|
Name |
Accession |
Description |
Interval |
E-value |
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
21-680 |
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: 1203.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 21 DQVDQLGVNTLRTLSIDAIQRANSGHPGLPMGAAPMAYVLWTRHLKINPKtHMNWVNRDRFVLSAGHGSALLYSLAHLAG 100
Cdd:COG0021 1 MPLDQLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKHNPA-NPKWPNRDRFVLSAGHGSMLLYSLLHLTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 101 YDVSMDDLKNFREWKSNTPGHPEYGCTDGVEATTGPLGQGISMAVGMAMAEAHLGKKFNREGYPVMDHYTYALIGDGDLM 180
Cdd:COG0021 80 YDLSLDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGIANAVGMAIAERHLAARFNRPGHDIVDHYTYVIAGDGDLM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 181 EGVASEAASLAGHLKLGKLIALYDSNGISLDGKTSASFTENVGARFEAYGWQYILVEDGFNLEEIDKAIVQAKAESDKPT 260
Cdd:COG0021 160 EGISHEAASLAGHLKLGKLIVLYDDNGISIDGDTDLAFSEDVAKRFEAYGWHVIRVEDGHDLEAIDAAIEAAKAETDKPT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 261 IIEIKTTIGYGSEN-QGTHKVHGSPLGEEGVAHAKEVYNWNYPPFTVPEEVSQRFKECLqDKGVKAENKWNEMFEAYKKE 339
Cdd:COG0021 240 LIICKTIIGYGSPNkQGTAKAHGAPLGAEEIAATKEALGWPPEPFEVPDEVYAHWRAAG-ERGAAAEAEWNERFAAYAAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 340 YSDLAQKFSDGFSNKVPNTLGDILPQYGEDD-SIATRAASQKAINALAKEVSSLWGGAADLASSNKTVIAGEGDFQPESY 418
Cdd:COG0021 319 YPELAAELERRLAGELPEDWDAALPAFEADAkGVATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIKGAGSFSPEDP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 419 EGRNIWFGVREFGMACAMNGIMLHGGTRIFGSTFFVFSDYLKAAIRLSAIQKLPVIYVLTHDSVAVGKDGPTHEPIEQLA 498
Cdd:COG0021 399 SGRNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFSDYMRPAIRLAALMKLPVIYVFTHDSIGLGEDGPTHQPVEQLA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 499 SLRTIPNVQVFRPADGNETSAAWKVALETLDKPTILVLSRQNLDTLPISKEKVfDGVEKGGYVVQGAENEADGILIATGS 578
Cdd:COG0021 479 SLRAIPNLDVIRPADANETAAAWKLALERKDGPTALILSRQNLPTLDRTAAAA-EGVAKGAYVLADAEGTPDVILIATGS 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 579 EVGLALKAKEELQKKGKDVIVVSLPSWERFEAQSEEYKNTVIPPELKKRMTIEAGTTYGWAKYAGDHGVMIGIDEFGMSA 658
Cdd:COG0021 558 EVSLAVEAAELLAAEGIKVRVVSMPSWELFEAQDAAYRESVLPPAVRARVAVEAGVTDGWYKYVGLDGAVIGIDTFGASA 637
|
650 660
....*....|....*....|..
4C7V_A 659 PSDIVLRELGMSVENIVDKYLE 680
Cdd:COG0021 638 PAKVLFEEFGFTVENVVAAAKE 659
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
28-677 |
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: 933.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 28 VNTLRTLSIDAIQRANSGHPGLPMGAAPMAYVLWTRHLKINPkTHMNWVNRDRFVLSAGHGSALLYSLAHLAGYDVSMDD 107
Cdd:TIGR00232 4 ANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKFNP-TNPKWINRDRFVLSNGHGSMLLYSLLHLTGYDLSIED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 108 LKNFREWKSNTPGHPEYGCTDGVEATTGPLGQGISMAVGMAMAEAHLGKKFNREGYPVMDHYTYALIGDGDLMEGVASEA 187
Cdd:TIGR00232 83 LKQFRQLHSKTPGHPEYGHTAGVEATTGPLGQGIANAVGMAIAEKTLAATFNKPGFEIVDHYTYVFVGDGCLQEGISYEV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 188 ASLAGHLKLGKLIALYDSNGISLDGKTSASFTENVGARFEAYGWQYILVEDGFNLEEIDKAIVQAKAESDKPTIIEIKTT 267
Cdd:TIGR00232 163 ASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDVAKRFEAYGWEVLEVEDGHDLAAIDAAIEEAKASTDKPTLIEVKTT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 268 IGYGSEN-QGTHKVHGSPLGEEGVAHAKEVYNWNYPPFTVPEEVSQRFKECLQDKGVKAENKWNEMFEAYKKEYSDLAQK 346
Cdd:TIGR00232 243 IGFGSPNkAGTHGVHGAPLGDEEVALTKKNLGWNYNPFEIPQEVYDHFKKTVKERGAKAEQEWNELFAAYKKKYPELAAE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 347 FSDGFSNKVPNTLGDILPQY-GEDDSIATRAASQKAINALAKEVSSLWGGAADLASSNKTVIAGEGDFqPESYEGRNIWF 425
Cdd:TIGR00232 323 FTRRLSGELPADWDKQLPEFkVKLQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKGSGDL-HENPLGNYIHY 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 426 GVREFGMACAMNGIMLHGGTRIFGSTFFVFSDYLKAAIRLSAIQKLPVIYVLTHDSVAVGKDGPTHEPIEQLASLRTIPN 505
Cdd:TIGR00232 402 GVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQLASLRAIPN 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 506 VQVFRPADGNETSAAWKVALETLDKPTILVLSRQNLDTLPiskEKVFDGVEKGGYVVQGAENeADGILIATGSEVGLALK 585
Cdd:TIGR00232 482 LSVWRPCDGNETAAAWKYALESQDGPTALILSRQNLPQLE---ESSLEKVLKGGYVLKDSKG-PDLILIATGSEVQLAVE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 586 AKEELQKKGKDVIVVSLPSWERFEAQSEEYKNTVIPPELkKRMTIEAGTTYGWAKYAGDHGVMIGIDEFGMSAPSDIVLR 665
Cdd:TIGR00232 558 AAKKLAAENIKVRVVSMPSFDLFDKQDEEYRESVLPANV-TRLAIEAGAADEWYKYAGLVGAILGMDSFGESAPGDKLFE 636
|
650
....*....|..
4C7V_A 666 ELGMSVENIVDK 677
Cdd:TIGR00232 637 EFGFTVENVVAK 648
|
|
| PLN02790 |
PLN02790 |
transketolase |
32-677 |
0e+00 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 925.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 32 RTLSIDAIQRANSGHPGLPMGAAPMAYVLWTRHLKINPKTHmNWVNRDRFVLSAGHGSALLYSLAHLAGYD-VSMDDLKN 110
Cdd:PLN02790 2 RFLAIDAVNKANSGHPGLPMGCAPMGHVLYDEVMKYNPKNP-YWFNRDRFVLSAGHGCMLQYALLHLAGYDsVQMEDLKQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 111 FREWKSNTPGHPEYGCTDGVEATTGPLGQGISMAVGMAMAEAHLGKKFNREGYPVMDHYTYALIGDGDLMEGVASEAASL 190
Cdd:PLN02790 81 FRQWGSRTPGHPENFETPGIEVTTGPLGQGIANAVGLALAEKHLAARFNKPDHKIVDHYTYCILGDGCQMEGISNEAASL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 191 AGHLKLGKLIALYDSNGISLDGKTSASFTENVGARFEAYGWQYILVEDGFN-LEEIDKAIVQAKAESDKPTIIEIKTTIG 269
Cdd:PLN02790 161 AGHWGLGKLIVLYDDNHISIDGDTEIAFTEDVDKRYEALGWHTIWVKNGNTdYDEIRAAIKEAKAVTDKPTLIKVTTTIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 270 YGSEN-QGTHKVHGSPLGEEGVAHAKEVYNWNYPPFTVPEEVSQRFKEClQDKGVKAENKWNEMFEAYKKEYSDLAQKFS 348
Cdd:PLN02790 241 YGSPNkANSYSVHGAALGEKEVDATRKNLGWPYEPFHVPEDVKSHWSKH-TKEGAALEAEWNAKFAEYKKKYPEEAAELK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 349 DGFSNKVPNTLGDILPQYGEDDSI-ATRAASQKAINALAKEVSSLWGGAADLASSNKTVIAGEGDFQPESYEGRNIWFGV 427
Cdd:PLN02790 320 SLISGELPSGWEKALPTFTPEDPAdATRNLSQKCLNALAKVLPGLIGGSADLASSNMTLLKDFGDFQKDTPEERNVRFGV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 428 REFGMACAMNGIMLHG-GTRIFGSTFFVFSDYLKAAIRLSAIQKLPVIYVLTHDSVAVGKDGPTHEPIEQLASLRTIPNV 506
Cdd:PLN02790 400 REHGMGAICNGIALHSsGLIPYCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLGEDGPTHQPIEHLASLRAMPNI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 507 QVFRPADGNETSAAWKVALETLDKPTILVLSRQNLDTLPISKekvFDGVEKGGYVVQG--AENEADGILIATGSEVGLAL 584
Cdd:PLN02790 480 LMLRPADGNETAGAYKVAVTNRKRPTVLALSRQKVPNLPGTS---IEGVEKGGYVISDnsSGNKPDLILIGTGSELEIAA 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 585 KAKEELQKKGKDVIVVSLPSWERFEAQSEEYKNTVIPPELKKRMTIEAGTTYGWAKYAGDHGVMIGIDEFGMSAPSDIVL 664
Cdd:PLN02790 557 KAAKELRKEGKKVRVVSMVCWELFEEQSDEYKESVLPSSVTARVSVEAGSTFGWEKYVGSKGKVIGVDRFGASAPAGILY 636
|
650
....*....|...
