLASL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 486 RLIPGMDVWRPCDTVESVVAWASAIERRDGASCLIFSRQNAAFIDRDEVDADAIAMGGYVVAEAplgEGEAQVVLLATGT 565
Cdd:COG0021 481 RAIPNLDVIRPADANETAAAWKLALERKDGPTALILSRQNLPTLDRTAAAAEGVAKGAYVLADA---EGTPDVILIATGS 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 566 EVGLAMDARAKLAALNINARVVSMPCTNRFDRQSTEYRQSVLPPGL-PVLAIEASKTDLWWKYFTGRGDVLGVDSFGESA 644
Cdd:COG0021 558 EVSLAVEAAELLAAEGIKVRVVSMPSWELFEAQDAAYRESVLPPAVrARVAVEAGVTDGWYKYVGLDGAVIGIDTFGASA 637
|
650 660
....*....|....*....|....
gi 512181214 645 PAKDLWIKFGFTVDNVVSKVEALL 668
Cdd:COG0021 638 PAKVLFEEFGFTVENVVAAAKELL 661
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
9-668 |
0e+00 |
|
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial transketolases. The group includes two from the yeast Saccharomyces cerevisiae but excludes dihydroxyactetone synthases (formaldehyde transketolases) from various yeasts and the even more distant mammalian transketolases. Among the family of thiamine diphosphate-dependent enzymes that includes transketolases, dihydroxyacetone synthases, pyruvate dehydrogenase E1-beta subunits, and deoxyxylulose-5-phosphate synthases, mammalian and bacterial transketolases seem not to be orthologous. [Energy metabolism, Pentose phosphate pathway]
Pssm-ID: 272974 [Multi-domain] Cd Length: 653 Bit Score: 993.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 9 MANAIRALAMDAVQKAKSGHPGMPMGMADIATALWTRHLRFNPQDPKWSGRDRFILSNGHGSMLQYALLHLTGFDLSMDD 88
Cdd:TIGR00232 3 LANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKFNPTNPKWINRDRFVLSNGHGSMLLYSLLHLTGYDLSIED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 89 LKAFRQLGSRTPGHPEVDITPGVETTTGPLGQGIANGVGMALAEKLLAAEFNRDGFPVVDNRTYVFLGDGCLMEGISHEV 168
Cdd:TIGR00232 83 LKQFRQLHSKTPGHPEYGHTAGVEATTGPLGQGIANAVGMAIAEKTLAATFNKPGFEIVDHYTYVFVGDGCLQEGISYEV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 169 CSLAGVWKLNKLIALYDDNGISIDGDVRGWFRDDTRGRFEAYGWNVIGPVDGHDINAVDQAIAQAKESAEKPTLIICRTT 248
Cdd:TIGR00232 163 ASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDVAKRFEAYGWEVLEVEDGHDLAAIDAAIEEAKASTDKPTLIEVKTT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 249 IGKGSPNRQGTAKVHGEALGDEEIAATKAALGWTYGPFEIPQDVY--AAWDHRAEGAKVEKEWQQTYAGYKAAYPELAKE 326
Cdd:TIGR00232 243 IGFGSPNKAGTHGVHGAPLGDEEVALTKKNLGWNYNPFEIPQEVYdhFKKTVKERGAKAEQEWNELFAAYKKKYPELAAE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 327 LERRLAGDLPDQWDAAVMdavcQAAEAAETVATRKASQKALNALAPVLPELLGGSADLTGSNLTNWSGSTSLNTgDFHAR 406
Cdd:TIGR00232 323 FTRRLSGELPADWDKQLP----EFKVKLQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKGSGDLHE-NPLGN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 407 HISYGVREFGMSAILNGIALYGGFIPYGATFLTFSDYSRNALRMSALMNLRAINVFTHDSIGLGEDGPTHQSVEHIPSLR 486
Cdd:TIGR00232 398 YIHYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQLASLR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 487 LIPGMDVWRPCDTVESVVAWASAIERRDGASCLIFSRQNAAFIdrDEVDADAIAMGGYVVAEAplgeGEAQVVLLATGTE 566
Cdd:TIGR00232 478 AIPNLSVWRPCDGNETAAAWKYALESQDGPTALILSRQNLPQL--EESSLEKVLKGGYVLKDS----KGPDLILIATGSE 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 567 VGLAMDARAKLAALNINARVVSMPCTNRFDRQSTEYRQSVLPPGLPVLAIEASKTDLWWKYFTGRGDVLGVDSFGESAPA 646
Cdd:TIGR00232 552 VQLAVEAAKKLAAENIKVRVVSMPSFDLFDKQDEEYRESVLPANVTRLAIEAGAADEWYKYAGLVGAILGMDSFGESAPG 631
|
650 660
....*....|....*....|..
gi 512181214 647 KDLWIKFGFTVDNVVSKVEALL 668
Cdd:TIGR00232 632 DKLFEEFGFTVENVVAKAKKLL 653
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
1-668 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 990.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 1 MSQVSPQTMANAIRALAMDAVQKAKSGHPGMPMGMADIATALWTRHLRFNPQDPKWSGRDRFILSNGHGSMLQYALLHLT 80
Cdd:PRK05899 3 MDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLHLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 81 GFDLSMDDLKAFRQLGSRTPGHPEVDITPGVETTTGPLGQGIANGVGMALAEKLLAAEFNRDGFPVVDNRTYVFLGDGCL 160
Cdd:PRK05899 83 GYDLSIDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGLANAVGMALAEKYLAALFNRPGLDIVDHYTYVLCGDGDL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 161 MEGISHEVCSLAGVWKLNKLIALYDDNGISIDGDVRGWFRDDTRGRFEAYGWNVIgPVDGHDINAVDQAIAQAKESaEKP 240
Cdd:PRK05899 163 MEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTEDVKKRFEAYGWHVI-EVDGHDVEAIDAAIEEAKAS-TKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 241 TLIICRTTIGKGSPNRQGTAKVHGEALGDEEIAATKAALGWTYgpfeipqdvyaawdhraegakvekewqqtyagykaay 320
Cdd:PRK05899 241 TLIIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAAAKKELGWDY------------------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 321 pelakelerrlagdlpdqwdaavmdavcqaaeaaetvatRKASQKALNALAPVLPELLGGSADLTGSNLTNWSGSTSLNT 400
Cdd:PRK05899 284 ---------------------------------------RKASGKALNALAKALPELVGGSADLAGSNNTKIKGSKDFAP 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 401 GDFHARHISYGVREFGMSAILNGIALYGGFIPYGATFLTFSDYSRNALRMSALMNLRAINVFTHDSIGLGEDGPTHQSVE 480
Cdd:PRK05899 325 EDYSGRYIHYGVREFAMAAIANGLALHGGFIPFGGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVE 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 481 HIPSLRLIPGMDVWRPCDTVESVVAWASAIERRDGASCLIFSRQNAAFIDRDEvDADAIAMGGYVVAEAPlgegeaQVVL 560
Cdd:PRK05899 405 QLASLRAIPNLTVIRPADANETAAAWKYALERKDGPSALVLTRQNLPVLERTA-QEEGVAKGGYVLRDDP------DVIL 477
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 561 LATGTEVGLAMDARAKLAALNINARVVSMPCTNRFDRQSTEYRQSVLPPGLPV-LAIEASKTDLWWKYFTGRGDVLGVDS 639
Cdd:PRK05899 478 IATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQDAAYKESVLPAAVTArVAVEAGVADGWYKYVGLDGKVLGIDT 557
|
650 660
....*....|....*....|....*....
gi 512181214 640 FGESAPAKDLWIKFGFTVDNVVSKVEALL 668
Cdd:PRK05899 558 FGASAPADELFKEFGFTVENIVAAAKELL 586
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
5-336 |
0e+00 |
|
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes EC:2.2.1.1. and also partially matches to 2-oxoisovalerate dehydrogenase beta subunit EC:1.2.4.4. Both these enzymes utilize thiamine pyrophosphate as a cofactor, suggesting there may be common aspects in their mechanism of catalysis.
