|
Name |
Accession |
Description |
Interval |
E-value |
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
3-666 |
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: 1321.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 3 HSIEQLSINTIRTLSIDAIEKANSGHPGMPMGAAPMAYTLWTQFMKHNPNNPTWFNRDRFVLSAGHGSMLLYSLLHLSGY 82
Cdd:COG0021 1 MPLDQLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKHNPANPKWPNRDRFVLSAGHGSMLLYSLLHLTGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 83 DVTMDDLKNFRQWGSKTPGHPEYGHTAGVDATTGPLGQGIATAVGMAMAERHLAAKYNRDAYNVVDHYTYAICGDGDLME 162
Cdd:COG0021 81 DLSLDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGIANAVGMAIAERHLAARFNRPGHDIVDHYTYVIAGDGDLME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 163 GVSAEASSLAAHLQLGRLVVLYDSNDISLDGDLNRSFSESVEDRYKAYGWQVIRVEDGNDIEAIAKAIEEAKADEKRPTL 242
Cdd:COG0021 161 GISHEAASLAGHLKLGKLIVLYDDNGISIDGDTDLAFSEDVAKRFEAYGWHVIRVEDGHDLEAIDAAIEAAKAETDKPTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 243 IEVRTTIGFGSPNKSGKSASHGSPLGVEETKLTKEAYAWTAEQdFHVAEEVYDNFRKTVQDvGETAQAEWNTMLGEYAQA 322
Cdd:COG0021 241 IICKTIIGYGSPNKQGTAKAHGAPLGAEEIAATKEALGWPPEP-FEVPDEVYAHWRAAGER-GAAAEAEWNERFAAYAAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 323 YPELANEFQAAMNGQLPEGWEQNLPTYELGSKA-ATRNSSGAVINAIAESVPSFFGGSADLAGSNKTYMNNEKDFTRDDY 401
Cdd:COG0021 319 YPELAAELERRLAGELPEDWDAALPAFEADAKGvATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIKGAGSFSPEDP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 402 SGKNIWYGVREFAMGAAMNGIALHGGLKTYGGTFFVFSDYLRPAIRLAALMQLPVTYVFTHDSIAVGEDGPTHEPIEQLA 481
Cdd:COG0021 399 SGRNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFSDYMRPAIRLAALMKLPVIYVFTHDSIGLGEDGPTHQPVEQLA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 482 ALRAMPNVSVIRPADGNESVAAWRLALESTNKPTALVLTRQDLPTLEGAKDDtYEKVAKGAYIVSASkKETADVILLATG 561
Cdd:COG0021 479 SLRAIPNLDVIRPADANETAAAWKLALERKDGPTALILSRQNLPTLDRTAAA-AEGVAKGAYVLADA-EGTPDVILIATG 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 562 SEVSLAVEAQKALAVDGVDASVVSMPSMDRFEAQTAEYKESVLPKAVTKRFAIEMGATFGWHRYVGLEGDVLGIDTFGAS 641
Cdd:COG0021 557 SEVSLAVEAAELLAAEGIKVRVVSMPSWELFEAQDAAYRESVLPPAVRARVAVEAGVTDGWYKYVGLDGAVIGIDTFGAS 636
|
650 660
....*....|....*....|....*
gi 487904947 642 APGEKIMEEYGFTVENVVRKVKEML 666
Cdd:COG0021 637 APAKVLFEEFGFTVENVVAAAKELL 661
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
8-666 |
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: 1048.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 8 LSINTIRTLSIDAIEKANSGHPGMPMGAAPMAYTLWTQFMKHNPNNPTWFNRDRFVLSAGHGSMLLYSLLHLSGYDVTMD 87
Cdd:TIGR00232 2 KLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKFNPTNPKWINRDRFVLSNGHGSMLLYSLLHLTGYDLSIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 88 DLKNFRQWGSKTPGHPEYGHTAGVDATTGPLGQGIATAVGMAMAERHLAAKYNRDAYNVVDHYTYAICGDGDLMEGVSAE 167
Cdd:TIGR00232 82 DLKQFRQLHSKTPGHPEYGHTAGVEATTGPLGQGIANAVGMAIAEKTLAATFNKPGFEIVDHYTYVFVGDGCLQEGISYE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 168 ASSLAAHLQLGRLVVLYDSNDISLDGDLNRSFSESVEDRYKAYGWQVIRVEDGNDIEAIAKAIEEAKADEKRPTLIEVRT 247
Cdd:TIGR00232 162 VASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDVAKRFEAYGWEVLEVEDGHDLAAIDAAIEEAKASTDKPTLIEVKT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 248 TIGFGSPNKSGKSASHGSPLGVEETKLTKEAYAWTAEQdFHVAEEVYDNFRKTVQDVGETAQAEWNTMLGEYAQAYPELA 327
Cdd:TIGR00232 242 TIGFGSPNKAGTHGVHGAPLGDEEVALTKKNLGWNYNP-FEIPQEVYDHFKKTVKERGAKAEQEWNELFAAYKKKYPELA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 328 NEFQAAMNGQLPEGWEQNLPTYEL-GSKAATRNSSGAVINAIAESVPSFFGGSADLAGSNKTYMNNEKDFtRDDYSGKNI 406
Cdd:TIGR00232 321 AEFTRRLSGELPADWDKQLPEFKVkLQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKGSGDL-HENPLGNYI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 407 WYGVREFAMGAAMNGIALHGGLKTYGGTFFVFSDYLRPAIRLAALMQLPVTYVFTHDSIAVGEDGPTHEPIEQLAALRAM 486
Cdd:TIGR00232 400 HYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQLASLRAI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 487 PNVSVIRPADGNESVAAWRLALESTNKPTALVLTRQDLPTLEGakdDTYEKVAKGAYIVSASKKetADVILLATGSEVSL 566
Cdd:TIGR00232 480 PNLSVWRPCDGNETAAAWKYALESQDGPTALILSRQNLPQLEE---SSLEKVLKGGYVLKDSKG--PDLILIATGSEVQL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 567 AVEAQKALAVDGVDASVVSMPSMDRFEAQTAEYKESVLPKAVTkRFAIEMGATFGWHRYVGLEGDVLGIDTFGASAPGEK 646
Cdd:TIGR00232 555 AVEAAKKLAAENIKVRVVSMPSFDLFDKQDEEYRESVLPANVT-RLAIEAGAADEWYKYAGLVGAILGMDSFGESAPGDK 633
|
650 660
....*....|....*....|
gi 487904947 647 IMEEYGFTVENVVRKVKEML 666
Cdd:TIGR00232 634 LFEEFGFTVENVVAKAKKLL 653
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
1-666 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 1014.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 1 MSHSIEQLSINTIRTLSIDAIEKANSGHPGMPMGAAPMAYTLWTQFMKHNPNNPTWFNRDRFVLSAGHGSMLLYSLLHLS 80
Cdd:PRK05899 3 MDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLHLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 81 GYDVTMDDLKNFRQWGSKTPGHPEYGHTAGVDATTGPLGQGIATAVGMAMAERHLAAKYNRDAYNVVDHYTYAICGDGDL 160
Cdd:PRK05899 83 GYDLSIDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGLANAVGMALAEKYLAALFNRPGLDIVDHYTYVLCGDGDL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 161 MEGVSAEASSLAAHLQLGRLVVLYDSNDISLDGDLNRSFSESVEDRYKAYGWQVIRVeDGNDIEAIAKAIEEAKAdEKRP 240
Cdd:PRK05899 163 MEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTEDVKKRFEAYGWHVIEV-DGHDVEAIDAAIEEAKA-STKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 241 TLIEVRTTIGFGSPNKSGKSASHGSPLGVEETKLTKEAYawtaeqdfhvaeevydnfrktvqdvgetaqaewntmlgeya 320
Cdd:PRK05899 241 TLIIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAAAKKEL----------------------------------------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 321 qaypelanefqaamngqlpeGWEQnlptyelgskaatRNSSGAVINAIAESVPSFFGGSADLAGSNKTYMNNEKDFTRDD 400
Cdd:PRK05899 280 --------------------GWDY-------------RKASGKALNALAKALPELVGGSADLAGSNNTKIKGSKDFAPED 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 401 YSGKNIWYGVREFAMGAAMNGIALHGGLKTYGGTFFVFSDYLRPAIRLAALMQLPVTYVFTHDSIAVGEDGPTHEPIEQL 480
Cdd:PRK05899 327 YSGRYIHYGVREFAMAAIANGLALHGGFIPFGGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQL 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 481 AALRAMPNVSVIRPADGNESVAAWRLALESTNKPTALVLTRQDLPTLEGAKDDtyEKVAKGAYIVsaskKETADVILLAT 560
Cdd:PRK05899 407 ASLRAIPNLTVIRPADANETAAAWKYALERKDGPSALVLTRQNLPVLERTAQE--EGVAKGGYVL----RDDPDVILIAT 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 561 GSEVSLAVEAQKALAVDGVDASVVSMPSMDRFEAQTAEYKESVLPKAVTKRFAIEMGATFGWHRYVGLEGDVLGIDTFGA 640
Cdd:PRK05899 481 GSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQDAAYKESVLPAAVTARVAVEAGVADGWYKYVGLDGKVLGIDTFGA 560
|
650 660
....*....|....*....|....*.