4C7V_A 665 RELGMSVENIVDK 677
Cdd:PLN02790 637 KEFGFTVENVVAA 649
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
23-356 |
5.21e-177 |
|
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: 507.31 E-value: 5.21e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 23 VDQLGVNTLRTLSIDAIQRANSGHPGLPMGAAPMAYVLWTRHLKINPkTHMNWVNRDRFVLSAGHGSALLYSLAHLAGYD 102
Cdd:pfam00456 1 IDKRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNP-NDPKWINRDRFVLSNGHGSMLLYSLLHLTGYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 103 VSMDDLKNFREWKSNTPGHPEYGCTDGVEATTGPLGQGISMAVGMAMAEAHLGKKFNREGYPVMDHYTYALIGDGDLMEG 182
Cdd:pfam00456 80 LSMEDLKSFRQLGSKTPGHPEFGHTAGVEVTTGPLGQGIANAVGMAIAERNLAATYNRPGFDIVDHYTYVFLGDGCLMEG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 183 VASEAASLAGHLKLGKLIALYDSNGISLDGKTSASFTENVGARFEAYGWQYILVEDGFNLEEIDKAIVQAKAESDKPTII 262
Cdd:pfam00456 160 VSSEASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDTAARFEAYGWHVIEVEDGHDVEAIAAAIEEAKAEKDKPTLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 263 EIKTTIGYGSEN-QGTHKVHGSPLGEEGVAHAKEVYNWN-YPPFTVPEEVSQRFKECLQDkGVKAENKWNEMFEAYKKEY 340
Cdd:pfam00456 240 KCRTVIGYGSPNkQGTHDVHGAPLGADEVAALKQKLGWDpYKPFEIPAEVYDAWKEKVAE-GAKAEAEWNELFAAYKKAY 318
|
330
....*....|....*.
4C7V_A 341 SDLAQKFSDGFSNKVP 356
Cdd:pfam00456 319 PELAAEFARRLSGELP 334
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
29-294 |
3.11e-137 |
|
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: 402.27 E-value: 3.11e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 29 NTLRTLSIDAIQRANSGHPGLPMGAAPMAYVLWTRHLKINPKtHMNWVNRDRFVLSAGHGSALLYSLAHLAGYDvSMDDL 108
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPA-DPKWPNRDRFVLSKGHASPALYAVLALAGYL-PEEDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 109 KNFREWKSNTPGHPEYGCTDGVEATTGPLGQGISMAVGMAMAEAHLGKkfnregypvmDHYTYALIGDGDLMEGVASEAA 188
Cdd:cd02012 79 KTFRQLGSRLPGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEKLLGF----------DYRVYVLLGDGELQEGSVWEAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 189 SLAGHLKLGKLIALYDSNGISLDGKTSA-SFTENVGARFEAYGWQYILVeDGFNLEEIDKAIVQAKAESDKPTIIEIKTT 267
Cdd:cd02012 149 SFAGHYKLDNLIAIVDSNRIQIDGPTDDiLFTEDLAKKFEAFGWNVIEV-DGHDVEEILAALEEAKKSKGKPTLIIAKTI 227
|
250 260
....*....|....*....|....*...
4C7V_A 268 IGYGSEN-QGTHKVHGSPLGEEGVAHAK 294
Cdd:cd02012 228 KGKGVPFmENTAKWHGKPLGEEEVELAK 255
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
423-541 |
6.81e-34 |
|
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: 126.06 E-value: 6.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 423 IWFGVREFGMACAMNGIMLHGGtRIFGSTFFVFSDYLKAAIRLSAIQKLpVIYVLTHDS-VAVGKDGPTHEPIEQLASLR 501
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFFDRAKDQIRSAGASGN-VPVVFRHDGgGGVGEDGPTHHSIEDEALLR 95
|
90 100 110 120
....*....|....*....|....*....|....*....|
4C7V_A 502 TIPNVQVFRPADGNETSAAWKVALEtLDKPTILVLSRQNL 541
Cdd:smart00861 96 AIPGLKVVAPSDPAEAKGLLRAAIR-DDGPVVIRLERKSL 134
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| TktA |
COG0021 |
Transketolase [Carbohydrate transport and metabolism]; Transketolase is part of the Pathway ... |
21-680 |
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: 1203.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 21 DQVDQLGVNTLRTLSIDAIQRANSGHPGLPMGAAPMAYVLWTRHLKINPKtHMNWVNRDRFVLSAGHGSALLYSLAHLAG 100
Cdd:COG0021 1 MPLDQLAANAIRALAMDAVQKANSGHPGLPMGMAPIAYVLWTKFLKHNPA-NPKWPNRDRFVLSAGHGSMLLYSLLHLTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 101 YDVSMDDLKNFREWKSNTPGHPEYGCTDGVEATTGPLGQGISMAVGMAMAEAHLGKKFNREGYPVMDHYTYALIGDGDLM 180
Cdd:COG0021 80 YDLSLDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGIANAVGMAIAERHLAARFNRPGHDIVDHYTYVIAGDGDLM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 181 EGVASEAASLAGHLKLGKLIALYDSNGISLDGKTSASFTENVGARFEAYGWQYILVEDGFNLEEIDKAIVQAKAESDKPT 260
Cdd:COG0021 160 EGISHEAASLAGHLKLGKLIVLYDDNGISIDGDTDLAFSEDVAKRFEAYGWHVIRVEDGHDLEAIDAAIEAAKAETDKPT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 261 IIEIKTTIGYGSEN-QGTHKVHGSPLGEEGVAHAKEVYNWNYPPFTVPEEVSQRFKECLqDKGVKAENKWNEMFEAYKKE 339
Cdd:COG0021 240 LIICKTIIGYGSPNkQGTAKAHGAPLGAEEIAATKEALGWPPEPFEVPDEVYAHWRAAG-ERGAAAEAEWNERFAAYAAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 340 YSDLAQKFSDGFSNKVPNTLGDILPQYGEDD-SIATRAASQKAINALAKEVSSLWGGAADLASSNKTVIAGEGDFQPESY 418
Cdd:COG0021 319 YPELAAELERRLAGELPEDWDAALPAFEADAkGVATRKASGKVLNALAPVLPELIGGSADLAGSNKTTIKGAGSFSPEDP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 419 EGRNIWFGVREFGMACAMNGIMLHGGTRIFGSTFFVFSDYLKAAIRLSAIQKLPVIYVLTHDSVAVGKDGPTHEPIEQLA 498
Cdd:COG0021 399 SGRNIHFGVREHAMGAIMNGIALHGGLRPYGGTFLVFSDYMRPAIRLAALMKLPVIYVFTHDSIGLGEDGPTHQPVEQLA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 499 SLRTIPNVQVFRPADGNETSAAWKVALETLDKPTILVLSRQNLDTLPISKEKVfDGVEKGGYVVQGAENEADGILIATGS 578
Cdd:COG0021 479 SLRAIPNLDVIRPADANETAAAWKLALERKDGPTALILSRQNLPTLDRTAAAA-EGVAKGAYVLADAEGTPDVILIATGS 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 579 EVGLALKAKEELQKKGKDVIVVSLPSWERFEAQSEEYKNTVIPPELKKRMTIEAGTTYGWAKYAGDHGVMIGIDEFGMSA 658
Cdd:COG0021 558 EVSLAVEAAELLAAEGIKVRVVSMPSWELFEAQDAAYRESVLPPAVRARVAVEAGVTDGWYKYVGLDGAVIGIDTFGASA 637
|
650 660
....*....|....*....|..