Pssm-ID: 395366 [Multi-domain] Cd Length: 334 Bit Score: 570.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 5 SPQTMANAIRALAMDAVQKAKSGHPGMPMGMADIATALWTRHLRFNPQDPKWSGRDRFILSNGHGSMLQYALLHLTGFDL 84
Cdd:pfam00456 1 IDKRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 85 SMDDLKAFRQLGSRTPGHPEVDITPGVETTTGPLGQGIANGVGMALAEKLLAAEFNRDGFPVVDNRTYVFLGDGCLMEGI 164
Cdd:pfam00456 81 SMEDLKSFRQLGSKTPGHPEFGHTAGVEVTTGPLGQGIANAVGMAIAERNLAATYNRPGFDIVDHYTYVFLGDGCLMEGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 165 SHEVCSLAGVWKLNKLIALYDDNGISIDGDVRGWFRDDTRGRFEAYGWNVIGPVDGHDINAVDQAIAQAKESAEKPTLII 244
Cdd:pfam00456 161 SSEASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDTAARFEAYGWHVIEVEDGHDVEAIAAAIEEAKAEKDKPTLIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 245 CRTTIGKGSPNRQGTAKVHGEALGDEEIAATKAALGW-TYGPFEIPQDVYAAWD-HRAEGAKVEKEWQQTYAGYKAAYPE 322
Cdd:pfam00456 241 CRTVIGYGSPNKQGTHDVHGAPLGADEVAALKQKLGWdPYKPFEIPAEVYDAWKeKVAEGAKAEAEWNELFAAYKKAYPE 320
|
330
....*....|....
gi 512181214 323 LAKELERRLAGDLP 336
Cdd:pfam00456 321 LAAEFARRLSGELP 334
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
11-276 |
2.58e-148 |
|
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.
Pssm-ID: 238970 [Multi-domain] Cd Length: 255 Bit Score: 430.39 E-value: 2.58e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 11 NAIRALAMDAVQKAKSGHPGMPMGMADIATALWTRHLRFNPQDPKWSGRDRFILSNGHGSMLQYALLHLTGFdLSMDDLK 90
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGY-LPEEDLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 91 AFRQLGSRTPGHPEVDITPGVETTTGPLGQGIANGVGMALAEKLLaaefnrdgfpVVDNRTYVFLGDGCLMEGISHEVCS 170
Cdd:cd02012 80 TFRQLGSRLPGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEKLL----------GFDYRVYVLLGDGELQEGSVWEAAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 171 LAGVWKLNKLIALYDDNGISIDGDVRG-WFRDDTRGRFEAYGWNVIgPVDGHDINAVDQAIAQAKESAEKPTLIICRTTI 249
Cdd:cd02012 150 FAGHYKLDNLIAIVDSNRIQIDGPTDDiLFTEDLAKKFEAFGWNVI-EVDGHDVEEILAALEEAKKSKGKPTLIIAKTIK 228
|
250 260
....*....|....*....|....*..
gi 512181214 250 GKGSPNRQGTAKVHGEALGDEEIAATK 276
Cdd:cd02012 229 GKGVPFMENTAKWHGKPLGEEEVELAK 255
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
408-525 |
5.62e-36 |
|
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: 131.84 E-value: 5.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 408 ISYGVREFGMSAILNGIALYGGfIPYGATFLTFSDYSRNALRMSALMNlRAINVFTHDS-IGLGEDGPTHQSVEHIPSLR 486
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFFDRAKDQIRSAGASG-NVPVVFRHDGgGGVGEDGPTHHSIEDEALLR 95
|
90 100 110
....*....|....*....|....*....|....*....
gi 512181214 487 LIPGMDVWRPCDTVESVVAWASAIeRRDGASCLIFSRQN 525
Cdd:smart00861 96 AIPGLKVVAPSDPAEAKGLLRAAI-RDDGPVVIRLERKS 133
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
7-668 |
0e+00 |
|
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway/BioSystem: Pentose phosphate pathway
Pssm-ID: 439792 [Multi-domain] Cd Length: 661 Bit Score: 1246.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 7 QTMANAIRALAMDAVQKAKSGHPGMPMGMADIATALWTRHLRFNPQDPKWSGRDRFILSNGHGSMLQYALLHLTGFDLSM 86
Cdd:COG0021 5 QLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKHNPANPKWPNRDRFVLSAGHGSMLLYSLLHLTGYDLSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 87 DDLKAFRQLGSRTPGHPEVDITPGVETTTGPLGQGIANGVGMALAEKLLAAEFNRDGFPVVDNRTYVFLGDGCLMEGISH 166
Cdd:COG0021 85 DDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGIANAVGMAIAERHLAARFNRPGHDIVDHYTYVIAGDGDLMEGISH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 167 EVCSLAGVWKLNKLIALYDDNGISIDGDVRGWFRDDTRGRFEAYGWNVIGPVDGHDINAVDQAIAQAKESAEKPTLIICR 246
Cdd:COG0021 165 EAASLAGHLKLGKLIVLYDDNGISIDGDTDLAFSEDVAKRFEAYGWHVIRVEDGHDLEAIDAAIEAAKAETDKPTLIICK 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 247 TTIGKGSPNRQGTAKVHGEALGDEEIAATKAALGWTYGPFEIPQDVYAAWDHRAE-GAKVEKEWQQTYAGYKAAYPELAK 325
Cdd:COG0021 245 TIIGYGSPNKQGTAKAHGAPLGAEEIAATKEALGWPPEPFEVPDEVYAHWRAAGErGAAAEAEWNERFAAYAAAYPELAA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 326 ELERRLAGDLPDQWDAAVMDAVcqaaEAAETVATRKASQKALNALAPVLPELLGGSADLTGSNLTNWSGSTSLNTGDFHA 405
Cdd:COG0021 325 ELERRLAGELPEDWDAALPAFE----ADAKGVATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIKGAGSFSPEDPSG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 406 RHISYGVREFGMSAILNGIALYGGFIPYGATFLTFSDYSRNALRMSALMNLRAINVFTHDSIGLGEDGPTHQSVEHIPSL 485
Cdd:COG0021 401 RNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFSDYMRPAIRLAALMKLPVIYVFTHDSIGLGEDGPTHQPVEQLASL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 486 RLIPGMDVWRPCDTVESVVAWASAIERRDGASCLIFSRQNAAFIDRDEVDADAIAMGGYVVAEAplgEGEAQVVLLATGT 565
Cdd:COG0021 481 RAIPNLDVIRPADANETAAAWKLALERKDGPTALILSRQNLPTLDRTAAAAEGVAKGAYVLADA---EGTPDVILIATGS 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 566 EVGLAMDARAKLAALNINARVVSMPCTNRFDRQSTEYRQSVLPPGL-PVLAIEASKTDLWWKYFTGRGDVLGVDSFGESA 644
Cdd:COG0021 558 EVSLAVEAAELLAAEGIKVRVVSMPSWELFEAQDAAYRESVLPPAVrARVAVEAGVTDGWYKYVGLDGAVIGIDTFGASA 637
|
650 660
....*....|....*....|....
