|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05269 |
PRK05269 |
transaldolase B; Provisional |
1-316 |
0e+00 |
|
transaldolase B; Provisional
Pssm-ID: 235381 [Multi-domain] Cd Length: 318 Bit Score: 666.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 1 TDKLTSLRQYTTVVADTGDIAAMKLYQPQDATTNPSLILNAAQIPEYRKLIDDAVAWAKQQSNDRAQQIVDATDKLAVNI 80
Cdd:PRK05269 2 TNKLEQLKQFTTVVADTGDIEAIKKYQPQDATTNPSLILKAAQIPEYAPLIDDAVAWAKQQSGDRAQQIDDAIDKLAVNF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 81 GLEILKLVPGRISTEVDARLSYDTEASIAKAKRLIKLYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSF 160
Cdd:PRK05269 82 GLEILKLIPGRVSTEVDARLSFDTEATIAKARKLIALYEEAGISKDRILIKIASTWEGIRAAEQLEKEGINCNLTLLFSF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 161 AQARACAEAGVFLIAPFVGRILDWYKANTDKKEYAPAEDPGVVSVSEIYQYYKEHGYETVVMGASFRNIGEILELAGCDR 240
Cdd:PRK05269 162 AQARACAEAGVFLISPFVGRILDWYKKNTGKKEYAPAEDPGVVSVTKIYNYYKKHGYKTVVMGASFRNTGQILELAGCDR 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1I2R_A 241 LTIAPALLKELAESEGAIERKLSYTGEVKARPARITESEFLWQHNQDPMAVDKLAEGIRKFAIDQEKLEKMIGDLL 316
Cdd:PRK05269 242 LTISPALLEELAASEGELERKLSPPGEAKARPVPLTEAEFRWQHNEDAMATEKLAEGIRKFAKDQEKLEKLIAAKL 317
|
|
| talAB |
TIGR00874 |
transaldolase; This family includes the majority of known and predicted transaldolase ... |
2-316 |
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: 587.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 2 DKLTSLRQYTTVVADTGDIAAMKLYQPQDATTNPSLILNAAQIPEYRKLIDDAVAWAKQQSNDRAQQIVDATDKLAVNIG 81
Cdd:TIGR00874 1 NQLDQLKQFTVVVADTGDIEAIKKYQPQDATTNPSLILAAAQLPKYAELIDEAVAWGKKQGKDDAQQVENALDKLAVNFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 82 LEILKLVPGRISTEVDARLSYDTEASIAKAKRLIKLYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFA 161
Cdd:TIGR00874 81 LEILKIVPGRVSTEVDARLSFDTEATVEKARHLIKLYEDAGVDKKRILIKIASTWEGIRAAEELEKEGIHCNLTLLFSFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 162 QARACAEAGVFLIAPFVGRILDWYKANTDKKEYAPAEDPGVVSVSEIYQYYKEHGYETVVMGASFRNIGEILELAGCDRL 241
Cdd:TIGR00874 161 QAIACAEAKVTLISPFVGRILDWYKAATGKKEYSIEEDPGVASVKKIYNYYKKHGYPTEVMGASFRNKEEILALAGCDRL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1I2R_A 242 TIAPALLKELAESEGAIERKLSYTGE--VKARPARITESEFLWQHNQDPMAVDKLAEGIRKFAIDQEKLEKMIGDLL 316
Cdd:TIGR00874 241 TISPALLDELKESTGPVERKLDPESAkkVDKQPIILDESEFRFLHNEDAMATEKLAEGIRKFAADQEKLEKLLEEKL 317
|
|
| Transaldolase_TalAB |
cd00957 |
Transaldolases including both TalA and TalB; Transaldolases including both TalA and TalB. The ... |
3-312 |
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: 541.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 3 KLTSLRQYTTVVADTGDIAAMKLYQPQDATTNPSLILNAAQIPEYRKLIDDAVAWAKQQSNDRAQQIVDATDKLAVNIGL 82
Cdd:cd00957 2 QLDQLKKFTTIVADTGDFEAIKKFKPQDATTNPSLILAAAKLPEYNKLVDEAIAYAKKKGGSDEDQISNALDKLLVNFGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 83 EILKLVPGRISTEVDARLSYDTEASIAKAKRLIKLYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQ 162
