|
Name |
Accession |
Description |
Interval |
E-value |
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
9-662 |
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: 1174.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 9 TEKDLLLINTIRFLSVDQVERAKSGHPGMPLGASHIAYLIYDRFLRFNPKNPNWINRDRFVLSAGHASAMLYSLLFVMGY 88
Cdd:COG0021 1 MPLDQLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKHNPANPKWPNRDRFVLSAGHGSMLLYSLLHLTGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 89 DLDIEDLKQFRQLNSKTPGHPESFLTPGVEATTGPLGQGIGNAVGMALAERFLSEKFNKEDFPIIDHYTFTLVSDGDLME 168
Cdd:COG0021 81 DLSLDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGIANAVGMAIAERHLAARFNRPGHDIVDHYTYVIAGDGDLME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 169 GVSSEVAQLAGHWKLNKLVVIWDNNRVSIDGPTSLAWSEDVLKRFEAFGWFVQEVEDGYDLEKLEKAIKKALEQKEKPSF 248
Cdd:COG0021 161 GISHEAASLAGHLKLGKLIVLYDDNGISIDGDTDLAFSEDVAKRFEAYGWHVIRVEDGHDLEAIDAAIEAAKAETDKPTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 249 ISVRTHLAYGSP-KQDDASAHGAPLGKELVLQTKRNFGWPEDEFFVPEEVWLYRSEKIKKGELLEKQWQEMFQEYVKKYP 327
Cdd:COG0021 241 IICKTIIGYGSPnKQGTAKAHGAPLGAEEIAATKEALGWPPEPFEVPDEVYAHWRAAGERGAAAEAEWNERFAAYAAAYP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 328 QEGELLLKVFSRDWGEDYKNVLPDF---REPMATRQASGKVLNSISKVIPTLFGGSADLSESNNTYLHEEGDF----PKG 400
Cdd:COG0021 321 ELAAELERRLAGELPEDWDAALPAFeadAKGVATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIKGAGSFspedPSG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 401 RNLHFGVREHAMGTILNGMAYHGGVLPYGGTFLVFSDYMRPSIRMAALSKLQVVYVFTHDSIGLGEDGPTHQPVEQLSSL 480
Cdd:COG0021 401 RNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFSDYMRPAIRLAALMKLPVIYVFTHDSIGLGEDGPTHQPVEQLASL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 481 RLIPNLFVLRPADANEVSVAWQIAIERKEGPTAIVLTRQKLPLIDRQKYSSHwECLKGAYVLADGGEETQVVIFASGSEV 560
Cdd:COG0021 481 RAIPNLDVIRPADANETAAAWKLALERKDGPTALILSRQNLPTLDRTAAAAE-GVAKGAYVLADAEGTPDVILIATGSEV 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 561 HPALKAKQILEEKGIKVSVVNVFSFELFETQPEEYKRKVLMRNVKKRVAVEAGRGLVWHKFVGMDGLIISMEEFGKSAPG 640
Cdd:COG0021 560 SLAVEAAELLAAEGIKVRVVSMPSWELFEAQDAAYRESVLPPAVRARVAVEAGVTDGWYKYVGLDGAVIGIDTFGASAPA 639
|
650 660
....*....|....*....|..
gi 2686872248 641 EKLMEHFGFVGEEIARRIERWL 662
Cdd:COG0021 640 KVLFEEFGFTVENVVAAAKELL 661
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
9-662 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 928.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 9 TEKDLLLINTIRFLSVDQVERAKSGHPGMPLGASHIAYLIYDRFLRFNPKNPNWINRDRFVLSAGHASAMLYSLLFVMGY 88
Cdd:PRK05899 5 MELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLHLAGY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 89 DLDIEDLKQFRQLNSKTPGHPESFLTPGVEATTGPLGQGIGNAVGMALAERFLSEKFNKEDFPIIDHYTFTLVSDGDLME 168
Cdd:PRK05899 85 DLSIDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGLANAVGMALAEKYLAALFNRPGLDIVDHYTYVLCGDGDLME 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 169 GVSSEVAQLAGHWKLNKLVVIWDNNRVSIDGPTSLAWSEDVLKRFEAFGWFVQEVeDGYDLEKLEKAIKKALEQKeKPSF 248
Cdd:PRK05899 165 GISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTEDVKKRFEAYGWHVIEV-DGHDVEAIDAAIEEAKAST-KPTL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 249 ISVRTHLAYGSP-KQDDASAHGAPLGKELVLQTKRNFGWPEdeffvpeevwlyrsekikkgellekqwqemfqeyvkkyp 327
Cdd:PRK05899 243 IIAKTIIGKGAPnKEGTHKVHGAPLGAEEIAAAKKELGWDY--------------------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 328 qegelllkvfsrdwgedyknvlpdfrepmatRQASGKVLNSISKVIPTLFGGSADLSESNNTYLHEEGDFPK----GRNL 403
Cdd:PRK05899 284 -------------------------------RKASGKALNALAKALPELVGGSADLAGSNNTKIKGSKDFAPedysGRYI 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 404 HFGVREHAMGTILNGMAYHGGVLPYGGTFLVFSDYMRPSIRMAALSKLQVVYVFTHDSIGLGEDGPTHQPVEQLSSLRLI 483
Cdd:PRK05899 333 HYGVREFAMAAIANGLALHGGFIPFGGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAI 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 484 PNLFVLRPADANEVSVAWQIAIERKEGPTAIVLTRQKLPLIDRQKYSShwECLKGAYVLADGGeetQVVIFASGSEVHPA 563
Cdd:PRK05899 413 PNLTVIRPADANETAAAWKYALERKDGPSALVLTRQNLPVLERTAQEE--GVAKGGYVLRDDP---DVILIATGSEVHLA 487
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 564 LKAKQILEEKGIKVSVVNVFSFELFETQPEEYKRKVLMRNVKKRVAVEAGRGLVWHKFVGMDGLIISMEEFGKSAPGEKL 643
Cdd:PRK05899 488 LEAADELEAEGIKVRVVSMPSTELFDEQDAAYKESVLPAAVTARVAVEAGVADGWYKYVGLDGKVLGIDTFGASAPADEL 567
|
650
....*....|....*....
