|
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: 671.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 1 MTDKLTSLRQFTTVVADTGDIAAMKLYQPQDATTNPSLILNAAQIPEYRKLIDDAVAWAKQQSNDRAQQIVDATDKLAVN 80
Cdd:PRK05269 1 MTNKLEQLKQFTTVVADTGDIEAIKKYQPQDATTNPSLILKAAQIPEYAPLIDDAVAWAKQQSGDRAQQIDDAIDKLAVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 81 IGLEILKLVPGRISTEVDARLSYDTDASIAKAKRLIKMYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFS 160
Cdd:PRK05269 81 FGLEILKLIPGRVSTEVDARLSFDTEATIAKARKLIALYEEAGISKDRILIKIASTWEGIRAAEQLEKEGINCNLTLLFS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 161 FAQARACAEAGVYLISPFVGRILDWYKANTDKKEYAPAEDPGVVSVTEIYEYYKQHGYETVVMGASFRNIGEIIELAGCD 240
Cdd:PRK05269 161 FAQARACAEAGVFLISPFVGRILDWYKKNTGKKEYAPAEDPGVVSVTKIYNYYKKHGYKTVVMGASFRNTGQILELAGCD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489109116 241 RLTIAPALLKELAESEGAIERKLSFSGEVKARPARITEAEFLWQHNQDPMAVDKLADGIRKFAVDQGKLEKMIGDLL 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: 580.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 3 DKLTSLRQFTTVVADTGDIAAMKLYQPQDATTNPSLILNAAQIPEYRKLIDDAVAWAKQQSNDRAQQIVDATDKLAVNIG 82
Cdd:TIGR00874 1 NQLDQLKQFTVVVADTGDIEAIKKYQPQDATTNPSLILAAAQLPKYAELIDEAVAWGKKQGKDDAQQVENALDKLAVNFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 83 LEILKLVPGRISTEVDARLSYDTDASIAKAKRLIKMYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFA 162
Cdd:TIGR00874 81 LEILKIVPGRVSTEVDARLSFDTEATVEKARHLIKLYEDAGVDKKRILIKIASTWEGIRAAEELEKEGIHCNLTLLFSFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 163 QARACAEAGVYLISPFVGRILDWYKANTDKKEYAPAEDPGVVSVTEIYEYYKQHGYETVVMGASFRNIGEIIELAGCDRL 242
Cdd:TIGR00874 161 QAIACAEAKVTLISPFVGRILDWYKAATGKKEYSIEEDPGVASVKKIYNYYKKHGYPTEVMGASFRNKEEILALAGCDRL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489109116 243 TIAPALLKELAESEGAIERKLSFSGE--VKARPARITEAEFLWQHNQDPMAVDKLADGIRKFAVDQGKLEKMIGDLL 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: 541.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 4 KLTSLRQFTTVVADTGDIAAMKLYQPQDATTNPSLILNAAQIPEYRKLIDDAVAWAKQQSNDRAQQIVDATDKLAVNIGL 83
Cdd:cd00957 2 QLDQLKKFTTIVADTGDFEAIKKFKPQDATTNPSLILAAAKLPEYNKLVDEAIAYAKKKGGSDEDQISNALDKLLVNFGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 84 EILKLVPGRISTEVDARLSYDTDASIAKAKRLIKMYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQ 163
Cdd:cd00957 82 EILKLIPGRVSTEVDARLSFDTNATIAKARKLIKLYEEAGIDKERILIKIAATWEGIQAAKQLEKEGIHCNLTLLFSFAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 164 ARACAEAGVYLISPFVGRILDWYKANTDKKEYAPAEDPGVVSVTEIYEYYKQHGYETVVMGASFRNIGEIIELAGCDRLT 243
Cdd:cd00957 162 AVACAEAGVTLISPFVGRILDWYKKHSGDKAYTAEEDPGVASVKKIYNYYKKFGYKTKVMGASFRNIGQILALAGCDYLT 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489109116 244 IAPALLKELAESEGAIERKLS--FSGEVKARPARITEAEFLWQHNQDPMAVDKLADGIRKFAVDQGKLEKMI 313