Cdd:cd00957 82 EILKLIPGRVSTEVDARLSFDTNATIAKARKLIKLYEEAGIDKERILIKIAATWEGIQAAKQLEKEGIHCNLTLLFSFAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 163 ARACAEAGVFLIAPFVGRILDWYKANTDKKEYAPAEDPGVVSVSEIYQYYKEHGYETVVMGASFRNIGEILELAGCDRLT 242
Cdd:cd00957 162 AVACAEAGVTLISPFVGRILDWYKKHSGDKAYTAEEDPGVASVKKIYNYYKKFGYKTKVMGASFRNIGQILALAGCDYLT 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1I2R_A 243 IAPALLKELAESEGAIERKLSY--TGEVKARPARITESEFLWQHNQDPMAVDKLAEGIRKFAIDQEKLEKMI 312
Cdd:cd00957 242 ISPALLEELKNSTAKVERKLDPaaSKALDIHPNFLDESAFRWALNEDAMAVEKLSEGIRGFAKDAVKLEKLI 313
|
|
| TAL_FSA |
pfam00923 |
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ... |
13-312 |
1.63e-95 |
|
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: 281.73 E-value: 1.63e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 13 VVADTGDIAAMKLYQP----QDATTNPSLILNAAqipEYRKLIDDAVAwakqqsndraqqivdatdklavniglEILKLV 88
Cdd:pfam00923 1 IWLDTADRDLIKKLIEeggiDGVTTNPSIFLKAI---EYSALYDEAIA--------------------------EIKEIG 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 89 PGRISTEVDARLSYDTEASIAKAKRLIKLYNDagisnDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAE 168
Cdd:pfam00923 52 DGPVSLEVDPRLADDTEGTIEEARRLIALYGR-----PNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALAAAE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 169 AGVFLIAPFVGRILDWYKANTDKkeyAPAEDPGVVSVSEIYQYYKEHGYETVVMGASFRNIGEILELAGCDRLTIAPALL 248
Cdd:pfam00923 127 AGASVISPFVGRIDDWGDKRLGA---ALRGDDGIANAKEIYQIYKKYGWSTGVLAASFRNVLYVLALAGCDTITIPPDTL 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
1I2R_A 249 KELAEsegaierklsytgevkarpariteseflwqhnqdpmavdklAEGIRKFAIDQEKLEKMI 312
Cdd:pfam00923 204 EALAK-----------------------------------------DEGVRKFAKDWEKLLGSI 226
|
|
| TalA |
COG0176 |
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ... |
11-308 |
9.67e-78 |
|
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: 236.13 E-value: 9.67e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 11 TTVVADTGDIAAMK----LYQPQDATTNPSLILNAAqipeyrkliddavawakqqsndraqqivdatDKLAVNIGLEILK 86
Cdd:COG0176 1 MKLWLDTADREEIKelidLGGVDGVTTNPSLIAKAG-------------------------------IKDFVEDIREICD 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 87 LVPGRISTEVdarLSYDTEASIAKAKRLIKLYndagisNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARAC 166
Cdd:COG0176 50 IVDGPVSAEV---LATDTEGMIAEARRLAALY------RPNVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQALLA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 167 AEAGVFLIAPFVGRILDWykantdkkeyapAEDpGVVSVSEIYQYYKEHGYETVVMGASFRNIGEILE--LAGCDRLTIA 244
Cdd:COG0176 121 AEAGASYVSPFVGRIDDI------------GID-GIALVREIYQIYKNYGARTRILAASFRNPLQVLEaaLAGADTVTIP 187
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