gi 2686872248 644 MEHFGFVGEEIARRIERWL 662
Cdd:PRK05899 568 FKEFGFTVENIVAAAKELL 586
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
14-662 |
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: 901.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 14 LLINTIRFLSVDQVERAKSGHPGMPLGASHIAYLIYDRFLRFNPKNPNWINRDRFVLSAGHASAMLYSLLFVMGYDLDIE 93
Cdd:TIGR00232 2 KLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKFNPTNPKWINRDRFVLSNGHGSMLLYSLLHLTGYDLSIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 94 DLKQFRQLNSKTPGHPESFLTPGVEATTGPLGQGIGNAVGMALAERFLSEKFNKEDFPIIDHYTFTLVSDGDLMEGVSSE 173
Cdd:TIGR00232 82 DLKQFRQLHSKTPGHPEYGHTAGVEATTGPLGQGIANAVGMAIAEKTLAATFNKPGFEIVDHYTYVFVGDGCLQEGISYE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 174 VAQLAGHWKLNKLVVIWDNNRVSIDGPTSLAWSEDVLKRFEAFGWFVQEVEDGYDLEKLEKAIKKALEQKEKPSFISVRT 253
Cdd:TIGR00232 162 VASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDVAKRFEAYGWEVLEVEDGHDLAAIDAAIEEAKASTDKPTLIEVKT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 254 HLAYGSP-KQDDASAHGAPLGKELVLQTKRNFGWPEDEFFVPEEVWLYRSEKIK-KGELLEKQWQEMFQEYVKKYPQEGE 331
Cdd:TIGR00232 242 TIGFGSPnKAGTHGVHGAPLGDEEVALTKKNLGWNYNPFEIPQEVYDHFKKTVKeRGAKAEQEWNELFAAYKKKYPELAA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 332 LLLKVFSRDWGEDYKNVLPDFR---EPMATRQASGKVLNSISKVIPTLFGGSADLSESNNTYLHEEGDFPK---GRNLHF 405
Cdd:TIGR00232 322 EFTRRLSGELPADWDKQLPEFKvklQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKGSGDLHEnplGNYIHY 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 406 GVREHAMGTILNGMAYHGGVLPYGGTFLVFSDYMRPSIRMAALSKLQVVYVFTHDSIGLGEDGPTHQPVEQLSSLRLIPN 485
Cdd:TIGR00232 402 GVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQLASLRAIPN 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 486 LFVLRPADANEVSVAWQIAIERKEGPTAIVLTRQKLPLIDRqkySSHWECLKGAYVLADgGEETQVVIFASGSEVHPALK 565
Cdd:TIGR00232 482 LSVWRPCDGNETAAAWKYALESQDGPTALILSRQNLPQLEE---SSLEKVLKGGYVLKD-SKGPDLILIATGSEVQLAVE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 566 AKQILEEKGIKVSVVNVFSFELFETQPEEYKRKVLMRNVkKRVAVEAGRGLVWHKFVGMDGLIISMEEFGKSAPGEKLME 645
Cdd:TIGR00232 558 AAKKLAAENIKVRVVSMPSFDLFDKQDEEYRESVLPANV-TRLAIEAGAADEWYKYAGLVGAILGMDSFGESAPGDKLFE 636
|
650
....*....|....*..
gi 2686872248 646 HFGFVGEEIARRIERWL 662
Cdd:TIGR00232 637 EFGFTVENVVAKAKKLL 653
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
12-335 |
1.24e-167 |
|
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: 482.66 E-value: 1.24e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 12 DLLLINTIRFLSVDQVERAKSGHPGMPLGASHIAYLIYDRFLRFNPKNPNWINRDRFVLSAGHASAMLYSLLFVMGYDLD 91
Cdd:pfam00456 2 DKRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYDLS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 92 IEDLKQFRQLNSKTPGHPESFLTPGVEATTGPLGQGIGNAVGMALAERFLSEKFNKEDFPIIDHYTFTLVSDGDLMEGVS 171
Cdd:pfam00456 82 MEDLKSFRQLGSKTPGHPEFGHTAGVEVTTGPLGQGIANAVGMAIAERNLAATYNRPGFDIVDHYTYVFLGDGCLMEGVS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 172 SEVAQLAGHWKLNKLVVIWDNNRVSIDGPTSLAWSEDVLKRFEAFGWFVQEVEDGYDLEKLEKAIKKALEQKEKPSFISV 251
Cdd:pfam00456 162 SEASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDTAARFEAYGWHVIEVEDGHDVEAIAAAIEEAKAEKDKPTLIKC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 252 RTHLAYGSP-KQDDASAHGAPLGKELVLQTKRNFGW-PEDEFFVPEEVWLYRSEKIKKGELLEKQWQEMFQEYVKKYPQE 329
Cdd:pfam00456 242 RTVIGYGSPnKQGTHDVHGAPLGADEVAALKQKLGWdPYKPFEIPAEVYDAWKEKVAEGAKAEAEWNELFAAYKKAYPEL 321
|
....*.
gi 2686872248 330 GELLLK 335
Cdd:pfam00456 322 AAEFAR 327
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
17-281 |
4.36e-135 |
|
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: 396.49 E-value: 4.36e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 17 NTIRFLSVDQVERAKSGHPGMPLGASHIAYLIYDRFLRFNPKNPNWINRDRFVLSAGHASAMLYSLLFVMGYdLDIEDLK 96
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGY-LPEEDLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 97 QFRQLNSKTPGHPESFLTPGVEATTGPLGQGIGNAVGMALAERFLsekfnkedfpIIDHYTFTLVSDGDLMEGVSSEVAQ 176
Cdd:cd02012 80 TFRQLGSRLPGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEKLL----------GFDYRVYVLLGDGELQEGSVWEAAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 177 LAGHWKLNKLVVIWDNNRVSIDGPTS-LAWSEDVLKRFEAFGWFVQEVeDGYDLEKLEKAIKKALEQKEKPSFISVRTHL 255
Cdd:cd02012 150 FAGHYKLDNLIAIVDSNRIQIDGPTDdILFTEDLAKKFEAFGWNVIEV-DGHDVEEILAALEEAKKSKGKPTLIIAKTIK 228
|
250 260
....*....|....*....|....*..
gi 2686872248 256 AYGSP-KQDDASAHGAPLGKELVLQTK 281
Cdd:cd02012 229 GKGVPfMENTAKWHGKPLGEEEVELAK 255
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
354-522 |
1.08e-42 |
|
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: 150.33 E-value: 1.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 354 EPMATRQASGKVLNSIskviptlfggsadlsesnntylheegdfpkgrNLHFGVREHAMGTILNGMAYHGGVlPYGGTFL 433
Cdd:smart00861 1 KKIATRKAFGEALAEL--------------------------------AIDTGIAEQAMVGFAAGLALHGLR-PVVEIFF 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 434 VFSDYMRPSIRMAALSKlQVVYVFTHDS-IGLGEDGPTHQPVEQLSSLRLIPNLFVLRPADANEVSVAWQIAIERKeGPT 512
Cdd:smart00861 48 TFFDRAKDQIRSAGASG-NVPVVFRHDGgGGVGEDGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDD-GPV 125
|
170
....*....|
gi 2686872248 513 AIVLTRQKLP 522
Cdd:smart00861 126 VIRLERKSLY 135
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
9-662 |
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: 1174.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 9 TEKDLLLINTIRFLSVDQVERAKSGHPGMPLGASHIAYLIYDRFLRFNPKNPNWINRDRFVLSAGHASAMLYSLLFVMGY 88
Cdd:COG0021 1 MPLDQLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKHNPANPKWPNRDRFVLSAGHGSMLLYSLLHLTGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 89 DLDIEDLKQFRQLNSKTPGHPESFLTPGVEATTGPLGQGIGNAVGMALAERFLSEKFNKEDFPIIDHYTFTLVSDGDLME 168
Cdd:COG0021 81 DLSLDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGIANAVGMAIAERHLAARFNRPGHDIVDHYTYVIAGDGDLME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 169 GVSSEVAQLAGHWKLNKLVVIWDNNRVSIDGPTSLAWSEDVLKRFEAFGWFVQEVEDGYDLEKLEKAIKKALEQKEKPSF 248
Cdd:COG0021 161 GISHEAASLAGHLKLGKLIVLYDDNGISIDGDTDLAFSEDVAKRFEAYGWHVIRVEDGHDLEAIDAAIEAAKAETDKPTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 249 ISVRTHLAYGSP-KQDDASAHGAPLGKELVLQTKRNFGWPEDEFFVPEEVWLYRSEKIKKGELLEKQWQEMFQEYVKKYP 327
Cdd:COG0021 241 IICKTIIGYGSPnKQGTAKAHGAPLGAEEIAATKEALGWPPEPFEVPDEVYAHWRAAGERGAAAEAEWNERFAAYAAAYP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 328 QEGELLLKVFSRDWGEDYKNVLPDF---REPMATRQASGKVLNSISKVIPTLFGGSADLSESNNTYLHEEGDF----PKG 400
Cdd:COG0021 321 ELAAELERRLAGELPEDWDAALPAFeadAKGVATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIKGAGSFspedPSG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 401 RNLHFGVREHAMGTILNGMAYHGGVLPYGGTFLVFSDYMRPSIRMAALSKLQVVYVFTHDSIGLGEDGPTHQPVEQLSSL 480
Cdd:COG0021 401 RNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFSDYMRPAIRLAALMKLPVIYVFTHDSIGLGEDGPTHQPVEQLASL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 481 RLIPNLFVLRPADANEVSVAWQIAIERKEGPTAIVLTRQKLPLIDRQKYSSHwECLKGAYVLADGGEETQVVIFASGSEV 560
Cdd:COG0021 481 RAIPNLDVIRPADANETAAAWKLALERKDGPTALILSRQNLPTLDRTAAAAE-GVAKGAYVLADAEGTPDVILIATGSEV 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 561 HPALKAKQILEEKGIKVSVVNVFSFELFETQPEEYKRKVLMRNVKKRVAVEAGRGLVWHKFVGMDGLIISMEEFGKSAPG 640
Cdd:COG0021 560 SLAVEAAELLAAEGIKVRVVSMPSWELFEAQDAAYRESVLPPAVRARVAVEAGVTDGWYKYVGLDGAVIGIDTFGASAPA 639
|
650 660
....*....|....*....|..