4C7V_A 659 PSDIVLRELGMSVENIVDKYLE 680
Cdd:COG0021 638 PAKVLFEEFGFTVENVVAAAKE 659
|
|
| tktlase_bact |
TIGR00232 |
transketolase, bacterial and yeast; This model is designed to capture orthologs of bacterial ... |
28-677 |
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: 933.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 28 VNTLRTLSIDAIQRANSGHPGLPMGAAPMAYVLWTRHLKINPkTHMNWVNRDRFVLSAGHGSALLYSLAHLAGYDVSMDD 107
Cdd:TIGR00232 4 ANAIRHLSMDAIQKAKSGHPGAPMGAAPIAEVLWTKFLKFNP-TNPKWINRDRFVLSNGHGSMLLYSLLHLTGYDLSIED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 108 LKNFREWKSNTPGHPEYGCTDGVEATTGPLGQGISMAVGMAMAEAHLGKKFNREGYPVMDHYTYALIGDGDLMEGVASEA 187
Cdd:TIGR00232 83 LKQFRQLHSKTPGHPEYGHTAGVEATTGPLGQGIANAVGMAIAEKTLAATFNKPGFEIVDHYTYVFVGDGCLQEGISYEV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 188 ASLAGHLKLGKLIALYDSNGISLDGKTSASFTENVGARFEAYGWQYILVEDGFNLEEIDKAIVQAKAESDKPTIIEIKTT 267
Cdd:TIGR00232 163 ASLAGHLKLGKLIVLYDSNRISIDGAVDGSFTEDVAKRFEAYGWEVLEVEDGHDLAAIDAAIEEAKASTDKPTLIEVKTT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 268 IGYGSEN-QGTHKVHGSPLGEEGVAHAKEVYNWNYPPFTVPEEVSQRFKECLQDKGVKAENKWNEMFEAYKKEYSDLAQK 346
Cdd:TIGR00232 243 IGFGSPNkAGTHGVHGAPLGDEEVALTKKNLGWNYNPFEIPQEVYDHFKKTVKERGAKAEQEWNELFAAYKKKYPELAAE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 347 FSDGFSNKVPNTLGDILPQY-GEDDSIATRAASQKAINALAKEVSSLWGGAADLASSNKTVIAGEGDFqPESYEGRNIWF 425
Cdd:TIGR00232 323 FTRRLSGELPADWDKQLPEFkVKLQALATRKYSQNVLNAIANVLPELLGGSADLAPSNLTKWKGSGDL-HENPLGNYIHY 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 426 GVREFGMACAMNGIMLHGGTRIFGSTFFVFSDYLKAAIRLSAIQKLPVIYVLTHDSVAVGKDGPTHEPIEQLASLRTIPN 505
Cdd:TIGR00232 402 GVREFAMGAIMNGIALHGGFKPYGGTFLMFVDYARPAIRLAALMKLPVIYVYTHDSIGVGEDGPTHQPIEQLASLRAIPN 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 506 VQVFRPADGNETSAAWKVALETLDKPTILVLSRQNLDTLPiskEKVFDGVEKGGYVVQGAENeADGILIATGSEVGLALK 585
Cdd:TIGR00232 482 LSVWRPCDGNETAAAWKYALESQDGPTALILSRQNLPQLE---ESSLEKVLKGGYVLKDSKG-PDLILIATGSEVQLAVE 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 586 AKEELQKKGKDVIVVSLPSWERFEAQSEEYKNTVIPPELkKRMTIEAGTTYGWAKYAGDHGVMIGIDEFGMSAPSDIVLR 665
Cdd:TIGR00232 558 AAKKLAAENIKVRVVSMPSFDLFDKQDEEYRESVLPANV-TRLAIEAGAADEWYKYAGLVGAILGMDSFGESAPGDKLFE 636
|
650
....*....|..
4C7V_A 666 ELGMSVENIVDK 677
Cdd:TIGR00232 637 EFGFTVENVVAK 648
|
|
| PLN02790 |
PLN02790 |
transketolase |
32-677 |
0e+00 |
|
transketolase
Pssm-ID: 215424 [Multi-domain] Cd Length: 654 Bit Score: 925.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 32 RTLSIDAIQRANSGHPGLPMGAAPMAYVLWTRHLKINPKTHmNWVNRDRFVLSAGHGSALLYSLAHLAGYD-VSMDDLKN 110
Cdd:PLN02790 2 RFLAIDAVNKANSGHPGLPMGCAPMGHVLYDEVMKYNPKNP-YWFNRDRFVLSAGHGCMLQYALLHLAGYDsVQMEDLKQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 111 FREWKSNTPGHPEYGCTDGVEATTGPLGQGISMAVGMAMAEAHLGKKFNREGYPVMDHYTYALIGDGDLMEGVASEAASL 190
Cdd:PLN02790 81 FRQWGSRTPGHPENFETPGIEVTTGPLGQGIANAVGLALAEKHLAARFNKPDHKIVDHYTYCILGDGCQMEGISNEAASL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 191 AGHLKLGKLIALYDSNGISLDGKTSASFTENVGARFEAYGWQYILVEDGFN-LEEIDKAIVQAKAESDKPTIIEIKTTIG 269
Cdd:PLN02790 161 AGHWGLGKLIVLYDDNHISIDGDTEIAFTEDVDKRYEALGWHTIWVKNGNTdYDEIRAAIKEAKAVTDKPTLIKVTTTIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 270 YGSEN-QGTHKVHGSPLGEEGVAHAKEVYNWNYPPFTVPEEVSQRFKEClQDKGVKAENKWNEMFEAYKKEYSDLAQKFS 348
Cdd:PLN02790 241 YGSPNkANSYSVHGAALGEKEVDATRKNLGWPYEPFHVPEDVKSHWSKH-TKEGAALEAEWNAKFAEYKKKYPEEAAELK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 349 DGFSNKVPNTLGDILPQYGEDDSI-ATRAASQKAINALAKEVSSLWGGAADLASSNKTVIAGEGDFQPESYEGRNIWFGV 427
Cdd:PLN02790 320 SLISGELPSGWEKALPTFTPEDPAdATRNLSQKCLNALAKVLPGLIGGSADLASSNMTLLKDFGDFQKDTPEERNVRFGV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 428 REFGMACAMNGIMLHG-GTRIFGSTFFVFSDYLKAAIRLSAIQKLPVIYVLTHDSVAVGKDGPTHEPIEQLASLRTIPNV 506
Cdd:PLN02790 400 REHGMGAICNGIALHSsGLIPYCATFFVFTDYMRAAMRLSALSEAGVIYVMTHDSIGLGEDGPTHQPIEHLASLRAMPNI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 507 QVFRPADGNETSAAWKVALETLDKPTILVLSRQNLDTLPISKekvFDGVEKGGYVVQG--AENEADGILIATGSEVGLAL 584
Cdd:PLN02790 480 LMLRPADGNETAGAYKVAVTNRKRPTVLALSRQKVPNLPGTS---IEGVEKGGYVISDnsSGNKPDLILIGTGSELEIAA 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 585 KAKEELQKKGKDVIVVSLPSWERFEAQSEEYKNTVIPPELKKRMTIEAGTTYGWAKYAGDHGVMIGIDEFGMSAPSDIVL 664
Cdd:PLN02790 557 KAAKELRKEGKKVRVVSMVCWELFEEQSDEYKESVLPSSVTARVSVEAGSTFGWEKYVGSKGKVIGVDRFGASAPAGILY 636
|
650
....*....|...
