|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05269 |
PRK05269 |
transaldolase B; Provisional |
1-317 |
0e+00 |
|
transaldolase B; Provisional
Pssm-ID: 235381 [Multi-domain] Cd Length: 318 Bit Score: 564.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 1 MTTALDQLKQYTTVVADTGDFQQLAQYKPQDATTNPSLILKAVQKDAYKPILEKTVR------DHRNESTDFIIDRLLIA 74
Cdd:PRK05269 1 MTNKLEQLKQFTTVVADTGDIEAIKKYQPQDATTNPSLILKAAQIPEYAPLIDDAVAwakqqsGDRAQQIDDAIDKLAVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 75 FGTEILKLIPGRVSTEVDARLSFDTQRSIDKGRELIKLYEAAGVGRERILIKLASTWEGIRAAEVLQKEGIKCNMTLLFS 154
Cdd:PRK05269 81 FGLEILKLIPGRVSTEVDARLSFDTEATIAKARKLIALYEEAGISKDRILIKIASTWEGIRAAEQLEKEGINCNLTLLFS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 155 LVQAAACAEAGAQLISPFVGRIYDWYKKQAGadwnEARDGGANDPGVQSVRRIYTYYKTFGYKTEVMGASFRTTSQIIEL 234
Cdd:PRK05269 161 FAQARACAEAGVFLISPFVGRILDWYKKNTG----KKEYAPAEDPGVVSVTKIYNYYKKHGYKTVVMGASFRNTGQILEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 235 AGCDLLTISPDLLQKLQESNDTVARKLSPDTLQDKPaeRVAIDEASFRFQLNDEAMATEKLAEGIRVFAADAVKLEKLID 314
Cdd:PRK05269 237 AGCDRLTISPALLEELAASEGELERKLSPPGEAKAR--PVPLTEAEFRWQHNEDAMATEKLAEGIRKFAKDQEKLEKLIA 314
|
...
gi 501469305 315 ALR 317
Cdd:PRK05269 315 AKL 317
|
|
| Transaldolase_TalAB |
cd00957 |
Transaldolases including both TalA and TalB; Transaldolases including both TalA and TalB. The ... |
3-313 |
5.90e-172 |
|
Transaldolases including both TalA and TalB; Transaldolases including both TalA and TalB. The enzyme catalyses the reversible transfer of a dyhydroxyacetone moiety, derived from fructose-6-phosphate to erythrose-4-phosphate yielding sedoheptulose-7-phosphate and glyceraldehyde-3-phosphate. The catalytic mechanism is similar to other class I aldolases. The enzyme is found in the non-oxidative branch of the pentose phosphate pathway and forms a dimer in solution.
Pssm-ID: 188644 [Multi-domain] Cd Length: 313 Bit Score: 479.04 E-value: 5.90e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 3 TALDQLKQYTTVVADTGDFQQLAQYKPQDATTNPSLILKAVQKDAYKPILEKTVRDHR------NESTDFIIDRLLIAFG 76
Cdd:cd00957 1 NQLDQLKKFTTIVADTGDFEAIKKFKPQDATTNPSLILAAAKLPEYNKLVDEAIAYAKkkggsdEDQISNALDKLLVNFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 77 TEILKLIPGRVSTEVDARLSFDTQRSIDKGRELIKLYEAAGVGRERILIKLASTWEGIRAAEVLQKEGIKCNMTLLFSLV 156
Cdd:cd00957 81 TEILKLIPGRVSTEVDARLSFDTNATIAKARKLIKLYEEAGIDKERILIKIAATWEGIQAAKQLEKEGIHCNLTLLFSFA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 157 QAAACAEAGAQLISPFVGRIYDWYKKQAGADWNEArdggANDPGVQSVRRIYTYYKTFGYKTEVMGASFRTTSQIIELAG 236
Cdd:cd00957 161 QAVACAEAGVTLISPFVGRILDWYKKHSGDKAYTA----EEDPGVASVKKIYNYYKKFGYKTKVMGASFRNIGQILALAG 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501469305 237 CDLLTISPDLLQKLQESNDTVARKLSPDTLQDKPAERVAIDEASFRFQLNDEAMATEKLAEGIRVFAADAVKLEKLI 313
Cdd:cd00957 237 CDYLTISPALLEELKNSTAKVERKLDPAASKALDIHPNFLDESAFRWALNEDAMAVEKLSEGIRGFAKDAVKLEKLI 313
|
|
| talAB |
TIGR00874 |
transaldolase; This family includes the majority of known and predicted transaldolase ... |
3-316 |
2.47e-156 |
|
