|
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: 670.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 1 MTDKLTSLRQYTTVVADTGDIAAMKLYQPQDATTNPSLILGAAQIPEYRKLIDDAVAWARSQSSDRAQQILDASDKLAVN 80
Cdd:PRK05269 1 MTNKLEQLKQFTTVVADTGDIEAIKKYQPQDATTNPSLILKAAQIPEYAPLIDDAVAWAKQQSGDRAQQIDDAIDKLAVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 81 IGLEILKLIPGRISTEVDARLSYDTEASIAKAKRIIKLYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFS 160
Cdd:PRK05269 81 FGLEILKLIPGRVSTEVDARLSFDTEATIAKARKLIALYEEAGISKDRILIKIASTWEGIRAAEQLEKEGINCNLTLLFS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 161 FAQARACAEAGVFLISPFVGRILDWYKANTDKKEYAPAEDPGVVSVSEIYEYYKQHGYETVVMGASFRNVGEILELAGCD 240
Cdd:PRK05269 161 FAQARACAEAGVFLISPFVGRILDWYKKNTGKKEYAPAEDPGVVSVTKIYNYYKKHGYKTVVMGASFRNTGQILELAGCD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2099470914 241 RLTIAPALLKELSESEGAVERKLVYTGEVKARPERITESEFLWQHNQDPMAVDKLAEGIRKFAIDQEKLEKMIGELL 317
Cdd:PRK05269 241 RLTISPALLEELAASEGELERKLSPPGEAKARPVPLTEAEFRWQHNEDAMATEKLAEGIRKFAKDQEKLEKLIAAKL 317
|
|
| talAB |
TIGR00874 |
transaldolase; This family includes the majority of known and predicted transaldolase ... |
3-317 |
0e+00 |
|
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: 579.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 3 DKLTSLRQYTTVVADTGDIAAMKLYQPQDATTNPSLILGAAQIPEYRKLIDDAVAWARSQSSDRAQQILDASDKLAVNIG 82
Cdd:TIGR00874 1 NQLDQLKQFTVVVADTGDIEAIKKYQPQDATTNPSLILAAAQLPKYAELIDEAVAWGKKQGKDDAQQVENALDKLAVNFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 83 LEILKLIPGRISTEVDARLSYDTEASIAKAKRIIKLYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFA 162
Cdd:TIGR00874 81 LEILKIVPGRVSTEVDARLSFDTEATVEKARHLIKLYEDAGVDKKRILIKIASTWEGIRAAEELEKEGIHCNLTLLFSFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 163 QARACAEAGVFLISPFVGRILDWYKANTDKKEYAPAEDPGVVSVSEIYEYYKQHGYETVVMGASFRNVGEILELAGCDRL 242
Cdd:TIGR00874 161 QAIACAEAKVTLISPFVGRILDWYKAATGKKEYSIEEDPGVASVKKIYNYYKKHGYPTEVMGASFRNKEEILALAGCDRL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2099470914 243 TIAPALLKELSESEGAVERKLVYTGE--VKARPERITESEFLWQHNQDPMAVDKLAEGIRKFAIDQEKLEKMIGELL 317
Cdd:TIGR00874 241 TISPALLDELKESTGPVERKLDPESAkkVDKQPIILDESEFRFLHNEDAMATEKLAEGIRKFAADQEKLEKLLEEKL 317
|
|
| Transaldolase_TalAB |
cd00957 |
Transaldolases including both TalA and TalB; Transaldolases including both TalA and TalB. The ... |
4-313 |
0e+00 |
|
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: 542.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 4 KLTSLRQYTTVVADTGDIAAMKLYQPQDATTNPSLILGAAQIPEYRKLIDDAVAWARSQSSDRAQQILDASDKLAVNIGL 83