1I2R_A 245 PALLKELAESegaierklsytgevkarpariteseflwqhnqdpmavDKLAEGIRKFAIDQEKL 308
Cdd:COG0176 188 PAVLEALADH-------------------------------------PLTDEGIEKFLADWEKL 214
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05269 |
PRK05269 |
transaldolase B; Provisional |
1-316 |
0e+00 |
|
transaldolase B; Provisional
Pssm-ID: 235381 [Multi-domain] Cd Length: 318 Bit Score: 666.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 1 TDKLTSLRQYTTVVADTGDIAAMKLYQPQDATTNPSLILNAAQIPEYRKLIDDAVAWAKQQSNDRAQQIVDATDKLAVNI 80
Cdd:PRK05269 2 TNKLEQLKQFTTVVADTGDIEAIKKYQPQDATTNPSLILKAAQIPEYAPLIDDAVAWAKQQSGDRAQQIDDAIDKLAVNF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 81 GLEILKLVPGRISTEVDARLSYDTEASIAKAKRLIKLYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSF 160
Cdd:PRK05269 82 GLEILKLIPGRVSTEVDARLSFDTEATIAKARKLIALYEEAGISKDRILIKIASTWEGIRAAEQLEKEGINCNLTLLFSF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 161 AQARACAEAGVFLIAPFVGRILDWYKANTDKKEYAPAEDPGVVSVSEIYQYYKEHGYETVVMGASFRNIGEILELAGCDR 240
Cdd:PRK05269 162 AQARACAEAGVFLISPFVGRILDWYKKNTGKKEYAPAEDPGVVSVTKIYNYYKKHGYKTVVMGASFRNTGQILELAGCDR 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1I2R_A 241 LTIAPALLKELAESEGAIERKLSYTGEVKARPARITESEFLWQHNQDPMAVDKLAEGIRKFAIDQEKLEKMIGDLL 316
Cdd:PRK05269 242 LTISPALLEELAASEGELERKLSPPGEAKARPVPLTEAEFRWQHNEDAMATEKLAEGIRKFAKDQEKLEKLIAAKL 317
|
|
| talAB |
TIGR00874 |
transaldolase; This family includes the majority of known and predicted transaldolase ... |
2-316 |
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: 587.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 2 DKLTSLRQYTTVVADTGDIAAMKLYQPQDATTNPSLILNAAQIPEYRKLIDDAVAWAKQQSNDRAQQIVDATDKLAVNIG 81
Cdd:TIGR00874 1 NQLDQLKQFTVVVADTGDIEAIKKYQPQDATTNPSLILAAAQLPKYAELIDEAVAWGKKQGKDDAQQVENALDKLAVNFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 82 LEILKLVPGRISTEVDARLSYDTEASIAKAKRLIKLYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFA 161
Cdd:TIGR00874 81 LEILKIVPGRVSTEVDARLSFDTEATVEKARHLIKLYEDAGVDKKRILIKIASTWEGIRAAEELEKEGIHCNLTLLFSFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 162 QARACAEAGVFLIAPFVGRILDWYKANTDKKEYAPAEDPGVVSVSEIYQYYKEHGYETVVMGASFRNIGEILELAGCDRL 241
Cdd:TIGR00874 161 QAIACAEAKVTLISPFVGRILDWYKAATGKKEYSIEEDPGVASVKKIYNYYKKHGYPTEVMGASFRNKEEILALAGCDRL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1I2R_A 242 TIAPALLKELAESEGAIERKLSYTGE--VKARPARITESEFLWQHNQDPMAVDKLAEGIRKFAIDQEKLEKMIGDLL 316
Cdd:TIGR00874 241 TISPALLDELKESTGPVERKLDPESAkkVDKQPIILDESEFRFLHNEDAMATEKLAEGIRKFAADQEKLEKLLEEKL 317
|
|
| PRK12346 |
PRK12346 |
transaldolase A; Provisional |
1-316 |
0e+00 |
|
transaldolase A; Provisional
Pssm-ID: 183458 Cd Length: 316 Bit Score: 561.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 1 TDKLTSLRQYTTVVADTGDIAAMKLYQPQDATTNPSLILNAAQIPEYRKLIDDAVAWAKQQSNDRAQQIVDATDKLAVNI 80