transaldolase; This family includes the majority of known and predicted transaldolase sequences, including E. coli TalA and TalB. It excluded two other families. The first includes E. coli transaldolase-like protein TalC. The second family includes the putative transaldolases of Helicobacter pylori and Mycobacterium tuberculosis. [Energy metabolism, Pentose phosphate pathway]
Pssm-ID: 162081 Cd Length: 317 Bit Score: 439.58 E-value: 2.47e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 3 TALDQLKQYTTVVADTGDFQQLAQYKPQDATTNPSLILKAVQKDAYKPILEKTV---RDHRNESTD---FIIDRLLIAFG 76
Cdd:TIGR00874 1 NQLDQLKQFTVVVADTGDIEAIKKYQPQDATTNPSLILAAAQLPKYAELIDEAVawgKKQGKDDAQqveNALDKLAVNFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 77 TEILKLIPGRVSTEVDARLSFDTQRSIDKGRELIKLYEAAGVGRERILIKLASTWEGIRAAEVLQKEGIKCNMTLLFSLV 156
Cdd:TIGR00874 81 LEILKIVPGRVSTEVDARLSFDTEATVEKARHLIKLYEDAGVDKKRILIKIASTWEGIRAAEELEKEGIHCNLTLLFSFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 157 QAAACAEAGAQLISPFVGRIYDWYKKQAGADwneaRDGGANDPGVQSVRRIYTYYKTFGYKTEVMGASFRTTSQIIELAG 236
Cdd:TIGR00874 161 QAIACAEAKVTLISPFVGRILDWYKAATGKK----EYSIEEDPGVASVKKIYNYYKKHGYPTEVMGASFRNKEEILALAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 237 CDLLTISPDLLQKLQESNDTVARKLSPDTLQDKPAERVAIDEASFRFQLNDEAMATEKLAEGIRVFAADAVKLEKLIDAL 316
Cdd:TIGR00874 237 CDRLTISPALLDELKESTGPVERKLDPESAKKVDKQPIILDESEFRFLHNEDAMATEKLAEGIRKFAADQEKLEKLLEEK 316
|
|
| TAL_FSA |
pfam00923 |
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ... |
14-313 |
5.46e-83 |
|
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose phosphate pathway (PPP) found almost ubiquitously in the three domains of life (Archaea, Bacteria, and Eukarya). TAL shares a high degree of structural similarity and sequence identity with fructose-6-phosphate aldolase (FSA). They both belong to the class I aldolase family. Their protein structures have been revealed.
Pssm-ID: 395737 [Multi-domain] Cd Length: 226 Bit Score: 250.15 E-value: 5.46e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 14 VVADTGDFQQLAQYKP----QDATTNPSLILKAVQ-KDAYKPILEktvrdhrnestdfiidrlliafgtEILKLIPGRVS 88
Cdd:pfam00923 1 IWLDTADRDLIKKLIEeggiDGVTTNPSIFLKAIEySALYDEAIA------------------------EIKEIGDGPVS 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 89 TEVDARLSFDTQRSIDKGRELIKLYEaagvgRERILIKLASTWEGIRAAEVLQKEGIKCNMTLLFSLVQAAACAEAGAQL 168
Cdd:pfam00923 57 LEVDPRLADDTEGTIEEARRLIALYG-----RPNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALAAAEAGASV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 169 ISPFVGRIYDWYKKQAGADWneardggANDPGVQSVRRIYTYYKTFGYKTEVMGASFRTTSQIIELAGCDLLTISPDLLQ 248
Cdd:pfam00923 132 ISPFVGRIDDWGDKRLGAAL-------RGDDGIANAKEIYQIYKKYGWSTGVLAASFRNVLYVLALAGCDTITIPPDTLE 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501469305 249 KLQEsndtvarklspdtlqdkpaervaideasfrfqlndeamateklAEGIRVFAADAVKLEKLI 313
Cdd:pfam00923 205 ALAK-------------------------------------------DEGVRKFAKDWEKLLGSI 226
|
|
| TalA |
COG0176 |
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ... |
12-309 |
1.43e-70 |
|