Cdd:cd00957 242 ISPALLEELKNSTAKVERKLDpaASKALDIHPNFLDESAFRWALNEDAMAVEKLSEGIRGFAKDAVKLEKLI 313
|
|
| TAL_FSA |
pfam00923 |
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ... |
14-257 |
5.86e-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: 282.89 E-value: 5.86e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 14 VVADTGDIAAMKLYQP----QDATTNPSLILNAAqipEYRKLIDDAVAwakqqsndraqqivdatdklavniglEILKLV 89
Cdd:pfam00923 1 IWLDTADRDLIKKLIEeggiDGVTTNPSIFLKAI---EYSALYDEAIA--------------------------EIKEIG 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 90 PGRISTEVDARLSYDTDASIAKAKRLIKMYNDagisnDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAE 169
Cdd:pfam00923 52 DGPVSLEVDPRLADDTEGTIEEARRLIALYGR-----PNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALAAAE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 170 AGVYLISPFVGRILDWYKANTDKkeyAPAEDPGVVSVTEIYEYYKQHGYETVVMGASFRNIGEIIELAGCDRLTIAPALL 249
Cdd:pfam00923 127 AGASVISPFVGRIDDWGDKRLGA---ALRGDDGIANAKEIYQIYKKYGWSTGVLAASFRNVLYVLALAGCDTITIPPDTL 203
|
....*...
gi 489109116 250 KELAESEG 257
Cdd:pfam00923 204 EALAKDEG 211
|
|
| TalA |
COG0176 |
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ... |
12-309 |
2.03e-76 |
|
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: 232.66 E-value: 2.03e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 12 TTVVADTGDIAAMK----LYQPQDATTNPSLILNAAqipeyrkliddavawakqqsndraqqivdatDKLAVNIGLEILK 87
Cdd:COG0176 1 MKLWLDTADREEIKelidLGGVDGVTTNPSLIAKAG-------------------------------IKDFVEDIREICD 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 88 LVPGRISTEVdarLSYDTDASIAKAKRLIKMYndagisNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARAC 167
Cdd:COG0176 50 IVDGPVSAEV---LATDTEGMIAEARRLAALY------RPNVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQALLA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 168 AEAGVYLISPFVGRILDWykantdkkeyapAEDpGVVSVTEIYEYYKQHGYETVVMGASFRNIGEIIE--LAGCDRLTIA 245
Cdd:COG0176 121 AEAGASYVSPFVGRIDDI------------GID-GIALVREIYQIYKNYGARTRILAASFRNPLQVLEaaLAGADTVTIP 187
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489109116 246 PALLKELAESegaierklsfsgevkarpariteaeflwqhnqdpmavDKLADGIRKFAVDQGKL 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: 671.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 1 MTDKLTSLRQFTTVVADTGDIAAMKLYQPQDATTNPSLILNAAQIPEYRKLIDDAVAWAKQQSNDRAQQIVDATDKLAVN 80
Cdd:PRK05269 1 MTNKLEQLKQFTTVVADTGDIEAIKKYQPQDATTNPSLILKAAQIPEYAPLIDDAVAWAKQQSGDRAQQIDDAIDKLAVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 81 IGLEILKLVPGRISTEVDARLSYDTDASIAKAKRLIKMYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFS 160
Cdd:PRK05269 81 FGLEILKLIPGRVSTEVDARLSFDTEATIAKARKLIALYEEAGISKDRILIKIASTWEGIRAAEQLEKEGINCNLTLLFS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 161 FAQARACAEAGVYLISPFVGRILDWYKANTDKKEYAPAEDPGVVSVTEIYEYYKQHGYETVVMGASFRNIGEIIELAGCD 240