Cdd:PRK12346 1 MNQLDGIKQFTTVVADSGDIESIRHYHPQDATTNPSLLLKAAGLPQYQHLIDDAIAWGKKQGGTQEQQVVAACDKLAVNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 81 GLEILKLVPGRISTEVDARLSYDTEASIAKAKRLIKLYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSF 160
Cdd:PRK12346 81 GAEILKSVPGRVSTEVDARLSFDREKSIEKARHLVDLYQQQGIDKSRILIKLASTWEGIRAAEELEKEGINCNLTLLFSF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 161 AQARACAEAGVFLIAPFVGRILDWYKANTDKKEYAPAEDPGVVSVSEIYQYYKEHGYETVVMGASFRNIGEILELAGCDR 240
Cdd:PRK12346 161 AQARACAEAGVFLISPFVGRIYDWYQARKPMDPYVVEEDPGVKSVRNIYDYYKQHRYETIVMGASFRRTEQILALAGCDR 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1I2R_A 241 LTIAPALLKELAESEGAIERKLSYTGEVKARPARITESEFLWQHNQDPMAVDKLAEGIRKFAIDQEKLEKMIGDLL 316
Cdd:PRK12346 241 LTISPNLLKELQESESPVERKLIPSSQTFPRPAPMSEAEFRWEHNQDAMAVEKLSEGIRLFAVDQRKLEDLLAAKL 316
|
|
| Transaldolase_TalAB |
cd00957 |
Transaldolases including both TalA and TalB; Transaldolases including both TalA and TalB. The ... |
3-312 |
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: 541.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 3 KLTSLRQYTTVVADTGDIAAMKLYQPQDATTNPSLILNAAQIPEYRKLIDDAVAWAKQQSNDRAQQIVDATDKLAVNIGL 82
Cdd:cd00957 2 QLDQLKKFTTIVADTGDFEAIKKFKPQDATTNPSLILAAAKLPEYNKLVDEAIAYAKKKGGSDEDQISNALDKLLVNFGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 83 EILKLVPGRISTEVDARLSYDTEASIAKAKRLIKLYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQ 162
Cdd:cd00957 82 EILKLIPGRVSTEVDARLSFDTNATIAKARKLIKLYEEAGIDKERILIKIAATWEGIQAAKQLEKEGIHCNLTLLFSFAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 163 ARACAEAGVFLIAPFVGRILDWYKANTDKKEYAPAEDPGVVSVSEIYQYYKEHGYETVVMGASFRNIGEILELAGCDRLT 242
Cdd:cd00957 162 AVACAEAGVTLISPFVGRILDWYKKHSGDKAYTAEEDPGVASVKKIYNYYKKFGYKTKVMGASFRNIGQILALAGCDYLT 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1I2R_A 243 IAPALLKELAESEGAIERKLSY--TGEVKARPARITESEFLWQHNQDPMAVDKLAEGIRKFAIDQEKLEKMI 312
Cdd:cd00957 242 ISPALLEELKNSTAKVERKLDPaaSKALDIHPNFLDESAFRWALNEDAMAVEKLSEGIRGFAKDAVKLEKLI 313
|
|
| PTZ00411 |
PTZ00411 |
transaldolase-like protein; Provisional |
4-316 |
6.22e-177 |
|
transaldolase-like protein; Provisional
Pssm-ID: 240406 Cd Length: 333 Bit Score: 492.33 E-value: 6.22e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 4 LTSLRQYTTVVADTGDIAAMKLYQPQDATTNPSLILNAAQIPEYRKLIDDAVAWAKQQS----------NDRAQQIVDAT 73
Cdd:PTZ00411 5 LEALKEHTTVVADTGDFSLLKKFQPEDATTNPSLVLAAAQMPEYAHLIDDAIKYAKANVsrlrdpllsdEEKEELVELVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 74 DKLAVNIGLEILKLVPGRISTEVDARLSYDTEASIAKAKRLIKLYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCN 153
Cdd:PTZ00411 85 DKLTVNFGVEILKIVPGRVSTEVDARLSFDKQAMVDKARKIIKMYEEAGISKDRILIKLASTWEGIQAAKALEKEGIHCN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 154 LTLLFSFAQARACAEAGVFLIAPFVGRILDWYKANTDKKEYAPAEDPGVVSVSEIYQYYKEHGYETVVMGASFRNIGEIL 233