gi 512181214 645 PAKDLWIKFGFTVDNVVSKVEALL 668
Cdd:COG0021 638 PAKVLFEEFGFTVENVVAAAKELL 661
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
9-668 |
0e+00 |
|
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial transketolases. The group includes two from the yeast Saccharomyces cerevisiae but excludes dihydroxyactetone synthases (formaldehyde transketolases) from various yeasts and the even more distant mammalian transketolases. Among the family of thiamine diphosphate-dependent enzymes that includes transketolases, dihydroxyacetone synthases, pyruvate dehydrogenase E1-beta subunits, and deoxyxylulose-5-phosphate synthases, mammalian and bacterial transketolases seem not to be orthologous. [Energy metabolism, Pentose phosphate pathway]
Pssm-ID: 272974 [Multi-domain] Cd Length: 653 Bit Score: 993.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 9 MANAIRALAMDAVQKAKSGHPGMPMGMADIATALWTRHLRFNPQDPKWSGRDRFILSNGHGSMLQYALLHLTGFDLSMDD 88
Cdd:TIGR00232 3 LANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKFNPTNPKWINRDRFVLSNGHGSMLLYSLLHLTGYDLSIED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 89 LKAFRQLGSRTPGHPEVDITPGVETTTGPLGQGIANGVGMALAEKLLAAEFNRDGFPVVDNRTYVFLGDGCLMEGISHEV 168
Cdd:TIGR00232 83 LKQFRQLHSKTPGHPEYGHTAGVEATTGPLGQGIANAVGMAIAEKTLAATFNKPGFEIVDHYTYVFVGDGCLQEGISYEV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 169 CSLAGVWKLNKLIALYDDNGISIDGDVRGWFRDDTRGRFEAYGWNVIGPVDGHDINAVDQAIAQAKESAEKPTLIICRTT 248
Cdd:TIGR00232 163 ASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDVAKRFEAYGWEVLEVEDGHDLAAIDAAIEEAKASTDKPTLIEVKTT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 249 IGKGSPNRQGTAKVHGEALGDEEIAATKAALGWTYGPFEIPQDVY--AAWDHRAEGAKVEKEWQQTYAGYKAAYPELAKE 326
Cdd:TIGR00232 243 IGFGSPNKAGTHGVHGAPLGDEEVALTKKNLGWNYNPFEIPQEVYdhFKKTVKERGAKAEQEWNELFAAYKKKYPELAAE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 327 LERRLAGDLPDQWDAAVMdavcQAAEAAETVATRKASQKALNALAPVLPELLGGSADLTGSNLTNWSGSTSLNTgDFHAR 406
Cdd:TIGR00232 323 FTRRLSGELPADWDKQLP----EFKVKLQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKGSGDLHE-NPLGN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 407 HISYGVREFGMSAILNGIALYGGFIPYGATFLTFSDYSRNALRMSALMNLRAINVFTHDSIGLGEDGPTHQSVEHIPSLR 486
Cdd:TIGR00232 398 YIHYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQLASLR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 487 LIPGMDVWRPCDTVESVVAWASAIERRDGASCLIFSRQNAAFIdrDEVDADAIAMGGYVVAEAplgeGEAQVVLLATGTE 566
Cdd:TIGR00232 478 AIPNLSVWRPCDGNETAAAWKYALESQDGPTALILSRQNLPQL--EESSLEKVLKGGYVLKDS----KGPDLILIATGSE 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 567 VGLAMDARAKLAALNINARVVSMPCTNRFDRQSTEYRQSVLPPGLPVLAIEASKTDLWWKYFTGRGDVLGVDSFGESAPA 646
Cdd:TIGR00232 552 VQLAVEAAKKLAAENIKVRVVSMPSFDLFDKQDEEYRESVLPANVTRLAIEAGAADEWYKYAGLVGAILGMDSFGESAPG 631
|
650 660
....*....|....*....|..
gi 512181214 647 KDLWIKFGFTVDNVVSKVEALL 668
Cdd:TIGR00232 632 DKLFEEFGFTVENVVAKAKKLL 653
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
1-668 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 990.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 1 MSQVSPQTMANAIRALAMDAVQKAKSGHPGMPMGMADIATALWTRHLRFNPQDPKWSGRDRFILSNGHGSMLQYALLHLT 80
Cdd:PRK05899 3 MDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLHLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 81 GFDLSMDDLKAFRQLGSRTPGHPEVDITPGVETTTGPLGQGIANGVGMALAEKLLAAEFNRDGFPVVDNRTYVFLGDGCL 160
Cdd:PRK05899 83 GYDLSIDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGLANAVGMALAEKYLAALFNRPGLDIVDHYTYVLCGDGDL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 161 MEGISHEVCSLAGVWKLNKLIALYDDNGISIDGDVRGWFRDDTRGRFEAYGWNVIgPVDGHDINAVDQAIAQAKESaEKP 240
Cdd:PRK05899 163 MEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTEDVKKRFEAYGWHVI-EVDGHDVEAIDAAIEEAKAS-TKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 241 TLIICRTTIGKGSPNRQGTAKVHGEALGDEEIAATKAALGWTYgpfeipqdvyaawdhraegakvekewqqtyagykaay 320
Cdd:PRK05899 241 TLIIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAAAKKELGWDY------------------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 321 pelakelerrlagdlpdqwdaavmdavcqaaeaaetvatRKASQKALNALAPVLPELLGGSADLTGSNLTNWSGSTSLNT 400
Cdd:PRK05899 284 ---------------------------------------RKASGKALNALAKALPELVGGSADLAGSNNTKIKGSKDFAP 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 401 GDFHARHISYGVREFGMSAILNGIALYGGFIPYGATFLTFSDYSRNALRMSALMNLRAINVFTHDSIGLGEDGPTHQSVE 480
Cdd:PRK05899 325 EDYSGRYIHYGVREFAMAAIANGLALHGGFIPFGGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVE 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 481 HIPSLRLIPGMDVWRPCDTVESVVAWASAIERRDGASCLIFSRQNAAFIDRDEvDADAIAMGGYVVAEAPlgegeaQVVL 560
Cdd:PRK05899 405 QLASLRAIPNLTVIRPADANETAAAWKYALERKDGPSALVLTRQNLPVLERTA-QEEGVAKGGYVLRDDP------DVIL 477
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 561 LATGTEVGLAMDARAKLAALNINARVVSMPCTNRFDRQSTEYRQSVLPPGLPV-LAIEASKTDLWWKYFTGRGDVLGVDS 639
Cdd:PRK05899 478 IATGSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQDAAYKESVLPAAVTArVAVEAGVADGWYKYVGLDGKVLGIDT 557
|
650 660
....*....|....*....|....*....
gi 512181214 640 FGESAPAKDLWIKFGFTVDNVVSKVEALL 668
Cdd:PRK05899 558 FGASAPADELFKEFGFTVENIVAAAKELL 586
|
|
| PLN02790 |
PLN02790 |
transketolase |
13-668 |
0e+00 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 870.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 13 IRALAMDAVQKAKSGHPGMPMGMADIATALWTRHLRFNPQDPKWSGRDRFILSNGHGSMLQYALLHLTGFD-LSMDDLKA 91
Cdd:PLN02790 1 IRFLAIDAVNKANSGHPGLPMGCAPMGHVLYDEVMKYNPKNPYWFNRDRFVLSAGHGCMLQYALLHLAGYDsVQMEDLKQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 92 FRQLGSRTPGHPEVDITPGVETTTGPLGQGIANGVGMALAEKLLAAEFNRDGFPVVDNRTYVFLGDGCLMEGISHEVCSL 171
Cdd:PLN02790 81 FRQWGSRTPGHPENFETPGIEVTTGPLGQGIANAVGLALAEKHLAARFNKPDHKIVDHYTYCILGDGCQMEGISNEAASL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 172 AGVWKLNKLIALYDDNGISIDGDVRGWFRDDTRGRFEAYGWNVIGPVDG-HDINAVDQAIAQAKESAEKPTLIICRTTIG 250
Cdd:PLN02790 161 AGHWGLGKLIVLYDDNHISIDGDTEIAFTEDVDKRYEALGWHTIWVKNGnTDYDEIRAAIKEAKAVTDKPTLIKVTTTIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 251 KGSPNRQGTAKVHGEALGDEEIAATKAALGWTYGPFEIPQDVYAAW-DHRAEGAKVEKEWQQTYAGYKAAYPELAKELER 329
Cdd:PLN02790 241 YGSPNKANSYSVHGAALGEKEVDATRKNLGWPYEPFHVPEDVKSHWsKHTKEGAALEAEWNAKFAEYKKKYPEEAAELKS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 330 RLAGDLPDQWDaavmDAVCQAAEAAETVATRKASQKALNALAPVLPELLGGSADLTGSNLTNWSGStslntGDFHA---- 405
Cdd:PLN02790 321 LISGELPSGWE----KALPTFTPEDPADATRNLSQKCLNALAKVLPGLIGGSADLASSNMTLLKDF-----GDFQKdtpe 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 406 -RHISYGVREFGMSAILNGIALYG-GFIPYGATFLTFSDYSRNALRMSALMNLRAINVFTHDSIGLGEDGPTHQSVEHIP 483
Cdd:PLN02790 392 eRNVRFGVREHGMGAICNGIALHSsGLIPYCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLGEDGPTHQPIEHLA 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 484 SLRLIPGMDVWRPCDTVESVVAWASAIERRDGASCLIFSRQNAAFIDRDEvdADAIAMGGYVVAEaPLGEGEAQVVLLAT 563
Cdd:PLN02790 472 SLRAMPNILMLRPADGNETAGAYKVAVTNRKRPTVLALSRQKVPNLPGTS--IEGVEKGGYVISD-NSSGNKPDLILIGT 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 564 GTEVGLAMDARAKLAALNINARVVSMPCTNRFDRQSTEYRQSVLPPGLPV-LAIEASKTDLWWKYFTGRGDVLGVDSFGE 642
Cdd:PLN02790 549 GSELEIAAKAAKELRKEGKKVRVVSMVCWELFEEQSDEYKESVLPSSVTArVSVEAGSTFGWEKYVGSKGKVIGVDRFGA 628
|
650 660
....*....|....*....|....*.