Cdd:PRK05269 161 FAQARACAEAGVFLISPFVGRILDWYKKNTGKKEYAPAEDPGVVSVTKIYNYYKKHGYKTVVMGASFRNTGQILELAGCD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489109116 241 RLTIAPALLKELAESEGAIERKLSFSGEVKARPARITEAEFLWQHNQDPMAVDKLADGIRKFAVDQGKLEKMIGDLL 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: 580.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 3 DKLTSLRQFTTVVADTGDIAAMKLYQPQDATTNPSLILNAAQIPEYRKLIDDAVAWAKQQSNDRAQQIVDATDKLAVNIG 82
Cdd:TIGR00874 1 NQLDQLKQFTVVVADTGDIEAIKKYQPQDATTNPSLILAAAQLPKYAELIDEAVAWGKKQGKDDAQQVENALDKLAVNFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 83 LEILKLVPGRISTEVDARLSYDTDASIAKAKRLIKMYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFA 162
Cdd:TIGR00874 81 LEILKIVPGRVSTEVDARLSFDTEATVEKARHLIKLYEDAGVDKKRILIKIASTWEGIRAAEELEKEGIHCNLTLLFSFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 163 QARACAEAGVYLISPFVGRILDWYKANTDKKEYAPAEDPGVVSVTEIYEYYKQHGYETVVMGASFRNIGEIIELAGCDRL 242
Cdd:TIGR00874 161 QAIACAEAKVTLISPFVGRILDWYKAATGKKEYSIEEDPGVASVKKIYNYYKKHGYPTEVMGASFRNKEEILALAGCDRL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489109116 243 TIAPALLKELAESEGAIERKLSFSGE--VKARPARITEAEFLWQHNQDPMAVDKLADGIRKFAVDQGKLEKMIGDLL 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: 569.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 2 TDKLTSLRQFTTVVADTGDIAAMKLYQPQDATTNPSLILNAAQIPEYRKLIDDAVAWAKQQSNDRAQQIVDATDKLAVNI 81
Cdd:PRK12346 1 MNQLDGIKQFTTVVADSGDIESIRHYHPQDATTNPSLLLKAAGLPQYQHLIDDAIAWGKKQGGTQEQQVVAACDKLAVNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 82 GLEILKLVPGRISTEVDARLSYDTDASIAKAKRLIKMYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSF 161
Cdd:PRK12346 81 GAEILKSVPGRVSTEVDARLSFDREKSIEKARHLVDLYQQQGIDKSRILIKLASTWEGIRAAEELEKEGINCNLTLLFSF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 162 AQARACAEAGVYLISPFVGRILDWYKANTDKKEYAPAEDPGVVSVTEIYEYYKQHGYETVVMGASFRNIGEIIELAGCDR 241
Cdd:PRK12346 161 AQARACAEAGVFLISPFVGRIYDWYQARKPMDPYVVEEDPGVKSVRNIYDYYKQHRYETIVMGASFRRTEQILALAGCDR 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489109116 242 LTIAPALLKELAESEGAIERKLSFSGEVKARPARITEAEFLWQHNQDPMAVDKLADGIRKFAVDQGKLEKMIGDLL 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: 541.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 4 KLTSLRQFTTVVADTGDIAAMKLYQPQDATTNPSLILNAAQIPEYRKLIDDAVAWAKQQSNDRAQQIVDATDKLAVNIGL 83
Cdd:cd00957 2 QLDQLKKFTTIVADTGDFEAIKKFKPQDATTNPSLILAAAKLPEYNKLVDEAIAYAKKKGGSDEDQISNALDKLLVNFGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 84 EILKLVPGRISTEVDARLSYDTDASIAKAKRLIKMYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQ 163
Cdd:cd00957 82 EILKLIPGRVSTEVDARLSFDTNATIAKARKLIKLYEEAGIDKERILIKIAATWEGIQAAKQLEKEGIHCNLTLLFSFAQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 164 ARACAEAGVYLISPFVGRILDWYKANTDKKEYAPAEDPGVVSVTEIYEYYKQHGYETVVMGASFRNIGEIIELAGCDRLT 243