gi 2686872248 641 EKLMEHFGFVGEEIARRIERWL 662
Cdd:COG0021 640 KVLFEEFGFTVENVVAAAKELL 661
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
9-662 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 928.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 9 TEKDLLLINTIRFLSVDQVERAKSGHPGMPLGASHIAYLIYDRFLRFNPKNPNWINRDRFVLSAGHASAMLYSLLFVMGY 88
Cdd:PRK05899 5 MELLQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPKNPKWPNRDRFVLSAGHGSMLLYSLLHLAGY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 89 DLDIEDLKQFRQLNSKTPGHPESFLTPGVEATTGPLGQGIGNAVGMALAERFLSEKFNKEDFPIIDHYTFTLVSDGDLME 168
Cdd:PRK05899 85 DLSIDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGLANAVGMALAEKYLAALFNRPGLDIVDHYTYVLCGDGDLME 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 169 GVSSEVAQLAGHWKLNKLVVIWDNNRVSIDGPTSLAWSEDVLKRFEAFGWFVQEVeDGYDLEKLEKAIKKALEQKeKPSF 248
Cdd:PRK05899 165 GISHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTEDVKKRFEAYGWHVIEV-DGHDVEAIDAAIEEAKAST-KPTL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 249 ISVRTHLAYGSP-KQDDASAHGAPLGKELVLQTKRNFGWPEdeffvpeevwlyrsekikkgellekqwqemfqeyvkkyp 327
Cdd:PRK05899 243 IIAKTIIGKGAPnKEGTHKVHGAPLGAEEIAAAKKELGWDY--------------------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 328 qegelllkvfsrdwgedyknvlpdfrepmatRQASGKVLNSISKVIPTLFGGSADLSESNNTYLHEEGDFPK----GRNL 403
Cdd:PRK05899 284 -------------------------------RKASGKALNALAKALPELVGGSADLAGSNNTKIKGSKDFAPedysGRYI 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 404 HFGVREHAMGTILNGMAYHGGVLPYGGTFLVFSDYMRPSIRMAALSKLQVVYVFTHDSIGLGEDGPTHQPVEQLSSLRLI 483
Cdd:PRK05899 333 HYGVREFAMAAIANGLALHGGFIPFGGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRAI 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 484 PNLFVLRPADANEVSVAWQIAIERKEGPTAIVLTRQKLPLIDRQKYSShwECLKGAYVLADGGeetQVVIFASGSEVHPA 563
Cdd:PRK05899 413 PNLTVIRPADANETAAAWKYALERKDGPSALVLTRQNLPVLERTAQEE--GVAKGGYVLRDDP---DVILIATGSEVHLA 487
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 564 LKAKQILEEKGIKVSVVNVFSFELFETQPEEYKRKVLMRNVKKRVAVEAGRGLVWHKFVGMDGLIISMEEFGKSAPGEKL 643
Cdd:PRK05899 488 LEAADELEAEGIKVRVVSMPSTELFDEQDAAYKESVLPAAVTARVAVEAGVADGWYKYVGLDGKVLGIDTFGASAPADEL 567
|
650
....*....|....*....
gi 2686872248 644 MEHFGFVGEEIARRIERWL 662
Cdd:PRK05899 568 FKEFGFTVENIVAAAKELL 586
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
14-662 |
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: 901.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 14 LLINTIRFLSVDQVERAKSGHPGMPLGASHIAYLIYDRFLRFNPKNPNWINRDRFVLSAGHASAMLYSLLFVMGYDLDIE 93
Cdd:TIGR00232 2 KLANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKFNPTNPKWINRDRFVLSNGHGSMLLYSLLHLTGYDLSIE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 94 DLKQFRQLNSKTPGHPESFLTPGVEATTGPLGQGIGNAVGMALAERFLSEKFNKEDFPIIDHYTFTLVSDGDLMEGVSSE 173
Cdd:TIGR00232 82 DLKQFRQLHSKTPGHPEYGHTAGVEATTGPLGQGIANAVGMAIAEKTLAATFNKPGFEIVDHYTYVFVGDGCLQEGISYE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 174 VAQLAGHWKLNKLVVIWDNNRVSIDGPTSLAWSEDVLKRFEAFGWFVQEVEDGYDLEKLEKAIKKALEQKEKPSFISVRT 253
Cdd:TIGR00232 162 VASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDVAKRFEAYGWEVLEVEDGHDLAAIDAAIEEAKASTDKPTLIEVKT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 254 HLAYGSP-KQDDASAHGAPLGKELVLQTKRNFGWPEDEFFVPEEVWLYRSEKIK-KGELLEKQWQEMFQEYVKKYPQEGE 331
Cdd:TIGR00232 242 TIGFGSPnKAGTHGVHGAPLGDEEVALTKKNLGWNYNPFEIPQEVYDHFKKTVKeRGAKAEQEWNELFAAYKKKYPELAA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 332 LLLKVFSRDWGEDYKNVLPDFR---EPMATRQASGKVLNSISKVIPTLFGGSADLSESNNTYLHEEGDFPK---GRNLHF 405
Cdd:TIGR00232 322 EFTRRLSGELPADWDKQLPEFKvklQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKGSGDLHEnplGNYIHY 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 406 GVREHAMGTILNGMAYHGGVLPYGGTFLVFSDYMRPSIRMAALSKLQVVYVFTHDSIGLGEDGPTHQPVEQLSSLRLIPN 485
Cdd:TIGR00232 402 GVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQLASLRAIPN 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 486 LFVLRPADANEVSVAWQIAIERKEGPTAIVLTRQKLPLIDRqkySSHWECLKGAYVLADgGEETQVVIFASGSEVHPALK 565
Cdd:TIGR00232 482 LSVWRPCDGNETAAAWKYALESQDGPTALILSRQNLPQLEE---SSLEKVLKGGYVLKD-SKGPDLILIATGSEVQLAVE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 566 AKQILEEKGIKVSVVNVFSFELFETQPEEYKRKVLMRNVkKRVAVEAGRGLVWHKFVGMDGLIISMEEFGKSAPGEKLME 645
Cdd:TIGR00232 558 AAKKLAAENIKVRVVSMPSFDLFDKQDEEYRESVLPANV-TRLAIEAGAADEWYKYAGLVGAILGMDSFGESAPGDKLFE 636
|
650
....*....|....*..