gi 512181214 643 SAPAKDLWIKFGFTVDNVVSKVEALL 668
Cdd:PLN02790 629 SAPAGILYKEFGFTVENVVAAAKSLL 654
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
10-668 |
0e+00 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 825.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 10 ANAIRALAMDAVQKAKSGHPGMPMGMADIATALWTRHLRFNPQDPKWSGRDRFILSNGHGSMLQYALLHLTGFDLSMDDL 89
Cdd:PTZ00089 10 ANEIRCLSADLVQKANSGHPGAPMGMAPIAHILWSEVMKYNPKDPRWINRDRFVLSNGHASALLYSMLHLTGYDLSMEDL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 90 KAFRQLGSRTPGHPEVDITPGVETTTGPLGQGIANGVGMALAEKLLAAEFNRDGFPVVDNRTYVFLGDGCLMEGISHEVC 169
Cdd:PTZ00089 90 KNFRQLGSRTPGHPERHITPGVEVTTGPLGQGIANAVGLAIAEKHLAAKFNRPGHPIFDNYVYVICGDGCLQEGVSQEAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 170 SLAGVWKLNKLIALYDDNGISIDGDVRGWFRDDTRGRFEAYGWNVIGPVDGH-DINAVDQAIAQAKESAEKPTLIICRTT 248
Cdd:PTZ00089 170 SLAGHLGLEKLIVLYDDNKITIDGNTDLSFTEDVEKKYEAYGWHVIEVDNGNtDFDGLRKAIEEAKKSKGKPKLIIVKTT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 249 IGKGSPNrQGTAKVHGEALGDEEIAATKAALGwtYGP---FEIPQDVYAAWDHRAE-GAKVEKEWQQTYAGYKAAYPELA 324
Cdd:PTZ00089 250 IGYGSSK-AGTEKVHGAPLGDEDIAQVKELFG--LDPekkFHVSEEVRQFFEQHVEkKKENYEAWKKRFAKYTAAFPKEA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 325 KELERRLAGDLPDQWdaavMDAVCQAAEAAETVATRKASQKALNALAPVLPELLGGSADLTGSNLTNWSGSTSLNTGDFH 404
Cdd:PTZ00089 327 QAIERRFKGELPPGW----EKKLPKYTTNDKAIATRKASENVLNPLFQILPELIGGSADLTPSNLTRPKEANDFTKASPE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 405 ARHISYGVREFGMSAILNGIALYGGFIPYGATFLTFSDYSRNALRMSALMNLRAINVFTHDSIGLGEDGPTHQSVEHIPS 484
Cdd:PTZ00089 403 GRYIRFGVREHAMCAIMNGIAAHGGFIPFGATFLNFYGYALGAVRLAALSHHPVIYVATHDSIGLGEDGPTHQPVETLAL 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 485 LRLIPGMDVWRPCDTVESVVAWASAIERRDGASCLIFSRQNAAFIDRDEvdADAIAMGGYVVAEAplgEGEAQVVLLATG 564
Cdd:PTZ00089 483 LRATPNLLVIRPADGTETSGAYALALANAKTPTILCLSRQNTPPLPGSS--IEGVLKGAYIVVDF---TNSPQLILVASG 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 565 TEVGLAMDArAKLAALNINARVVSMPCTNRFDRQSTEYRQSVLP-PGLPVLAIEASKTDLWWKYFTGRgdvLGVDSFGES 643
Cdd:PTZ00089 558 SEVSLCVEA-AKALSKELNVRVVSMPCWELFDQQSEEYQQSVLPsGGVPVLSVEAYVSFGWEKYSHVH---VGISGFGAS 633
|
650 660
....*....|....*....|....*
gi 512181214 644 APAKDLWIKFGFTVDNVVSKVEALL 668
Cdd:PTZ00089 634 APANALYKHFGFTVENVVEKARALA 658
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
5-336 |
0e+00 |
|
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes EC:2.2.1.1. and also partially matches to 2-oxoisovalerate dehydrogenase beta subunit EC:1.2.4.4. Both these enzymes utilize thiamine pyrophosphate as a cofactor, suggesting there may be common aspects in their mechanism of catalysis.
Pssm-ID: 395366 [Multi-domain] Cd Length: 334 Bit Score: 570.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 5 SPQTMANAIRALAMDAVQKAKSGHPGMPMGMADIATALWTRHLRFNPQDPKWSGRDRFILSNGHGSMLQYALLHLTGFDL 84
Cdd:pfam00456 1 IDKRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 85 SMDDLKAFRQLGSRTPGHPEVDITPGVETTTGPLGQGIANGVGMALAEKLLAAEFNRDGFPVVDNRTYVFLGDGCLMEGI 164
Cdd:pfam00456 81 SMEDLKSFRQLGSKTPGHPEFGHTAGVEVTTGPLGQGIANAVGMAIAERNLAATYNRPGFDIVDHYTYVFLGDGCLMEGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 165 SHEVCSLAGVWKLNKLIALYDDNGISIDGDVRGWFRDDTRGRFEAYGWNVIGPVDGHDINAVDQAIAQAKESAEKPTLII 244
Cdd:pfam00456 161 SSEASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDTAARFEAYGWHVIEVEDGHDVEAIAAAIEEAKAEKDKPTLIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 245 CRTTIGKGSPNRQGTAKVHGEALGDEEIAATKAALGW-TYGPFEIPQDVYAAWD-HRAEGAKVEKEWQQTYAGYKAAYPE 322
Cdd:pfam00456 241 CRTVIGYGSPNKQGTHDVHGAPLGADEVAALKQKLGWdPYKPFEIPAEVYDAWKeKVAEGAKAEAEWNELFAAYKKAYPE 320
|
330
....*....|....
gi 512181214 323 LAKELERRLAGDLP 336
Cdd:pfam00456 321 LAAEFARRLSGELP 334
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
11-276 |
2.58e-148 |
|
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. In addition, the enzyme plays a central role in the Calvin cycle in plants. Typically, TKs are homodimers. They require TPP and divalent cations, such as magnesium ions, for activity.