gi 487904947 641 SAPGEKIMEEYGFTVENVVRKVKEML 666
Cdd:PRK05899 561 SAPADELFKEFGFTVENIVAAAKELL 586
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
5-339 |
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: 565.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 5 IEQLSINTIRTLSIDAIEKANSGHPGMPMGAAPMAYTLWTQFMKHNPNNPTWFNRDRFVLSAGHGSMLLYSLLHLSGYDV 84
Cdd:pfam00456 1 IDKRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 85 TMDDLKNFRQWGSKTPGHPEYGHTAGVDATTGPLGQGIATAVGMAMAERHLAAKYNRDAYNVVDHYTYAICGDGDLMEGV 164
Cdd:pfam00456 81 SMEDLKSFRQLGSKTPGHPEFGHTAGVEVTTGPLGQGIANAVGMAIAERNLAATYNRPGFDIVDHYTYVFLGDGCLMEGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 165 SAEASSLAAHLQLGRLVVLYDSNDISLDGDLNRSFSESVEDRYKAYGWQVIRVEDGNDIEAIAKAIEEAKADEKRPTLIE 244
Cdd:pfam00456 161 SSEASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDTAARFEAYGWHVIEVEDGHDVEAIAAAIEEAKAEKDKPTLIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 245 VRTTIGFGSPNKSGKSASHGSPLGVEETKLTKEAYAWTAEQDFHVAEEVYDNFRKTVQDvGETAQAEWNTMLGEYAQAYP 324
Cdd:pfam00456 241 CRTVIGYGSPNKQGTHDVHGAPLGADEVAALKQKLGWDPYKPFEIPAEVYDAWKEKVAE-GAKAEAEWNELFAAYKKAYP 319
|
330
....*....|....*
gi 487904947 325 ELANEFQAAMNGQLP 339
Cdd:pfam00456 320 ELAAEFARRLSGELP 334
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
11-276 |
2.40e-146 |
|
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: 425.38 E-value: 2.40e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 11 NTIRTLSIDAIEKANSGHPGMPMGAAPMAYTLWTQFMKHNPNNPTWFNRDRFVLSAGHGSMLLYSLLHLSGYDvTMDDLK 90
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYL-PEEDLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 91 NFRQWGSKTPGHPEYGHTAGVDATTGPLGQGIATAVGMAMAERHLaakynrdaynVVDHYTYAICGDGDLMEGVSAEASS 170
Cdd:cd02012 80 TFRQLGSRLPGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEKLL----------GFDYRVYVLLGDGELQEGSVWEAAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 171 LAAHLQLGRLVVLYDSNDISLDGDLNR-SFSESVEDRYKAYGWQVIRVeDGNDIEAIAKAIEEAKADEKRPTLIEVRTTI 249
Cdd:cd02012 150 FAGHYKLDNLIAIVDSNRIQIDGPTDDiLFTEDLAKKFEAFGWNVIEV-DGHDVEEILAALEEAKKSKGKPTLIIAKTIK 228
|
250 260
....*....|....*....|....*..
gi 487904947 250 GFGSPNKSGKSASHGSPLGVEETKLTK 276
Cdd:cd02012 229 GKGVPFMENTAKWHGKPLGEEEVELAK 255
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
406-525 |
6.82e-37 |
|
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: 134.54 E-value: 6.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 406 IWYGVREFAMGAAMNGIALHGgLKTYGGTFFVFSDYLRPAIRLAALMQLpVTYVFTHDS-IAVGEDGPTHEPIEQLAALR 484
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHG-LRPVVEIFFTFFDRAKDQIRSAGASGN-VPVVFRHDGgGGVGEDGPTHHSIEDEALLR 95
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 487904947 485 AMPNVSVIRPADGNESVAAWRLALEStNKPTALVLTRQDLP 525
Cdd:smart00861 96 AIPGLKVVAPSDPAEAKGLLRAAIRD-DGPVVIRLERKSLY 135
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
3-666 |
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: 1321.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 3 HSIEQLSINTIRTLSIDAIEKANSGHPGMPMGAAPMAYTLWTQFMKHNPNNPTWFNRDRFVLSAGHGSMLLYSLLHLSGY 82
Cdd:COG0021 1 MPLDQLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKHNPANPKWPNRDRFVLSAGHGSMLLYSLLHLTGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 83 DVTMDDLKNFRQWGSKTPGHPEYGHTAGVDATTGPLGQGIATAVGMAMAERHLAAKYNRDAYNVVDHYTYAICGDGDLME 162
Cdd:COG0021 81 DLSLDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGIANAVGMAIAERHLAARFNRPGHDIVDHYTYVIAGDGDLME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 163 GVSAEASSLAAHLQLGRLVVLYDSNDISLDGDLNRSFSESVEDRYKAYGWQVIRVEDGNDIEAIAKAIEEAKADEKRPTL 242
Cdd:COG0021 161 GISHEAASLAGHLKLGKLIVLYDDNGISIDGDTDLAFSEDVAKRFEAYGWHVIRVEDGHDLEAIDAAIEAAKAETDKPTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 243 IEVRTTIGFGSPNKSGKSASHGSPLGVEETKLTKEAYAWTAEQdFHVAEEVYDNFRKTVQDvGETAQAEWNTMLGEYAQA 322
Cdd:COG0021 241 IICKTIIGYGSPNKQGTAKAHGAPLGAEEIAATKEALGWPPEP-FEVPDEVYAHWRAAGER-GAAAEAEWNERFAAYAAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 323 YPELANEFQAAMNGQLPEGWEQNLPTYELGSKA-ATRNSSGAVINAIAESVPSFFGGSADLAGSNKTYMNNEKDFTRDDY 401
Cdd:COG0021 319 YPELAAELERRLAGELPEDWDAALPAFEADAKGvATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIKGAGSFSPEDP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 402 SGKNIWYGVREFAMGAAMNGIALHGGLKTYGGTFFVFSDYLRPAIRLAALMQLPVTYVFTHDSIAVGEDGPTHEPIEQLA 481
Cdd:COG0021 399 SGRNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFSDYMRPAIRLAALMKLPVIYVFTHDSIGLGEDGPTHQPVEQLA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 482 ALRAMPNVSVIRPADGNESVAAWRLALESTNKPTALVLTRQDLPTLEGAKDDtYEKVAKGAYIVSASkKETADVILLATG 561