Cdd:cd00957 2 QLDQLKKFTTIVADTGDFEAIKKFKPQDATTNPSLILAAAKLPEYNKLVDEAIAYAKKKGGSDEDQISNALDKLLVNFGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 84 EILKLIPGRISTEVDARLSYDTEASIAKAKRIIKLYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQ 163
Cdd:cd00957 82 EILKLIPGRVSTEVDARLSFDTNATIAKARKLIKLYEEAGIDKERILIKIAATWEGIQAAKQLEKEGIHCNLTLLFSFAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 164 ARACAEAGVFLISPFVGRILDWYKANTDKKEYAPAEDPGVVSVSEIYEYYKQHGYETVVMGASFRNVGEILELAGCDRLT 243
Cdd:cd00957 162 AVACAEAGVTLISPFVGRILDWYKKHSGDKAYTAEEDPGVASVKKIYNYYKKFGYKTKVMGASFRNIGQILALAGCDYLT 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2099470914 244 IAPALLKELSESEGAVERKLVY--TGEVKARPERITESEFLWQHNQDPMAVDKLAEGIRKFAIDQEKLEKMI 313
Cdd:cd00957 242 ISPALLEELKNSTAKVERKLDPaaSKALDIHPNFLDESAFRWALNEDAMAVEKLSEGIRGFAKDAVKLEKLI 313
|
|
| TAL_FSA |
pfam00923 |
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ... |
14-313 |
5.14e-96 |
|
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: 283.27 E-value: 5.14e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 14 VVADTGDIAAMKLYQP----QDATTNPSLILGAAqipEYRKLIDDAVAwarsqssdraqqildasdklavniglEILKLI 89
Cdd:pfam00923 1 IWLDTADRDLIKKLIEeggiDGVTTNPSIFLKAI---EYSALYDEAIA--------------------------EIKEIG 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 90 PGRISTEVDARLSYDTEASIAKAKRIIKLYNDagisnDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAE 169
Cdd:pfam00923 52 DGPVSLEVDPRLADDTEGTIEEARRLIALYGR-----PNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALAAAE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 170 AGVFLISPFVGRILDWYKANTDKkeyAPAEDPGVVSVSEIYEYYKQHGYETVVMGASFRNVGEILELAGCDRLTIAPALL 249
Cdd:pfam00923 127 AGASVISPFVGRIDDWGDKRLGA---ALRGDDGIANAKEIYQIYKKYGWSTGVLAASFRNVLYVLALAGCDTITIPPDTL 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2099470914 250 KELSEsegaverklvytgevkarperiteseflwqhnqdpmavdklAEGIRKFAIDQEKLEKMI 313
Cdd:pfam00923 204 EALAK-----------------------------------------DEGVRKFAKDWEKLLGSI 226
|
|
| TalA |
COG0176 |
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ... |
12-309 |
1.88e-77 |
|
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: 235.35 E-value: 1.88e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 12 TTVVADTGDIAAMK----LYQPQDATTNPSLILGAAqipeyrkliddavawarsqssdraqqildasDKLAVNIGLEILK 87
Cdd:COG0176 1 MKLWLDTADREEIKelidLGGVDGVTTNPSLIAKAG-------------------------------IKDFVEDIREICD 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 88 LIPGRISTEVdarLSYDTEASIAKAKRIIKLYndagisNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARAC 167