4C7V_A 665 RELGMSVENIVDK 677
Cdd:PLN02790 637 KEFGFTVENVVAA 649
|
|
| PRK05899 |
PRK05899 |
transketolase; Reviewed |
24-680 |
0e+00 |
|
transketolase; Reviewed
Pssm-ID: 235639 [Multi-domain] Cd Length: 586 Bit Score: 919.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 24 DQLGVNTLRTLSIDAIQRANSGHPGLPMGAAPMAYVLWTRHLKINPKtHMNWVNRDRFVLSAGHGSALLYSLAHLAGYDV 103
Cdd:PRK05899 8 LQLLANAIRVLSIDAVQKANSGHPGMPMGAADIAYVLWTRFLRHDPK-NPKWPNRDRFVLSAGHGSMLLYSLLHLAGYDL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 104 SMDDLKNFREWKSNTPGHPEYGCTDGVEATTGPLGQGISMAVGMAMAEAHLGKKFNREGYPVMDHYTYALIGDGDLMEGV 183
Cdd:PRK05899 87 SIDDLKNFRQLGSKTPGHPEYGHTPGVETTTGPLGQGLANAVGMALAEKYLAALFNRPGLDIVDHYTYVLCGDGDLMEGI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 184 ASEAASLAGHLKLGKLIALYDSNGISLDGKTSASFTENVGARFEAYGWQYILVeDGFNLEEIDKAIVQAKAeSDKPTIIE 263
Cdd:PRK05899 167 SHEACSLAGHLKLGNLIVIYDDNRISIDGPTEGWFTEDVKKRFEAYGWHVIEV-DGHDVEAIDAAIEEAKA-STKPTLII 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 264 IKTTIGYGSEN-QGTHKVHGSPLGEEGVAHAKEVYNWNYppftvpeevsqrfkeclqdkgvkaenkwnemfeaykkeysd 342
Cdd:PRK05899 245 AKTIIGKGAPNkEGTHKVHGAPLGAEEIAAAKKELGWDY----------------------------------------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 343 laqkfsdgfsnkvpntlgdilpqygeddsiatRAASQKAINALAKEVSSLWGGAADLASSNKTVIAGEGDFQPESYEGRN 422
Cdd:PRK05899 284 --------------------------------RKASGKALNALAKALPELVGGSADLAGSNNTKIKGSKDFAPEDYSGRY 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 423 IWFGVREFGMACAMNGIMLHGGTRIFGSTFFVFSDYLKAAIRLSAIQKLPVIYVLTHDSVAVGKDGPTHEPIEQLASLRT 502
Cdd:PRK05899 332 IHYGVREFAMAAIANGLALHGGFIPFGGTFLVFSDYARNAIRLAALMKLPVIYVFTHDSIGVGEDGPTHQPVEQLASLRA 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 503 IPNVQVFRPADGNETSAAWKVALETLDKPTILVLSRQNLDTLPisKEKVFDGVEKGGYVVqgaENEADGILIATGSEVGL 582
Cdd:PRK05899 412 IPNLTVIRPADANETAAAWKYALERKDGPSALVLTRQNLPVLE--RTAQEEGVAKGGYVL---RDDPDVILIATGSEVHL 486
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 583 ALKAKEELQKKGKDVIVVSLPSWERFEAQSEEYKNTVIPPELKKRMTIEAGTTYGWAKYAGDHGVMIGIDEFGMSAPSDI 662
Cdd:PRK05899 487 ALEAADELEAEGIKVRVVSMPSTELFDEQDAAYKESVLPAAVTARVAVEAGVADGWYKYVGLDGKVLGIDTFGASAPADE 566
|
650
....*....|....*...
4C7V_A 663 VLRELGMSVENIVDKYLE 680
Cdd:PRK05899 567 LFKEFGFTVENIVAAAKE 584
|
|
| PTZ00089 |
PTZ00089 |
transketolase; Provisional |
21-677 |
0e+00 |
|
transketolase; Provisional
Pssm-ID: 173383 [Multi-domain] Cd Length: 661 Bit Score: 847.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 21 DQVDQLGVNTLRTLSIDAIQRANSGHPGLPMGAAPMAYVLWTRHLKINPKtHMNWVNRDRFVLSAGHGSALLYSLAHLAG 100
Cdd:PTZ00089 3 GAIDEKCANEIRCLSADLVQKANSGHPGAPMGMAPIAHILWSEVMKYNPK-DPRWINRDRFVLSNGHASALLYSMLHLTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 101 YDVSMDDLKNFREWKSNTPGHPEYGCTDGVEATTGPLGQGISMAVGMAMAEAHLGKKFNREGYPVMDHYTYALIGDGDLM 180
Cdd:PTZ00089 82 YDLSMEDLKNFRQLGSRTPGHPERHITPGVEVTTGPLGQGIANAVGLAIAEKHLAAKFNRPGHPIFDNYVYVICGDGCLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 181 EGVASEAASLAGHLKLGKLIALYDSNGISLDGKTSASFTENVGARFEAYGWQYILVEDG-FNLEEIDKAIVQAKAESDKP 259
Cdd:PTZ00089 162 EGVSQEALSLAGHLGLEKLIVLYDDNKITIDGNTDLSFTEDVEKKYEAYGWHVIEVDNGnTDFDGLRKAIEEAKKSKGKP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 260 TIIEIKTTIGYGSENQGTHKVHGSPLGEEGVAHAKEVYNWNypP---FTVPEEVSQRFKEcLQDKGVKAENKWNEMFEAY 336
Cdd:PTZ00089 242 KLIIVKTTIGYGSSKAGTEKVHGAPLGDEDIAQVKELFGLD--PekkFHVSEEVRQFFEQ-HVEKKKENYEAWKKRFAKY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 337 KKEYSDLAQKFSDGFSNKVPNTLGDILPQYGEDDS-IATRAASQKAINALAKEVSSLWGGAADLASSNKTVIAGEGDFQP 415
Cdd:PTZ00089 319 TAAFPKEAQAIERRFKGELPPGWEKKLPKYTTNDKaIATRKASENVLNPLFQILPELIGGSADLTPSNLTRPKEANDFTK 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 416 ESYEGRNIWFGVREFGMACAMNGIMLHGGTRIFGSTFFVFSDYLKAAIRLSAIQKLPVIYVLTHDSVAVGKDGPTHEPIE 495
Cdd:PTZ00089 399 ASPEGRYIRFGVREHAMCAIMNGIAAHGGFIPFGATFLNFYGYALGAVRLAALSHHPVIYVATHDSIGLGEDGPTHQPVE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 496 QLASLRTIPNVQVFRPADGNETSAAWKVALETLDKPTILVLSRQNLDTLPISKekvFDGVEKGGYVVQGAENEADGILIA 575
Cdd:PTZ00089 479 TLALLRATPNLLVIRPADGTETSGAYALALANAKTPTILCLSRQNTPPLPGSS---IEGVLKGAYIVVDFTNSPQLILVA 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 576 TGSEVGLALKAKEELqKKGKDVIVVSLPSWERFEAQSEEYKNTVIPPELKKRMTIEAGTTYGWAKYAGDHgvmIGIDEFG 655
Cdd:PTZ00089 556 SGSEVSLCVEAAKAL-SKELNVRVVSMPCWELFDQQSEEYQQSVLPSGGVPVLSVEAYVSFGWEKYSHVH---VGISGFG 631
|
650 660
....*....|....*....|..
4C7V_A 656 MSAPSDIVLRELGMSVENIVDK 677
Cdd:PTZ00089 632 ASAPANALYKHFGFTVENVVEK 653
|
|
| Transketolase_N |
pfam00456 |
Transketolase, thiamine diphosphate binding domain; This family includes transketolase enzymes ... |
23-356 |
5.21e-177 |
|
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: 507.31 E-value: 5.21e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 23 VDQLGVNTLRTLSIDAIQRANSGHPGLPMGAAPMAYVLWTRHLKINPkTHMNWVNRDRFVLSAGHGSALLYSLAHLAGYD 102
Cdd:pfam00456 1 IDKRAVNAIRALAMDAVEKANSGHPGAPMGMAPIAEVLFKRFLKHNP-NDPKWINRDRFVLSNGHGSMLLYSLLHLTGYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 103 VSMDDLKNFREWKSNTPGHPEYGCTDGVEATTGPLGQGISMAVGMAMAEAHLGKKFNREGYPVMDHYTYALIGDGDLMEG 182
Cdd:pfam00456 80 LSMEDLKSFRQLGSKTPGHPEFGHTAGVEVTTGPLGQGIANAVGMAIAERNLAATYNRPGFDIVDHYTYVFLGDGCLMEG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 183 VASEAASLAGHLKLGKLIALYDSNGISLDGKTSASFTENVGARFEAYGWQYILVEDGFNLEEIDKAIVQAKAESDKPTII 262
Cdd:pfam00456 160 VSSEASSLAGHLGLGNLIVFYDDNQISIDGETKISFTEDTAARFEAYGWHVIEVEDGHDVEAIAAAIEEAKAEKDKPTLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 263 EIKTTIGYGSEN-QGTHKVHGSPLGEEGVAHAKEVYNWN-YPPFTVPEEVSQRFKECLQDkGVKAENKWNEMFEAYKKEY 340
Cdd:pfam00456 240 KCRTVIGYGSPNkQGTHDVHGAPLGADEVAALKQKLGWDpYKPFEIPAEVYDAWKEKVAE-GAKAEAEWNELFAAYKKAY 318
|
330
....*....|....*.