Cdd:cd00957 162 AVACAEAGVTLISPFVGRILDWYKKHSGDKAYTAEEDPGVASVKKIYNYYKKFGYKTKVMGASFRNIGQILALAGCDYLT 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489109116 244 IAPALLKELAESEGAIERKLS--FSGEVKARPARITEAEFLWQHNQDPMAVDKLADGIRKFAVDQGKLEKMI 313
Cdd:cd00957 242 ISPALLEELKNSTAKVERKLDpaASKALDIHPNFLDESAFRWALNEDAMAVEKLSEGIRGFAKDAVKLEKLI 313
|
|
| PTZ00411 |
PTZ00411 |
transaldolase-like protein; Provisional |
1-317 |
2.74e-180 |
|
transaldolase-like protein; Provisional
Pssm-ID: 240406 Cd Length: 333 Bit Score: 500.81 E-value: 2.74e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 1 MTDKLTSLRQFTTVVADTGDIAAMKLYQPQDATTNPSLILNAAQIPEYRKLIDDAVAWAKQQS----------NDRAQQI 70
Cdd:PTZ00411 1 MPNQLEALKEHTTVVADTGDFSLLKKFQPEDATTNPSLVLAAAQMPEYAHLIDDAIKYAKANVsrlrdpllsdEEKEELV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 71 VDATDKLAVNIGLEILKLVPGRISTEVDARLSYDTDASIAKAKRLIKMYNDAGISNDRILIKLASTWQGIRAAEQLEKEG 150
Cdd:PTZ00411 81 ELVVDKLTVNFGVEILKIVPGRVSTEVDARLSFDKQAMVDKARKIIKMYEEAGISKDRILIKLASTWEGIQAAKALEKEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 151 INCNLTLLFSFAQARACAEAGVYLISPFVGRILDWYKANTDKKEYAPAEDPGVVSVTEIYEYYKQHGYETVVMGASFRNI 230
Cdd:PTZ00411 161 IHCNLTLLFSFAQAVACAQAGVTLISPFVGRILDWYKKPEKAESYVGAQDPGVISVTKIYNYYKKHGYKTIVMGASFRNT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 231 GEIIELAGCDRLTIAPALLKELAESEGA-IERKLSFSGEVKARPARI--TEAEFLWQHNQDPMAVDKLADGIRKFAVDQG 307
Cdd:PTZ00411 241 GEILELAGCDKLTISPKLLEELANTEDGpVERKLDPEKLTEDTEKLPelTEKEFRWELNEDAMATEKLAEGIRNFAKDLE 320
|
330
....*....|
gi 489109116 308 KLEKMIGDLL 317
Cdd:PTZ00411 321 KLENVIRAKL 330
|
|
| PRK12309 |
PRK12309 |
transaldolase; |
1-317 |
2.18e-169 |
|
transaldolase;
Pssm-ID: 183426 [Multi-domain] Cd Length: 391 Bit Score: 475.76 E-value: 2.18e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 1 MTDKLTSLRQFTTVVADTGDIAAMKLYQPQDATTNPSLILNAAQIPEYRKLIDDAVAWAKQQSNDRA--QQIV-DATDKL 77
Cdd:PRK12309 2 MASLLEQLRQMTVVVADTGDIQAIEKFTPRDATTNPSLITAAAQMPQYQSIVDETLRQARKELGSDApvEDVVaLAFDRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 78 AVNIGLEILKLVPGRISTEVDARLSYDTDASIAKAKRLIKMYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTL 157
Cdd:PRK12309 82 AVAFGLKILKIVPGRVSTEVDARLSYDTEATIAKARKLISLYEDAGISRDRVLIKIASTWEGIKAAEVLEKEGIHCNLTL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 158 LFSFAQARACAEAGVYLISPFVGRILDWYKANTDKKEYAPAEDPGVVSVTEIYEYYKQHGYETVVMGASFRNIGEIIELA 237
Cdd:PRK12309 162 LFGFHQAIACAEAGVTLISPFVGRILDWYKKETGRDSYPGAEDPGVQSVTQIYNYYKKFGYKTEVMGASFRNIGEIIELA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 238 GCDRLTIAPALLKELAESEGAIERKLSFSGEVKARPARIT--EAEFLWQHNQDPMAVDKLADGIRKFAVDQGKLEKMIGD 315
Cdd:PRK12309 242 GCDLLTISPKLLEQLRSTEAELPRKLDPANAAGMEIEKIHmdRATFDKMHAEDRMASEKLDEGIKGFSKALETLEKLLAH 321
|
..