Cdd:PTZ00411 165 LTLLFSFAQAVACAQAGVTLISPFVGRILDWYKKPEKAESYVGAQDPGVISVTKIYNYYKKHGYKTIVMGASFRNTGEIL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 234 ELAGCDRLTIAPALLKELAESEGA-IERKLSYTGEVKARPARI--TESEFLWQHNQDPMAVDKLAEGIRKFAIDQEKLEK 310
Cdd:PTZ00411 245 ELAGCDKLTISPKLLEELANTEDGpVERKLDPEKLTEDTEKLPelTEKEFRWELNEDAMATEKLAEGIRNFAKDLEKLEN 324
|
....*.
1I2R_A 311 MIGDLL 316
Cdd:PTZ00411 325 VIRAKL 330
|
|
| PRK12309 |
PRK12309 |
transaldolase; |
4-316 |
2.56e-168 |
|
transaldolase;
Pssm-ID: 183426 [Multi-domain] Cd Length: 391 Bit Score: 472.68 E-value: 2.56e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 4 LTSLRQYTTVVADTGDIAAMKLYQPQDATTNPSLILNAAQIPEYRKLIDDAVAWAKQQSNDRA--QQIV-DATDKLAVNI 80
Cdd:PRK12309 6 LEQLRQMTVVVADTGDIQAIEKFTPRDATTNPSLITAAAQMPQYQSIVDETLRQARKELGSDApvEDVVaLAFDRLAVAF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 81 GLEILKLVPGRISTEVDARLSYDTEASIAKAKRLIKLYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSF 160
Cdd:PRK12309 86 GLKILKIVPGRVSTEVDARLSYDTEATIAKARKLISLYEDAGISRDRVLIKIASTWEGIKAAEVLEKEGIHCNLTLLFGF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 161 AQARACAEAGVFLIAPFVGRILDWYKANTDKKEYAPAEDPGVVSVSEIYQYYKEHGYETVVMGASFRNIGEILELAGCDR 240
Cdd:PRK12309 166 HQAIACAEAGVTLISPFVGRILDWYKKETGRDSYPGAEDPGVQSVTQIYNYYKKFGYKTEVMGASFRNIGEIIELAGCDL 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1I2R_A 241 LTIAPALLKELAESEGAIERKLSYTGEVKARPARIT--ESEFLWQHNQDPMAVDKLAEGIRKFAIDQEKLEKMIGDLL 316
Cdd:PRK12309 246 LTISPKLLEQLRSTEAELPRKLDPANAAGMEIEKIHmdRATFDKMHAEDRMASEKLDEGIKGFSKALETLEKLLAHRL 323
|
|
| TAL_FSA |
pfam00923 |
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ... |
13-312 |
1.63e-95 |
|
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: 281.73 E-value: 1.63e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 13 VVADTGDIAAMKLYQP----QDATTNPSLILNAAqipEYRKLIDDAVAwakqqsndraqqivdatdklavniglEILKLV 88
Cdd:pfam00923 1 IWLDTADRDLIKKLIEeggiDGVTTNPSIFLKAI---EYSALYDEAIA--------------------------EIKEIG 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 89 PGRISTEVDARLSYDTEASIAKAKRLIKLYNDagisnDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAE 168
Cdd:pfam00923 52 DGPVSLEVDPRLADDTEGTIEEARRLIALYGR-----PNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALAAAE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 169 AGVFLIAPFVGRILDWYKANTDKkeyAPAEDPGVVSVSEIYQYYKEHGYETVVMGASFRNIGEILELAGCDRLTIAPALL 248
Cdd:pfam00923 127 AGASVISPFVGRIDDWGDKRLGA---ALRGDDGIANAKEIYQIYKKYGWSTGVLAASFRNVLYVLALAGCDTITIPPDTL 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
1I2R_A 249 KELAEsegaierklsytgevkarpariteseflwqhnqdpmavdklAEGIRKFAIDQEKLEKMI 312
Cdd:pfam00923 204 EALAK-----------------------------------------DEGVRKFAKDWEKLLGSI 226
|
|
| Transaldolase |
cd00439 |
Transaldolase; Transaldolase. Enzymes found in the non-oxidative branch of the pentose ... |
12-252 |