4C7V_A 341 SDLAQKFSDGFSNKVP 356
Cdd:pfam00456 319 PELAAEFARRLSGELP 334
|
|
| TPP_TK |
cd02012 |
Thiamine pyrophosphate (TPP) family, Transketolase (TK) subfamily, TPP-binding module; TK ... |
29-294 |
3.11e-137 |
|
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: 402.27 E-value: 3.11e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 29 NTLRTLSIDAIQRANSGHPGLPMGAAPMAYVLWTRHLKINPKtHMNWVNRDRFVLSAGHGSALLYSLAHLAGYDvSMDDL 108
Cdd:cd02012 1 NRIRRLSIDMVQKAGSGHPGGSLSAADILAVLYFKVLKYDPA-DPKWPNRDRFVLSKGHASPALYAVLALAGYL-PEEDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 109 KNFREWKSNTPGHPEYGCTDGVEATTGPLGQGISMAVGMAMAEAHLGKkfnregypvmDHYTYALIGDGDLMEGVASEAA 188
Cdd:cd02012 79 KTFRQLGSRLPGHPEYGLTPGVEVTTGSLGQGLSVAVGMALAEKLLGF----------DYRVYVLLGDGELQEGSVWEAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 189 SLAGHLKLGKLIALYDSNGISLDGKTSA-SFTENVGARFEAYGWQYILVeDGFNLEEIDKAIVQAKAESDKPTIIEIKTT 267
Cdd:cd02012 149 SFAGHYKLDNLIAIVDSNRIQIDGPTDDiLFTEDLAKKFEAFGWNVIEV-DGHDVEEILAALEEAKKSKGKPTLIIAKTI 227
|
250 260
....*....|....*....|....*...
4C7V_A 268 IGYGSEN-QGTHKVHGSPLGEEGVAHAK 294
Cdd:cd02012 228 KGKGVPFmENTAKWHGKPLGEEEVELAK 255
|
|
| TktA1 |
COG3959 |
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism]; |
31-288 |
1.31e-66 |
|
Transketolase, N-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443159 [Multi-domain] Cd Length: 277 Bit Score: 220.33 E-value: 1.31e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 31 LRTLSIDAIQRANSGHPGLPMGAAPMAYVLWTRHLKINPKtHMNWVNRDRFVLSAGHGSALLYS-LAHlAGYdVSMDDLK 109
Cdd:COG3959 15 IRRDILRMIYAAGSGHPGGSLSAADILAALYFKVMNIDPK-NPDWPDRDRFILSKGHAAPALYAvLAE-KGY-FPKEELA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 110 NFREWKSNTPGHPEYGCTDGVEATTGPLGQGISMAVGMAmaeahLGKKFNREgypvmDHYTYALIGDGDLMEGVASEAAS 189
Cdd:COG3959 92 TFRKLGSRLQGHPDMKKTPGVEMSTGSLGQGLSVAVGMA-----LAAKLDGK-----DYRVYVLLGDGELQEGQVWEAAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 190 LAGHLKLGKLIALYDSNGISLDGKTSASF-TENVGARFEAYGWQYILVeDGFNLEEIDKAIVQAKAESDKPTIIEIKTTI 268
Cdd:COG3959 162 AAAHYKLDNLIAIVDRNGLQIDGPTEDVMsLEPLAEKWEAFGWHVIEV-DGHDIEALLAALDEAKAVKGKPTVIIAHTVK 240
|
250 260
....*....|....*....|.
4C7V_A 269 GYG-SENQGTHKVHGSPLGEE 288
Cdd:COG3959 241 GKGvSFMENRPKWHGKAPNDE 261
|
|
| Transket_pyr |
pfam02779 |
Transketolase, pyrimidine binding domain; This family includes transketolase enzymes, pyruvate ... |
370-541 |
4.10e-60 |
|
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: 199.31 E-value: 4.10e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 370 DSIATRAASQKAINALAKEVSSLWGGAADLASSNKTVIAGEGDFQPEsyeGRNIWFGVREFGMACAMNGIMLHGG-TRIF 448
Cdd:pfam02779 1 KKIATRKASGEALAELAKRDPRVVGGGADLAGGTFTVTKGLLHPQGA---GRVIDTGIAEQAMVGFANGMALHGPlLPPV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 449 GSTFFVFSDYLKAAIR-LSAIQKLPVIYVLTHDSVAVGKDGPTHEPIEQLASLRTIPNVQVFRPADGNETSAAWKVALET 527
Cdd:pfam02779 78 EATFSDFLNRADDAIRhGAALGKLPVPFVVTRDPIGVGEDGPTHQSVEDLAFLRAIPGLKVVRPSDAAETKGLLRAAIRR 157
|
170
....*....|....*
4C7V_A 528 LD-KPTILVLSRQNL 541
Cdd:pfam02779 158 DGrKPVVLRLPRQLL 172
|
|
| TPP_PYR_DXS_TK_like |
cd07033 |
Pyrimidine (PYR) binding domain of 1-deoxy-D-xylulose-5-phosphate synthase (DXS), ... |
376-538 |
5.04e-60 |
|
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: 198.43 E-value: 5.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 376 AASQKAINALAKEVSSLWGGAADLASSNKTVIAGEGdfqpesYEGRNIWFGVREFGMACAMNGIMLHGgTRIFGSTFFVF 455
Cdd:cd07033 1 KAFGEALLELAKKDPRIVALSADLGGSTGLDKFAKK------FPDRFIDVGIAEQNMVGIAAGLALHG-LKPFVSTFSFF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 456 SDYLKAAIR-LSAIQKLPVIYVLTHDSVAVGKDGPTHEPIEQLASLRTIPNVQVFRPADGNETSAAWKVALETlDKPTIL 534
Cdd:cd07033 74 LQRAYDQIRhDVALQNLPVKFVGTHAGISVGEDGPTHQGIEDIALLRAIPNMTVLRPADANETAAALEAALEY-DGPVYI 152
|
....
4C7V_A 535 VLSR 538
Cdd:cd07033 153 RLPR 156
|
|
| Transket_pyr |
smart00861 |
Transketolase, pyrimidine binding domain; Transketolase (TK) catalyzes the reversible transfer ... |
423-541 |
6.81e-34 |
|
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: 126.06 E-value: 6.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 423 IWFGVREFGMACAMNGIMLHGGtRIFGSTFFVFSDYLKAAIRLSAIQKLpVIYVLTHDS-VAVGKDGPTHEPIEQLASLR 501
Cdd:smart00861 18 IDTGIAEQAMVGFAAGLALHGL-RPVVEIFFTFFDRAKDQIRSAGASGN-VPVVFRHDGgGGVGEDGPTHHSIEDEALLR 95
|
90 100 110 120
....*....|....*....|....*....|....*....|
4C7V_A 502 TIPNVQVFRPADGNETSAAWKVALEtLDKPTILVLSRQNL 541
Cdd:smart00861 96 AIPGLKVVAPSDPAEAKGLLRAAIR-DDGPVVIRLERKSL 134
|
|
| TktA2 |
COG3958 |
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism]; |
370-677 |
3.39e-29 |
|
Transketolase, C-terminal subunit [Carbohydrate transport and metabolism];
Pssm-ID: 443158 [Multi-domain] Cd Length: 308 Bit Score: 118.27 E-value: 3.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 370 DSIATRAASQKAINALAKEVSSLWGGAADLASSNKTviageGDFQpESYEGRNIWFGVRE---FGMACAMNgimlHGGTR 446
Cdd:COG3958 2 EKKAMRDAFGEALVELAEEDPDIVVLDADLGGSTKL-----DKFA-KAFPDRFFNVGIAEqnmVGVAAGLA----LAGKI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 447 IFGSTFFVFSdYLKAA--IRLS-AIQKLPVIYVLTHDSVAVGKDGPTHEPIEQLASLRTIPNVQVFRPADGNETSAAWKV 523
Cdd:COG3958 72 PFVSTFAPFL-TGRAYeqIRNDiAYPNLNVKIVGSHAGLSYGEDGATHQALEDIALMRALPNMTVIVPADAVETEAAVRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 524 ALETlDKPTILVLSRQNLdtlpiskEKVFDGVEK----GGYVV-QGaeneADGILIATGSEVGLALKAKEELQKKGKDVI 598
Cdd:COG3958 151 AAEH-DGPVYLRLGRGAV-------PVVYDEDYEfeigKARVLrEG----KDVTIIATGIMVAEALEAAELLAKEGISAR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 599 VVSLPS-----WERFEAQSEEYKNTVippelkkrmTIEAGTTYG-----WAKYAGDHG----VMIGI-DEFGMSAPSDIV 663
Cdd:COG3958 219 VINMHTikpldEEAILKAARKTGAVV---------TAEEHSIIGglgsaVAEVLAENYpvplRRIGVpDRFGESGSPEEL 289
|
330
....*....|....