gi 489109116 316 LL 317
Cdd:PRK12309 322 RL 323
|
|
| TAL_FSA |
pfam00923 |
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ... |
14-257 |
5.86e-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: 282.89 E-value: 5.86e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 14 VVADTGDIAAMKLYQP----QDATTNPSLILNAAqipEYRKLIDDAVAwakqqsndraqqivdatdklavniglEILKLV 89
Cdd:pfam00923 1 IWLDTADRDLIKKLIEeggiDGVTTNPSIFLKAI---EYSALYDEAIA--------------------------EIKEIG 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 90 PGRISTEVDARLSYDTDASIAKAKRLIKMYNDagisnDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAE 169
Cdd:pfam00923 52 DGPVSLEVDPRLADDTEGTIEEARRLIALYGR-----PNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALAAAE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 170 AGVYLISPFVGRILDWYKANTDKkeyAPAEDPGVVSVTEIYEYYKQHGYETVVMGASFRNIGEIIELAGCDRLTIAPALL 249
Cdd:pfam00923 127 AGASVISPFVGRIDDWGDKRLGA---ALRGDDGIANAKEIYQIYKKYGWSTGVLAASFRNVLYVLALAGCDTITIPPDTL 203
|
....*...
gi 489109116 250 KELAESEG 257
Cdd:pfam00923 204 EALAKDEG 211
|
|
| Transaldolase |
cd00439 |
Transaldolase; Transaldolase. Enzymes found in the non-oxidative branch of the pentose ... |
13-253 |
2.46e-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: 239.18 E-value: 2.46e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 13 TVVADTGDIAAMKLYQ----PQDATTNPSLILNAAQIPEYRKLIDDAVAWAKQQSNDRAQQIVDATDKLAVNIGLEILKL 88
Cdd:cd00439 1 SPWYDTLDRPATDLLPlirgVRGVTTNPSIIQAAISTSNAYNDQFRTLVESGKDIESAYWELVVKDIQDACKLFEPIYDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 89 V--PGRISTEVDARLSYDTDASIAKAKRLIKMYNDagisnDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARA 166
Cdd:cd00439 81 TeaDGRVSVEVSARLADDTQGMVEAAKYLSKVVNR-----RNIYIKIPATAEGIPAIKDLIAAGISVNVTLIFSIAQYEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 167 CAEAGVYLISPFVGRILDWYKANTDKKEYAPAEDPGVVSVTEIYEYYKQHGYETVVMGASFRNIGEIIELAGCDRLTIAP 246
Cdd:cd00439 156 VADAGTSVASPFVSRIDTLMDKMLEQIGLDLRGKAGVAQVTLAYKLYKQKFKKQRVLWASFSDTLYVAPLIGCDTVTTMP 235
|
....*..
gi 489109116 247 ALLKELA 253
Cdd:cd00439 236 DQALEAG 242
|
|
| TalA |
COG0176 |
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ... |
12-309 |
2.03e-76 |
|
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: 232.66 E-value: 2.03e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 12 TTVVADTGDIAAMK----LYQPQDATTNPSLILNAAqipeyrkliddavawakqqsndraqqivdatDKLAVNIGLEILK 87
Cdd:COG0176 1 MKLWLDTADREEIKelidLGGVDGVTTNPSLIAKAG-------------------------------IKDFVEDIREICD 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 88 LVPGRISTEVdarLSYDTDASIAKAKRLIKMYndagisNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARAC 167
Cdd:COG0176 50 IVDGPVSAEV---LATDTEGMIAEARRLAALY------RPNVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQALLA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 168 AEAGVYLISPFVGRILDWykantdkkeyapAEDpGVVSVTEIYEYYKQHGYETVVMGASFRNIGEIIE--LAGCDRLTIA 245
Cdd:COG0176 121 AEAGASYVSPFVGRIDDI------------GID-GIALVREIYQIYKNYGARTRILAASFRNPLQVLEaaLAGADTVTIP 187
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489109116 246 PALLKELAESegaierklsfsgevkarpariteaeflwqhnqdpmavDKLADGIRKFAVDQGKL 309
Cdd:COG0176 188 PAVLEALADH-------------------------------------PLTDEGIEKFLADWEKL 214
|
|
| Transaldolase_FSA |
cd00956 |
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ... |
17-256 |
2.70e-31 |
|
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: 116.52 E-value: 2.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 17 DTGDIAAMKLYQPQ----DATTNPSLIlnaaqipeyrkliddavawAKQQSNDRAQQIvdatdklavnigLEILKLVPGR 92
Cdd:cd00956 5 DTADLEEIKKASETglldGVTTNPSLI-------------------AKSGRIDFEAVL------------KEICEIIDGP 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 93 ISTEVDARlsyDTDASIAKAKRLIKMyndagisNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAEAGV 172
Cdd:cd00956 54 VSAQVVST---DAEGMVAEARKLASL-------GGNVVVKIPVTEDGLKAIKKLSEEGIKTNVTAIFSAAQALLAAKAGA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 173 YLISPFVGRIldwykANTdkkeyapAEDPGVVsVTEIYEYYKQHGYETVVMGASFRNIGEIIE--LAGCDRLTIAPALLK 250
Cdd:cd00956 124 TYVSPFVGRI-----DDL-------GGDGMEL-IREIRTIFDNYGFDTKILAASIRNPQHVIEaaLAGADAITLPPDVLE 190
|
....*.