Cdd:COG0021 479 SLRAIPNLDVIRPADANETAAAWKLALERKDGPTALILSRQNLPTLDRTAAA-AEGVAKGAYVLADA-EGTPDVILIATG 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 562 SEVSLAVEAQKALAVDGVDASVVSMPSMDRFEAQTAEYKESVLPKAVTKRFAIEMGATFGWHRYVGLEGDVLGIDTFGAS 641
Cdd:COG0021 557 SEVSLAVEAAELLAAEGIKVRVVSMPSWELFEAQDAAYRESVLPPAVRARVAVEAGVTDGWYKYVGLDGAVIGIDTFGAS 636
|
650 660
....*....|....*....|....*
gi 487904947 642 APGEKIMEEYGFTVENVVRKVKEML 666
Cdd:COG0021 637 APAKVLFEEFGFTVENVVAAAKELL 661
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
8-666 |
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: 1048.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 8 LSINTIRTLSIDAIEKANSGHPGMPMGAAPMAYTLWTQFMKHNPNNPTWFNRDRFVLSAGHGSMLLYSLLHLSGYDVTMD 87
Cdd:TIGR00232 2 KLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKFNPTNPKWINRDRFVLSNGHGSMLLYSLLHLTGYDLSIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 88 DLKNFRQWGSKTPGHPEYGHTAGVDATTGPLGQGIATAVGMAMAERHLAAKYNRDAYNVVDHYTYAICGDGDLMEGVSAE 167
Cdd:TIGR00232 82 DLKQFRQLHSKTPGHPEYGHTAGVEATTGPLGQGIANAVGMAIAEKTLAATFNKPGFEIVDHYTYVFVGDGCLQEGISYE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 168 ASSLAAHLQLGRLVVLYDSNDISLDGDLNRSFSESVEDRYKAYGWQVIRVEDGNDIEAIAKAIEEAKADEKRPTLIEVRT 247
Cdd:TIGR00232 162 VASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDVAKRFEAYGWEVLEVEDGHDLAAIDAAIEEAKASTDKPTLIEVKT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 248 TIGFGSPNKSGKSASHGSPLGVEETKLTKEAYAWTAEQdFHVAEEVYDNFRKTVQDVGETAQAEWNTMLGEYAQAYPELA 327
Cdd:TIGR00232 242 TIGFGSPNKAGTHGVHGAPLGDEEVALTKKNLGWNYNP-FEIPQEVYDHFKKTVKERGAKAEQEWNELFAAYKKKYPELA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 328 NEFQAAMNGQLPEGWEQNLPTYEL-GSKAATRNSSGAVINAIAESVPSFFGGSADLAGSNKTYMNNEKDFtRDDYSGKNI 406
Cdd:TIGR00232 321 AEFTRRLSGELPADWDKQLPEFKVkLQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKGSGDL-HENPLGNYI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 407 WYGVREFAMGAAMNGIALHGGLKTYGGTFFVFSDYLRPAIRLAALMQLPVTYVFTHDSIAVGEDGPTHEPIEQLAALRAM 486
Cdd:TIGR00232 400 HYGVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQLASLRAI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 487 PNVSVIRPADGNESVAAWRLALESTNKPTALVLTRQDLPTLEGakdDTYEKVAKGAYIVSASKKetADVILLATGSEVSL 566
Cdd:TIGR00232 480 PNLSVWRPCDGNETAAAWKYALESQDGPTALILSRQNLPQLEE---SSLEKVLKGGYVLKDSKG--PDLILIATGSEVQL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 567 AVEAQKALAVDGVDASVVSMPSMDRFEAQTAEYKESVLPKAVTkRFAIEMGATFGWHRYVGLEGDVLGIDTFGASAPGEK 646
Cdd:TIGR00232 555 AVEAAKKLAAENIKVRVVSMPSFDLFDKQDEEYRESVLPANVT-RLAIEAGAADEWYKYAGLVGAILGMDSFGESAPGDK 633
|
650 660
....*....|....*....|
gi 487904947 647 IMEEYGFTVENVVRKVKEML 666
Cdd:TIGR00232 634 LFEEFGFTVENVVAKAKKLL 653
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
1-666 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 1014.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 1 MSHSIEQLSINTIRTLSIDAIEKANSGHPGMPMGAAPMAYTLWTQFMKHNPNNPTWFNRDRFVLSAGHGSMLLYSLLHLS 80
Cdd:PRK05899 3 MDMELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLHLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 81 GYDVTMDDLKNFRQWGSKTPGHPEYGHTAGVDATTGPLGQGIATAVGMAMAERHLAAKYNRDAYNVVDHYTYAICGDGDL 160
Cdd:PRK05899 83 GYDLSIDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGLANAVGMALAEKYLAALFNRPGLDIVDHYTYVLCGDGDL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 161 MEGVSAEASSLAAHLQLGRLVVLYDSNDISLDGDLNRSFSESVEDRYKAYGWQVIRVeDGNDIEAIAKAIEEAKAdEKRP 240
Cdd:PRK05899 163 MEGISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTEDVKKRFEAYGWHVIEV-DGHDVEAIDAAIEEAKA-STKP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 241 TLIEVRTTIGFGSPNKSGKSASHGSPLGVEETKLTKEAYawtaeqdfhvaeevydnfrktvqdvgetaqaewntmlgeya 320
Cdd:PRK05899 241 TLIIAKTIIGKGAPNKEGTHKVHGAPLGAEEIAAAKKEL----------------------------------------- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 321 qaypelanefqaamngqlpeGWEQnlptyelgskaatRNSSGAVINAIAESVPSFFGGSADLAGSNKTYMNNEKDFTRDD 400
Cdd:PRK05899 280 --------------------GWDY-------------RKASGKALNALAKALPELVGGSADLAGSNNTKIKGSKDFAPED 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 401 YSGKNIWYGVREFAMGAAMNGIALHGGLKTYGGTFFVFSDYLRPAIRLAALMQLPVTYVFTHDSIAVGEDGPTHEPIEQL 480
Cdd:PRK05899 327 YSGRYIHYGVREFAMAAIANGLALHGGFIPFGGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQL 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 481 AALRAMPNVSVIRPADGNESVAAWRLALESTNKPTALVLTRQDLPTLEGAKDDtyEKVAKGAYIVsaskKETADVILLAT 560
Cdd:PRK05899 407 ASLRAIPNLTVIRPADANETAAAWKYALERKDGPSALVLTRQNLPVLERTAQE--EGVAKGGYVL----RDDPDVILIAT 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 561 GSEVSLAVEAQKALAVDGVDASVVSMPSMDRFEAQTAEYKESVLPKAVTKRFAIEMGATFGWHRYVGLEGDVLGIDTFGA 640
Cdd:PRK05899 481 GSEVHLALEAADELEAEGIKVRVVSMPSTELFDEQDAAYKESVLPAAVTARVAVEAGVADGWYKYVGLDGKVLGIDTFGA 560
|
650 660
....*....|....*....|....*.