Cdd:COG0176 50 IVDGPVSAEV---LATDTEGMIAEARRLAALY------RPNVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQALLA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 168 AEAGVFLISPFVGRILDWykantdkkeyapAEDpGVVSVSEIYEYYKQHGYETVVMGASFRNVGEILE--LAGCDRLTIA 245
Cdd:COG0176 121 AEAGASYVSPFVGRIDDI------------GID-GIALVREIYQIYKNYGARTRILAASFRNPLQVLEaaLAGADTVTIP 187
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2099470914 246 PALLKELSESegaverklvytgevkarperiteseflwqhnqdpmavDKLAEGIRKFAIDQEKL 309
Cdd:COG0176 188 PAVLEALADH-------------------------------------PLTDEGIEKFLADWEKL 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: 670.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 1 MTDKLTSLRQYTTVVADTGDIAAMKLYQPQDATTNPSLILGAAQIPEYRKLIDDAVAWARSQSSDRAQQILDASDKLAVN 80
Cdd:PRK05269 1 MTNKLEQLKQFTTVVADTGDIEAIKKYQPQDATTNPSLILKAAQIPEYAPLIDDAVAWAKQQSGDRAQQIDDAIDKLAVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 81 IGLEILKLIPGRISTEVDARLSYDTEASIAKAKRIIKLYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFS 160
Cdd:PRK05269 81 FGLEILKLIPGRVSTEVDARLSFDTEATIAKARKLIALYEEAGISKDRILIKIASTWEGIRAAEQLEKEGINCNLTLLFS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 161 FAQARACAEAGVFLISPFVGRILDWYKANTDKKEYAPAEDPGVVSVSEIYEYYKQHGYETVVMGASFRNVGEILELAGCD 240
Cdd:PRK05269 161 FAQARACAEAGVFLISPFVGRILDWYKKNTGKKEYAPAEDPGVVSVTKIYNYYKKHGYKTVVMGASFRNTGQILELAGCD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2099470914 241 RLTIAPALLKELSESEGAVERKLVYTGEVKARPERITESEFLWQHNQDPMAVDKLAEGIRKFAIDQEKLEKMIGELL 317
Cdd:PRK05269 241 RLTISPALLEELAASEGELERKLSPPGEAKARPVPLTEAEFRWQHNEDAMATEKLAEGIRKFAKDQEKLEKLIAAKL 317
|
|
| talAB |
TIGR00874 |
transaldolase; This family includes the majority of known and predicted transaldolase ... |
3-317 |
0e+00 |
|
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: 579.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 3 DKLTSLRQYTTVVADTGDIAAMKLYQPQDATTNPSLILGAAQIPEYRKLIDDAVAWARSQSSDRAQQILDASDKLAVNIG 82
Cdd:TIGR00874 1 NQLDQLKQFTVVVADTGDIEAIKKYQPQDATTNPSLILAAAQLPKYAELIDEAVAWGKKQGKDDAQQVENALDKLAVNFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 83 LEILKLIPGRISTEVDARLSYDTEASIAKAKRIIKLYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFA 162
Cdd:TIGR00874 81 LEILKIVPGRVSTEVDARLSFDTEATVEKARHLIKLYEDAGVDKKRILIKIASTWEGIRAAEELEKEGIHCNLTLLFSFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 163 QARACAEAGVFLISPFVGRILDWYKANTDKKEYAPAEDPGVVSVSEIYEYYKQHGYETVVMGASFRNVGEILELAGCDRL 242