4.97e-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: 238.40 E-value: 4.97e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 12 TVVADTGDIAAMKLYQ----PQDATTNPSLILNAAQIPEYRKLIDDAVAWAKQQSNDRAQQIVDATDKLAVNIGLEILKL 87
Cdd:cd00439 1 SPWYDTLDRPATDLLPlirgVRGVTTNPSIIQAAISTSNAYNDQFRTLVESGKDIESAYWELVVKDIQDACKLFEPIYDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 88 V--PGRISTEVDARLSYDTEASIAKAKRLIKLYNDagisnDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARA 165
Cdd:cd00439 81 TeaDGRVSVEVSARLADDTQGMVEAAKYLSKVVNR-----RNIYIKIPATAEGIPAIKDLIAAGISVNVTLIFSIAQYEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 166 CAEAGVFLIAPFVGRILDWYKANTDKKEYAPAEDPGVVSVSEIYQYYKEHGYETVVMGASFRNIGEILELAGCDRLTIAP 245
Cdd:cd00439 156 VADAGTSVASPFVSRIDTLMDKMLEQIGLDLRGKAGVAQVTLAYKLYKQKFKKQRVLWASFSDTLYVAPLIGCDTVTTMP 235
|
....*..
1I2R_A 246 ALLKELA 252
Cdd:cd00439 236 DQALEAG 242
|
|
| TalA |
COG0176 |
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ... |
11-308 |
9.67e-78 |
|
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: 236.13 E-value: 9.67e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 11 TTVVADTGDIAAMK----LYQPQDATTNPSLILNAAqipeyrkliddavawakqqsndraqqivdatDKLAVNIGLEILK 86
Cdd:COG0176 1 MKLWLDTADREEIKelidLGGVDGVTTNPSLIAKAG-------------------------------IKDFVEDIREICD 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 87 LVPGRISTEVdarLSYDTEASIAKAKRLIKLYndagisNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARAC 166
Cdd:COG0176 50 IVDGPVSAEV---LATDTEGMIAEARRLAALY------RPNVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQALLA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 167 AEAGVFLIAPFVGRILDWykantdkkeyapAEDpGVVSVSEIYQYYKEHGYETVVMGASFRNIGEILE--LAGCDRLTIA 244
Cdd:COG0176 121 AEAGASYVSPFVGRIDDI------------GID-GIALVREIYQIYKNYGARTRILAASFRNPLQVLEaaLAGADTVTIP 187
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
1I2R_A 245 PALLKELAESegaierklsytgevkarpariteseflwqhnqdpmavDKLAEGIRKFAIDQEKL 308
Cdd:COG0176 188 PAVLEALADH-------------------------------------PLTDEGIEKFLADWEKL 214
|
|
| Transaldolase_FSA |
cd00956 |
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ... |
16-255 |
1.16e-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: 114.98 E-value: 1.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 16 DTGDIAAMKLYQPQ----DATTNPSLIlnaaqipeyrkliddavawAKQQSNDRAQQIvdatdklavnigLEILKLVPGR 91
Cdd:cd00956 5 DTADLEEIKKASETglldGVTTNPSLI-------------------AKSGRIDFEAVL------------KEICEIIDGP 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 92 ISTEVDARlsyDTEASIAKAKRLIKLyndagisNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAEAGV 171
Cdd:cd00956 54 VSAQVVST---DAEGMVAEARKLASL-------GGNVVVKIPVTEDGLKAIKKLSEEGIKTNVTAIFSAAQALLAAKAGA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 172 FLIAPFVGRIldwykANTdkkeyapAEDPGVVsVSEIYQYYKEHGYETVVMGASFRNIGEILE--LAGCDRLTIAPALLK 249
Cdd:cd00956 124 TYVSPFVGRI-----DDL-------GGDGMEL-IREIRTIFDNYGFDTKILAASIRNPQHVIEaaLAGADAITLPPDVLE 190
|
....*.