gi 487904947 641 SAPGEKIMEEYGFTVENVVRKVKEML 666
Cdd:PRK05899 561 SAPADELFKEFGFTVENIVAAAKELL 586
|
|
| PLN02790 |
PLN02790 |
transketolase |
13-666 |
0e+00 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 979.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 13 IRTLSIDAIEKANSGHPGMPMGAAPMAYTLWTQFMKHNPNNPTWFNRDRFVLSAGHGSMLLYSLLHLSGYD-VTMDDLKN 91
Cdd:PLN02790 1 IRFLAIDAVNKANSGHPGLPMGCAPMGHVLYDEVMKYNPKNPYWFNRDRFVLSAGHGCMLQYALLHLAGYDsVQMEDLKQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 92 FRQWGSKTPGHPEYGHTAGVDATTGPLGQGIATAVGMAMAERHLAAKYNRDAYNVVDHYTYAICGDGDLMEGVSAEASSL 171
Cdd:PLN02790 81 FRQWGSRTPGHPENFETPGIEVTTGPLGQGIANAVGLALAEKHLAARFNKPDHKIVDHYTYCILGDGCQMEGISNEAASL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 172 AAHLQLGRLVVLYDSNDISLDGDLNRSFSESVEDRYKAYGWQVIRVEDGN-DIEAIAKAIEEAKADEKRPTLIEVRTTIG 250
Cdd:PLN02790 161 AGHWGLGKLIVLYDDNHISIDGDTEIAFTEDVDKRYEALGWHTIWVKNGNtDYDEIRAAIKEAKAVTDKPTLIKVTTTIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 251 FGSPNKSGKSASHGSPLGVEETKLTKEAYAWTAEQdFHVAEEVYDNFRKtVQDVGETAQAEWNTMLGEYAQAYPELANEF 330
Cdd:PLN02790 241 YGSPNKANSYSVHGAALGEKEVDATRKNLGWPYEP-FHVPEDVKSHWSK-HTKEGAALEAEWNAKFAEYKKKYPEEAAEL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 331 QAAMNGQLPEGWEQNLPTYELGSKA-ATRNSSGAVINAIAESVPSFFGGSADLAGSNKTYMNNEKDFTRDDYSGKNIWYG 409
Cdd:PLN02790 319 KSLISGELPSGWEKALPTFTPEDPAdATRNLSQKCLNALAKVLPGLIGGSADLASSNMTLLKDFGDFQKDTPEERNVRFG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 410 VREFAMGAAMNGIALHG-GLKTYGGTFFVFSDYLRPAIRLAALMQLPVTYVFTHDSIAVGEDGPTHEPIEQLAALRAMPN 488
Cdd:PLN02790 399 VREHGMGAICNGIALHSsGLIPYCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLGEDGPTHQPIEHLASLRAMPN 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 489 VSVIRPADGNESVAAWRLALESTNKPTALVLTRQDLPTLEGakdDTYEKVAKGAYIVS-ASKKETADVILLATGSEVSLA 567
Cdd:PLN02790 479 ILMLRPADGNETAGAYKVAVTNRKRPTVLALSRQKVPNLPG---TSIEGVEKGGYVISdNSSGNKPDLILIGTGSELEIA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 568 VEAQKALAVDGVDASVVSMPSMDRFEAQTAEYKESVLPKAVTKRFAIEMGATFGWHRYVGLEGDVLGIDTFGASAPGEKI 647
Cdd:PLN02790 556 AKAAKELRKEGKKVRVVSMVCWELFEEQSDEYKESVLPSSVTARVSVEAGSTFGWEKYVGSKGKVIGVDRFGASAPAGIL 635
|
650
....*....|....*....
gi 487904947 648 MEEYGFTVENVVRKVKEML 666
Cdd:PLN02790 636 YKEFGFTVENVVAAAKSLL 654
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
1-666 |
0e+00 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 910.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 1 MSHSIEQLSINTIRTLSIDAIEKANSGHPGMPMGAAPMAYTLWTQFMKHNPNNPTWFNRDRFVLSAGHGSMLLYSLLHLS 80
Cdd:PTZ00089 1 MDGAIDEKCANEIRCLSADLVQKANSGHPGAPMGMAPIAHILWSEVMKYNPKDPRWINRDRFVLSNGHASALLYSMLHLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 81 GYDVTMDDLKNFRQWGSKTPGHPEYGHTAGVDATTGPLGQGIATAVGMAMAERHLAAKYNRDAYNVVDHYTYAICGDGDL 160
Cdd:PTZ00089 81 GYDLSMEDLKNFRQLGSRTPGHPERHITPGVEVTTGPLGQGIANAVGLAIAEKHLAAKFNRPGHPIFDNYVYVICGDGCL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 161 MEGVSAEASSLAAHLQLGRLVVLYDSNDISLDGDLNRSFSESVEDRYKAYGWQVIRVEDGN-DIEAIAKAIEEAKADEKR 239
Cdd:PTZ00089 161 QEGVSQEALSLAGHLGLEKLIVLYDDNKITIDGNTDLSFTEDVEKKYEAYGWHVIEVDNGNtDFDGLRKAIEEAKKSKGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 240 PTLIEVRTTIGFGSpNKSGKSASHGSPLGVEETKLTKEAYAWTAEQDFHVAEEVYDNFRKtVQDVGETAQAEWNTMLGEY 319
Cdd:PTZ00089 241 PKLIIVKTTIGYGS-SKAGTEKVHGAPLGDEDIAQVKELFGLDPEKKFHVSEEVRQFFEQ-HVEKKKENYEAWKKRFAKY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 320 AQAYPELANEFQAAMNGQLPEGWEQNLPTYELGSKA-ATRNSSGAVINAIAESVPSFFGGSADLAGSNKTYMNNEKDFTR 398
Cdd:PTZ00089 319 TAAFPKEAQAIERRFKGELPPGWEKKLPKYTTNDKAiATRKASENVLNPLFQILPELIGGSADLTPSNLTRPKEANDFTK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 399 DDYSGKNIWYGVREFAMGAAMNGIALHGGLKTYGGTFFVFSDYLRPAIRLAALMQLPVTYVFTHDSIAVGEDGPTHEPIE 478
Cdd:PTZ00089 399 ASPEGRYIRFGVREHAMCAIMNGIAAHGGFIPFGATFLNFYGYALGAVRLAALSHHPVIYVATHDSIGLGEDGPTHQPVE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 479 QLAALRAMPNVSVIRPADGNESVAAWRLALESTNKPTALVLTRQDLPTLEGAKddtYEKVAKGAYIVS---ASKKetadV 555
Cdd:PTZ00089 479 TLALLRATPNLLVIRPADGTETSGAYALALANAKTPTILCLSRQNTPPLPGSS---IEGVLKGAYIVVdftNSPQ----L 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 556 ILLATGSEVSLAVEAQKALaVDGVDASVVSMPSMDRFEAQTAEYKESVLPKAVTKRFAIEMGATFGWHRYVGLEgdvLGI 635
Cdd:PTZ00089 552 ILVASGSEVSLCVEAAKAL-SKELNVRVVSMPCWELFDQQSEEYQQSVLPSGGVPVLSVEAYVSFGWEKYSHVH---VGI 627
|
650 660 670
....*....|....*....|....*....|.