Cdd:TIGR00874 161 QAIACAEAKVTLISPFVGRILDWYKAATGKKEYSIEEDPGVASVKKIYNYYKKHGYPTEVMGASFRNKEEILALAGCDRL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2099470914 243 TIAPALLKELSESEGAVERKLVYTGE--VKARPERITESEFLWQHNQDPMAVDKLAEGIRKFAIDQEKLEKMIGELL 317
Cdd:TIGR00874 241 TISPALLDELKESTGPVERKLDPESAkkVDKQPIILDESEFRFLHNEDAMATEKLAEGIRKFAADQEKLEKLLEEKL 317
|
|
| PRK12346 |
PRK12346 |
transaldolase A; Provisional |
2-317 |
0e+00 |
|
transaldolase A; Provisional
Pssm-ID: 183458 Cd Length: 316 Bit Score: 565.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 2 TDKLTSLRQYTTVVADTGDIAAMKLYQPQDATTNPSLILGAAQIPEYRKLIDDAVAWARSQSSDRAQQILDASDKLAVNI 81
Cdd:PRK12346 1 MNQLDGIKQFTTVVADSGDIESIRHYHPQDATTNPSLLLKAAGLPQYQHLIDDAIAWGKKQGGTQEQQVVAACDKLAVNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 82 GLEILKLIPGRISTEVDARLSYDTEASIAKAKRIIKLYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSF 161
Cdd:PRK12346 81 GAEILKSVPGRVSTEVDARLSFDREKSIEKARHLVDLYQQQGIDKSRILIKLASTWEGIRAAEELEKEGINCNLTLLFSF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 162 AQARACAEAGVFLISPFVGRILDWYKANTDKKEYAPAEDPGVVSVSEIYEYYKQHGYETVVMGASFRNVGEILELAGCDR 241
Cdd:PRK12346 161 AQARACAEAGVFLISPFVGRIYDWYQARKPMDPYVVEEDPGVKSVRNIYDYYKQHRYETIVMGASFRRTEQILALAGCDR 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2099470914 242 LTIAPALLKELSESEGAVERKLVYTGEVKARPERITESEFLWQHNQDPMAVDKLAEGIRKFAIDQEKLEKMIGELL 317
Cdd:PRK12346 241 LTISPNLLKELQESESPVERKLIPSSQTFPRPAPMSEAEFRWEHNQDAMAVEKLSEGIRLFAVDQRKLEDLLAAKL 316
|
|
| Transaldolase_TalAB |
cd00957 |
Transaldolases including both TalA and TalB; Transaldolases including both TalA and TalB. The ... |
4-313 |
0e+00 |
|
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: 542.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 4 KLTSLRQYTTVVADTGDIAAMKLYQPQDATTNPSLILGAAQIPEYRKLIDDAVAWARSQSSDRAQQILDASDKLAVNIGL 83
Cdd:cd00957 2 QLDQLKKFTTIVADTGDFEAIKKFKPQDATTNPSLILAAAKLPEYNKLVDEAIAYAKKKGGSDEDQISNALDKLLVNFGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 84 EILKLIPGRISTEVDARLSYDTEASIAKAKRIIKLYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQ 163
Cdd:cd00957 82 EILKLIPGRVSTEVDARLSFDTNATIAKARKLIKLYEEAGIDKERILIKIAATWEGIQAAKQLEKEGIHCNLTLLFSFAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 164 ARACAEAGVFLISPFVGRILDWYKANTDKKEYAPAEDPGVVSVSEIYEYYKQHGYETVVMGASFRNVGEILELAGCDRLT 243
Cdd:cd00957 162 AVACAEAGVTLISPFVGRILDWYKKHSGDKAYTAEEDPGVASVKKIYNYYKKFGYKTKVMGASFRNIGQILALAGCDYLT 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2099470914 244 IAPALLKELSESEGAVERKLVY--TGEVKARPERITESEFLWQHNQDPMAVDKLAEGIRKFAIDQEKLEKMI 313