4C7V_A 664 LRELGMSVENIVDK 677
Cdd:COG3958 290 LEKYGLDAEGIVAA 303
|
|
| dxs |
TIGR00204 |
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent ... |
19-679 |
6.16e-19 |
|
1-deoxy-D-xylulose-5-phosphate synthase; DXP synthase is a thiamine diphosphate-dependent enzyme related to transketolase and the pyruvate dehydrogenase E1-beta subunit. By an acyloin condensation of pyruvate with glyceraldehyde 3-phosphate, it produces 1-deoxy-D-xylulose 5-phosphate, a precursor of thiamine diphosphate (TPP), pyridoxal phosphate, and the isoprenoid building block isopentenyl diphosphate (IPP). [Biosynthesis of cofactors, prosthetic groups, and carriers, Other, Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine, Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
Pssm-ID: 129308 [Multi-domain] Cd Length: 617 Bit Score: 90.99 E-value: 6.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 19 PYDQVDQLgVNTLRTLSIDAIQrANSGHPGLPMGAAPMAYVLwtrHLKIN-PKthmnwvnrDRFVLSAGHGSallYSLAH 97
Cdd:TIGR00204 14 SIDELEKL-CDELRRYLLESVS-ASGGHLASGLGTVELTVAL---HYVFNtPK--------DQFIWDVGHQA---YPHKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 98 LAGYDVSMDDLKNFRewksNTPGHPEYGCTDGVEATTGPLGQGISMAVGMAMAeahlgkkFNREGypvMDHYTYALIGDG 177
Cdd:TIGR00204 78 LTGRREKFSTLRQKK----GLHGFPKRSESEYDVFSAGHSSTSISAGLGIAVA-------AEKKG---ADRKTVCVIGDG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 178 DLMEGVASEAASLAGHLKLGKLIALYDSN-GIS-------------LDGKTSASFTENV--------------------- 222
Cdd:TIGR00204 144 AITAGMAFEALNHAGDLKTDMIVILNDNEmSISenvgalsnhlaqlRSGSLYQSLRDGLkkifsklppiknylakrtees 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 223 -------GARFEAYGWQYILVEDGFNLEEIDKAIVQAKaESDKPTIIEIKTTIGYGSEnqgthKVHGSPLGEEGVahake 295
Cdd:TIGR00204 224 mkglvvpGTFFEELGFNYIGPVDGHDLLELIETLKNAK-KLKGPVFLHIQTKKGKGYK-----PAEKDPIGWHGV----- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 296 vynwnyPPFTVpeevsqrfkeclqDKGVKAENKwnEMFEAYKKEYSDLAQKfsdgfsnkvpntlgdilpqygeddsiatr 375
Cdd:TIGR00204 293 ------GPFDL-------------STGCLPKSK--SALPSYSKIFSDTLCE----------------------------- 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 376 aasqkainaLAKEVSSLWGGAADLASSNKTViagegDFQPEsyegrniwFGVREFGMACA------MNGIMLHGGTRIFG 449
Cdd:TIGR00204 323 ---------LAKKDNKIVGITPAMPEGSGLD-----KFSRK--------FPDRYFDVAIAeqhavtFAAGMAIEGYKPFV 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 450 StffVFSDYLKAA----IRLSAIQKLPVIYVLTHDSVaVGKDGPTHEPIEQLASLRTIPNVQVFRPADGNETSAAWKVAL 525
Cdd:TIGR00204 381 A---IYSTFLQRAydqvVHDVCIQKLPVLFAIDRAGI-VGADGETHQGAFDISYLRCIPNMVIMAPSDENELRQMLYTGY 456
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 526 ETLDKPTILVLSRQN---------LDTLPISKEKVfdgVEKGGyvvqgaeneaDGILIATGSEVGLALKAKEELQKKGKD 596
Cdd:TIGR00204 457 HYDDGPIAVRYPRGNavgveltpePEKLPIGKSEV---LRKGE----------KILILGFGTLVPEALEVAESLNEKGIE 523
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 597 VIVVSLpsweRFEAQSEEYKNTVIPPELKKRMTIEAGTTYGW-----AKYAGDHGVM-----IGI-DEFGMSAPSDIVLR 665
Cdd:TIGR00204 524 ATVVDA----RFVKPLDEELILEIAASHEKLVTVEENAIMGGagsavLEFLMDQNKLvpvkrLGIpDFFIPHGTQEEVLA 599
|
730
....*....|....
4C7V_A 666 ELGMSVENIVDKYL 679
Cdd:TIGR00204 600 ELGLDTAGMEAKIL 613
|
|
| PRK05444 |
PRK05444 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
141-677 |
7.13e-17 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 235470 [Multi-domain] Cd Length: 580 Bit Score: 84.36 E-value: 7.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 141 ISMAVGMAMAEAHLGKKfnregypvmDHYTYALIGDGDLMEGVASEAASLAGHLKLGKLIALYDsNGISLDgktsasftE 220
Cdd:PRK05444 123 ISAALGMAKARDLKGGE---------DRKVVAVIGDGALTGGMAFEALNNAGDLKSDLIVILND-NEMSIS--------P 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 221 NVGA--------R----FEAYGWQYILVEDGFNLEEIDKAIVQAKaESDKPTIIEIKTTIGYG---SENQGThKVHGSpl 285
Cdd:PRK05444 185 NVGAlsnylarlRsstlFEELGFNYIGPIDGHDLDALIETLKNAK-DLKGPVLLHVVTKKGKGyapAEADPI-KYHGV-- 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 286 geegvahakevynwnyPPFTVpeevsqrfkeclqDKGVKaenkwnemfeayKKEYSDLAQKFSDGFSnkvpNTLGDILpq 365
Cdd:PRK05444 261 ----------------GKFDP-------------ETGEQ------------PKSSKPGKPSYTKVFG----ETLCELA-- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 366 yGEDDSIAtraasqkAINALAKEVSSLwggaadlassnktviageGDFQ---PESYegrniwF--GVRE-----F--GMA 433
Cdd:PRK05444 294 -EKDPKIV-------AITAAMPEGTGL------------------VKFSkrfPDRY------FdvGIAEqhavtFaaGLA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 434 CamngimlhGGTRIFG---STFF------VFSDYlkaairlsAIQKLPVIYVLthDSvA--VGKDGPTHEPIEQLASLRT 502
Cdd:PRK05444 342 T--------EGLKPVVaiySTFLqraydqVIHDV--------ALQNLPVTFAI--DR-AglVGADGPTHQGAFDLSYLRC 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 503 IPNVQVFRPADGNETSAAWKVALETLDKPTILVLSRQNLDTLPISKEKVFDgVEKGGYVVQGaeneADGILIATGSEVGL 582
Cdd:PRK05444 403 IPNMVIMAPSDENELRQMLYTALAYDDGPIAIRYPRGNGVGVELPELEPLP-IGKGEVLREG----EDVAILAFGTMLAE 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 583 ALKAKEELqkkgKDVIVVSLpsweRF---------EAQSEEYKNTVippelkkrmTIEAGTTYGWA-----KYAGDHGVM 648
Cdd:PRK05444 478 ALKAAERL----ASATVVDA----RFvkpldeellLELAAKHDLVV---------TVEEGAIMGGFgsavlEFLADHGLD 540
|
570 580 590
....*....|....*....|....*....|....*
4C7V_A 649 -----IGI-DEFGMSAPSDIVLRELGMSVENIVDK 677
Cdd:PRK05444 541 vpvlnLGLpDEFIDHGSREELLAELGLDAEGIARR 575
|
|
| Dxs |
COG1154 |
Deoxyxylulose-5-phosphate synthase [Coenzyme transport and metabolism, Lipid transport and ... |
467-680 |
1.96e-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: 80.06 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 467 AIQKLPVIYVLthDSvA--VGKDGPTHEPIEQLASLRTIPNVQVFRPADGNETSAAWKVALEtLDKPTIL---------V 535
Cdd:COG1154 406 ALQNLPVTFAI--DR-AglVGADGPTHHGVFDLSYLRCIPNMVIMAPKDENELRHMLYTALA-YDGPTAIryprgngpgV 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 536 LSRQNLDTLPISK-EKVFDGvekggyvvqgaeneADGILIATGSEVGLALKAKEELQKKGKDVIVVSLpsweRFeaqsee 614
Cdd:COG1154 482 ELPAELEPLPIGKgEVLREG--------------KDVAILAFGTMVAEALEAAERLAAEGISATVVDA----RF------ 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 615 ykntVIP--PELKKRM--------TIEAGTT---YGWA--KYAGDHGV-----MIGI-DEFGMSAPSDIVLRELGMSVEN 673
Cdd:COG1154 538 ----VKPldEELILELarehdlvvTVEEGVLaggFGSAvlEFLADAGLdvpvlRLGLpDRFIEHGSRAELLAELGLDAEG 613
|
....*..
4C7V_A 674 IVDKYLE 680
Cdd:COG1154 614 IARAILE 620
|
|
| TPP_DXS |
cd02007 |
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; ... |
133-271 |
6.19e-15 |
|
Thiamine pyrophosphate (TPP) family, DXS subfamily, TPP-binding module; 1-Deoxy-D-xylulose-5-phosphate synthase (DXS) is a regulatory enzyme of the mevalonate-independent pathway involved in terpenoid biosynthesis. Terpeniods are plant natural products with important pharmaceutical activity. DXS catalyzes a transketolase-type condensation of pyruvate with D-glyceraldehyde-3-phosphate to form 1-deoxy-D-xylulose-5-phosphate (DXP) and carbon dioxide. The formation of DXP leads to the formation of the terpene precursor IPP (isopentyl diphosphate) and to the formation of thiamine (vitamin B1) and pyridoxal (vitamin B6).