gi 487904947 636 DTFGASAPGEKIMEEYGFTVENVVRKVKEML 666
Cdd:PTZ00089 628 SGFGASAPANALYKHFGFTVENVVEKARALA 658
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
5-339 |
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: 565.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 5 IEQLSINTIRTLSIDAIEKANSGHPGMPMGAAPMAYTLWTQFMKHNPNNPTWFNRDRFVLSAGHGSMLLYSLLHLSGYDV 84
Cdd:pfam00456 1 IDKRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 85 TMDDLKNFRQWGSKTPGHPEYGHTAGVDATTGPLGQGIATAVGMAMAERHLAAKYNRDAYNVVDHYTYAICGDGDLMEGV 164
Cdd:pfam00456 81 SMEDLKSFRQLGSKTPGHPEFGHTAGVEVTTGPLGQGIANAVGMAIAERNLAATYNRPGFDIVDHYTYVFLGDGCLMEGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 165 SAEASSLAAHLQLGRLVVLYDSNDISLDGDLNRSFSESVEDRYKAYGWQVIRVEDGNDIEAIAKAIEEAKADEKRPTLIE 244
Cdd:pfam00456 161 SSEASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDTAARFEAYGWHVIEVEDGHDVEAIAAAIEEAKAEKDKPTLIK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 245 VRTTIGFGSPNKSGKSASHGSPLGVEETKLTKEAYAWTAEQDFHVAEEVYDNFRKTVQDvGETAQAEWNTMLGEYAQAYP 324
Cdd:pfam00456 241 CRTVIGYGSPNKQGTHDVHGAPLGADEVAALKQKLGWDPYKPFEIPAEVYDAWKEKVAE-GAKAEAEWNELFAAYKKAYP 319
|
330
....*....|....*
gi 487904947 325 ELANEFQAAMNGQLP 339
Cdd:pfam00456 320 ELAAEFARRLSGELP 334
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
11-276 |
2.40e-146 |
|
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: 425.38 E-value: 2.40e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 11 NTIRTLSIDAIEKANSGHPGMPMGAAPMAYTLWTQFMKHNPNNPTWFNRDRFVLSAGHGSMLLYSLLHLSGYDvTMDDLK 90
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGYL-PEEDLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 91 NFRQWGSKTPGHPEYGHTAGVDATTGPLGQGIATAVGMAMAERHLaakynrdaynVVDHYTYAICGDGDLMEGVSAEASS 170
Cdd:cd02012 80 TFRQLGSRLPGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEKLL----------GFDYRVYVLLGDGELQEGSVWEAAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 171 LAAHLQLGRLVVLYDSNDISLDGDLNR-SFSESVEDRYKAYGWQVIRVeDGNDIEAIAKAIEEAKADEKRPTLIEVRTTI 249
Cdd:cd02012 150 FAGHYKLDNLIAIVDSNRIQIDGPTDDiLFTEDLAKKFEAFGWNVIEV-DGHDVEEILAALEEAKKSKGKPTLIIAKTIK 228
|
250 260
....*....|....*....|....*..
gi 487904947 250 GFGSPNKSGKSASHGSPLGVEETKLTK 276
Cdd:cd02012 229 GKGVPFMENTAKWHGKPLGEEEVELAK 255
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
13-271 |
3.81e-75 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 242.29 E-value: 3.81e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 13 IRTLSIDAIEKANSGHPGMPMGAAPMAYTLWTQFMKHNPNNPTWFNRDRFVLSAGHGSMLLYSLLHLSGYdVTMDDLKNF 92
Cdd:COG3959 15 IRRDILRMIYAAGSGHPGGSLSAADILAALYFKVMNIDPKNPDWPDRDRFILSKGHAAPALYAVLAEKGY-FPKEELATF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 93 RQWGSKTPGHPEYGHTAGVDATTGPLGQGIATAVGMAmaerhLAAKYNRDAYNVvdhytYAICGDGDLMEGVSAEASSLA 172
Cdd:COG3959 94 RKLGSRLQGHPDMKKTPGVEMSTGSLGQGLSVAVGMA-----LAAKLDGKDYRV-----YVLLGDGELQEGQVWEAAMAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 173 AHLQLGRLVVLYDSNDISLDG---DLNRsfSESVEDRYKAYGWQVIRVeDGNDIEAIAKAIEEAKADEKRPTLIEVRTTI 249
Cdd:COG3959 164 AHYKLDNLIAIVDRNGLQIDGpteDVMS--LEPLAEKWEAFGWHVIEV-DGHDIEALLAALDEAKAVKGKPTVIIAHTVK 240
|
250 260
....*....|....*....|..
gi 487904947 250 GFGSPNKSGKSASHGSPLGVEE 271
Cdd:COG3959 241 GKGVSFMENRPKWHGKAPNDEE 262
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
359-521 |
6.05e-64 |
|
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), transketolase (TK), and related proteins; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), transketolase (TK), and the beta subunits of the E1 component of the human pyruvate dehydrogenase complex (E1- PDHc), subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Like many TPP-dependent enzymes DXS and TK are homodimers having a PYR and a PP domain on the same subunit. TK has two active sites per dimer which lie between PYR and PP domains of different subunits. For DXS each active site is located at the interface of a PYR and a PP domain from the same subunit. E1-PDHc is an alpha2beta2 dimer-of-heterodimers having two active sites but having the PYR and PP domains arranged on separate subunits, the PYR domains on the beta subunits, the PP domains on the alpha subunits. DXS is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis, it catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. TK catalyzes the transfer of a two-carbon unit from ketose phosphates to aldose phosphates. In heterotrophic organisms, TK provides a link between glycolysis and the pentose phosphate pathway and provides precursors for nucleotide, aromatic amino acid and vitamin biosynthesis. TK also plays a central role in the Calvin cycle in plants. PDHc catalyzes the irreversible oxidative decarboxylation of pyruvate to produce acetyl-CoA in the bridging step between glycolysis and the citric acid cycle. This subfamily includes the beta subunits of the E1 component of the acetoin dehydrogenase complex (ADC) and the branched chain alpha-keto acid dehydrogenase/2-oxoisovalerate dehydrogenase complex (BCADC). ADC participates in the breakdown of acetoin. BCADC catalyzes the oxidative decarboxylation of 4-methyl-2-oxopentanoate, 3-methyl-2-oxopentanoate and 3-methyl-2-oxobutanoate during the breakdown of branched chain amino acids.