gi 2686872248 646 HFGFVGEEIARRIERWL 662
Cdd:TIGR00232 637 EFGFTVENVVAKAKKLL 653
|
|
| PLN02790 |
PLN02790 |
transketolase |
19-659 |
0e+00 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 883.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 19 IRFLSVDQVERAKSGHPGMPLGASHIAYLIYDRFLRFNPKNPNWINRDRFVLSAGHASAMLYSLLFVMGYD-LDIEDLKQ 97
Cdd:PLN02790 1 IRFLAIDAVNKANSGHPGLPMGCAPMGHVLYDEVMKYNPKNPYWFNRDRFVLSAGHGCMLQYALLHLAGYDsVQMEDLKQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 98 FRQLNSKTPGHPESFLTPGVEATTGPLGQGIGNAVGMALAERFLSEKFNKEDFPIIDHYTFTLVSDGDLMEGVSSEVAQL 177
Cdd:PLN02790 81 FRQWGSRTPGHPENFETPGIEVTTGPLGQGIANAVGLALAEKHLAARFNKPDHKIVDHYTYCILGDGCQMEGISNEAASL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 178 AGHWKLNKLVVIWDNNRVSIDGPTSLAWSEDVLKRFEAFGWFVQEVEDGY-DLEKLEKAIKKALEQKEKPSFISVRTHLA 256
Cdd:PLN02790 161 AGHWGLGKLIVLYDDNHISIDGDTEIAFTEDVDKRYEALGWHTIWVKNGNtDYDEIRAAIKEAKAVTDKPTLIKVTTTIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 257 YGSP-KQDDASAHGAPLGKELVLQTKRNFGWPEDEFFVPEEVWLYRSEKIKKGELLEKQWQEMFQEYVKKYPQEGELLLK 335
Cdd:PLN02790 241 YGSPnKANSYSVHGAALGEKEVDATRKNLGWPYEPFHVPEDVKSHWSKHTKEGAALEAEWNAKFAEYKKKYPEEAAELKS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 336 VFSRDWGEDYKNVLPDFRE---PMATRQASGKVLNSISKVIPTLFGGSADLSESNNTYLHEEGDF----PKGRNLHFGVR 408
Cdd:PLN02790 321 LISGELPSGWEKALPTFTPedpADATRNLSQKCLNALAKVLPGLIGGSADLASSNMTLLKDFGDFqkdtPEERNVRFGVR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 409 EHAMGTILNGMAYHG-GVLPYGGTFLVFSDYMRPSIRMAALSKLQVVYVFTHDSIGLGEDGPTHQPVEQLSSLRLIPNLF 487
Cdd:PLN02790 401 EHGMGAICNGIALHSsGLIPYCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLGEDGPTHQPIEHLASLRAMPNIL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 488 VLRPADANEVSVAWQIAIERKEGPTAIVLTRQKLPLIDrqkYSSHWECLKGAYVLAD--GGEETQVVIFASGSEVHPALK 565
Cdd:PLN02790 481 MLRPADGNETAGAYKVAVTNRKRPTVLALSRQKVPNLP---GTSIEGVEKGGYVISDnsSGNKPDLILIGTGSELEIAAK 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 566 AKQILEEKGIKVSVVNVFSFELFETQPEEYKRKVLMRNVKKRVAVEAGRGLVWHKFVGMDGLIISMEEFGKSAPGEKLME 645
Cdd:PLN02790 558 AAKELRKEGKKVRVVSMVCWELFEEQSDEYKESVLPSSVTARVSVEAGSTFGWEKYVGSKGKVIGVDRFGASAPAGILYK 637
|
650
....*....|....
gi 2686872248 646 HFGFVGEEIARRIE 659
Cdd:PLN02790 638 EFGFTVENVVAAAK 651
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
10-660 |
0e+00 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 820.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 10 EKDLLLINTIRFLSVDQVERAKSGHPGMPLGASHIAYLIYDRFLRFNPKNPNWINRDRFVLSAGHASAMLYSLLFVMGYD 89
Cdd:PTZ00089 4 AIDEKCANEIRCLSADLVQKANSGHPGAPMGMAPIAHILWSEVMKYNPKDPRWINRDRFVLSNGHASALLYSMLHLTGYD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 90 LDIEDLKQFRQLNSKTPGHPESFLTPGVEATTGPLGQGIGNAVGMALAERFLSEKFNKEDFPIIDHYTFTLVSDGDLMEG 169
Cdd:PTZ00089 84 LSMEDLKNFRQLGSRTPGHPERHITPGVEVTTGPLGQGIANAVGLAIAEKHLAAKFNRPGHPIFDNYVYVICGDGCLQEG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 170 VSSEVAQLAGHWKLNKLVVIWDNNRVSIDGPTSLAWSEDVLKRFEAFGWFVQEVEDG-YDLEKLEKAIKKALEQKEKPSF 248
Cdd:PTZ00089 164 VSQEALSLAGHLGLEKLIVLYDDNKITIDGNTDLSFTEDVEKKYEAYGWHVIEVDNGnTDFDGLRKAIEEAKKSKGKPKL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 249 ISVRTHLAYGSPKQDDASAHGAPLGKELVLQTKRNFGW-PEDEFFVPEEVWLYRSEKIKKGELLEKQWQEMFQEYVKKYP 327
Cdd:PTZ00089 244 IIVKTTIGYGSSKAGTEKVHGAPLGDEDIAQVKELFGLdPEKKFHVSEEVRQFFEQHVEKKKENYEAWKKRFAKYTAAFP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 328 QEGELLLKVFSRDWGEDYKNVLPDFR---EPMATRQASGKVLNSISKVIPTLFGGSADLSESNNTYLHEEGDF----PKG 400
Cdd:PTZ00089 324 KEAQAIERRFKGELPPGWEKKLPKYTtndKAIATRKASENVLNPLFQILPELIGGSADLTPSNLTRPKEANDFtkasPEG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 401 RNLHFGVREHAMGTILNGMAYHGGVLPYGGTFLVFSDYMRPSIRMAALSKLQVVYVFTHDSIGLGEDGPTHQPVEQLSSL 480
Cdd:PTZ00089 404 RYIRFGVREHAMCAIMNGIAAHGGFIPFGATFLNFYGYALGAVRLAALSHHPVIYVATHDSIGLGEDGPTHQPVETLALL 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 481 RLIPNLFVLRPADANEVSVAWQIAIERKEGPTAIVLTRQKLPlidRQKYSSHWECLKGAYVLADGGEETQVVIFASGSEV 560
Cdd:PTZ00089 484 RATPNLLVIRPADGTETSGAYALALANAKTPTILCLSRQNTP---PLPGSSIEGVLKGAYIVVDFTNSPQLILVASGSEV 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 561 HPALKAKQILeEKGIKVSVVNVFSFELFETQPEEYKRKVLMRNVKKRVAVEAGRGLVWHKFVGMDgliISMEEFGKSAPG 640
Cdd:PTZ00089 561 SLCVEAAKAL-SKELNVRVVSMPCWELFDQQSEEYQQSVLPSGGVPVLSVEAYVSFGWEKYSHVH---VGISGFGASAPA 636
|
650 660
....*....|....*....|
gi 2686872248 641 EKLMEHFGFVGEEIARRIER 660
Cdd:PTZ00089 637 NALYKHFGFTVENVVEKARA 656
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
12-335 |
1.24e-167 |
|