Pssm-ID: 238970 [Multi-domain] Cd Length: 255 Bit Score: 430.39 E-value: 2.58e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 11 NAIRALAMDAVQKAKSGHPGMPMGMADIATALWTRHLRFNPQDPKWSGRDRFILSNGHGSMLQYALLHLTGFdLSMDDLK 90
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGY-LPEEDLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 91 AFRQLGSRTPGHPEVDITPGVETTTGPLGQGIANGVGMALAEKLLaaefnrdgfpVVDNRTYVFLGDGCLMEGISHEVCS 170
Cdd:cd02012 80 TFRQLGSRLPGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEKLL----------GFDYRVYVLLGDGELQEGSVWEAAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 171 LAGVWKLNKLIALYDDNGISIDGDVRG-WFRDDTRGRFEAYGWNVIgPVDGHDINAVDQAIAQAKESAEKPTLIICRTTI 249
Cdd:cd02012 150 FAGHYKLDNLIAIVDSNRIQIDGPTDDiLFTEDLAKKFEAFGWNVI-EVDGHDVEEILAALEEAKKSKGKPTLIIAKTIK 228
|
250 260
....*....|....*....|....*..
gi 512181214 250 GKGSPNRQGTAKVHGEALGDEEIAATK 276
Cdd:cd02012 229 GKGVPFMENTAKWHGKPLGEEEVELAK 255
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
9-280 |
5.55e-88 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 276.19 E-value: 5.55e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 9 MANAIRALAMDAVQKAKSGHPGMPMGMADIATALWTRHLRFNPQDPKWSGRDRFILSNGHGSMLQYALLHLTGFdLSMDD 88
Cdd:COG3959 11 KARQIRRDILRMIYAAGSGHPGGSLSAADILAALYFKVMNIDPKNPDWPDRDRFILSKGHAAPALYAVLAEKGY-FPKEE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 89 LKAFRQLGSRTPGHPEVDITPGVETTTGPLGQGIANGVGMALAEKLlaaefnrDGFpvvDNRTYVFLGDGCLMEGISHEV 168
Cdd:COG3959 90 LATFRKLGSRLQGHPDMKKTPGVEMSTGSLGQGLSVAVGMALAAKL-------DGK---DYRVYVLLGDGELQEGQVWEA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 169 CSLAGVWKLNKLIALYDDNGISIDG---DVRGwfRDDTRGRFEAYGWNVIgPVDGHDINAVDQAIAQAKESAEKPTLIIC 245
Cdd:COG3959 160 AMAAAHYKLDNLIAIVDRNGLQIDGpteDVMS--LEPLAEKWEAFGWHVI-EVDGHDIEALLAALDEAKAVKGKPTVIIA 236
|
250 260 270
....*....|....*....|....*....|....*
gi 512181214 246 RTTIGKGSPNRQGTAKVHGEALGDEEIAATKAALG 280
Cdd:COG3959 237 HTVKGKGVSFMENRPKWHGKAPNDEELEQALAELE 271
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
361-523 |
5.79e-55 |
|
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: 184.57 E-value: 5.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 361 KASQKALNALAPVLPELLGGSADLTGSNLTNWSGStslntgDFHARHISYGVREFGMSAILNGIALYGgFIPYGATFLTF 440
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAK------KFPDRFIDVGIAEQNMVGIAAGLALHG-LKPFVSTFSFF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 441 SDYSRNALR-MSALMNLRAINVFTHDSIGLGEDGPTHQSVEHIPSLRLIPGMDVWRPCDTVESVVAWASAIErRDGASCL 519
Cdd:cd07033 74 LQRAYDQIRhDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALE-YDGPVYI 152
|
....
gi 512181214 520 IFSR 523
Cdd:cd07033 153 RLPR 156
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
360-525 |
1.26e-54 |
|
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: 184.29 E-value: 1.26e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 360 RKASQKALNALAPVLPELLGGSADLTGSNLTNWSGStslntGDFHA--RHISYGVREFGMSAILNGIALYGG-FIPYGAT 436
Cdd:pfam02779 6 RKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGL-----LHPQGagRVIDTGIAEQAMVGFANGMALHGPlLPPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 437 FLTFSDYSRNALR-MSALMNLRAINVFTHDSIGLGEDGPTHQSVEHIPSLRLIPGMDVWRPCDTVESVVAWASAIERRD- 514
Cdd:pfam02779 81 FSDFLNRADDAIRhGAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGr 160
|
170
....*....|.
gi 512181214 515 GASCLIFSRQN 525
Cdd:pfam02779 161 KPVVLRLPRQL 171
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
408-525 |
5.62e-36 |
|
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: 131.84 E-value: 5.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 408 ISYGVREFGMSAILNGIALYGGfIPYGATFLTFSDYSRNALRMSALMNlRAINVFTHDS-IGLGEDGPTHQSVEHIPSLR 486
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFFDRAKDQIRSAGASG-NVPVVFRHDGgGGVGEDGPTHHSIEDEALLR 95
|
90 100 110
....*....|....*....|....*....|....*....
gi 512181214 487 LIPGMDVWRPCDTVESVVAWASAIeRRDGASCLIFSRQN 525
Cdd:smart00861 96 AIPGLKVVAPSDPAEAKGLLRAAI-RDDGPVVIRLERKS 133
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
360-668 |
2.15e-27 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 112.87 E-value: 2.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 360 RKASQKALNALAPVLPELLGGSADLTGSNLTNWsgstslntgdFHA----RHISYGVRE---FGMSAilnGIALyGGFIP 432
Cdd:COG3958 7 RDAFGEALVELAEEDPDIVVLDADLGGSTKLDK----------FAKafpdRFFNVGIAEqnmVGVAA---GLAL-AGKIP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 433 YGATFLTFSdySRNAL---RMS-ALMNLRAINVFTHDSIGLGEDGPTHQSVEHIPSLRLIPGMDVWRPCDTVE--SVVAW 506
Cdd:COG3958 73 FVSTFAPFL--TGRAYeqiRNDiAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVEteAAVRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 507 ASAIerrDGASCLIFSRQNAAFIDRDEVDadaIAMGGYVVaeapLGEGEAqVVLLATGTEVGLAMDARAKLAALNINARV 586
Cdd:COG3958 151 AAEH---DGPVYLRLGRGAVPVVYDEDYE---FEIGKARV----LREGKD-VTIIATGIMVAEALEAAELLAKEGISARV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 587 VSMPCTNRFDRQSTeyRQSVLPPGLPVLAIEASKTdlwwkyfTGRGDV---------------LGV-DSFGESAPAKDLW 650
Cdd:COG3958 220 INMHTIKPLDEEAI--LKAARKTGAVVTAEEHSII-------GGLGSAvaevlaenypvplrrIGVpDRFGESGSPEELL 290
|
330
....*....|....*...
gi 512181214 651 IKFGFTVDNVVSKVEALL 668
Cdd:COG3958 291 EKYGLDAEGIVAAAKELL 308
|
|
| dxs |
TIGR00204 |
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ... |
13-617 |
5.58e-19 |
|
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: 90.99 E-value: 5.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 13 IRALAMDAVQkAKSGHPGMPMGMADIATALwtrHLRFNPQdpkwsgRDRFILSNGHGSmlqYALLHLTGFDLSMDDLKAF 92
Cdd:TIGR00204 25 LRRYLLESVS-ASGGHLASGLGTVELTVAL---HYVFNTP------KDQFIWDVGHQA---YPHKLLTGRREKFSTLRQK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 93 RQL-GSRTPGHPEVDITpgvetTTGPLGQGIANGVGMALAekllaaeFNRDGfpvVDNRTYVFLGDGCLMEGISHEVCSL 171
Cdd:TIGR00204 92 KGLhGFPKRSESEYDVF-----SAGHSSTSISAGLGIAVA-------AEKKG---ADRKTVCVIGDGAITAGMAFEALNH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 172 AGVWKLNKLIALyDDNGISIDGDVRG---------------WFRDDTRGR----------------------------FE 208
Cdd:TIGR00204 157 AGDLKTDMIVIL-NDNEMSISENVGAlsnhlaqlrsgslyqSLRDGLKKIfsklppiknylakrteesmkglvvpgtfFE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 209 AYGWNVIGPVDGHDINAVDQAIAQAKESAEkPTLIICRTTIGKG-SPNRQGTAKVHGEalgdeeiaatkaalgwtyGPFE 287
Cdd:TIGR00204 236 ELGFNYIGPVDGHDLLELIETLKNAKKLKG-PVFLHIQTKKGKGyKPAEKDPIGWHGV------------------GPFD 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 288 IpqdvyaawdhrAEGAkvekewqqtYAGYKAAYPelakelerrlagdlpdQWDAAVMDAVCQAAeaaetvatrkASQKAL 367
Cdd:TIGR00204 297 L-----------STGC---------LPKSKSALP----------------SYSKIFSDTLCELA----------KKDNKI 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 368 NALAPVLPEllggsadltGSNLTNWSGStslntgdFHARHISYGVREFGMSAILNGIALyGGFIPYGATFLTFSDYSRNA 447
Cdd:TIGR00204 331 VGITPAMPE---------GSGLDKFSRK-------FPDRYFDVAIAEQHAVTFAAGMAI-EGYKPFVAIYSTFLQRAYDQ 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 448 LRMSALmnLRAINV-FTHDSIGL-GEDGPTHQSVEHIPSLRLIPGMDVWRPCDTVESVVAWASAIERRDGASCLIFSRQN 525
Cdd:TIGR00204 394 VVHDVC--IQKLPVlFAIDRAGIvGADGETHQGAFDISYLRCIPNMVIMAPSDENELRQMLYTGYHYDDGPIAVRYPRGN 471
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 526 AAFIDRDEVDAdaiamgGYVVAEAPLGEGEAQVVLLATGTEVGLAMDARAKLAALNINARVVSMpctnRFDRQ-STEYRQ 604
Cdd:TIGR00204 472 AVGVELTPEPE------KLPIGKSEVLRKGEKILILGFGTLVPEALEVAESLNEKGIEATVVDA----RFVKPlDEELIL 541
|
650
....*....|...