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; Transaldolase/fructose-6-phosphate aldolase is part of the Pathway/BioSystem: Pentose phosphate pathway
Pssm-ID: 439946 [Multi-domain] Cd Length: 214 Bit Score: 218.02 E-value: 1.43e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 12 TTVVADTGDFQQLAQYK----PQDATTNPSLILKAVQKDAykpilektvrdhrnestdfiidrllIAFGTEILKLIPGRV 87
Cdd:COG0176 1 MKLWLDTADREEIKELIdlggVDGVTTNPSLIAKAGIKDF-------------------------VEDIREICDIVDGPV 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 88 STEVdarLSFDTQRSIDKGRELIKLYeaagvgRERILIKLASTWEGIRAAEVLQKEGIKCNMTLLFSLVQAAACAEAGAQ 167
Cdd:COG0176 56 SAEV---LATDTEGMIAEARRLAALY------RPNVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQALLAAEAGAS 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 168 LISPFVGRIYDWykkqaGADwneardggandpGVQSVRRIYTYYKTFGYKTEVMGASFRTTSQIIE--LAGCDLLTISPD 245
Cdd:COG0176 127 YVSPFVGRIDDI-----GID------------GIALVREIYQIYKNYGARTRILAASFRNPLQVLEaaLAGADTVTIPPA 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501469305 246 LLQKLqesndtvarklspdtlqdkpaervaideasfrfqlndeaMATEKLAEGIRVFAADAVKL 309
Cdd:COG0176 190 VLEAL---------------------------------------ADHPLTDEGIEKFLADWEKL 214
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05269 |
PRK05269 |
transaldolase B; Provisional |
1-317 |
0e+00 |
|
transaldolase B; Provisional
Pssm-ID: 235381 [Multi-domain] Cd Length: 318 Bit Score: 564.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 1 MTTALDQLKQYTTVVADTGDFQQLAQYKPQDATTNPSLILKAVQKDAYKPILEKTVR------DHRNESTDFIIDRLLIA 74
Cdd:PRK05269 1 MTNKLEQLKQFTTVVADTGDIEAIKKYQPQDATTNPSLILKAAQIPEYAPLIDDAVAwakqqsGDRAQQIDDAIDKLAVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 75 FGTEILKLIPGRVSTEVDARLSFDTQRSIDKGRELIKLYEAAGVGRERILIKLASTWEGIRAAEVLQKEGIKCNMTLLFS 154
Cdd:PRK05269 81 FGLEILKLIPGRVSTEVDARLSFDTEATIAKARKLIALYEEAGISKDRILIKIASTWEGIRAAEQLEKEGINCNLTLLFS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 155 LVQAAACAEAGAQLISPFVGRIYDWYKKQAGadwnEARDGGANDPGVQSVRRIYTYYKTFGYKTEVMGASFRTTSQIIEL 234
Cdd:PRK05269 161 FAQARACAEAGVFLISPFVGRILDWYKKNTG----KKEYAPAEDPGVVSVTKIYNYYKKHGYKTVVMGASFRNTGQILEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 235 AGCDLLTISPDLLQKLQESNDTVARKLSPDTLQDKPaeRVAIDEASFRFQLNDEAMATEKLAEGIRVFAADAVKLEKLID 314
Cdd:PRK05269 237 AGCDRLTISPALLEELAASEGELERKLSPPGEAKAR--PVPLTEAEFRWQHNEDAMATEKLAEGIRKFAKDQEKLEKLIA 314
|
...
gi 501469305 315 ALR 317
Cdd:PRK05269 315 AKL 317
|
|
| Transaldolase_TalAB |
cd00957 |
Transaldolases including both TalA and TalB; Transaldolases including both TalA and TalB. The ... |
3-313 |
5.90e-172 |
|
Transaldolases including both TalA and TalB; Transaldolases including both TalA and TalB. The enzyme catalyses the reversible transfer of a dyhydroxyacetone moiety, derived from fructose-6-phosphate to erythrose-4-phosphate yielding sedoheptulose-7-phosphate and glyceraldehyde-3-phosphate. The catalytic mechanism is similar to other class I aldolases. The enzyme is found in the non-oxidative branch of the pentose phosphate pathway and forms a dimer in solution.