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: 482.66 E-value: 1.24e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 12 DLLLINTIRFLSVDQVERAKSGHPGMPLGASHIAYLIYDRFLRFNPKNPNWINRDRFVLSAGHASAMLYSLLFVMGYDLD 91
Cdd:pfam00456 2 DKRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNPNDPKWINRDRFVLSNGHGSMLLYSLLHLTGYDLS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 92 IEDLKQFRQLNSKTPGHPESFLTPGVEATTGPLGQGIGNAVGMALAERFLSEKFNKEDFPIIDHYTFTLVSDGDLMEGVS 171
Cdd:pfam00456 82 MEDLKSFRQLGSKTPGHPEFGHTAGVEVTTGPLGQGIANAVGMAIAERNLAATYNRPGFDIVDHYTYVFLGDGCLMEGVS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 172 SEVAQLAGHWKLNKLVVIWDNNRVSIDGPTSLAWSEDVLKRFEAFGWFVQEVEDGYDLEKLEKAIKKALEQKEKPSFISV 251
Cdd:pfam00456 162 SEASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDTAARFEAYGWHVIEVEDGHDVEAIAAAIEEAKAEKDKPTLIKC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 252 RTHLAYGSP-KQDDASAHGAPLGKELVLQTKRNFGW-PEDEFFVPEEVWLYRSEKIKKGELLEKQWQEMFQEYVKKYPQE 329
Cdd:pfam00456 242 RTVIGYGSPnKQGTHDVHGAPLGADEVAALKQKLGWdPYKPFEIPAEVYDAWKEKVAEGAKAEAEWNELFAAYKKAYPEL 321
|
....*.
gi 2686872248 330 GELLLK 335
Cdd:pfam00456 322 AAEFAR 327
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
17-281 |
4.36e-135 |
|
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: 396.49 E-value: 4.36e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 17 NTIRFLSVDQVERAKSGHPGMPLGASHIAYLIYDRFLRFNPKNPNWINRDRFVLSAGHASAMLYSLLFVMGYdLDIEDLK 96
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPADPKWPNRDRFVLSKGHASPALYAVLALAGY-LPEEDLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 97 QFRQLNSKTPGHPESFLTPGVEATTGPLGQGIGNAVGMALAERFLsekfnkedfpIIDHYTFTLVSDGDLMEGVSSEVAQ 176
Cdd:cd02012 80 TFRQLGSRLPGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEKLL----------GFDYRVYVLLGDGELQEGSVWEAAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 177 LAGHWKLNKLVVIWDNNRVSIDGPTS-LAWSEDVLKRFEAFGWFVQEVeDGYDLEKLEKAIKKALEQKEKPSFISVRTHL 255
Cdd:cd02012 150 FAGHYKLDNLIAIVDSNRIQIDGPTDdILFTEDLAKKFEAFGWNVIEV-DGHDVEEILAALEEAKKSKGKPTLIIAKTIK 228
|
250 260
....*....|....*....|....*..
gi 2686872248 256 AYGSP-KQDDASAHGAPLGKELVLQTK 281
Cdd:cd02012 229 GKGVPfMENTAKWHGKPLGEEEVELAK 255
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
6-275 |
1.80e-78 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 251.15 E-value: 1.80e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 6 RKATEKDLLLI-NTIRFLSVDQVERAKSGHPGMPLGASHI-AYLiYDRFLRFNPKNPNWINRDRFVLSAGHASAMLYSLL 83
Cdd:COG3959 1 TKEDIKELEEKaRQIRRDILRMIYAAGSGHPGGSLSAADIlAAL-YFKVMNIDPKNPDWPDRDRFILSKGHAAPALYAVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 84 FVMGYdLDIEDLKQFRQLNSKTPGHPESFLTPGVEATTGPLGQGIGNAVGMALAerflsEKFNKEdfpiiDHYTFTLVSD 163
Cdd:COG3959 80 AEKGY-FPKEELATFRKLGSRLQGHPDMKKTPGVEMSTGSLGQGLSVAVGMALA-----AKLDGK-----DYRVYVLLGD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 164 GDLMEGVSSEVAQLAGHWKLNKLVVIWDNNRVSIDGPTslawsEDVL------KRFEAFGWFVQEVeDGYDLEKLEKAIK 237
Cdd:COG3959 149 GELQEGQVWEAAMAAAHYKLDNLIAIVDRNGLQIDGPT-----EDVMsleplaEKWEAFGWHVIEV-DGHDIEALLAALD 222
|
250 260 270
....*....|....*....|....*....|....*....
gi 2686872248 238 KALEQKEKPSFISVRTHLAYGSPK-QDDASAHGAPLGKE 275
Cdd:COG3959 223 EAKAVKGKPTVIIAHTVKGKGVSFmENRPKWHGKAPNDE 261
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
360-518 |
7.45e-67 |
|
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: 216.15 E-value: 7.45e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 360 QASGKVLNSISKVIPTLFGGSADLSESNNTYLHEEGdFPkGRNLHFGVREHAMGTILNGMAYHGgVLPYGGTFLVFSDYM 439
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAKK-FP-DRFIDVGIAEQNMVGIAAGLALHG-LKPFVSTFSFFLQRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 440 RPSIR-MAALSKLQVVYVFTHDSIGLGEDGPTHQPVEQLSSLRLIPNLFVLRPADANEVSVAWQIAIERKeGPTAIVLTR 518
Cdd:cd07033 78 YDQIRhDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEYD-GPVYIRLPR 156
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
354-522 |
1.58e-64 |
|
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: 210.48 E-value: 1.58e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 354 EPMATRQASGKVLNSISKVIPTLFGGSADLSESNNTYLHEEGD-FPKGRNLHFGVREHAMGTILNGMAYHGGVL-PYGGT 431
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHpQGAGRVIDTGIAEQAMVGFANGMALHGPLLpPVEAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 432 FLVFSDYMRPSIR-MAALSKLQVVYVFTHDSIGLGEDGPTHQPVEQLSSLRLIPNLFVLRPADANEVSVAWQIAIERKE- 509
Cdd:pfam02779 81 FSDFLNRADDAIRhGAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRRDGr 160
|
170
....*....|...