Cdd:cd00957 242 ISPALLEELKNSTAKVERKLDPaaSKALDIHPNFLDESAFRWALNEDAMAVEKLSEGIRGFAKDAVKLEKLI 313
|
|
| PTZ00411 |
PTZ00411 |
transaldolase-like protein; Provisional |
1-317 |
3.02e-179 |
|
transaldolase-like protein; Provisional
Pssm-ID: 240406 Cd Length: 333 Bit Score: 498.11 E-value: 3.02e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 1 MTDKLTSLRQYTTVVADTGDIAAMKLYQPQDATTNPSLILGAAQIPEYRKLIDDAVAWARSQSSDRAQQILD-------- 72
Cdd:PTZ00411 1 MPNQLEALKEHTTVVADTGDFSLLKKFQPEDATTNPSLVLAAAQMPEYAHLIDDAIKYAKANVSRLRDPLLSdeekeelv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 73 --ASDKLAVNIGLEILKLIPGRISTEVDARLSYDTEASIAKAKRIIKLYNDAGISNDRILIKLASTWQGIRAAEQLEKEG 150
Cdd:PTZ00411 81 elVVDKLTVNFGVEILKIVPGRVSTEVDARLSFDKQAMVDKARKIIKMYEEAGISKDRILIKLASTWEGIQAAKALEKEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 151 INCNLTLLFSFAQARACAEAGVFLISPFVGRILDWYKANTDKKEYAPAEDPGVVSVSEIYEYYKQHGYETVVMGASFRNV 230
Cdd:PTZ00411 161 IHCNLTLLFSFAQAVACAQAGVTLISPFVGRILDWYKKPEKAESYVGAQDPGVISVTKIYNYYKKHGYKTIVMGASFRNT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 231 GEILELAGCDRLTIAPALLKELSESEGA-VERKLVYTGEVKARPERI--TESEFLWQHNQDPMAVDKLAEGIRKFAIDQE 307
Cdd:PTZ00411 241 GEILELAGCDKLTISPKLLEELANTEDGpVERKLDPEKLTEDTEKLPelTEKEFRWELNEDAMATEKLAEGIRNFAKDLE 320
|
330
....*....|
gi 2099470914 308 KLEKMIGELL 317
Cdd:PTZ00411 321 KLENVIRAKL 330
|
|
| PRK12309 |
PRK12309 |
transaldolase; |
1-317 |
2.50e-168 |
|
transaldolase;
Pssm-ID: 183426 [Multi-domain] Cd Length: 391 Bit Score: 473.07 E-value: 2.50e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 1 MTDKLTSLRQYTTVVADTGDIAAMKLYQPQDATTNPSLILGAAQIPEYRKLIDDAVAWARSQSSDRA---QQILDASDKL 77
Cdd:PRK12309 2 MASLLEQLRQMTVVVADTGDIQAIEKFTPRDATTNPSLITAAAQMPQYQSIVDETLRQARKELGSDApveDVVALAFDRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 78 AVNIGLEILKLIPGRISTEVDARLSYDTEASIAKAKRIIKLYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTL 157
Cdd:PRK12309 82 AVAFGLKILKIVPGRVSTEVDARLSYDTEATIAKARKLISLYEDAGISRDRVLIKIASTWEGIKAAEVLEKEGIHCNLTL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 158 LFSFAQARACAEAGVFLISPFVGRILDWYKANTDKKEYAPAEDPGVVSVSEIYEYYKQHGYETVVMGASFRNVGEILELA 237
Cdd:PRK12309 162 LFGFHQAIACAEAGVTLISPFVGRILDWYKKETGRDSYPGAEDPGVQSVTQIYNYYKKFGYKTEVMGASFRNIGEIIELA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 238 GCDRLTIAPALLKELSESEGAVERKLVYTGEVKARPERIT--ESEFLWQHNQDPMAVDKLAEGIRKFAIDQEKLEKMIGE 315
Cdd:PRK12309 242 GCDLLTISPKLLEQLRSTEAELPRKLDPANAAGMEIEKIHmdRATFDKMHAEDRMASEKLDEGIKGFSKALETLEKLLAH 321
|
..