gi 489109116 251 ELAESE 256
Cdd:cd00956 191 QLLKHP 196
|
|
| fsa_talC_mipB |
TIGR00875 |
fructose-6-phosphate aldolase, TalC/MipB family; This model represents a family that includes ... |
84-261 |
1.84e-20 |
|
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: 87.61 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 84 EILKLVPGRISTEVdarLSYDTDASIAKAKRLIKMyndagisNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQ 163
Cdd:TIGR00875 45 EIQEAVEGPVSAET---ISLDAEGMVEEAKELAKL-------APNIVVKIPMTSEGLKAVKILKKEGIKTNVTLVFSAAQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 164 ARACAEAGVYLISPFVGRILDwykantdkkeyapAEDPGVVSVTEIYEYYKQHGYETVVMGASFRNIGEIIE--LAGCDR 241
Cdd:TIGR00875 115 ALLAAKAGATYVSPFVGRLDD-------------IGGDGMKLIEEVKTIFENHAPDTEVIAASVRHPRHVLEaaLIGADI 181
|
170 180
....*....|....*....|...
gi 489109116 242 LTIAPALLKELAE---SEGAIER 261
Cdd:TIGR00875 182 ATMPLDVMQQLFNhplTDIGLER 204
|
|
| Transaldolase_like |
cd00955 |
Transaldolase-like proteins from plants and bacteria; Transaldolase-like proteins from plants ... |
32-216 |
2.97e-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: 86.61 E-value: 2.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 32 ATTNPSLILNA-AQIPEYrkliDDAVAWAKQQSNDRA--------QQIVDATDKLAVNigLEILKLVPGRISTEVDARLS 102
Cdd:cd00955 29 VTSNPAIFEKAiAGSAAY----DDQIRALKGQGLDAEaiyealaiEDIQDACDLLAPV--YEQTGGNDGYVSLEVSPRLA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 103 YDTDASIAKAKRLikmYNDAGISNdrILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAEAgvYL-------- 174
Cdd:cd00955 103 DDTQGTIAEAKRL---WKAVGRPN--LMIKIPATEAGLPAIEELIAAGISVNVTLIFSLEQYEAVAEA--YLrglerrve 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489109116 175 -----------ISPFVGRIldwyKANTDKKEYAPAEDP-----GVVSVTEIYEYYKQH 216
Cdd:cd00955 176 gggdlsqvasvASFFVSRV----DTLIDKKLDAPEAKAlqgkvAIANAKLAYQEYQEK 229
|
|
| PRK03903 |
PRK03903 |
transaldolase; Provisional |
91-226 |
4.95e-16 |
|
transaldolase; Provisional
Pssm-ID: 235171 Cd Length: 274 Bit Score: 76.56 E-value: 4.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 91 GRISTEVDARLSYDTDASIAKAKRLIKmyndaGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAEA 170
Cdd:PRK03903 43 GFISIEIDPFLEDDAAGSIEEGKRLYK-----TIGRPNVMIKVPATKAGYEAMSALMKKGISVNATLIFSPEQAKECAEA 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489109116 171 -------------GVylISPFVGRI---LDwykaNTDKKEYAPAEdPGVVSVTEIYEY-YKQHGYETVVMGAS 226
Cdd:PRK03903 118 lneglkkntkdpkAV--ISVFVSRFdrlLD----PKLAPKNLQAK-SGIMNATKCYNQiEQHANKNIRTLFAS 183
|
|
| PRK03343 |
PRK03343 |
transaldolase; Validated |
33-170 |
6.75e-15 |
|
transaldolase; Validated