gi 2686872248 510 GPTAIVLTRQKLP 522
Cdd:pfam02779 161 KPVVLRLPRQLLR 173
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
354-522 |
1.08e-42 |
|
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: 150.33 E-value: 1.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 354 EPMATRQASGKVLNSIskviptlfggsadlsesnntylheegdfpkgrNLHFGVREHAMGTILNGMAYHGGVlPYGGTFL 433
Cdd:smart00861 1 KKIATRKAFGEALAEL--------------------------------AIDTGIAEQAMVGFAAGLALHGLR-PVVEIFF 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 434 VFSDYMRPSIRMAALSKlQVVYVFTHDS-IGLGEDGPTHQPVEQLSSLRLIPNLFVLRPADANEVSVAWQIAIERKeGPT 512
Cdd:smart00861 48 TFFDRAKDQIRSAGASG-NVPVVFRHDGgGGVGEDGPTHHSIEDEALLRAIPGLKVVAPSDPAEAKGLLRAAIRDD-GPV 125
|
170
....*....|
gi 2686872248 513 AIVLTRQKLP 522
Cdd:smart00861 126 VIRLERKSLY 135
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
354-662 |
1.66e-41 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 152.93 E-value: 1.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 354 EPMATRQASGKVLNSISKVIPTLFGGSADLSESNNTYLHEEgDFPkGRNLHFGVREHAMGTILNGMAyHGGVLPYGGTFL 433
Cdd:COG3958 2 EKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKLDKFAK-AFP-DRFFNVGIAEQNMVGVAAGLA-LAGKIPFVSTFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 434 VFSdYMRPS--IRMA-ALSKLQVVYVFTHDSIGLGEDGPTHQPVEQLSSLRLIPNLFVLRPADANEVSVAWQIAIERKeG 510
Cdd:COG3958 79 PFL-TGRAYeqIRNDiAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRAAAEHD-G 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 511 PTAIVLTRQKLPLIDRQKYSshWEcLKGAYVLADGGEetqVVIFASGSEVHPALKAKQILEEKGIKVSVVNVFSF----- 585
Cdd:COG3958 157 PVYLRLGRGAVPVVYDEDYE--FE-IGKARVLREGKD---VTIIATGIMVAEALEAAELLAKEGISARVINMHTIkplde 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 586 ELFETQPEEYKR------------------KVLMRNVKKRVaveagrglvwhKFVGMDgliismEEFGKSAPGEKLMEHF 647
Cdd:COG3958 231 EAILKAARKTGAvvtaeehsiigglgsavaEVLAENYPVPL-----------RRIGVP------DRFGESGSPEELLEKY 293
|
330
....*....|....*
gi 2686872248 648 GFVGEEIARRIERWL 662
Cdd:COG3958 294 GLDAEGIVAAAKELL 308
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
447-581 |
5.85e-15 |
|
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: 78.13 E-value: 5.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 447 ALSKLQVVyvFTHDSIGL-GEDGPTHQPVEQLSSLRLIPNLFVLRPADANEVS--VAWQIAIerkEGPTAIVLTRQKLPL 523
Cdd:COG1154 406 ALQNLPVT--FAIDRAGLvGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRhmLYTALAY---DGPTAIRYPRGNGPG 480
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2686872248 524 IDRQKYSSHWEcLKGAYVLADGGEetqVVIFASGSEVHPALKAKQILEEKGIKVSVVN 581
Cdd:COG1154 481 VELPAELEPLP-IGKGEVLREGKD---VAILAFGTMVAEALEAAERLAAEGISATVVD 534
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
128-581 |
3.00e-13 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 72.81 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 128 IGNAVGMALAERFLSEKfnkedfpiiDHYTFTLVSDGDLMEGVSSEVAQLAGHWKLNKLVVIWDNNRvSIDGPT-SLAws 206
Cdd:PRK05444 123 ISAALGMAKARDLKGGE---------DRKVVAVIGDGALTGGMAFEALNNAGDLKSDLIVILNDNEM-SISPNVgALS-- 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 207 eDVLKR------FEAFGWFVQEVEDGYDLEKLEKAIKKALEQKeKPSFISVRTH--LAYGSPKQDDASAHGAPLgkelvl 278
Cdd:PRK05444 191 -NYLARlrsstlFEELGFNYIGPIDGHDLDALIETLKNAKDLK-GPVLLHVVTKkgKGYAPAEADPIKYHGVGK------ 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 279 qtkrnfgwpedefFVPEEvwlyrSEKIKKGELLEKQWQEMFqeyvkkypqeGELLLKVFSRDwgedyKNVL---Pdfrep 355
Cdd:PRK05444 263 -------------FDPET-----GEQPKSSKPGKPSYTKVF----------GETLCELAEKD-----PKIVaitA----- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 356 mATRQASGkvLNSISKviptlfggsadlsesnntylheegDFPKgrnlHF---GVRE-HAMgTILNGMAYHGG--VLPYG 429
Cdd:PRK05444 305 -AMPEGTG--LVKFSK------------------------RFPD----RYfdvGIAEqHAV-TFAAGLATEGLkpVVAIY 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 430 GTFL------VFSDymrpsirmAALSKLQVVYVFthDSIGL-GEDGPTHQPVEQLSSLRLIPNLFVLRPADANEVS--VA 500
Cdd:PRK05444 353 STFLqraydqVIHD--------VALQNLPVTFAI--DRAGLvGADGPTHQGAFDLSYLRCIPNMVIMAPSDENELRqmLY 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 501 WqiAIERKEGPTAIVLTRQKLPLIDRQKYSSH----WECLKgayvladggEETQVVIFASGSEVHPALKAKQILEEkgik 576
Cdd:PRK05444 423 T--ALAYDDGPIAIRYPRGNGVGVELPELEPLpigkGEVLR---------EGEDVAILAFGTMLAEALKAAERLAS---- 487
|
....*
gi 2686872248 577 VSVVN 581
Cdd:PRK05444 488 ATVVD 492
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
65-253 |
1.02e-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: 66.51 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 65 RDRFVLSAGHASAMLYSLLFvmgydldiedlkqfrqlnsktPGHPESFLTPGveaTTGPLGQGIGNAVGMALAERflsek 144
Cdd:cd00568 13 DAIVVNDAGNSAYWAYRYLP---------------------LRRGRRFLTST---GFGAMGYGLPAAIGAALAAP----- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 145 fnkedfpiiDHYTFTLVSDGDLMEGVsSEVAqLAGHWKLNKLVVIWDNN----------RVSIDGPTSLAWSE-DVLKRF 213
Cdd:cd00568 64 ---------DRPVVCIAGDGGFMMTG-QELA-TAVRYGLPVIVVVFNNGgygtirmhqeAFYGGRVSGTDLSNpDFAALA 132
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2686872248 214 EAFGWFVQEVEdgyDLEKLEKAIKKALEQKeKPSFISVRT 253
Cdd:cd00568 133 EAYGAKGVRVE---DPEDLEAALAEALAAG-GPALIEVKT 168
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
547-654 |
3.92e-12 |
|
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: 63.77 E-value: 3.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 547 EETQVVIFASGSEVHPALKAKQILEEKGIKVSVVNVFSFELFETQP-----EEYKRKVLMRNVKKRVAVEAGRGLVW--H 619
Cdd:pfam02780 8 EGDDVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETilesvKKTGRLVTVEEAVPRGGFGSEVAAALaeE 87
|
90 100 110
....*....|....*....|....*....|....*..