gi 2099470914 316 LL 317
Cdd:PRK12309 322 RL 323
|
|
| TAL_FSA |
pfam00923 |
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ... |
14-313 |
5.14e-96 |
|
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: 283.27 E-value: 5.14e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 14 VVADTGDIAAMKLYQP----QDATTNPSLILGAAqipEYRKLIDDAVAwarsqssdraqqildasdklavniglEILKLI 89
Cdd:pfam00923 1 IWLDTADRDLIKKLIEeggiDGVTTNPSIFLKAI---EYSALYDEAIA--------------------------EIKEIG 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 90 PGRISTEVDARLSYDTEASIAKAKRIIKLYNDagisnDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAE 169
Cdd:pfam00923 52 DGPVSLEVDPRLADDTEGTIEEARRLIALYGR-----PNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALAAAE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 170 AGVFLISPFVGRILDWYKANTDKkeyAPAEDPGVVSVSEIYEYYKQHGYETVVMGASFRNVGEILELAGCDRLTIAPALL 249
Cdd:pfam00923 127 AGASVISPFVGRIDDWGDKRLGA---ALRGDDGIANAKEIYQIYKKYGWSTGVLAASFRNVLYVLALAGCDTITIPPDTL 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2099470914 250 KELSEsegaverklvytgevkarperiteseflwqhnqdpmavdklAEGIRKFAIDQEKLEKMI 313
Cdd:pfam00923 204 EALAK-----------------------------------------DEGVRKFAKDWEKLLGSI 226
|
|
| Transaldolase |
cd00439 |
Transaldolase; Transaldolase. Enzymes found in the non-oxidative branch of the pentose ... |
13-252 |
3.40e-78 |
|
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: 238.79 E-value: 3.40e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 13 TVVADTGDIAAMKLYQ----PQDATTNPSLILGAAQIPEYRKLIDDAVAWARSQSSDRAQQILDASDKLAVNIGLEILKL 88
Cdd:cd00439 1 SPWYDTLDRPATDLLPlirgVRGVTTNPSIIQAAISTSNAYNDQFRTLVESGKDIESAYWELVVKDIQDACKLFEPIYDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 89 I--PGRISTEVDARLSYDTEASIAKAKRIIKLYNDagisnDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARA 166
Cdd:cd00439 81 TeaDGRVSVEVSARLADDTQGMVEAAKYLSKVVNR-----RNIYIKIPATAEGIPAIKDLIAAGISVNVTLIFSIAQYEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 167 CAEAGVFLISPFVGRILDWYKANTDKKEYAPAEDPGVVSVSEIYEYYKQHGYETVVMGASFRNVGEILELAGCDRLTIAP 246
Cdd:cd00439 156 VADAGTSVASPFVSRIDTLMDKMLEQIGLDLRGKAGVAQVTLAYKLYKQKFKKQRVLWASFSDTLYVAPLIGCDTVTTMP 235
|
....*.
gi 2099470914 247 ALLKEL 252
Cdd:cd00439 236 DQALEA 241
|
|
| TalA |
COG0176 |
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ... |
12-309 |
1.88e-77 |
|
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: 235.35 E-value: 1.88e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 12 TTVVADTGDIAAMK----LYQPQDATTNPSLILGAAqipeyrkliddavawarsqssdraqqildasDKLAVNIGLEILK 87
Cdd:COG0176 1 MKLWLDTADREEIKelidLGGVDGVTTNPSLIAKAG-------------------------------IKDFVEDIREICD 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 88 LIPGRISTEVdarLSYDTEASIAKAKRIIKLYndagisNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARAC 167
Cdd:COG0176 50 IVDGPVSAEV---LATDTEGMIAEARRLAALY------RPNVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQALLA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 168 AEAGVFLISPFVGRILDWykantdkkeyapAEDpGVVSVSEIYEYYKQHGYETVVMGASFRNVGEILE--LAGCDRLTIA 245
Cdd:COG0176 121 AEAGASYVSPFVGRIDDI------------GID-GIALVREIYQIYKNYGARTRILAASFRNPLQVLEaaLAGADTVTIP 187
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2099470914 246 PALLKELSESegaverklvytgevkarperiteseflwqhnqdpmavDKLAEGIRKFAIDQEKL 309
Cdd:COG0176 188 PAVLEALADH-------------------------------------PLTDEGIEKFLADWEKL 214
|
|
| Transaldolase_FSA |
cd00956 |
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ... |
17-252 |
4.38e-33 |
|
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: 121.14 E-value: 4.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 17 DTGDIAAMKLYQPQ----DATTNPSLIlgaaqipeyrkliddavawARSQSSDRAQQILdasdklavniglEILKLIPGR 92
Cdd:cd00956 5 DTADLEEIKKASETglldGVTTNPSLI-------------------AKSGRIDFEAVLK------------EICEIIDGP 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 93 ISTEVDARlsyDTEASIAKAKRIIKLyndagisNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAEAGV 172
Cdd:cd00956 54 VSAQVVST---DAEGMVAEARKLASL-------GGNVVVKIPVTEDGLKAIKKLSEEGIKTNVTAIFSAAQALLAAKAGA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 173 FLISPFVGRIldwykANTdkkeyapAEDPGVVsVSEIYEYYKQHGYETVVMGASFRNVGEILE--LAGCDRLTIAPALLK 250
Cdd:cd00956 124 TYVSPFVGRI-----DDL-------GGDGMEL-IREIRTIFDNYGFDTKILAASIRNPQHVIEaaLAGADAITLPPDVLE 190
|
..