Pssm-ID: 188644 [Multi-domain] Cd Length: 313 Bit Score: 479.04 E-value: 5.90e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 3 TALDQLKQYTTVVADTGDFQQLAQYKPQDATTNPSLILKAVQKDAYKPILEKTVRDHR------NESTDFIIDRLLIAFG 76
Cdd:cd00957 1 NQLDQLKKFTTIVADTGDFEAIKKFKPQDATTNPSLILAAAKLPEYNKLVDEAIAYAKkkggsdEDQISNALDKLLVNFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 77 TEILKLIPGRVSTEVDARLSFDTQRSIDKGRELIKLYEAAGVGRERILIKLASTWEGIRAAEVLQKEGIKCNMTLLFSLV 156
Cdd:cd00957 81 TEILKLIPGRVSTEVDARLSFDTNATIAKARKLIKLYEEAGIDKERILIKIAATWEGIQAAKQLEKEGIHCNLTLLFSFA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 157 QAAACAEAGAQLISPFVGRIYDWYKKQAGADWNEArdggANDPGVQSVRRIYTYYKTFGYKTEVMGASFRTTSQIIELAG 236
Cdd:cd00957 161 QAVACAEAGVTLISPFVGRILDWYKKHSGDKAYTA----EEDPGVASVKKIYNYYKKFGYKTKVMGASFRNIGQILALAG 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501469305 237 CDLLTISPDLLQKLQESNDTVARKLSPDTLQDKPAERVAIDEASFRFQLNDEAMATEKLAEGIRVFAADAVKLEKLI 313
Cdd:cd00957 237 CDYLTISPALLEELKNSTAKVERKLDPAASKALDIHPNFLDESAFRWALNEDAMAVEKLSEGIRGFAKDAVKLEKLI 313
|
|
| PRK12346 |
PRK12346 |
transaldolase A; Provisional |
5-317 |
1.76e-157 |
|
transaldolase A; Provisional
Pssm-ID: 183458 Cd Length: 316 Bit Score: 442.62 E-value: 1.76e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 5 LDQLKQYTTVVADTGDFQQLAQYKPQDATTNPSLILKAVQKDAYKPILEKTVRDHRNES----TDFI--IDRLLIAFGTE 78
Cdd:PRK12346 4 LDGIKQFTTVVADSGDIESIRHYHPQDATTNPSLLLKAAGLPQYQHLIDDAIAWGKKQGgtqeQQVVaaCDKLAVNFGAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 79 ILKLIPGRVSTEVDARLSFDTQRSIDKGRELIKLYEAAGVGRERILIKLASTWEGIRAAEVLQKEGIKCNMTLLFSLVQA 158
Cdd:PRK12346 84 ILKSVPGRVSTEVDARLSFDREKSIEKARHLVDLYQQQGIDKSRILIKLASTWEGIRAAEELEKEGINCNLTLLFSFAQA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 159 AACAEAGAQLISPFVGRIYDWYKKQAGADWNEARDgganDPGVQSVRRIYTYYKTFGYKTEVMGASFRTTSQIIELAGCD 238
Cdd:PRK12346 164 RACAEAGVFLISPFVGRIYDWYQARKPMDPYVVEE----DPGVKSVRNIYDYYKQHRYETIVMGASFRRTEQILALAGCD 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501469305 239 LLTISPDLLQKLQESNDTVARKLSPDTlQDKPaERVAIDEASFRFQLNDEAMATEKLAEGIRVFAADAVKLEKLIDALR 317
Cdd:PRK12346 240 RLTISPNLLKELQESESPVERKLIPSS-QTFP-RPAPMSEAEFRWEHNQDAMAVEKLSEGIRLFAVDQRKLEDLLAAKL 316
|
|
| talAB |
TIGR00874 |
transaldolase; This family includes the majority of known and predicted transaldolase ... |
3-316 |
2.47e-156 |
|
transaldolase; This family includes the majority of known and predicted transaldolase sequences, including E. coli TalA and TalB. It excluded two other families. The first includes E. coli transaldolase-like protein TalC. The second family includes the putative transaldolases of Helicobacter pylori and Mycobacterium tuberculosis. [Energy metabolism, Pentose phosphate pathway]
Pssm-ID: 162081 Cd Length: 317 Bit Score: 439.58 E-value: 2.47e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 3 TALDQLKQYTTVVADTGDFQQLAQYKPQDATTNPSLILKAVQKDAYKPILEKTV---RDHRNESTD---FIIDRLLIAFG 76
Cdd:TIGR00874 1 NQLDQLKQFTVVVADTGDIEAIKKYQPQDATTNPSLILAAAQLPKYAELIDEAVawgKKQGKDDAQqveNALDKLAVNFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 77 TEILKLIPGRVSTEVDARLSFDTQRSIDKGRELIKLYEAAGVGRERILIKLASTWEGIRAAEVLQKEGIKCNMTLLFSLV 156
Cdd:TIGR00874 81 LEILKIVPGRVSTEVDARLSFDTEATVEKARHLIKLYEDAGVDKKRILIKIASTWEGIRAAEELEKEGIHCNLTLLFSFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 157 QAAACAEAGAQLISPFVGRIYDWYKKQAGADwneaRDGGANDPGVQSVRRIYTYYKTFGYKTEVMGASFRTTSQIIELAG 236