Pssm-ID: 238965 [Multi-domain] Cd Length: 195 Bit Score: 73.73 E-value: 6.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 133 TTGPLGQGISMAVGMAMAEAHLGKKFNregypvmdhyTYALIGDGDLMEGVASEAASLAGHLKlGKLIALYDSNGISLDg 212
Cdd:cd02007 73 GTGHSSTSISAALGMAVARDLKGKKRK----------VIAVIGDGALTGGMAFEALNNAGYLK-SNMIVILNDNEMSIS- 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
4C7V_A 213 ktsasftENVGAR---FEAYGWQYILVEDGFNLEEIDKAIVQAKaESDKPTIIEIKTTIGYG 271
Cdd:cd02007 141 -------PNVGTPgnlFEELGFRYIGPVDGHNIEALIKVLKEVK-DLKGPVLLHVVTKKGKG 194
|
|
| PRK12571 |
PRK12571 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
141-676 |
7.63e-14 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 183601 [Multi-domain] Cd Length: 641 Bit Score: 74.76 E-value: 7.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 141 ISMAVGMAMAEAhLGKKfnregypvmDHYTYALIGDGDLMEGVASEAASLAGHLKlGKLIALYDSNGISLDGKTSA---- 216
Cdd:PRK12571 125 ISAALGFAKARA-LGQP---------DGDVVAVIGDGSLTAGMAYEALNNAGAAD-RRLIVILNDNEMSIAPPVGAlaay 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 217 --------------SFTENVGAR-------------------------FEAYGWQYILVEDGFNLEEIDKAIVQAKAESD 257
Cdd:PRK12571 194 lstlrssdpfarlrAIAKGVEERlpgplrdgarrarelvtgmigggtlFEELGFTYVGPIDGHDMEALLSVLRAARARAD 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 258 KPTIIEIKTTIGYGsenqgthkvhgsplgeegvahakevynwnYPPftvpeevsqrfKECLQDKgvkaenkwnemFEAYK 337
Cdd:PRK12571 274 GPVLVHVVTEKGRG-----------------------------YAP-----------AEADEDK-----------YHAVG 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 338 KeysdlaqkfsdgfsnkvpntlgdILPQYGEDDSIATRAAS-----QKAINALAKEVSSLWGGAADLASSnktviAGEGD 412
Cdd:PRK12571 303 K-----------------------FDVVTGLQKKSAPSAPSytsvfGEELTKEAAEDSDIVAITAAMPLG-----TGLDK 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 413 FQpESYEGRNIWFGVRE-FGMACAMNgiMLHGGTRIFgstFFVFSDYLKAA----IRLSAIQKLPVIYVLTHDSVaVGKD 487
Cdd:PRK12571 355 LQ-KRFPNRVFDVGIAEqHAVTFAAG--LAAAGLKPF---CAVYSTFLQRGydqlLHDVALQNLPVRFVLDRAGL-VGAD 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 488 GPTHEPIEQLASLRTIPNVQVFRPADGNETSAAWKVALETLDKPTILVLSRQNLDTLPISKEKVFDGVEKGGYVVQGaen 567
Cdd:PRK12571 428 GATHAGAFDLAFLTNLPNMTVMAPRDEAELRHMLRTAAAHDDGPIAVRFPRGEGVGVEIPAEGTILGIGKGRVPREG--- 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 568 eADGILIATGSEVGLALKAKEELQKKGKDVIVVSlPSW-----ERFEAQSEEYKNTVIppelkkrmTIEAGTTYGW---- 638
Cdd:PRK12571 505 -PDVAILSVGAHLHECLDAADLLEAEGISVTVAD-PRFvkpldEALTDLLVRHHIVVI--------VEEQGAMGGFgahv 574
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
4C7V_A 639 AKYAGDHGVM--------IGI-DEFGMSAPSDIVLRELGMSVENIVD 676
Cdd:PRK12571 575 LHHLADTGLLdgglklrtLGLpDRFIDHASREEMYAEAGLTAPDIAA 621
|
|
| Transketolase_C |
pfam02780 |
Transketolase, C-terminal domain; The C-terminal domain of transketolase has been proposed as ... |
559-674 |
1.14e-13 |
|
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: 68.01 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 559 GYVVQGAENEaDGILIATGSEVGLALKAKEELQKKGKDVIVVSLPSWERFEAQS-----EEYKNTVIPPELKKRMTIEAG 633
Cdd:pfam02780 1 GKAEILREGD-DVTIVAYGSMVEEALEAAELLAKEGISAEVVDLRTIKPLDKETilesvKKTGRLVTVEEAVPRGGFGSE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
4C7V_A 634 TTYGWAKYAGDHG----VMIGIDEFGMSAPSDIVLRELGMSVENI 674
Cdd:pfam02780 80 VAAALAEEAFDGLdapvLRVGGPDFPEPGSADELEKLYGLTPEKI 124
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
121-266 |
1.64e-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: 66.12 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 121 HPEYGCTDGVEATTGPLGQGISMAVGMAMAEAhlgkkfnregypvmDHYTYALIGDGDLMEGVAsEAASlAGHLKLgKLI 200
Cdd:cd00568 32 PLRRGRRFLTSTGFGAMGYGLPAAIGAALAAP--------------DRPVVCIAGDGGFMMTGQ-ELAT-AVRYGL-PVI 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
4C7V_A 201 ALYDSNGISLDGKTSAS------------FTENVGARFEAYGWQYILVEDgfnLEEIDKAIVQAKAeSDKPTIIEIKT 266
Cdd:cd00568 95 VVVFNNGGYGTIRMHQEafyggrvsgtdlSNPDFAALAEAYGAKGVRVED---PEDLEAALAEALA-AGGPALIEVKT 168
|
|
| PRK12315 |
PRK12315 |
1-deoxy-D-xylulose-5-phosphate synthase; Provisional |
141-676 |
1.49e-10 |
|
1-deoxy-D-xylulose-5-phosphate synthase; Provisional
Pssm-ID: 237053 [Multi-domain] Cd Length: 581 Bit Score: 64.26 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 141 ISMAVGMAMAEAHLGKKFNregypVMdhytyALIGDGDLMEGVASEAASLAGHLKlGKLIALYDSNGISLD--------- 211
Cdd:PRK12315 119 IALATGLAKARDLKGEKGN-----II-----AVIGDGSLSGGLALEGLNNAAELK-SNLIIIVNDNQMSIAenhgglykn 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 212 --------GKTSASFtenvgarFEAYGWQYILVEDGFNLEEIDKAIVQAKaESDKPTIIEIKTTIGYGSEnqgthkvhgs 283
Cdd:PRK12315 188 lkelrdtnGQSENNL-------FKAMGLDYRYVEDGNDIESLIEAFKEVK-DIDHPIVLHIHTLKGKGYQ---------- 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 284 PLGEEgvahaKEVYNWNYpPFTVpeevsqrfkECLQDKgvkaenkwnemFEAYKKEYSDLAQKFsdgfsnkvpntlgdIL 363
Cdd:PRK12315 250 PAEEN-----KEAFHWHM-PFDL---------ETGQSK-----------VPASGESYSSVTLDY--------------LL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 364 PQYGEDDSIAtraasqkAINAlakevsslwggaadlasSNKTVIaGEGDFQPEsYEGRNIWFGVREfGMACAMNGIMLHG 443
Cdd:PRK12315 290 KKIKEGKPVV-------AINA-----------------AIPGVF-GLKEFRKK-YPDQYVDVGIAE-QESVAFASGIAAN 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 444 GTRIFgstFFVFSDYLKAAI-RLS---AIQKLPVIYVLTHDSVAvGKDgPTHEPIEQLASLRTIPNVQVFRPADGNETSA 519
Cdd:PRK12315 343 GARPV---IFVNSTFLQRAYdQLShdlAINNNPAVMIVFGGSIS-GND-VTHLGIFDIPMISNIPNLVYLAPTTKEELIA 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 520 AWKVALETLDKPtilVLSRQNLDTLPISKEKVFDGVEKGGYVVQGAENEAdgiLIATGSEVGLALKAKEELQKK-GKDVI 598
Cdd:PRK12315 418 MLEWALTQHEHP---VAIRVPEHGVESGPTVDTDYSTLKYEVTKAGEKVA---ILALGDFYELGEKVAKKLKEElGIDAT 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 599 VV-----SLPSWERFEAQSEEYKnTVIppelkkrmTIEAGTTYGW-----AKYAGDHGVMI---GID-EFGMSAPSDIVL 664
Cdd:PRK12315 492 LInpkfiTGLDEELLEKLKEDHE-LVV--------TLEDGILDGGfgekiARYYGNSDMKVlnyGAKkEFNDRVPVEELY 562
|
570
....*....|..