Pssm-ID: 132916 [Multi-domain] Cd Length: 156 Bit Score: 208.45 E-value: 6.05e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 359 NSSGAVINAIAESVPSFFGGSADLAGSNKTYMNNEKdftrddYSGKNIWYGVREFAMGAAMNGIALHGgLKTYGGTFFVF 438
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAKK------FPDRFIDVGIAEQNMVGIAAGLALHG-LKPFVSTFSFF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 439 SDYLRPAIR-LAALMQLPVTYVFTHDSIAVGEDGPTHEPIEQLAALRAMPNVSVIRPADGNESVAAWRLALEStNKPTAL 517
Cdd:cd07033 74 LQRAYDQIRhDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEY-DGPVYI 152
|
....
gi 487904947 518 VLTR 521
Cdd:cd07033 153 RLPR 156
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
353-526 |
4.78e-57 |
|
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: 190.84 E-value: 4.78e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 353 SKAATRNSSGAVINAIAESVPSFFGGSADLAGSNKTYMNNEKDFtrdDYSGKNIWYGVREFAMGAAMNGIALHGGLKT-Y 431
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHP---QGAGRVIDTGIAEQAMVGFANGMALHGPLLPpV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 432 GGTFFVFSDYLRPAIR-LAALMQLPVTYVFTHDSIAVGEDGPTHEPIEQLAALRAMPNVSVIRPADGNESVAAWRLALES 510
Cdd:pfam02779 78 EATFSDFLNRADDAIRhGAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRR 157
|
170
....*....|....*..
gi 487904947 511 -TNKPTALVLTRQDLPT 526
Cdd:pfam02779 158 dGRKPVVLRLPRQLLRP 174
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
406-525 |
6.82e-37 |
|
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: 134.54 E-value: 6.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 406 IWYGVREFAMGAAMNGIALHGgLKTYGGTFFVFSDYLRPAIRLAALMQLpVTYVFTHDS-IAVGEDGPTHEPIEQLAALR 484
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHG-LRPVVEIFFTFFDRAKDQIRSAGASGN-VPVVFRHDGgGGVGEDGPTHHSIEDEALLR 95
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 487904947 485 AMPNVSVIRPADGNESVAAWRLALEStNKPTALVLTRQDLP 525
Cdd:smart00861 96 AIPGLKVVAPSDPAEAKGLLRAAIRD-DGPVVIRLERKSLY 135
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
354-666 |
2.13e-36 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 138.68 E-value: 2.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 354 KAATRNSSGAVINAIAESVPSFFGGSADLAGSNKTymnneKDFtRDDYSGKNIWYGVREFAM-GAAMnGIALhGGLKTYG 432
Cdd:COG3958 3 KKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKL-----DKF-AKAFPDRFFNVGIAEQNMvGVAA-GLAL-AGKIPFV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 433 GTFFVFSdYLRPA--IRLA-ALMQLPVTYVFTHDSIAVGEDGPTHEPIEQLAALRAMPNVSVIRPADGNESVAAWRLALE 509
Cdd:COG3958 75 STFAPFL-TGRAYeqIRNDiAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 510 sTNKPTALVLTRQDLPTLegaKDDTYEKVAKGAYIVsaskKETADVILLATGSEVSLAVEAQKALAVDGVDASVVSMPSM 589
Cdd:COG3958 154 -HDGPVYLRLGRGAVPVV---YDEDYEFEIGKARVL----REGKDVTIIATGIMVAEALEAAELLAKEGISARVINMHTI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 590 DRFEAQ-------------TAEykE------------SVLPKAVTKRFaiemgatfgwhRYVGLEgdvlgiDTFGASAPG 644
Cdd:COG3958 226 KPLDEEailkaarktgavvTAE--EhsiigglgsavaEVLAENYPVPL-----------RRIGVP------DRFGESGSP 286
|
330 340
....*....|....*....|..
gi 487904947 645 EKIMEEYGFTVENVVRKVKEML 666
Cdd:COG3958 287 EELLEKYGLDAEGIVAAAKELL 308
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
122-666 |
5.75e-16 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 81.59 E-value: 5.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 122 IATAVGMAMAeRHLAAKYNrdayNVVdhytyAICGDGDLMEGVSAEASSLAAHLQlGRLVVLYDSNDISLD--------- 192
Cdd:PRK12315 119 IALATGLAKA-RDLKGEKG----NII-----AVIGDGSLSGGLALEGLNNAAELK-SNLIIIVNDNQMSIAenhgglykn 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 193 -GDLNRSFSESVEDRYKAYGWQVIRVEDGNDIEAIAKAIEEAKaDEKRPTLIEVRTTIGfgspnksgksasHGSPLGVEE 271
Cdd:PRK12315 188 lKELRDTNGQSENNLFKAMGLDYRYVEDGNDIESLIEAFKEVK-DIDHPIVLHIHTLKG------------KGYQPAEEN 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 272 tkltKEAYAWTAEqdFHVAeevydNFRKTVQDVGETaqaewntmlgeyaqaYPELANEFqaamngqlpegweqnlptyeL 351
Cdd:PRK12315 255 ----KEAFHWHMP--FDLE-----TGQSKVPASGES---------------YSSVTLDY--------------------L 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 352 GSKAATRNSsgavINAIAESVPSFFGgsadlagsnktymnnEKDFTRDdysgkniwYGVREFAMG-AAMNGIALHGGLKT 430
Cdd:PRK12315 289 LKKIKEGKP----VVAINAAIPGVFG---------------LKEFRKK--------YPDQYVDVGiAEQESVAFASGIAA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 431 YGGT--FFVFSDYLRPA----IRLAALMQLPVTYVFTHDSIavGEDGPTHEPIEQLAALRAMPNVSVIRPADGNESVAAW 504
Cdd:PRK12315 342 NGARpvIFVNSTFLQRAydqlSHDLAINNNPAVMIVFGGSI--SGNDVTHLGIFDIPMISNIPNLVYLAPTTKEELIAML 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 505 RLALESTNKPTALVLTRQDLPTLEGAKDD----TYEKVAKGayivsaskketADVILLATGSEVSLAVEAQKALAVD-GV 579
Cdd:PRK12315 420 EWALTQHEHPVAIRVPEHGVESGPTVDTDystlKYEVTKAG-----------EKVAILALGDFYELGEKVAKKLKEElGI 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 580 DASVVSMPSMDRFEAQTAEYKESVLPKAVTKRFAIEMGAtFGWH--RYVGLEG-DVL--GIDT-FGASAPGEKIMEEYGF 653
Cdd:PRK12315 489 DATLINPKFITGLDEELLEKLKEDHELVVTLEDGILDGG-FGEKiaRYYGNSDmKVLnyGAKKeFNDRVPVEELYKRNHL 567
|
570
....*....|...
gi 487904947 654 TVENVVRKVKEML 666
Cdd:PRK12315 568 TPEQIVEDILSVL 580
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
549-658 |
1.59e-15 |
|
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: 73.40 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 549 KKETADVILLATGSEVSLAVEAQKALAVDGVDASVVSMPSMDRFEAQT-----AEYKESVLPKAVTKRFAIEMG--ATFG 621
Cdd:pfam02780 6 LREGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETilesvKKTGRLVTVEEAVPRGGFGSEvaAALA 85
|
90 100 110
....*....|....*....|....*....|....*....
gi 487904947 622 WHRYVGLEGDV--LGIDTFGASAPGEKIMEEYGFTVENV 658
Cdd:pfam02780 86 EEAFDGLDAPVlrVGGPDFPEPGSADELEKLYGLTPEKI 124
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
450-666 |
1.04e-13 |
|
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: 74.28 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 450 ALMQLPVTYVfthdsI--A--VGEDGPTHEPIEQLAALRAMPNVSVIRPADGNESVAAWRLALEStNKPTAL-------- 517
Cdd:COG1154 406 ALQNLPVTFA-----IdrAglVGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALAY-DGPTAIryprgngp 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 518 -VLTRQDLPTLEgakddtyekVAKGAYIvsaskKETADVILLATGSEVSLAVEAQKALAVDGVDASVVSMpsmdRFeaqt 596
Cdd:COG1154 480 gVELPAELEPLP---------IGKGEVL-----REGKDVAILAFGTMVAEALEAAERLAAEGISATVVDA----RF---- 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 597 aeykesVLP--KAVTKRFA--------IEMGAT---FGWH-----RYVGLEGDV--LGI-DTFGASAPGEKIMEEYGFTV 655
Cdd:COG1154 538 ------VKPldEELILELArehdlvvtVEEGVLaggFGSAvleflADAGLDVPVlrLGLpDRFIEHGSRAELLAELGLDA 611
|
250
....*....|.