Cdd:TIGR00874 161 QAIACAEAKVTLISPFVGRILDWYKAATGKK----EYSIEEDPGVASVKKIYNYYKKHGYPTEVMGASFRNKEEILALAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 237 CDLLTISPDLLQKLQESNDTVARKLSPDTLQDKPAERVAIDEASFRFQLNDEAMATEKLAEGIRVFAADAVKLEKLIDAL 316
Cdd:TIGR00874 237 CDRLTISPALLDELKESTGPVERKLDPESAKKVDKQPIILDESEFRFLHNEDAMATEKLAEGIRKFAADQEKLEKLLEEK 316
|
|
| PTZ00411 |
PTZ00411 |
transaldolase-like protein; Provisional |
1-316 |
6.00e-153 |
|
transaldolase-like protein; Provisional
Pssm-ID: 240406 Cd Length: 333 Bit Score: 431.85 E-value: 6.00e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 1 MTTALDQLKQYTTVVADTGDFQQLAQYKPQDATTNPSLILKAVQKDAYKPILEKTVR----------------DHRNEST 64
Cdd:PTZ00411 1 MPNQLEALKEHTTVVADTGDFSLLKKFQPEDATTNPSLVLAAAQMPEYAHLIDDAIKyakanvsrlrdpllsdEEKEELV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 65 DFIIDRLLIAFGTEILKLIPGRVSTEVDARLSFDTQRSIDKGRELIKLYEAAGVGRERILIKLASTWEGIRAAEVLQKEG 144
Cdd:PTZ00411 81 ELVVDKLTVNFGVEILKIVPGRVSTEVDARLSFDKQAMVDKARKIIKMYEEAGISKDRILIKLASTWEGIQAAKALEKEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 145 IKCNMTLLFSLVQAAACAEAGAQLISPFVGRIYDWYKKQAGADWNEardgGANDPGVQSVRRIYTYYKTFGYKTEVMGAS 224
Cdd:PTZ00411 161 IHCNLTLLFSFAQAVACAQAGVTLISPFVGRILDWYKKPEKAESYV----GAQDPGVISVTKIYNYYKKHGYKTIVMGAS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 225 FRTTSQIIELAGCDLLTISPDLLQKLQESNDT-VARKLSPDTLQDKPAERVAIDEASFRFQLNDEAMATEKLAEGIRVFA 303
Cdd:PTZ00411 237 FRNTGEILELAGCDKLTISPKLLEELANTEDGpVERKLDPEKLTEDTEKLPELTEKEFRWELNEDAMATEKLAEGIRNFA 316
|
330
....*....|...
gi 501469305 304 ADAVKLEKLIDAL 316
Cdd:PTZ00411 317 KDLEKLENVIRAK 329
|
|
| PRK12309 |
PRK12309 |
transaldolase; |
1-313 |
2.94e-152 |
|
transaldolase;
Pssm-ID: 183426 [Multi-domain] Cd Length: 391 Bit Score: 432.24 E-value: 2.94e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 1 MTTALDQLKQYTTVVADTGDFQQLAQYKPQDATTNPSLILKAVQKDAYKPILEKTVRDHRNESTD---------FIIDRL 71
Cdd:PRK12309 2 MASLLEQLRQMTVVVADTGDIQAIEKFTPRDATTNPSLITAAAQMPQYQSIVDETLRQARKELGSdapvedvvaLAFDRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 72 LIAFGTEILKLIPGRVSTEVDARLSFDTQRSIDKGRELIKLYEAAGVGRERILIKLASTWEGIRAAEVLQKEGIKCNMTL 151
Cdd:PRK12309 82 AVAFGLKILKIVPGRVSTEVDARLSYDTEATIAKARKLISLYEDAGISRDRVLIKIASTWEGIKAAEVLEKEGIHCNLTL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 152 LFSLVQAAACAEAGAQLISPFVGRIYDWYKKQAGADWNEardgGANDPGVQSVRRIYTYYKTFGYKTEVMGASFRTTSQI 231
Cdd:PRK12309 162 LFGFHQAIACAEAGVTLISPFVGRILDWYKKETGRDSYP----GAEDPGVQSVTQIYNYYKKFGYKTEVMGASFRNIGEI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 232 IELAGCDLLTISPDLLQKLQESNDTVARKLSPDTLQDKPAERVAIDEASFRFQLNDEAMATEKLAEGIRVFAADAVKLEK 311
Cdd:PRK12309 238 IELAGCDLLTISPKLLEQLRSTEAELPRKLDPANAAGMEIEKIHMDRATFDKMHAEDRMASEKLDEGIKGFSKALETLEK 317
|
..
gi 501469305 312 LI 313
Cdd:PRK12309 318 LL 319
|
|
| TAL_FSA |
pfam00923 |
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ... |
14-313 |
5.46e-83 |
|
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose phosphate pathway (PPP) found almost ubiquitously in the three domains of life (Archaea, Bacteria, and Eukarya). TAL shares a high degree of structural similarity and sequence identity with fructose-6-phosphate aldolase (FSA). They both belong to the class I aldolase family. Their protein structures have been revealed.