1I2R_A 250 ELAESE 255
Cdd:cd00956 191 QLLKHP 196
|
|
| fsa_talC_mipB |
TIGR00875 |
fructose-6-phosphate aldolase, TalC/MipB family; This model represents a family that includes ... |
83-260 |
2.53e-22 |
|
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: 92.62 E-value: 2.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 83 EILKLVPGRISTEVdarLSYDTEASIAKAKRLIKLyndagisNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQ 162
Cdd:TIGR00875 45 EIQEAVEGPVSAET---ISLDAEGMVEEAKELAKL-------APNIVVKIPMTSEGLKAVKILKKEGIKTNVTLVFSAAQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 163 ARACAEAGVFLIAPFVGRILDwykantdkkeyapAEDPGVVSVSEIYQYYKEHGYETVVMGASFRNIGEILE--LAGCDR 240
Cdd:TIGR00875 115 ALLAAKAGATYVSPFVGRLDD-------------IGGDGMKLIEEVKTIFENHAPDTEVIAASVRHPRHVLEaaLIGADI 181
|
170 180
....*....|....*....|...
1I2R_A 241 LTIAPALLKELAE---SEGAIER 260
Cdd:TIGR00875 182 ATMPLDVMQQLFNhplTDIGLER 204
|
|
| Transaldolase_like |
cd00955 |
Transaldolase-like proteins from plants and bacteria; Transaldolase-like proteins from plants ... |
31-215 |
7.26e-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: 85.45 E-value: 7.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 31 ATTNPSLILNA-AQIPEYrkliDDAVAWAKQQSNDRA--------QQIVDATDKLAVNigLEILKLVPGRISTEVDARLS 101
Cdd:cd00955 29 VTSNPAIFEKAiAGSAAY----DDQIRALKGQGLDAEaiyealaiEDIQDACDLLAPV--YEQTGGNDGYVSLEVSPRLA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 102 YDTEASIAKAKRLiklYNDAGISNdrILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAEA------------ 169
Cdd:cd00955 103 DDTQGTIAEAKRL---WKAVGRPN--LMIKIPATEAGLPAIEELIAAGISVNVTLIFSLEQYEAVAEAylrglerrvegg 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
1I2R_A 170 ----GVFLIAP-FVGRIldwyKANTDKKEYAPAEDP-----GVVSVSEIYQYYKEH 215
Cdd:cd00955 178 gdlsQVASVASfFVSRV----DTLIDKKLDAPEAKAlqgkvAIANAKLAYQEYQEK 229
|
|
| PRK03343 |
PRK03343 |
transaldolase; Validated |
32-169 |
3.47e-15 |
|
transaldolase; Validated
Pssm-ID: 235117 Cd Length: 368 Bit Score: 75.24 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 32 TTNPSLILNA--------AQIPE-----------YRKLIDDAVAWAKqqsnDRAQQIVDATDKlavnigleilklVPGRI 92
Cdd:PRK03343 43 TSNPAIFQKAiaggdaydAQIAElaaagadveeaYEELTTADVRNAC----DVLRPVYEATGG------------VDGRV 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1I2R_A 93 STEVDARLSYDTEASIAKAKRLIKLyndagISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAEA 169
Cdd:PRK03343 107 SIEVSPRLAHDTEATIAEARRLWAA-----VDRPNLMIKIPATPEGLPAIEALIAEGISVNVTLIFSVERYRAVADA 178
|
|
| PRK03903 |
PRK03903 |
transaldolase; Provisional |