gi 2686872248 620 KFVGMDGLIISM--EEFGKSAPGEKLMEHFGFVGEEI 654
Cdd:pfam02780 88 AFDGLDAPVLRVggPDFPEPGSADELEKLYGLTPEKI 124
|
|
| dxs |
TIGR00204 |
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ... |
13-581 |
9.89e-12 |
|
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: 67.88 E-value: 9.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 13 LLLINT---IRFLSVDQVER--------------AKSGHPGMPLGASHIAYLIYDRFlrfnpKNPnwinRDRFVLSAGHA 75
Cdd:TIGR00204 1 LSLINSpqeLRLLSIDELEKlcdelrryllesvsASGGHLASGLGTVELTVALHYVF-----NTP----KDQFIWDVGHQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 76 SamlYSLLFVMGYDLDIEDLKQFRQLnSKTPGHPES---FLTPGVEATTgplgqgIGNAVGMALAerflSEKFNKedfpi 152
Cdd:TIGR00204 72 A---YPHKLLTGRREKFSTLRQKKGL-HGFPKRSESeydVFSAGHSSTS------ISAGLGIAVA----AEKKGA----- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 153 iDHYTFTLVSDGDLMEGVSSEVAQLAGHWKlNKLVVIWDNNRVSIDGPTSlAWSEDVLKRFEafGWFVQEVEDGydLEKL 232
Cdd:TIGR00204 133 -DRKTVCVIGDGAITAGMAFEALNHAGDLK-TDMIVILNDNEMSISENVG-ALSNHLAQLRS--GSLYQSLRDG--LKKI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 233 EK---AIKKALEQKEKPSFISVrthLAYGSPKQDDASAHGAPLGKELVLQTKRNFGWPEDeffVPEEVWLYRSEKIKKGE 309
Cdd:TIGR00204 206 FSklpPIKNYLAKRTEESMKGL---VVPGTFFEELGFNYIGPVDGHDLLELIETLKNAKK---LKGPVFLHIQTKKGKGY 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 310 LLEKQWQEMFQEYVKKYPQEGELllkVFSRDWGEDYKNVLPDFREPMATRQasgkvlNSISKVIPTLFGGSA--DLSESn 387
Cdd:TIGR00204 280 KPAEKDPIGWHGVGPFDLSTGCL---PKSKSALPSYSKIFSDTLCELAKKD------NKIVGITPAMPEGSGldKFSRK- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 388 ntylheegdFPKgRNLHFGVREHAMGTILNGMAYhGGVLPYggtFLVFSDYMRPS----IRMAALSKLQVVyvFTHDSIG 463
Cdd:TIGR00204 350 ---------FPD-RYFDVAIAEQHAVTFAAGMAI-EGYKPF---VAIYSTFLQRAydqvVHDVCIQKLPVL--FAIDRAG 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 464 L-GEDGPTHQPVEQLSSLRLIPNLFVLRPADANEVSVAWQIAIERKEGPTAIVLTRQKLPLIDRQKYSSHWECLKGAyVL 542
Cdd:TIGR00204 414 IvGADGETHQGAFDISYLRCIPNMVIMAPSDENELRQMLYTGYHYDDGPIAVRYPRGNAVGVELTPEPEKLPIGKSE-VL 492
|
570 580 590
....*....|....*....|....*....|....*....
gi 2686872248 543 ADGGEetqVVIFASGSEVHPALKAKQILEEKGIKVSVVN 581
Cdd:TIGR00204 493 RKGEK---ILILGFGTLVPEALEVAESLNEKGIEATVVD 528
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
106-267 |
1.77e-10 |
|
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: 62.51 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 106 PGHPeSFLTPGVEATTGPLGQGIGNAVGMALAErflseKFNKEDfpiidHYTFTLVSDGDLMEGVSSEVAQLAGHWKLNK 185
Cdd:cd02000 89 SMHI-GDKEKNFFGGNGIVGGQVPLAAGAALAL-----KYRGED-----RVAVCFFGDGATNEGDFHEALNFAALWKLPV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 186 LVVIWdNNRVSIDGPTSLA-WSEDVLKRFEAFGWFVQEVeDGYDLEKLEKAIKKALE---QKEKPSFISVRTHLAYGSPK 261
Cdd:cd02000 158 IFVCE-NNGYAISTPTSRQtAGTSIADRAAAYGIPGIRV-DGNDVLAVYEAAKEAVErarAGGGPTLIEAVTYRLGGHST 235
|
....*.
gi 2686872248 262 QDDASA 267
Cdd:cd02000 236 SDDPSR 241
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
397-581 |
2.64e-10 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 63.59 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 397 FPKgRNLHFGVREHAMGTILNGMAyHGGVLPYggtFLVFSDYMRPS----IRMAALSKLQVVYVFthDSIGL-GEDGPTH 471
Cdd:PRK12571 359 FPN-RVFDVGIAEQHAVTFAAGLA-AAGLKPF---CAVYSTFLQRGydqlLHDVALQNLPVRFVL--DRAGLvGADGATH 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 472 QPVEQLSSLRLIPNLFVLRPADANEVSVAWQIAIERKEGPTAIVLTRQKLPLIDRQKYSShwecLKGAYVLADGGEETQV 551
Cdd:PRK12571 432 AGAFDLAFLTNLPNMTVMAPRDEAELRHMLRTAAAHDDGPIAVRFPRGEGVGVEIPAEGT----ILGIGKGRVPREGPDV 507
|
170 180 190
....*....|....*....|....*....|
gi 2686872248 552 VIFASGSEVHPALKAKQILEEKGIKVSVVN 581
Cdd:PRK12571 508 AILSVGAHLHECLDAADLLEAEGISVTVAD 537
|
|
| TPP_E1_EcPDC_like |
cd02017 |
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ... |
33-232 |
5.06e-10 |
|
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: 61.94 E-value: 5.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 33 GHPGMPLGASHIAYLIYDRFLRfnPKNpNWINRDRfVLSAGHASAMLYSLLFVMGyDLDIEDLKQFRQLNSKT--PGHPE 110
Cdd:cd02017 31 GHIATFASAATLYEVGFNHFFR--ARG-EGGGGDL-VYFQGHASPGIYARAFLEG-RLTEEQLDNFRQEVGGGglSSYPH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 111 SFLTPG-VEATTGPLGQGIGNAVGMALAERFLSEKFNKEDfpiIDHYTFTLVSDGDLMEGVSSEVAQLAGHWKLNKLVVI 189
Cdd:cd02017 106 PWLMPDfWEFPTVSMGLGPIQAIYQARFNRYLEDRGLKDT---SDQKVWAFLGDGEMDEPESLGAIGLAAREKLDNLIFV 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2686872248 190 WDNNRVSIDGP---TSLAWSEdvLKR-FEAFGWFVQEVEDGYDLEKL 232
Cdd:cd02017 183 VNCNLQRLDGPvrgNGKIIQE--LEGiFRGAGWNVIKVIWGSKWDEL 227
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
105-253 |
6.75e-09 |
|
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: 55.68 E-value: 6.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 105 TPGHPESFLTPgveaTTGPLGQGIGNAVGMALAERflsekfnkedfpiiDHYTFTLVSDGDLMEGVSSevAQLAGHWKLN 184
Cdd:cd02002 36 PLTRPGSYFTL----RGGGLGWGLPAAVGAALANP--------------DRKVVAIIGDGSFMYTIQA--LWTAARYGLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 185 KLVVIWDNN----------RVSIDGPTSLAWseDVLKRF----------EAFGWFVQEVEDGydlEKLEKAIKKALEQKe 244
Cdd:cd02002 96 VTVVILNNRgygalrsflkRVGPEGPGENAP--DGLDLLdpgidfaaiaKAFGVEAERVETP---EELDEALREALAEG- 169
|
....*....