Pssm-ID: 395737 [Multi-domain] Cd Length: 226 Bit Score: 250.15 E-value: 5.46e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 14 VVADTGDFQQLAQYKP----QDATTNPSLILKAVQ-KDAYKPILEktvrdhrnestdfiidrlliafgtEILKLIPGRVS 88
Cdd:pfam00923 1 IWLDTADRDLIKKLIEeggiDGVTTNPSIFLKAIEySALYDEAIA------------------------EIKEIGDGPVS 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 89 TEVDARLSFDTQRSIDKGRELIKLYEaagvgRERILIKLASTWEGIRAAEVLQKEGIKCNMTLLFSLVQAAACAEAGAQL 168
Cdd:pfam00923 57 LEVDPRLADDTEGTIEEARRLIALYG-----RPNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALAAAEAGASV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 169 ISPFVGRIYDWYKKQAGADWneardggANDPGVQSVRRIYTYYKTFGYKTEVMGASFRTTSQIIELAGCDLLTISPDLLQ 248
Cdd:pfam00923 132 ISPFVGRIDDWGDKRLGAAL-------RGDDGIANAKEIYQIYKKYGWSTGVLAASFRNVLYVLALAGCDTITIPPDTLE 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501469305 249 KLQEsndtvarklspdtlqdkpaervaideasfrfqlndeamateklAEGIRVFAADAVKLEKLI 313
Cdd:pfam00923 205 ALAK-------------------------------------------DEGVRKFAKDWEKLLGSI 226
|
|
| TalA |
COG0176 |
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ... |
12-309 |
1.43e-70 |
|
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; Transaldolase/fructose-6-phosphate aldolase is part of the Pathway/BioSystem: Pentose phosphate pathway
Pssm-ID: 439946 [Multi-domain] Cd Length: 214 Bit Score: 218.02 E-value: 1.43e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 12 TTVVADTGDFQQLAQYK----PQDATTNPSLILKAVQKDAykpilektvrdhrnestdfiidrllIAFGTEILKLIPGRV 87
Cdd:COG0176 1 MKLWLDTADREEIKELIdlggVDGVTTNPSLIAKAGIKDF-------------------------VEDIREICDIVDGPV 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 88 STEVdarLSFDTQRSIDKGRELIKLYeaagvgRERILIKLASTWEGIRAAEVLQKEGIKCNMTLLFSLVQAAACAEAGAQ 167
Cdd:COG0176 56 SAEV---LATDTEGMIAEARRLAALY------RPNVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQALLAAEAGAS 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 168 LISPFVGRIYDWykkqaGADwneardggandpGVQSVRRIYTYYKTFGYKTEVMGASFRTTSQIIE--LAGCDLLTISPD 245
Cdd:COG0176 127 YVSPFVGRIDDI-----GID------------GIALVREIYQIYKNYGARTRILAASFRNPLQVLEaaLAGADTVTIPPA 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501469305 246 LLQKLqesndtvarklspdtlqdkpaervaideasfrfqlndeaMATEKLAEGIRVFAADAVKL 309
Cdd:COG0176 190 VLEAL---------------------------------------ADHPLTDEGIEKFLADWEKL 214
|
|
| Transaldolase |
cd00439 |
Transaldolase; Transaldolase. Enzymes found in the non-oxidative branch of the pentose ... |
13-250 |
1.44e-59 |
|
Transaldolase; Transaldolase. Enzymes found in the non-oxidative branch of the pentose phosphate pathway, that catalyze the reversible transfer of a dihydroxyacetone group from fructose-6-phosphate to erythrose-4-phosphate yielding sedoheptulose-7-phosphate and glyceraldehyde-3-phosphate. They are members of the class I aldolases, who are characterized by using a Schiff-base mechanism for stabilization of the reaction intermediates.
Pssm-ID: 188631 [Multi-domain] Cd Length: 252 Bit Score: 191.41 E-value: 1.44e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 13 TVVADTGDFQQLAQYK----PQDATTNPSLILKAVQKDAYKPILEKTVRDHRNESTD------FIIDRLLIAFGTEILKL 82
Cdd:cd00439 1 SPWYDTLDRPATDLLPlirgVRGVTTNPSIIQAAISTSNAYNDQFRTLVESGKDIESaywelvVKDIQDACKLFEPIYDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 83 I--PGRVSTEVDARLSFDTQRSIDKGRELIKLYEaagvgRERILIKLASTWEGIRAAEVLQKEGIKCNMTLLFSLVQAAA 160
Cdd:cd00439 81 TeaDGRVSVEVSARLADDTQGMVEAAKYLSKVVN-----RRNIYIKIPATAEGIPAIKDLIAAGISVNVTLIFSIAQYEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 161 CAEAGAQLISPFVGRIYDWYKKQAGADWNEARDgganDPGVQSVRRIYTYYKTFGYKTEVMGASFRTTSQIIELAGCDLL 240
Cdd:cd00439 156 VADAGTSVASPFVSRIDTLMDKMLEQIGLDLRG----KAGVAQVTLAYKLYKQKFKKQRVLWASFSDTLYVAPLIGCDTV 231
|
250
....*....|
gi 501469305 241 TISPDLLQKL 250
Cdd:cd00439 232 TTMPDQALEA 241
|
|
| Transaldolase_FSA |
cd00956 |
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ... |
33-250 |
8.84e-30 |
|
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea, which are member of the MipB/TalC subfamily of class I aldolases. FSA catalyze an aldol cleavage of fructose 6-phosphate and do not utilize fructose, fructose 1-phosphate, fructose 1,6-phosphate, or dihydroxyacetone phosphate. The enzymes belong to the transaldolase family that serves in transfer reactions in the pentose phosphate cycle, and are more distantly related to fructose 1,6-bisphosphate aldolase.