gi 512181214 605 SVLPPGLPVLAIE 617
Cdd:TIGR00204 542 EIAASHEKLVTVE 554
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
26-252 |
3.41e-15 |
|
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; 1-Deoxy-D-xylulose-5-phosphate synthase (DXS) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. DXS catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. The formation of DXP leads to the formation of the terpene precursor IPP (isopentyl diphosphate) and to the formation of thiamine (vitamin B1) and pyridoxal (vitamin B6).
Pssm-ID: 238965 [Multi-domain] Cd Length: 195 Bit Score: 74.51 E-value: 3.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 26 SGHPGMPMGMADIATALwtrHLRFNPQdpkwsgRDRFILSNGHGSmlqYALLHLTGFDLSMDDLkafRQLGSRTpGHPEV 105
Cdd:cd02007 1 GGHLGSNLGVVELTLAL---HYVFDSP------KDKIIWDVGHQA---YPHKILTGRRDQFHTL---RQYGGLS-GFTKR 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 106 DITPGVETTTGPLGQGIANGVGMALAEKLLAAefnrdgfpvvDNRTYVFLGDGCLMEGISHEVCSLAGVWKlNKLIALYD 185
Cdd:cd02007 65 SESEYDAFGTGHSSTSISAALGMAVARDLKGK----------KRKVIAVIGDGALTGGMAFEALNNAGYLK-SNMIVILN 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 512181214 186 DNGISIDGDVrgwfrddtrGR----FEAYGWNVIGPVDGHDINAVDQAIAQAKESAeKPTLIICRTTIGKG 252
Cdd:cd02007 134 DNEMSISPNV---------GTpgnlFEELGFRYIGPVDGHNIEALIKVLKEVKDLK-GPVLLHVVTKKGKG 194
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
1-589 |
6.78e-14 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 75.14 E-value: 6.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 1 MSQVSPQTMANAIRALAMDAVQKAkSGHPGMPMGMADIATALwtrHLRFNpqdpkwSGRDRFILSNGHGSmlqYALLHLT 80
Cdd:PRK12571 21 LSDAELEQLADELRAEVISAVSET-GGHLGSSLGVVELTVAL---HAVFN------TPKDKLVWDVGHQC---YPHKILT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 81 GfdlSMDDLKAFRQLGSRTpGHPEVDitpgvETTTGPLGQG-----IANGVGMALAEKLLAAefnrdgfpvvDNRTYVFL 155
Cdd:PRK12571 88 G---RRDRFRTLRQKGGLS-GFTKRS-----ESEYDPFGAAhsstsISAALGFAKARALGQP----------DGDVVAVI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 156 GDGCLMEGISHEVCSLAGVWKlNKLIALYDDNGISID---------------GDVRGWFRDDTRGR-------------- 206
Cdd:PRK12571 149 GDGSLTAGMAYEALNNAGAAD-RRLIVILNDNEMSIAppvgalaaylstlrsSDPFARLRAIAKGVeerlpgplrdgarr 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 207 --------------FEAYGWNVIGPVDGHDINAVDQAIAQAKESAEKPTLIICRTTIGKG-SPNRQGTAKVHG-----EA 266
Cdd:PRK12571 228 arelvtgmigggtlFEELGFTYVGPIDGHDMEALLSVLRAARARADGPVLVHVVTEKGRGyAPAEADEDKYHAvgkfdVV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 267 LGDEEIAATKAAlGWTygpfeipqDVYAAwdhraegakvekewqqtyagykaaypELAKELERRlagdlPDQwdAAVMDA 346
Cdd:PRK12571 308 TGLQKKSAPSAP-SYT--------SVFGE--------------------------ELTKEAAED-----SDI--VAITAA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 347 VCQAAeaaetvatrkasqkALNALAPVLPEllggsadltgsnltnwsgstslntgdfhaRHISYGVREFGMSAILNGIAl 426
Cdd:PRK12571 346 MPLGT--------------GLDKLQKRFPN-----------------------------RVFDVGIAEQHAVTFAAGLA- 381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 427 YGGFIPYGATFLTFSDYSRNALRMS-ALMNLRAinVFTHDSIGL-GEDGPTHQSVEHIPSLRLIPGMDVWRPCDTVESVV 504
Cdd:PRK12571 382 AAGLKPFCAVYSTFLQRGYDQLLHDvALQNLPV--RFVLDRAGLvGADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRH 459
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 505 AWASAIERRDGASCLIFSRQNAAFIDRDEVdADAIAMG-GYVVAEAPlgegeaQVVLLATGTEVGLAMDARAKLAALNIN 583
Cdd:PRK12571 460 MLRTAAAHDDGPIAVRFPRGEGVGVEIPAE-GTILGIGkGRVPREGP------DVAILSVGAHLHECLDAADLLEAEGIS 532
|
....*.
gi 512181214 584 ARVVSM 589
Cdd:PRK12571 533 VTVADP 538
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
122-595 |
6.64e-13 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 71.65 E-value: 6.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 122 IANGVGMALAEKLLAAEfnrdgfpvvDNRTYVFLGDGCL---M--EGISHevcslAGVWKLNKLIALyDDNGISIDGDVr 196
Cdd:PRK05444 123 ISAALGMAKARDLKGGE---------DRKVVAVIGDGALtggMafEALNN-----AGDLKSDLIVIL-NDNEMSISPNV- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 197 GWF-----RDDTRGRFEAYGWNVIGPVDGHDINAVDQAIAQAKEsAEKPTLIICRTTIGKGSPnrqgtakvhgealgdee 271
Cdd:PRK05444 187 GALsnylaRLRSSTLFEELGFNYIGPIDGHDLDALIETLKNAKD-LKGPVLLHVVTKKGKGYA----------------- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 272 iAATKAALGW-TYGPFEIpqdvyaawdhrAEGAKVekewqqtyAGYKAAYPelakelerrlagdlpdQWDAAVMDAVCqa 350
Cdd:PRK05444 249 -PAEADPIKYhGVGKFDP-----------ETGEQP--------KSSKPGKP----------------SYTKVFGETLC-- 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 351 aeaaetvatRKASQ-KALNALAPVLPEllggsadltGSNLTnwsgstslntgDFHARhisYGVREF--G--------MSA 419
Cdd:PRK05444 291 ---------ELAEKdPKIVAITAAMPE---------GTGLV-----------KFSKR---FPDRYFdvGiaeqhavtFAA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 420 ilnGIALyGGFIPYGA---TFLT------FSDYsrnalrmsALMNLRAinVFTHDSIGL-GEDGPTHQSVEHIPSLRLIP 489
Cdd:PRK05444 339 ---GLAT-EGLKPVVAiysTFLQraydqvIHDV--------ALQNLPV--TFAIDRAGLvGADGPTHQGAFDLSYLRCIP 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 490 GMDVWRPCDTVESVVAWASAIERRDGASCLIFSRQNAAFIDRDEVDADAIamGGYVVaeapLGEGEaQVVLLATGTEVGL 569
Cdd:PRK05444 405 NMVIMAPSDENELRQMLYTALAYDDGPIAIRYPRGNGVGVELPELEPLPI--GKGEV----LREGE-DVAILAFGTMLAE 477
|
490 500
....*....|....*....|....*.