90-169 |
3.90e-15 |
|
transaldolase; Provisional
Pssm-ID: 235171 Cd Length: 274 Bit Score: 73.86 E-value: 3.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 90 GRISTEVDARLSYDTEASIAKAKRLIKLyndagISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAEA 169
Cdd:PRK03903 43 GFISIEIDPFLEDDAAGSIEEGKRLYKT-----IGRPNVMIKVPATKAGYEAMSALMKKGISVNATLIFSPEQAKECAEA 117
|
|
| PRK09533 |
PRK09533 |
bifunctional transaldolase/phosoglucose isomerase; Validated |
90-169 |
8.01e-11 |
|
bifunctional transaldolase/phosoglucose isomerase; Validated
Pssm-ID: 236551 [Multi-domain] Cd Length: 948 Bit Score: 63.07 E-value: 8.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 90 GRISTEVDARLSYDTEASIAKAKRLIKLYNdagisNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAEA 169
Cdd:PRK09533 104 GFVSLEVSPYLALDTEGTIAEARRLWAAVD-----RPNLMIKVPATPEGLPAIRQLIAEGINVNVTLLFSQDVYEEVAEA 178
|
|
| PRK12653 |
PRK12653 |
fructose-6-phosphate aldolase; Reviewed |
16-243 |
2.69e-08 |
|
fructose-6-phosphate aldolase; Reviewed
Pssm-ID: 183653 [Multi-domain] Cd Length: 220 Bit Score: 53.24 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 16 DTGDIAAMK----LYQPQDATTNPSLilnaaqipeyrkliddaVAWAKQQSNDRAQQIVDAtdklavnIGLEilklvpGR 91
Cdd:PRK12653 6 DTSDVVAVKalsrIFPLAGVTTNPSI-----------------IAAGKKPLEVVLPQLHEA-------MGGQ------GR 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 92 ISTEVdarLSYDTEASIAKAKRLIKLYNDagisndrILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAEAGV 171
Cdd:PRK12653 56 LFAQV---MATTAEGMVNDARKLRSIIAD-------IVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGA 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1I2R_A 172 FLIAPFVGRIlDWYKANtdkkeyapaedpGVVSVSEIYQYYKEHGYETVVMGASFRNIGEILE--LAGCDRLTI 243
Cdd:PRK12653 126 EYVAPYVNRI-DAQGGS------------GIQTVTDLQQLLKMHAPQAKVLAASFKTPRQALDclLAGCESITL 186
|
|
| PRK12656 |
PRK12656 |
fructose-6-phosphate aldolase; Reviewed |
103-249 |
9.64e-05 |
|
fructose-6-phosphate aldolase; Reviewed
Pssm-ID: 183656 [Multi-domain] Cd Length: 222 Bit Score: 42.80 E-value: 9.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1I2R_A 103 DTEASIAKAKRLIKLYNDAgisndrILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAEAGVFLIAPFVGRIL 182
Cdd:PRK12656 65 DYEGILKDAHEIRRQCGDD------VYIKVPVTPAGLAAIKTLKAEGYHITATAIYTVFQGLLAIEAGADYLAPYYNRME 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1I2R_A 183 DwykANTDKKEYapaedpgvvsVSEIYQYYKEHGYETVVMGASFRNIGEILE--LAGCDRLTIAPALLK 249
Cdd:PRK12656 139 N---LNIDSNAV----------IGQLAEAIDRENSDSKILAASFKNVAQVNKafALGAQAVTAGPDVFE 194
|
|
| |