Pssm-ID: 235117 Cd Length: 368 Bit Score: 74.47 E-value: 6.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 33 TTNPSLILNA--------AQIPE-----------YRKLIDDAVAWAKqqsnDRAQQIVDATDKlavnigleilklVPGRI 93
Cdd:PRK03343 43 TSNPAIFQKAiaggdaydAQIAElaaagadveeaYEELTTADVRNAC----DVLRPVYEATGG------------VDGRV 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489109116 94 STEVDARLSYDTDASIAKAKRLIKMyndagISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAEA 170
Cdd:PRK03343 107 SIEVSPRLAHDTEATIAEARRLWAA-----VDRPNLMIKIPATPEGLPAIEALIAEGISVNVTLIFSVERYRAVADA 178
|
|
| PRK09533 |
PRK09533 |
bifunctional transaldolase/phosoglucose isomerase; Validated |
91-170 |
1.18e-10 |
|
bifunctional transaldolase/phosoglucose isomerase; Validated
Pssm-ID: 236551 [Multi-domain] Cd Length: 948 Bit Score: 62.30 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 91 GRISTEVDARLSYDTDASIAKAKRLIKMYNdagisNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAEA 170
Cdd:PRK09533 104 GFVSLEVSPYLALDTEGTIAEARRLWAAVD-----RPNLMIKVPATPEGLPAIRQLIAEGINVNVTLLFSQDVYEEVAEA 178
|
|
| PRK12653 |
PRK12653 |
fructose-6-phosphate aldolase; Reviewed |
17-244 |
1.48e-06 |
|
fructose-6-phosphate aldolase; Reviewed
Pssm-ID: 183653 [Multi-domain] Cd Length: 220 Bit Score: 48.24 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 17 DTGDIAAMK----LYQPQDATTNPSLilnaaqipeyrkliddaVAWAKQQSNDRAQQIVDAtdklavnIGLEilklvpGR 92
Cdd:PRK12653 6 DTSDVVAVKalsrIFPLAGVTTNPSI-----------------IAAGKKPLEVVLPQLHEA-------MGGQ------GR 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 93 ISTEVdarLSYDTDASIAKAKRLIKMYNDagisndrILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAEAGV 172
Cdd:PRK12653 56 LFAQV---MATTAEGMVNDARKLRSIIAD-------IVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGA 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489109116 173 YLISPFVGRIlDWYKANtdkkeyapaedpGVVSVTEIYEYYKQHGYETVVMGASFRNIGEIIE--LAGCDRLTI 244
Cdd:PRK12653 126 EYVAPYVNRI-DAQGGS------------GIQTVTDLQQLLKMHAPQAKVLAASFKTPRQALDclLAGCESITL 186
|
|
| PRK12656 |
PRK12656 |
fructose-6-phosphate aldolase; Reviewed |
104-250 |
2.77e-03 |
|
fructose-6-phosphate aldolase; Reviewed
Pssm-ID: 183656 [Multi-domain] Cd Length: 222 Bit Score: 38.57 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489109116 104 DTDASIAKAKRLIKMYNDAgisndrILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAEAGVYLISPFVGRIL 183
Cdd:PRK12656 65 DYEGILKDAHEIRRQCGDD------VYIKVPVTPAGLAAIKTLKAEGYHITATAIYTVFQGLLAIEAGADYLAPYYNRME 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489109116 184 DwykANTDKKEYapaedpgvvsVTEIYEYYKQHGYETVVMGASFRNIGEIIE--LAGCDRLTIAPALLK 250
Cdd:PRK12656 139 N---LNIDSNAV----------IGQLAEAIDRENSDSKILAASFKNVAQVNKafALGAQAVTAGPDVFE 194
|
|
| |