gi 2099470914 251 EL 252
Cdd:cd00956 191 QL 192
|
|
| fsa_talC_mipB |
TIGR00875 |
fructose-6-phosphate aldolase, TalC/MipB family; This model represents a family that includes ... |
84-252 |
3.09e-21 |
|
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: 89.92 E-value: 3.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 84 EILKLIPGRISTEVdarLSYDTEASIAKAKRIIKLyndagisNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQ 163
Cdd:TIGR00875 45 EIQEAVEGPVSAET---ISLDAEGMVEEAKELAKL-------APNIVVKIPMTSEGLKAVKILKKEGIKTNVTLVFSAAQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 164 ARACAEAGVFLISPFVGRILDwykantdkkeyapAEDPGVVSVSEIYEYYKQHGYETVVMGASFRNVGEILE--LAGCDR 241
Cdd:TIGR00875 115 ALLAAKAGATYVSPFVGRLDD-------------IGGDGMKLIEEVKTIFENHAPDTEVIAASVRHPRHVLEaaLIGADI 181
|
170
....*....|.
gi 2099470914 242 LTIAPALLKEL 252
Cdd:TIGR00875 182 ATMPLDVMQQL 192
|
|
| Transaldolase_like |
cd00955 |
Transaldolase-like proteins from plants and bacteria; Transaldolase-like proteins from plants ... |
32-216 |
1.37e-19 |
|
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: 87.76 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 32 ATTNPSLILGA-AQIPEYRKLIDDAVAwaRSQSSDRA------QQILDASDKLAVNigLEILKLIPGRISTEVDARLSYD 104
Cdd:cd00955 29 VTSNPAIFEKAiAGSAAYDDQIRALKG--QGLDAEAIyealaiEDIQDACDLLAPV--YEQTGGNDGYVSLEVSPRLADD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 105 TEASIAKAKRiikLYNDAGISNdrILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAEAgvFL---------- 174
Cdd:cd00955 105 TQGTIAEAKR---LWKAVGRPN--LMIKIPATEAGLPAIEELIAAGISVNVTLIFSLEQYEAVAEA--YLrglerrvegg 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2099470914 175 ---------ISPFVGRIldwyKANTDKKEYAPAEDP-----GVVSVSEIYEYYKQH 216
Cdd:cd00955 178 gdlsqvasvASFFVSRV----DTLIDKKLDAPEAKAlqgkvAIANAKLAYQEYQEK 229
|
|
| PRK03903 |
PRK03903 |
transaldolase; Provisional |
91-182 |
2.31e-15 |
|
transaldolase; Provisional
Pssm-ID: 235171 Cd Length: 274 Bit Score: 74.63 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 91 GRISTEVDARLSYDTEASIAKAKRiikLYNdaGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAEA 170
Cdd:PRK03903 43 GFISIEIDPFLEDDAAGSIEEGKR---LYK--TIGRPNVMIKVPATKAGYEAMSALMKKGISVNATLIFSPEQAKECAEA 117
|
90 100
....*....|....*....|....*
gi 2099470914 171 -------------GVflISPFVGRI 182
Cdd:PRK03903 118 lneglkkntkdpkAV--ISVFVSRF 140
|
|
| PRK03343 |
PRK03343 |
transaldolase; Validated |
33-170 |
3.98e-15 |
|
transaldolase; Validated