Pssm-ID: 188643 [Multi-domain] Cd Length: 211 Bit Score: 112.67 E-value: 8.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 33 TTNPSLILKAVQKDAYkpilektvrdhrnestdfiidrlliAFGTEILKLIPGRVSTEVDARlsfDTQRSIDKGRELIKL 112
Cdd:cd00956 25 TTNPSLIAKSGRIDFE-------------------------AVLKEICEIIDGPVSAQVVST---DAEGMVAEARKLASL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 113 YEaagvgreRILIKLASTWEGIRAAEVLQKEGIKCNMTLLFSLVQAAACAEAGAQLISPFVGRIYDwykkqagadwnEAR 192
Cdd:cd00956 77 GG-------NVVVKIPVTEDGLKAIKKLSEEGIKTNVTAIFSAAQALLAAKAGATYVSPFVGRIDD-----------LGG 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 193 DggandpGVQSVRRIYTYYKTFGYKTEVMGASFRTTSQIIE--LAGCDLLTISPDLLQKL 250
Cdd:cd00956 139 D------GMELIREIRTIFDNYGFDTKILAASIRNPQHVIEaaLAGADAITLPPDVLEQL 192
|
|
| fsa_talC_mipB |
TIGR00875 |
fructose-6-phosphate aldolase, TalC/MipB family; This model represents a family that includes ... |
16-250 |
1.46e-23 |
|
fructose-6-phosphate aldolase, TalC/MipB family; This model represents a family that includes the E. coli transaldolase homologs TalC and MipB, both shown to be fructose-6-phosphate aldolases rather than transaldolases as previously thought. It is related to but distinct from the transaldolase family of E. coli TalA and TalB. The member from Bacillus subtilis becomes phosphorylated during early stationary phase but not during exponential growth. [Energy metabolism, Pentose phosphate pathway]
Pssm-ID: 129953 [Multi-domain] Cd Length: 213 Bit Score: 96.08 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 16 ADTGDFQQLAQYKPQDA-TTNPSLILKavQKDAYKPILEktvrdhrnestdfiidrlliafgtEILKLIPGRVSTEVdar 94
Cdd:TIGR00875 8 ANVEEIKKAAELGILAGvTTNPSLIAK--EGRSFWEVLK------------------------EIQEAVEGPVSAET--- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 95 LSFDTQRSIDKGRELIKLYEAagvgrerILIKLASTWEGIRAAEVLQKEGIKCNMTLLFSLVQAAACAEAGAQLISPFVG 174
Cdd:TIGR00875 59 ISLDAEGMVEEAKELAKLAPN-------IVVKIPMTSEGLKAVKILKKEGIKTNVTLVFSAAQALLAAKAGATYVSPFVG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501469305 175 RIYDwykkqAGADwneardggandpGVQSVRRIYTYYKTFGYKTEVMGASFRTTSQIIE--LAGCDLLTISPDLLQKL 250
Cdd:TIGR00875 132 RLDD-----IGGD------------GMKLIEEVKTIFENHAPDTEVIAASVRHPRHVLEaaLIGADIATMPLDVMQQL 192
|
|
| Transaldolase_like |
cd00955 |
Transaldolase-like proteins from plants and bacteria; Transaldolase-like proteins from plants ... |
32-157 |
1.35e-14 |
|
Transaldolase-like proteins from plants and bacteria; Transaldolase-like proteins from plants and bacteria. Transaldolase is found in the non-oxidative branch of the pentose phosphate pathway, that catalyze the reversible transfer of a dihydroxyacetone group from fructose-6-phosphate to erythrose-4-phosphate yielding sedoheptulose-7-phosphate and glyceraldehyde-3-phosphate. They are members of the class I aldolases, who are characterized by using a Schiff-base mechanism for stabilization of the reaction intermediates.