gi 487904947 656 ENVVRKVKEML 666
Cdd:COG1154 612 EGIARAILELL 622
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
122-666 |
2.14e-13 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 73.19 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 122 IATAVGMAMAeRHLAAKynrDAYNVVdhytyAICGDGDLMEGVSAEASSLAAHLQLGRLVVLYDsNDISLD---GDLNRS 198
Cdd:PRK05444 123 ISAALGMAKA-RDLKGG---EDRKVV-----AVIGDGALTGGMAFEALNNAGDLKSDLIVILND-NEMSISpnvGALSNY 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 199 FSesvedR------YKAYGWQVIRVEDGNDIEAIAKAIEEAKaDEKRPTLIEVRTTIGFGspnksgksashgsplgveet 272
Cdd:PRK05444 193 LA-----RlrsstlFEELGFNYIGPIDGHDLDALIETLKNAK-DLKGPVLLHVVTKKGKG-------------------- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 273 kltkeaYAWtAEQD---FHvAEEVYDnfrktvqdvgetaqaewntmlgeyaqayPElanefqaamNGQLPEGWEQNLPTY 349
Cdd:PRK05444 247 ------YAP-AEADpikYH-GVGKFD----------------------------PE---------TGEQPKSSKPGKPSY 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 350 ---------ELGSK--------AATRNSSGavINAIAESVPS-FFggsaDLagsnktymnnekdftrddysgkniwyGVR 411
Cdd:PRK05444 282 tkvfgetlcELAEKdpkivaitAAMPEGTG--LVKFSKRFPDrYF----DV--------------------------GIA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 412 E-----FAMGAAMngialhGGLK----TYGgTFF------VFSDylrpairlAALMQLPVTYVfthdsI--A--VGEDGP 472
Cdd:PRK05444 330 EqhavtFAAGLAT------EGLKpvvaIYS-TFLqraydqVIHD--------VALQNLPVTFA-----IdrAglVGADGP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 473 THEPIEQLAALRAMPNVSVIRPADGNESVAAWRLALESTNKPTALVLTR-----QDLPTLEGAKDDTYEKVAKGayivsa 547
Cdd:PRK05444 390 THQGAFDLSYLRCIPNMVIMAPSDENELRQMLYTALAYDDGPIAIRYPRgngvgVELPELEPLPIGKGEVLREG------ 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 548 skketADVILLATGSEVSLAVEAQKALAvdgvDASVVSMpsmdRFeaqtaeykesVLP--KAVTKRFA--------IEMG 617
Cdd:PRK05444 464 -----EDVAILAFGTMLAEALKAAERLA----SATVVDA----RF----------VKPldEELLLELAakhdlvvtVEEG 520
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 618 AT---FGWH-----RYVGLEGDV--LGI-DTFGASAPGEKIMEEYGFTVENVVRKVKEML 666
Cdd:PRK05444 521 AImggFGSAvleflADHGLDVPVlnLGLpDEFIDHGSREELLAELGLDAEGIARRILELL 580
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
13-666 |
3.25e-13 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 72.83 E-value: 3.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 13 IRTLSIDAIEKAnSGHPGMPMGAAPMAYTLWTQFmkhnpNNPtwfnRDRFVLSAGHGSmllYSLLHLSGydvTMDDLKNF 92
Cdd:PRK12571 33 LRAEVISAVSET-GGHLGSSLGVVELTVALHAVF-----NTP----KDKLVWDVGHQC---YPHKILTG---RRDRFRTL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 93 RQWG--------SKTPGHP-EYGHTAGVdattgplgqgIATAVGMAMAerhlaakynRDAYNVVDHyTYAICGDGDLMEG 163
Cdd:PRK12571 97 RQKGglsgftkrSESEYDPfGAAHSSTS----------ISAALGFAKA---------RALGQPDGD-VVAVIGDGSLTAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 164 VSAEASSLAAHLQlGRLVVLYDSNDISLD---GDLN---------------RSFSESVEDR------------------- 206
Cdd:PRK12571 157 MAYEALNNAGAAD-RRLIVILNDNEMSIAppvGALAaylstlrssdpfarlRAIAKGVEERlpgplrdgarrarelvtgm 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 207 ------YKAYGWQVIRVEDGNDIEAIAKAIEEAKADEKRPTLIEVRTTIGFG-SPNKSGKSASHG----SPLGVEETKLT 275
Cdd:PRK12571 236 igggtlFEELGFTYVGPIDGHDMEALLSVLRAARARADGPVLVHVVTEKGRGyAPAEADEDKYHAvgkfDVVTGLQKKSA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 276 KEAYAWTA---EQDFHVAEEvydnfRKTVqdVGETAQAEWNTMLGEYAQAYPElanefqaamngqlpegweqnlPTYELG 352
Cdd:PRK12571 316 PSAPSYTSvfgEELTKEAAE-----DSDI--VAITAAMPLGTGLDKLQKRFPN---------------------RVFDVG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 353 skaatrnssgavinaIAESvpsffggsadlagsnktymnnekdftrddysgkniwYGVrEFAMGAAmngialHGGLKTYg 432
Cdd:PRK12571 368 ---------------IAEQ------------------------------------HAV-TFAAGLA------AAGLKPF- 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 433 gtFFVFSDYLRPA----IRLAALMQLPVTYVFTHDSIaVGEDGPTHEPIEQLAALRAMPNVSVIRPADGNESVAAWRLAL 508
Cdd:PRK12571 389 --CAVYSTFLQRGydqlLHDVALQNLPVRFVLDRAGL-VGADGATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLRTAA 465
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 509 ESTNKPTALVLTRQDLPTLEGAKDDTYEKVAKGAYIvsaskKETADVILLATGSEVSLAVEAQKALAVDGVDASVVSMps 588
Cdd:PRK12571 466 AHDDGPIAVRFPRGEGVGVEIPAEGTILGIGKGRVP-----REGPDVAILSVGAHLHECLDAADLLEAEGISVTVADP-- 538
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 589 mdRFeaqTAEYKESVLPKAVTKRFAI---EMGAT--FGWH------RYVGLEGDV----LGI-DTFGASAPGEKIMEEYG 652
Cdd:PRK12571 539 --RF---VKPLDEALTDLLVRHHIVViveEQGAMggFGAHvlhhlaDTGLLDGGLklrtLGLpDRFIDHASREEMYAEAG 613
|
730
....*....|....