4C7V_A 665 RELGMSVENIVD 676
Cdd:PRK12315 563 KRNHLTPEQIVE 574
|
|
| TPP_E1_EcPDC_like |
cd02017 |
Thiamine pyrophosphate (TPP) family, E1 of E. coli PDC-like subfamily, TPP-binding module; ... |
38-236 |
5.29e-08 |
|
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: 55.39 E-value: 5.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 38 AIQRANS------GHPGLPMGAAPMAYVLWTrHLKinpKTHMNWVNRDRfVLSAGHGSALLYSLAHLAGyDVSMDDLKNF 111
Cdd:cd02017 18 MVHRANKkdlgigGHIATFASAATLYEVGFN-HFF---RARGEGGGGDL-VYFQGHASPGIYARAFLEG-RLTEEQLDNF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 112 REWKSNtPGHPEY----GCTDGVEATTGPLGQGISMAVGMAMAEAHLGKKfnreGYPVM-DHYTYALIGDGDLMEGVASE 186
Cdd:cd02017 92 RQEVGG-GGLSSYphpwLMPDFWEFPTVSMGLGPIQAIYQARFNRYLEDR----GLKDTsDQKVWAFLGDGEMDEPESLG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
4C7V_A 187 AASLAGHLKLGKLIALYDSNGISLDGKTSASFT--ENVGARFEAYGWQYILV 236
Cdd:cd02017 167 AIGLAAREKLDNLIFVVNCNLQRLDGPVRGNGKiiQELEGIFRGAGWNVIKV 218
|
|
| TPP_E1_PDC_ADC_BCADC |
cd02000 |
Thiamine pyrophosphate (TPP) family, E1 of PDC_ADC_BCADC subfamily, TPP-binding module; ... |
132-266 |
1.44e-07 |
|
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: 53.65 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 132 ATTGPLGQGISMAVGMAMAEAHLGKkfnregypvmDHYTYALIGDGDLMEGVASEAASLAGHLKLGKLIALYDsNGISLD 211
Cdd:cd02000 101 GGNGIVGGQVPLAAGAALALKYRGE----------DRVAVCFFGDGATNEGDFHEALNFAALWKLPVIFVCEN-NGYAIS 169
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
4C7V_A 212 GKTS-ASFTENVGARFEAYGWQYILVeDGFNLEEIDKAIVQAKA---ESDKPTIIEIKT 266
Cdd:cd02000 170 TPTSrQTAGTSIADRAAAYGIPGIRV-DGNDVLAVYEAAKEAVErarAGGGPTLIEAVT 227
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
87-266 |
2.63e-05 |
|
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: 45.28 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 87 HGSALLYSLAHLAGYDVSMDD--LKNFREWKSNTPG---HPEYGCTdgveatTGPLGQGISMAVGMAMAEAhlgkkfnre 161
Cdd:cd02002 2 TPEYLAAALAAALPEDAIIVDeaVTNGLPLRDQLPLtrpGSYFTLR------GGGLGWGLPAAVGAALANP--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 162 gypvmDHYTYALIGDGDLMEGVasEAASLAGHLKLGKLIALYDSNGISldgkTSASFTENVGA----------------- 224
Cdd:cd02002 67 -----DRKVVAIIGDGSFMYTI--QALWTAARYGLPVTVVILNNRGYG----ALRSFLKRVGPegpgenapdgldlldpg 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
4C7V_A 225 -RF----EAYGWQYILVEDGfnlEEIDKAIVQAKAEsDKPTIIEIKT 266
Cdd:cd02002 136 iDFaaiaKAFGVEAERVETP---EELDEALREALAE-GGPALIEVVV 178
|
|
| E1_dh |
pfam00676 |
Dehydrogenase E1 component; This family uses thiamine pyrophosphate as a cofactor. This family ... |
135-346 |
6.56e-04 |
|
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: 42.31 E-value: 6.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 135 GPLGQGISMAVGMAMAEAHLGKKfnregypvmdHYTYALIGDGDLMEGVASEAASLAGHLKLgKLIALYDSN--GISLDG 212
Cdd:pfam00676 101 GILGAQVPLGAGIALAAKYRGKK----------EVAITLYGDGAANQGDFFEGLNFAALWKL-PVIFVCENNqyGISTPA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 213 KTSASfTENVGARFEAYGWQYILVeDGFNLEEIDKAIVQAKA---ESDKPTIIEIKTtigygsenqgtHKVHGSPLGEEG 289
Cdd:pfam00676 170 ERASA-STTYADRARGYGIPGLHV-DGMDPLAVYQASKFAAErarTGKGPFLIELVT-----------YRYGGHSMSDDP 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
4C7V_A 290 VAH--AKEVYNWNYPPftvpeEVSQRFKECLQDKGVKAENKWNEMFEAYKKEYSDLAQK 346
Cdd:pfam00676 237 STYrtRDEYEEVRKKK-----DPIQRFKEHLVSKGVWSEEELKAIEKEVRKEVEEAFKK 290
|
|
| AcoA |
COG1071 |
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and ... |
133-267 |
8.36e-04 |
|
TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; TPP-dependent pyruvate or acetoin dehydrogenase subunit alpha is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440689 [Multi-domain] Cd Length: 348 Bit Score: 42.05 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 133 TTGPLGQGISMAVGMAMAEAHLGKkfnregypvmDHYTYALIGDGDLMEGVASEAASLAGHLKLGKLIALYDsNG--ISl 210
Cdd:COG1071 125 GSGIVGGQLPHAVGAALAAKLRGE----------DEVAVAFFGDGATSEGDFHEALNFAAVWKLPVVFVCEN-NGyaIS- 192
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
4C7V_A 211 dgkTS---ASFTENVGARFEAYGWQYILVeDGFNLEE----IDKAIVQAKAEsDKPTIIEIKTT 267
Cdd:COG1071 193 ---TPverQTAVETIADRAAGYGIPGVRV-DGNDVLAvyaaVKEAVERARAG-EGPTLIEAKTY 251
|
|
| PLN02234 |
PLN02234 |
1-deoxy-D-xylulose-5-phosphate synthase |
134-271 |
2.53e-03 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 177878 [Multi-domain] Cd Length: 641 Bit Score: 40.85 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 134 TGPLGQGISMAVGMAMAEAHLGkkfnregypvMDHYTYALIGDGDLMEGVASEAASLAGHLKLGKLIALYDSNGISLDGK 213
Cdd:PLN02234 176 TGHSSTTLSAGLGMAVGRDLKG----------MNNSVVSVIGDGAMTAGQAYEAMNNAGYLHSNMIVILNDNKQVSLPTA 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 214 TSASFTENVGA---------------------RFEAYGWQYILVEDGFNLEEIDKAIVQAKA-ESDKPTIIEIKTTIGYG 271
Cdd:PLN02234 246 NLDGPTQPVGAlscalsrlqsncgmiretsstLFEELGFHYVGPVDGHNIDDLVSILETLKStKTIGPVLIHVVTEKGRG 325
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
468-599 |
6.55e-03 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 39.88 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 468 IQKLPVIYVLTHDSVaVGKDGPTHEPIEQLASLRTIPNVQVFRPADGNETSAAWKVALETLDKPTILVLSRQN--LDTLP 545
Cdd:PLN02582 446 LQKLPVRFAMDRAGL-VGADGPTHCGAFDVTYMACLPNMVVMAPSDEAELFHMVATAAAIDDRPSCFRYPRGNgiGVQLP 524
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
4C7V_A 546 ISKEKVFDGVEKGGYVVQGAENEadgiLIATGSEVGLALKAKEELQKKGKDVIV 599
Cdd:PLN02582 525 PNNKGIPIEVGKGRILLEGERVA----LLGYGTAVQSCLAAASLLERHGLSATV 574
|
|
| PLN02582 |
PLN02582 |
1-deoxy-D-xylulose-5-phosphate synthase |
125-224 |
9.22e-03 |
|
1-deoxy-D-xylulose-5-phosphate synthase
Pssm-ID: 178194 [Multi-domain] Cd Length: 677 Bit Score: 39.11 E-value: 9.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4C7V_A 125 GCTDGVEATTGPLGQG-----ISMAVGMAMAEAHLGKKFNregypvmdhyTYALIGDGDLMEGVASEAASLAGHLKLGKL 199
Cdd:PLN02582 129 GFTKRAESEYDCFGTGhssttISAGLGMAVGRDLKGKKNN----------VVAVIGDGAMTAGQAYEAMNNAGYLDSDMI 198
|
90 100
....*....|....*....|....*
4C7V_A 200 IALYDSNGISLDGKTSASFTENVGA 224
Cdd:PLN02582 199 VILNDNKQVSLPTATLDGPAPPVGA 223
|
|
| |