gi 2686872248 245 KPSFISVRT 253
Cdd:cd02002 170 GPALIEVVV 178
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
128-584 |
8.17e-07 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 52.32 E-value: 8.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 128 IGNAVGMALAERFLSEKFNkedfpIIdhytfTLVSDGDLMEGVSSEVAQLAGHWKLNkLVVIWDNNRVSIDGP-----TS 202
Cdd:PRK12315 119 IALATGLAKARDLKGEKGN-----II-----AVIGDGSLSGGLALEGLNNAAELKSN-LIIIVNDNQMSIAENhgglyKN 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 203 LA-------WSEDVLkrFEAFGWFVQEVEDGYDLEKLEKAIKKaLEQKEKPsfISVRTHLAYGSpkqddasahgaplGKE 275
Cdd:PRK12315 188 LKelrdtngQSENNL--FKAMGLDYRYVEDGNDIESLIEAFKE-VKDIDHP--IVLHIHTLKGK-------------GYQ 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 276 LVLQTKRNFGW--PEDeffvpeevwlyrsekIKKGELLEKqwqemfqeyvkkypqegelllkvfsrDWGEDYKNVLPDFr 353
Cdd:PRK12315 250 PAEENKEAFHWhmPFD---------------LETGQSKVP--------------------------ASGESYSSVTLDY- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 354 epMATRQASGKVLNSISKVIPTLFGgsadLSESNNTYlheegdfpkGRNLH-FGVREHAMGTILNGMAYHGG--VLPYGG 430
Cdd:PRK12315 288 --LLKKIKEGKPVVAINAAIPGVFG----LKEFRKKY---------PDQYVdVGIAEQESVAFASGIAANGArpVIFVNS 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 431 TFLVFSdYMRPSIRMAaLSKLQVVYVFTHDSIGlGEDgPTHQPVEQLSSLRLIPNLFVLRPADANEVSVAWQIAIERKEG 510
Cdd:PRK12315 353 TFLQRA-YDQLSHDLA-INNNPAVMIVFGGSIS-GND-VTHLGIFDIPMISNIPNLVYLAPTTKEELIAMLEWALTQHEH 428
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2686872248 511 PTAIVLTRQKLPL--IDRQKYSshweclKGAYVLADGGEEtqVVIFASGSEVHPALKAKQILEEK-GIKVSVVNVFS 584
Cdd:PRK12315 429 PVAIRVPEHGVESgpTVDTDYS------TLKYEVTKAGEK--VAILALGDFYELGEKVAKKLKEElGIDATLINPKF 497
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
120-253 |
2.92e-06 |
|
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: 48.31 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 120 TTGPLGQGIGNAVGMALAERFLSEKFNKedFPIIDhytftlvsDGDLMEGVSSEVAQLAGHWKlNKLVVIWDNNRVSIDG 199
Cdd:cd02007 73 GTGHSSTSISAALGMAVARDLKGKKRKV--IAVIG--------DGALTGGMAFEALNNAGYLK-SNMIVILNDNEMSISP 141
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2686872248 200 PTSlawSEDVLkrFEAFGWFVQEVEDGYDLEKLEKAIKKALEQKeKPSFISVRT 253
Cdd:cd02007 142 NVG---TPGNL--FEELGFRYIGPVDGHNIEALIKVLKEVKDLK-GPVLLHVVT 189
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
397-581 |
2.51e-05 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 47.59 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 397 FPKgRNLHFGVREHAMGTILNGMAYHGgVLPYGGtflVFSDYM-RPSIRMAALSKLQVVYV-FTHDSIGL-GEDGPTHQP 473
Cdd:PLN02582 396 FPT-RCFDVGIAEQHAVTFAAGLACEG-LKPFCA---IYSSFLqRGYDQVVHDVDLQKLPVrFAMDRAGLvGADGPTHCG 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 474 VEQLSSLRLIPNLFVLRPADANEV--SVAWQIAIERKegPTAIVLTRQK---LPLIDRQKySSHWECLKGAYVLadggEE 548
Cdd:PLN02582 471 AFDVTYMACLPNMVVMAPSDEAELfhMVATAAAIDDR--PSCFRYPRGNgigVQLPPNNK-GIPIEVGKGRILL----EG 543
|
170 180 190
....*....|....*....|....*....|...
gi 2686872248 549 TQVVIFASGSEVHPALKAKQILEEKGIKVSVVN 581
Cdd:PLN02582 544 ERVALLGYGTAVQSCLAAASLLERHGLSATVAD 576
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
109-251 |
6.20e-05 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 43.73 E-value: 6.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 109 PESFLTPGVeatTGPLGQGIGNAVGMALAERflsekfnkeDFPIIDhytftLVSDGDLMeGVSSEVAQLAGHwKLNKLVV 188
Cdd:pfam02775 18 PRRYLTSGG---LGTMGYGLPAAIGAKLARP---------DRPVVA-----IAGDGGFQ-MNLQELATAVRY-NLPITVV 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2686872248 189 IWDNN----------------RVSIDGPTSLAWseDVLKRFEAFGWFVQEVEDGydlEKLEKAIKKALEQKeKPSFISV 251
Cdd:pfam02775 79 VLNNGgygmtrgqqtpfgggrYSGPSGKILPPV--DFAKLAEAYGAKGARVESP---EELEEALKEALEHD-GPALIDV 151
|
|
| PLN02374 |
PLN02374 |
pyruvate dehydrogenase (acetyl-transferring) |
124-254 |
6.46e-04 |
|
pyruvate dehydrogenase (acetyl-transferring)
Pssm-ID: 215213 [Multi-domain] Cd Length: 433 Bit Score: 42.62 E-value: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2686872248 124 LGQGIGNAVGMALAERFLSEKFNKEDfpiIDHYTFTLVSDGDLMEGVSSEVAQLAGHWKLNKLVVIwDNNRVSIdGPTSL 203
Cdd:PLN02374 196 IGEGIPVATGAAFSSKYRREVLKEES---CDDVTLAFFGDGTCNNGQFFECLNMAALWKLPIVFVV-ENNLWAI-GMSHL 270
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2686872248 204 AWSED--VLKRFEAFGWFVQEVeDGYDLEKLEKAIKKALEQK---EKPSFISVRTH 254
Cdd:PLN02374 271 RATSDpeIWKKGPAFGMPGVHV-DGMDVLKVREVAKEAIERArrgEGPTLVECETY 325
|
|
| PRK13012 |
PRK13012 |
2-oxoacid dehydrogenase subunit E1; Provisional |
536-587 |
1.01e-03 |
|
2-oxoacid dehydrogenase subunit E1; Provisional
Pssm-ID: 237267 [Multi-domain] Cd Length: 896 Bit Score: 42.23 E-value: 1.01e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2686872248 536 LKGAYVLADGGEETQVVIFASGSEVHPALKAKQILEEK-GIKVSVVNVFSF-EL 587
Cdd:PRK13012 720 LKGMYRLAAAAEAPRVQLLGSGAILREVLAAARLLADDwGVDADVWSVTSFtEL 773
|
|
| |