Pssm-ID: 235117 Cd Length: 368 Bit Score: 74.86 E-value: 3.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 33 TTNPSlILGAA---------QIPE-----------YRKLIDDAVAWArsqsSDRAQQILDASDKLAvnigleilklipGR 92
Cdd:PRK03343 43 TSNPA-IFQKAiaggdaydaQIAElaaagadveeaYEELTTADVRNA----CDVLRPVYEATGGVD------------GR 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2099470914 93 ISTEVDARLSYDTEASIAKAKRiikLYNDAGISNdrILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAEA 170
Cdd:PRK03343 106 VSIEVSPRLAHDTEATIAEARR---LWAAVDRPN--LMIKIPATPEGLPAIEALIAEGISVNVTLIFSVERYRAVADA 178
|
|
| PRK09533 |
PRK09533 |
bifunctional transaldolase/phosoglucose isomerase; Validated |
91-170 |
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 2099470914 91 GRISTEVDARLSYDTEASIAKAKRIIKLYNdagisNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAEA 170
Cdd:PRK09533 104 GFVSLEVSPYLALDTEGTIAEARRLWAAVD-----RPNLMIKVPATPEGLPAIRQLIAEGINVNVTLLFSQDVYEEVAEA 178
|
|
| PRK12653 |
PRK12653 |
fructose-6-phosphate aldolase; Reviewed |
17-244 |
1.80e-07 |
|
fructose-6-phosphate aldolase; Reviewed
Pssm-ID: 183653 [Multi-domain] Cd Length: 220 Bit Score: 50.93 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 17 DTGDIAAMK----LYQPQDATTNPSlILGAAQIPEyrkliddAVAWARSQSSDRAQqildasdklavnigleilklipGR 92
Cdd:PRK12653 6 DTSDVVAVKalsrIFPLAGVTTNPS-IIAAGKKPL-------EVVLPQLHEAMGGQ----------------------GR 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 93 ISTEVdarLSYDTEASIAKAKRIIKLYNDagisndrILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAEAGV 172
Cdd:PRK12653 56 LFAQV---MATTAEGMVNDARKLRSIIAD-------IVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGA 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2099470914 173 FLISPFVGRIlDWYKANtdkkeyapaedpGVVSVSEIYEYYKQHGYETVVMGASFRNVGEILE--LAGCDRLTI 244
Cdd:PRK12653 126 EYVAPYVNRI-DAQGGS------------GIQTVTDLQQLLKMHAPQAKVLAASFKTPRQALDclLAGCESITL 186
|
|
| PRK12656 |
PRK12656 |
fructose-6-phosphate aldolase; Reviewed |
104-250 |
2.11e-05 |
|
fructose-6-phosphate aldolase; Reviewed
Pssm-ID: 183656 [Multi-domain] Cd Length: 222 Bit Score: 44.73 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2099470914 104 DTEASIAKAKRIIKLYNDAgisndrILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAEAGVFLISPFVGRIL 183
Cdd:PRK12656 65 DYEGILKDAHEIRRQCGDD------VYIKVPVTPAGLAAIKTLKAEGYHITATAIYTVFQGLLAIEAGADYLAPYYNRME 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2099470914 184 DwykANTDKKEYapaedpgvvsVSEIYEYYKQHGYETVVMGASFRNVGEILE--LAGCDRLTIAPALLK 250
Cdd:PRK12656 139 N---LNIDSNAV----------IGQLAEAIDRENSDSKILAASFKNVAQVNKafALGAQAVTAGPDVFE 194
|
|
| |