Pssm-ID: 188642 [Multi-domain] Cd Length: 338 Bit Score: 73.13 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 32 ATTNPSLILKAVQKDA-YKPILEKTVRdhRNESTDFIIDRLLIAfgtEIL----KLIP---------GRVSTEVDARLSF 97
Cdd:cd00955 29 VTSNPAIFEKAIAGSAaYDDQIRALKG--QGLDAEAIYEALAIE---DIQdacdLLAPvyeqtggndGYVSLEVSPRLAD 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 98 DTQRSIDKGRELIKLyeaagVGRERILIKLASTWEGIRAAEVLQKEGIKCNMTLLFSLVQ 157
Cdd:cd00955 104 DTQGTIAEAKRLWKA-----VGRPNLMIKIPATEAGLPAIEELIAAGISVNVTLIFSLEQ 158
|
|
| PRK03343 |
PRK03343 |
transaldolase; Validated |
33-155 |
7.73e-13 |
|
transaldolase; Validated
Pssm-ID: 235117 Cd Length: 368 Bit Score: 68.31 E-value: 7.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 33 TTNPSLILKAV-QKDAYKPILEKTVRdhRNESTDFIIDRLLIA---FGTEILKLI-------PGRVSTEVDARLSFDTQR 101
Cdd:PRK03343 43 TSNPAIFQKAIaGGDAYDAQIAELAA--AGADVEEAYEELTTAdvrNACDVLRPVyeatggvDGRVSIEVSPRLAHDTEA 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 501469305 102 SIDKGRELIKLyeaagVGRERILIKLASTWEGIRAAEVLQKEGIKCNMTLLFSL 155
Cdd:PRK03343 121 TIAEARRLWAA-----VDRPNLMIKIPATPEGLPAIEALIAEGISVNVTLIFSV 169
|
|
| PRK09533 |
PRK09533 |
bifunctional transaldolase/phosoglucose isomerase; Validated |
18-155 |
3.69e-10 |
|
bifunctional transaldolase/phosoglucose isomerase; Validated
Pssm-ID: 236551 [Multi-domain] Cd Length: 948 Bit Score: 60.75 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 18 TGDFQQLAQykpQDA----TTNPSLILKAV-QKDAYKPILEKTVRDHRNESTDfIIDRLLIA---FGTEILKLI------ 83
Cdd:PRK09533 26 KGELKRLVE---EDGlrgvTSNPAIFEKAIgSSDEYDDAIKAALAEGDRSVIE-LYETLAIEdiqAAADVLRPVydatdg 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501469305 84 -PGRVSTEVDARLSFDTQRSIDKGRELIKlyeaaGVGRERILIKLASTWEGIRAAEVLQKEGIKCNMTLLFSL 155
Cdd:PRK09533 102 aDGFVSLEVSPYLALDTEGTIAEARRLWA-----AVDRPNLMIKVPATPEGLPAIRQLIAEGINVNVTLLFSQ 169
|
|
| PRK03903 |
PRK03903 |
transaldolase; Provisional |
85-157 |
9.48e-10 |
|
transaldolase; Provisional
Pssm-ID: 235171 Cd Length: 274 Bit Score: 58.45 E-value: 9.48e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501469305 85 GRVSTEVDARLSFDTQRSIDKGrelIKLYEAagVGRERILIKLASTWEGIRAAEVLQKEGIKCNMTLLFSLVQ 157
Cdd:PRK03903 43 GFISIEIDPFLEDDAAGSIEEG---KRLYKT--IGRPNVMIKVPATKAGYEAMSALMKKGISVNATLIFSPEQ 110
|
|
| PRK12653 |
PRK12653 |
fructose-6-phosphate aldolase; Reviewed |
16-250 |
7.86e-06 |
|
fructose-6-phosphate aldolase; Reviewed
Pssm-ID: 183653 [Multi-domain] Cd Length: 220 Bit Score: 46.31 E-value: 7.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 16 ADTGDFQQLAQYKP-QDATTNPSLILKAVQKdaykpiLEKTvrdhrnestdfiIDRLLIAFGTEilklipGRVSTEVDAR 94
Cdd:PRK12653 8 SDVVAVKALSRIFPlAGVTTNPSIIAAGKKP------LEVV------------LPQLHEAMGGQ------GRLFAQVMAT 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501469305 95 LSFDTQRSIDKGRELIKlyeaagvgreRILIKLASTWEGIRAAEVLQKEGIKCNMTLLFSLVQAAACAEAGAQLISPFVG 174
Cdd:PRK12653 64 TAEGMVNDARKLRSIIA----------DIVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGAEYVAPYVN 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501469305 175 RIydwykkqagadwnEARDGGandpGVQSVRRIYTYYKTFGYKTEVMGASFRTTSQIIE--LAGCDLLTISPDLLQKL 250
Cdd:PRK12653 134 RI-------------DAQGGS----GIQTVTDLQQLLKMHAPQAKVLAASFKTPRQALDclLAGCESITLPLDVAQQM 194
|
|
| |