gi 487904947 653 FTVENVVRKVKEML 666
Cdd:PRK12571 614 LTAPDIAAAVTGAL 627
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
102-247 |
2.77e-12 |
|
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: 65.35 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 102 HPEYGHTAGVDATTGPLGQGIATAVGMAMAERhlaakynrdaynvvDHYTYAICGDGDLMEGVsAEASSlAAHLQLGrLV 181
Cdd:cd00568 32 PLRRGRRFLTSTGFGAMGYGLPAAIGAALAAP--------------DRPVVCIAGDGGFMMTG-QELAT-AVRYGLP-VI 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487904947 182 VLYDSNDI--------SLDGDLNRSFSESVEDRY----KAYGWQVIRVEdgnDIEAIAKAIEEAKAdEKRPTLIEVRT 247
Cdd:cd00568 95 VVVFNNGGygtirmhqEAFYGGRVSGTDLSNPDFaalaEAYGAKGVRVE---DPEDLEAALAEALA-AGGPALIEVKT 168
|
|
| TPP_E1_EcPDC_like |
cd02017 |
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ... |
4-217 |
4.97e-12 |
|
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: 68.10 E-value: 4.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 4 SIEQLSINTIRTLSIDAIEKANS------GHPGMPMGAAPMAYTLWTQFmKHNPNNPTWFNRdrfVLSAGHGSMLLYSLL 77
Cdd:cd02017 2 EIERRIRSLIRWNAMAMVHRANKkdlgigGHIATFASAATLYEVGFNHF-FRARGEGGGGDL---VYFQGHASPGIYARA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 78 HLSGyDVTMDDLKNFRQWGSKtPGHPEYGHTAG----VDATTGPLGQGIATAVGMAMAERHLAAK-YNRDAynvvDHYTY 152
Cdd:cd02017 78 FLEG-RLTEEQLDNFRQEVGG-GGLSSYPHPWLmpdfWEFPTVSMGLGPIQAIYQARFNRYLEDRgLKDTS----DQKVW 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487904947 153 AICGDGDLMEGVSAEASSLAAHLQLGRLVVLYDSNDISLDGDL--NRSFSESVEDRYKAYGWQVIRV 217
Cdd:cd02017 152 AFLGDGEMDEPESLGAIGLAAREKLDNLIFVVNCNLQRLDGPVrgNGKIIQELEGIFRGAGWNVIKV 218
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
113-247 |
1.16e-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: 65.98 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 113 ATTGPLGQGIATAVGMAMAerhlaAKYNRDaynvvDHYTYAICGDGDLMEGVSAEASSLAAHLQLGRLVVLYDsNDISLD 192
Cdd:cd02000 101 GGNGIVGGQVPLAAGAALA-----LKYRGE-----DRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFVCEN-NGYAIS 169
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 487904947 193 GDLNRSF-SESVEDRYKAYGWQVIRVeDGNDIEAIAKAIEEAKA---DEKRPTLIEVRT 247
Cdd:cd02000 170 TPTSRQTaGTSIADRAAAYGIPGIRV-DGNDVLAVYEAAKEAVErarAGGGPTLIEAVT 227
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
114-252 |
1.40e-09 |
|
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: 57.94 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 114 TTGPLGQGIATAVGMAmaerhLAAKYNRDAYNVVdhytyAICGDGDLMEGVSAEASSLAAHLQLGRLVVLYDsNDISLdg 193
Cdd:cd02007 73 GTGHSSTSISAALGMA-----VARDLKGKKRKVI-----AVIGDGALTGGMAFEALNNAGYLKSNMIVILND-NEMSI-- 139
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487904947 194 dlnrsfSESVEDR---YKAYGWQVIRVEDGNDIEAIAKAIEEAKaDEKRPTLIEVRTTIGFG 252
Cdd:cd02007 140 ------SPNVGTPgnlFEELGFRYIGPVDGHNIEALIKVLKEVK-DLKGPVLLHVVTKKGKG 194
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
113-247 |
3.14e-08 |
|
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins similar to Pseudomonas putida benzoylformate decarboxylase (BFDC). P. putida BFDC plays a role in the mandelate pathway, catalyzing the conversion of benzoylformate to benzaldehyde and carbon dioxide. This enzyme is dependent on TPP and a divalent metal cation as cofactors.
Pssm-ID: 238960 [Multi-domain] Cd Length: 178 Bit Score: 53.75 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 113 ATTGPLGQGIATAVGMAMAERhlaakynrdaynvvDHYTYAICGDGDLMEGVSAEASslAAHLQLGRLVVLYD------- 185
Cdd:cd02002 46 LRGGGLGWGLPAAVGAALANP--------------DRKVVAIIGDGSFMYTIQALWT--AARYGLPVTVVILNnrgygal 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487904947 186 ---------SNDISLDGDLNRSFSESVedRY----KAYGWQVIRVEDGNDIEAiakAIEEAKAdEKRPTLIEVRT 247
Cdd:cd02002 110 rsflkrvgpEGPGENAPDGLDLLDPGI--DFaaiaKAFGVEAERVETPEELDE---ALREALA-EGGPALIEVVV 178
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
93-245 |
9.43e-07 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 48.74 E-value: 9.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 93 RQWGSKTPGH--PEYGHtagvdattGPLGQGIATAVGMAMAERHlaakynrdaYNVVdhytyAICGDGDLMegVSAEASS 170
Cdd:pfam02775 11 QYYRFRPPRRylTSGGL--------GTMGYGLPAAIGAKLARPD---------RPVV-----AIAGDGGFQ--MNLQELA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 171 LAAHLQLGRLVVLYDsNDI-------SLDGDLNRSFSESVEDRY--------KAYGWQVIRVEDGNDIEAiakAIEEAKa 235
Cdd:pfam02775 67 TAVRYNLPITVVVLN-NGGygmtrgqQTPFGGGRYSGPSGKILPpvdfaklaEAYGAKGARVESPEELEE---ALKEAL- 141
|
170
....*....|
gi 487904947 236 DEKRPTLIEV 245
Cdd:pfam02775 142 EHDGPALIDV 151
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
113-329 |
3.81e-06 |
|
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: 49.25 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 113 ATTGPLGQGIAtavgmamaerhLAAKYNRDayNVVdhyTYAICGDGDLMEGVSAEASSLAAHLQLGrlVVLYDSND---I 189
Cdd:pfam00676 104 GAQVPLGAGIA-----------LAAKYRGK--KEV---AITLYGDGAANQGDFFEGLNFAALWKLP--VIFVCENNqygI 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 190 SLDGDLNRSfSESVEDRYKAYGWQVIRVeDGNDIEAIAKAIEEAKA---DEKRPTLIEVrTTIGFGSPNKSGKSASHGSP 266
Cdd:pfam00676 166 STPAERASA-STTYADRARGYGIPGLHV-DGMDPLAVYQASKFAAErarTGKGPFLIEL-VTYRYGGHSMSDDPSTYRTR 242
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487904947 267 LGVEETKLTK---EAYAWTAEQDFHVAEEVYDNFRKTVQDVGETAQAEwntmlgeyAQAYPELANE 329
Cdd:pfam00676 243 DEYEEVRKKKdpiQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKK--------AESAPEPHPE 300
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
116-247 |
1.21e-05 |
|
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439799 [Multi-domain] Cd Length: 548 Bit Score: 48.23 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487904947 116 GPLGQGIATAVGMAMAerhlaakyNRDAyNVVdhytyAICGDGDLMEGVSAEASslAAHLQLGRLVVLYDsndislDGDL 195
Cdd:COG0028 412 GTMGYGLPAAIGAKLA--------RPDR-PVV-----AITGDGGFQMNLQELAT--AVRYGLPVKVVVLN------NGGL 469
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487904947 196 N--RSFSESV-EDRY--------------KAYGWQVIRVEDGNDIEAiakAIEEAKAdEKRPTLIEVRT 247
Cdd:COG0028 470 GmvRQWQELFyGGRYsgtdlpnpdfaklaEAFGAKGERVETPEELEA---ALEEALA-SDGPALIDVRV 534
|
|
| |