gi 512181214 570 AMDARAKLAAlninARVVSMpctnRF 595
Cdd:PRK05444 478 ALKAAERLAS----ATVVDA----RF 495
|
|
| TPP_E1_EcPDC_like |
cd02017 |
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ... |
13-254 |
2.34e-11 |
|
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; composed of proteins similar to the E1 component of the Escherichia coli pyruvate dehydrogenase multienzyme complex (PDC). PDC catalyzes the oxidative decarboxylation of pyruvate and the subsequent acetylation of coenzyme A to acetyl-CoA. The E1 component of PDC catalyzes the first step of the multistep process, using TPP and a divalent cation as cofactors. E. coli PDC is a homodimeric enzyme.
Pssm-ID: 238975 [Multi-domain] Cd Length: 386 Bit Score: 66.17 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 13 IRALAMDAVQKAKS------GHPGMPMGMADIATALWTRHLRFNPQDpkwSGRDRfILSNGHGSMLQYALLHLTGfDLSM 86
Cdd:cd02017 11 IRWNAMAMVHRANKkdlgigGHIATFASAATLYEVGFNHFFRARGEG---GGGDL-VYFQGHASPGIYARAFLEG-RLTE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 87 DDLKAFRQLG-----SRTPgHPEVDITPgVETTTGPLGQGIANGVGMALAEKLLAAEfnrdGFPV-VDNRTYVFLGDGCL 160
Cdd:cd02017 86 EQLDNFRQEVgggglSSYP-HPWLMPDF-WEFPTVSMGLGPIQAIYQARFNRYLEDR----GLKDtSDQKVWAFLGDGEM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 161 MEGISHEVCSLAGVWKLNKLIALYDDNGISIDGDVRGWFRDDTR--GRFEAYGWNVI----------------------- 215
Cdd:cd02017 160 DEPESLGAIGLAAREKLDNLIFVVNCNLQRLDGPVRGNGKIIQEleGIFRGAGWNVIkviwgskwdellakdgggalrqr 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 216 --------------------------------GPVD-------------GHDINAVDQAIAQAKESAEKPTLIICRTTIG 250
Cdd:cd02017 240 meetvdgdyqtlkakdgayvrehffgkypelkALVTdlsdedlwalnrgGHDPRKVYAAYKKAVEHKGKPTVILAKTIKG 319
|
....
gi 512181214 251 KGSP 254
Cdd:cd02017 320 YGLG 323
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
96-247 |
3.58e-11 |
|
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; composed of proteins similar to the E1 components of the human pyruvate dehydrogenase complex (PDC), the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). PDC catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. ADC participates in the breakdown of acetoin while BCADC participates in the breakdown of branched chain amino acids. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate (branched chain 2-oxo acids derived from the transamination of leucine, valine and isoleucine).
Pssm-ID: 238958 [Multi-domain] Cd Length: 293 Bit Score: 64.44 E-value: 3.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 96 GSRTPGHPeVDITPGVETTTGPLGQGIANGVGMALAEKLLAAefnrdgfpvvDNRTYVFLGDGCLMEGISHEVCSLAGVW 175
Cdd:cd02000 85 GRGGSMHI-GDKEKNFFGGNGIVGGQVPLAAGAALALKYRGE----------DRVAVCFFGDGATNEGDFHEALNFAALW 153
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 512181214 176 KLNkLIALYDDNGISIDGDVRGWFRDDT-RGRFEAYGWNVIgPVDGHDINAVDQAIAQAKESA---EKPTLIICRT 247
Cdd:cd02000 154 KLP-VIFVCENNGYAISTPTSRQTAGTSiADRAAAYGIPGI-RVDGNDVLAVYEAAKEAVERAragGGPTLIEAVT 227
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
452-595 |
7.07e-11 |
|
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: 65.42 E-value: 7.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 452 ALMNLraiNV-FTHDSIGL-GEDGPTHQSVEHIPSLRLIPGMDVWRPCDTVE--SVVAWASAIerrDGASCLIFSRQNAA 527
Cdd:COG1154 406 ALQNL---PVtFAIDRAGLvGADGPTHHGVFDLSYLRCIPNMVIMAPKDENElrHMLYTALAY---DGPTAIRYPRGNGP 479
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 512181214 528 FIDRDEvDADAIAMGGYVVaeapLGEGEaQVVLLATGTEVGLAMDARAKLAALNINARVVSMpctnRF 595
Cdd:COG1154 480 GVELPA-ELEPLPIGKGEV----LREGK-DVAILAFGTMVAEALEAAERLAAEGISATVVDA----RF 537
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
553-660 |
1.20e-10 |
|
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: 59.53 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 553 EGEaQVVLLATGTEVGLAMDARAKLAALNINARVVSMPCTNRFDRQS-----TEYRQSVLPP-GLPVLAIEASKTDLW-- 624
Cdd:pfam02780 8 EGD-DVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETilesvKKTGRLVTVEeAVPRGGFGSEVAAALae 86
|
90 100 110
....*....|....*....|....*....|....*...
gi 512181214 625 WKYFTGRGDVLGVDS--FGESAPAKDLWIKFGFTVDNV 660
Cdd:pfam02780 87 EAFDGLDAPVLRVGGpdFPEPGSADELEKLYGLTPEKI 124
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
108-247 |
3.51e-08 |
|
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.
Pssm-ID: 238318 [Multi-domain] Cd Length: 168 Bit Score: 53.41 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 108 TPGVETTTGPLGQGIANGVGMALAEKllaaefnrdgfpvvDNRTYVFLGDGCLMEGISHevCSLAGVWKLNkLIALYDDN 187
Cdd:cd00568 38 RFLTSTGFGAMGYGLPAAIGAALAAP--------------DRPVVCIAGDGGFMMTGQE--LATAVRYGLP-VIVVVFNN 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512181214 188 GISIDGDVR------------GWFRDDTRGRFEAYGWNVIGPVDGHDInavDQAIAQAKESaEKPTLIICRT 247
Cdd:cd00568 101 GGYGTIRMHqeafyggrvsgtDLSNPDFAALAEAYGAKGVRVEDPEDL---EAALAEALAA-GGPALIEVKT 168
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
7-264 |
5.54e-07 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 52.79 E-value: 5.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 7 QTMANAIRALAMDAVQKAkSGHPGMPMGMADIATALwtrHLRFNpqdpkwSGRDRFILSNGHGSmlqYALLHLTGFDLSM 86
Cdd:PLN02234 85 KVLSDELRSDVIFNVSKT-GGHLGSNLGVVELTVAL---HYIFN------TPHDKILWDVGHQS---YPHKILTGRRGKM 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 87 DDLKAFRQLGSRTPGHPEVDITPGvettTGPLGQGIANGVGMALAEKLLAaefnrdgfpvVDNRTYVFLGDGCLMEGISH 166
Cdd:PLN02234 152 KTIRQTNGLSGYTKRRESEHDSFG----TGHSSTTLSAGLGMAVGRDLKG----------MNNSVVSVIGDGAMTAGQAY 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 167 EVCSLAGVWKLNKLIALYDDNGISI-----DGDVR----------------GWFRDDTRGRFEAYGWNVIGPVDGHDINA 225
Cdd:PLN02234 218 EAMNNAGYLHSNMIVILNDNKQVSLptanlDGPTQpvgalscalsrlqsncGMIRETSSTLFEELGFHYVGPVDGHNIDD 297
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 512181214 226 VDQAIAQAKESAE-KPTLIICRTTIGKGSP-NRQGTAKVHG 264
Cdd:PLN02234 298 LVSILETLKSTKTiGPVLIHVVTEKGRGYPyAERADDKYHG 338
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
9-252 |
4.53e-06 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 49.62 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 9 MANAIRALAMDAVQkAKSGHPGMPMGMADIATALwtrHLRFNpqdpkwSGRDRFILSNGHGSmlqYALLHLTGfdlsmdd 88
Cdd:PRK12315 23 LASEIRTALLEKDS-AHGGHVGPNLGVVELTIAL---HYVFN------SPKDKIVWDVSHQS---YPHKMLTG------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 89 lkafRQLGSRTPGHPEvDITPGVET--------TTGPLGQGIANGVGMALAEKLLAAEfnrdgfpvvDNRTYVfLGDGCL 160
Cdd:PRK12315 83 ----RKEAFLDPDHYD-DVTGYTNPeesehdffTVGHTSTSIALATGLAKARDLKGEK---------GNIIAV-IGDGSL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 161 MEGISHEVCSLAGVWKLNkLIALYDDNGISIDGDVRGWFRD-----DTRGR-----FEAYGWNVIGPVDGHDINAVDQAI 230
Cdd:PRK12315 148 SGGLALEGLNNAAELKSN-LIIIVNDNQMSIAENHGGLYKNlkelrDTNGQsennlFKAMGLDYRYVEDGNDIESLIEAF 226
|
250 260
....*....|....*....|..
gi 512181214 231 AQAKESaEKPTLIICRTTIGKG 252
Cdd:PRK12315 227 KEVKDI-DHPIVLHIHTLKGKG 247
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
7-586 |
5.62e-06 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 49.51 E-value: 5.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 7 QTMANAIRALAMDAVQKAkSGHPGMPMGMADIATALwtrHLRFN-PQDpkwsgrdRFILSNGHGSmlqYALLHLTGfdlS 85
Cdd:PLN02582 52 KQLADELRSDVIFNVSKT-GGHLGSSLGVVELTVAL---HYVFNaPQD-------KILWDVGHQS---YPHKILTG---R 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 86 MDDLKAFRQLGSRTpghpevDITPGVETTTGPLGQG-----IANGVGMALAEKLLAAEfnrdgfpvvdNRTYVFLGDGCL 160
Cdd:PLN02582 115 RDKMHTMRQTNGLS------GFTKRAESEYDCFGTGhssttISAGLGMAVGRDLKGKK----------NNVVAVIGDGAM 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 161 MEGISHEVCSLAGVWKLNKLIALYDDNGISI-----DGDV---------------------------------------- 195
Cdd:PLN02582 179 TAGQAYEAMNNAGYLDSDMIVILNDNKQVSLptatlDGPAppvgalssalsrlqssrplrelrevakgvtkqiggpmhel 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 196 --------RGWFRDDTRGRFEAYGWNVIGPVDGHDINAVDQAIAQAKESAEK-PTLIICRTTIGKGSPNRQGTA-KVHGE 265
Cdd:PLN02582 259 aakvdeyaRGMISGSGSTLFEELGLYYIGPVDGHNIDDLVTILREVKSTKTTgPVLIHVVTEKGRGYPYAERAAdKYHGV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 266 ALGDEEiaatkaalgwTYGPFEIPQDVYAAWDHRAEGAKVEKEWQQTYAGYKAAypelakelerrlagdlpdqwdaavmd 345
Cdd:PLN02582 339 VKFDPA----------TGKQFKVKAKTQSYTTYFAEALIAEAEVDKDVVAIHAA-------------------------- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 346 avcqaaeaaetvatrkasqkalnalapvlpelLGGSadlTGSNLTnwsgstslnTGDFHARHISYGVREFGMSAILNGIA 425
Cdd:PLN02582 383 --------------------------------MGGG---TGLNLF---------ARRFPTRCFDVGIAEQHAVTFAAGLA 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 426 LYGgFIPYGATFLTFsdYSRNALRMSALMNLRAINV-FTHDSIGL-GEDGPTHQSVEHIPSLRLIPGMDVWRPCDTVE-- 501
Cdd:PLN02582 419 CEG-LKPFCAIYSSF--LQRGYDQVVHDVDLQKLPVrFAMDRAGLvGADGPTHCGAFDVTYMACLPNMVVMAPSDEAElf 495
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 502 SVVAWASAIErrDGASCLIFSRQNAAFIDRDEVDADA-IAMGGYVVaeapLGEGEaQVVLLATGTEVGLAMDARAKLAAL 580
Cdd:PLN02582 496 HMVATAAAID--DRPSCFRYPRGNGIGVQLPPNNKGIpIEVGKGRI----LLEGE-RVALLGYGTAVQSCLAAASLLERH 568
|
....*.
gi 512181214 581 NINARV 586
Cdd:PLN02582 569 GLSATV 574
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
113-247 |
3.43e-05 |
|
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family includes pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase and 2-oxoisovalerate dehydrogenase.
Pssm-ID: 395548 [Multi-domain] Cd Length: 300 Bit Score: 46.16 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 113 TTTGPLGQGIANGVGMALAEKllaaefnRDGFPVVdnrTYVFLGDGCLMEGISHEVCSLAGVWKLnKLIALYDDNGISID 192
Cdd:pfam00676 98 GGNGILGAQVPLGAGIALAAK-------YRGKKEV---AITLYGDGAANQGDFFEGLNFAALWKL-PVIFVCENNQYGIS 166
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 512181214 193 GDVRGWFRDDT---RGRfeayGWNVIG-PVDGHDINAVDQAIAQAKESA---EKPTLIICRT 247
Cdd:pfam00676 167 TPAERASASTTyadRAR----GYGIPGlHVDGMDPLAVYQASKFAAERArtgKGPFLIELVT 224
|
|
| DXP_synthase_N |
pfam13292 |
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate ... |
207-243 |
4.05e-04 |
|
1-deoxy-D-xylulose-5-phosphate synthase; This family contains 1-deoxyxylulose-5-phosphate synthase (DXP synthase), an enzyme which catalyzes the thiamine pyrophosphoate-dependent acyloin condensation reaction between carbon atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate, to yield 1-deoxy-D- xylulose-5-phosphate, a precursor in the biosynthetic pathway to isoprenoids, thiamine (vitamin B1), and pyridoxol (vitamin B6).
Pssm-ID: 463832 [Multi-domain] Cd Length: 274 Bit Score: 42.78 E-value: 4.05e-04
10 20 30
....*....|....*....|....*....|....*..
gi 512181214 207 FEAYGWNVIGPVDGHDINAVDQAIAQAKEsAEKPTLI 243
Cdd:pfam13292 235 FEELGFKYIGPIDGHDLDALVKVLENAKD-LKGPVLL 270
|
|
| odpA |
CHL00149 |
pyruvate dehydrogenase E1 component alpha subunit; Reviewed |
151-243 |
8.81e-03 |
|
pyruvate dehydrogenase E1 component alpha subunit; Reviewed
Pssm-ID: 177069 [Multi-domain] Cd Length: 341 Bit Score: 38.69 E-value: 8.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 512181214 151 TYVFLGDGCLMEGISHEVCSLAGVWKLnKLIALYDDNGISID-GDVRGWFRDDTRGRFEAYGWNVIgPVDGHDINAVDQA 229
Cdd:CHL00149 160 TACFFGDGTTNNGQFFECLNMAVLWKL-PIIFVVENNQWAIGmAHHRSTSIPEIHKKAEAFGLPGI-EVDGMDVLAVREV 237
|
90
....*....|....*..
gi 512181214 230 IAQAKESAEK---PTLI 243
Cdd:CHL00149 238 AKEAVERARQgdgPTLI 254
|
|
| |
