|
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: 586.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 1 MTSKLEQLRAITTVVADTGDIEAVARLKPVDCTTNPTIVLKALGTPAFADAVKEAVAWGKKQGGQSDAVVAAVADRLAIS 80
Cdd:PRK05269 1 MTNKLEQLKQFTTVVADTGDIEAIKKYQPQDATTNPSLILKAAQIPEYAPLIDDAVAWAKQQSGDRAQQIDDAIDKLAVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 81 VGAALAGLVPGRVSTEVDADLSFDTEASITKARHIIAAYKERGIERERILIKLASTWEGIKAAEVLQSEGIDCNLTLLFS 160
Cdd:PRK05269 81 FGLEILKLIPGRVSTEVDARLSFDTEATIAKARKLIALYEEAGISKDRILIKIASTWEGIRAAEQLEKEGINCNLTLLFS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 161 QAQAIACAEAKVFLISPFVGRILDWYKKSTGE-NYTAETDPGVVSVRSIYNYYKANGISTVVMGASFRNVGEIEALAGCD 239
Cdd:PRK05269 161 FAQARACAEAGVFLISPFVGRILDWYKKNTGKkEYAPAEDPGVVSVTKIYNYYKKHGYKTVVMGASFRNTGQILELAGCD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490580215 240 RLTISPALLEELDKDTGKLERKLSADNVKAEPLQSLDEKAFRWALNEDAMATEKLSEGIRLFAKDLVTLREMVRKEL 316
Cdd:PRK05269 241 RLTISPALLEELAASEGELERKLSPPGEAKARPVPLTEAEFRWQHNEDAMATEKLAEGIRKFAKDQEKLEKLIAAKL 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: 511.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 3 SKLEQLRAITTVVADTGDIEAVARLKPVDCTTNPTIVLKALGTPAFADAVKEAVAWGKKQGGQSDAVVAAVADRLAISVG 82
Cdd:cd00957 1 NQLDQLKKFTTIVADTGDFEAIKKFKPQDATTNPSLILAAAKLPEYNKLVDEAIAYAKKKGGSDEDQISNALDKLLVNFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 83 AALAGLVPGRVSTEVDADLSFDTEASITKARHIIAAYKERGIERERILIKLASTWEGIKAAEVLQSEGIDCNLTLLFSQA 162
Cdd:cd00957 81 TEILKLIPGRVSTEVDARLSFDTNATIAKARKLIKLYEEAGIDKERILIKIAATWEGIQAAKQLEKEGIHCNLTLLFSFA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 163 QAIACAEAKVFLISPFVGRILDWYKKSTG-ENYTAETDPGVVSVRSIYNYYKANGISTVVMGASFRNVGEIEALAGCDRL 241
Cdd:cd00957 161 QAVACAEAGVTLISPFVGRILDWYKKHSGdKAYTAEEDPGVASVKKIYNYYKKFGYKTKVMGASFRNIGQILALAGCDYL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490580215 242 TISPALLEELDKDTGKLERKLSADNVKAEPLQS--LDEKAFRWALNEDAMATEKLSEGIRLFAKDLVTLREMV 312
Cdd:cd00957 241 TISPALLEELKNSTAKVERKLDPAASKALDIHPnfLDESAFRWALNEDAMAVEKLSEGIRGFAKDAVKLEKLI 313
|
|
| talAB |
TIGR00874 |
transaldolase; This family includes the majority of known and predicted transaldolase ... |
3-316 |
3.20e-163 |
|
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: 457.30 E-value: 3.20e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 3 SKLEQLRAITTVVADTGDIEAVARLKPVDCTTNPTIVLKALGTPAFADAVKEAVAWGKKQGGQSDAVVAAVADRLAISVG 82
Cdd:TIGR00874 1 NQLDQLKQFTVVVADTGDIEAIKKYQPQDATTNPSLILAAAQLPKYAELIDEAVAWGKKQGKDDAQQVENALDKLAVNFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 83 AALAGLVPGRVSTEVDADLSFDTEASITKARHIIAAYKERGIERERILIKLASTWEGIKAAEVLQSEGIDCNLTLLFSQA 162
Cdd:TIGR00874 81 LEILKIVPGRVSTEVDARLSFDTEATVEKARHLIKLYEDAGVDKKRILIKIASTWEGIRAAEELEKEGIHCNLTLLFSFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 163 QAIACAEAKVFLISPFVGRILDWYKKSTG-ENYTAETDPGVVSVRSIYNYYKANGISTVVMGASFRNVGEIEALAGCDRL 241
Cdd:TIGR00874 161 QAIACAEAKVTLISPFVGRILDWYKAATGkKEYSIEEDPGVASVKKIYNYYKKHGYPTEVMGASFRNKEEILALAGCDRL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490580215 242 TISPALLEELDKDTGKLERKL---SADNVKAEPlQSLDEKAFRWALNEDAMATEKLSEGIRLFAKDLVTLREMVRKEL 316
Cdd:TIGR00874 241 TISPALLDELKESTGPVERKLdpeSAKKVDKQP-IILDESEFRFLHNEDAMATEKLAEGIRKFAADQEKLEKLLEEKL 317
|
|
| TAL_FSA |
pfam00923 |
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ... |
14-256 |
5.22e-88 |
|
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: 262.86 E-value: 5.22e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 14 VVADTGDIEAVARLKP----VDCTTNPTIVLKAL-GTPAFADAVKEavawgkkqggqsdavvaavadrlaisvgaaLAGL 88
Cdd:pfam00923 1 IWLDTADRDLIKKLIEeggiDGVTTNPSIFLKAIeYSALYDEAIAE------------------------------IKEI 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 89 VPGRVSTEVDADLSFDTEASITKARHIIAAYkergiERERILIKLASTWEGIKAAEVLQSEGIDCNLTLLFSQAQAIACA 168
Cdd:pfam00923 51 GDGPVSLEVDPRLADDTEGTIEEARRLIALY-----GRPNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALAAA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 169 EAKVFLISPFVGRILDWYKKSTGEnyTAETDPGVVSVRSIYNYYKANGISTVVMGASFRNVGEIEALAGCDRLTISPALL 248
Cdd:pfam00923 126 EAGASVISPFVGRIDDWGDKRLGA--ALRGDDGIANAKEIYQIYKKYGWSTGVLAASFRNVLYVLALAGCDTITIPPDTL 203
|
....*...
gi 490580215 249 EELDKDTG 256
Cdd:pfam00923 204 EALAKDEG 211
|
|
| TalA |
COG0176 |
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ... |
12-254 |
7.52e-69 |
|
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: 213.78 E-value: 7.52e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 12 TTVVADTGDIEAVARLK----PVDCTTNPTIVLKALGTPAFADavkeavawgkkqggqsdavvaavadrlaisvGAALAG 87
Cdd:COG0176 1 MKLWLDTADREEIKELIdlggVDGVTTNPSLIAKAGIKDFVED-------------------------------IREICD 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 88 LVPGRVSTEVdadLSFDTEASITKARHIIAAYkergieRERILIKLASTWEGIKAAEVLQSEGIDCNLTLLFSQAQAIAC 167
Cdd:COG0176 50 IVDGPVSAEV---LATDTEGMIAEARRLAALY------RPNVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQALLA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 168 AEAKVFLISPFVGRILDWykkstGENytaetdpGVVSVRSIYNYYKANGISTVVMGASFRNVGEIE--ALAGCDRLTISP 245
Cdd:COG0176 121 AEAGASYVSPFVGRIDDI-----GID-------GIALVREIYQIYKNYGARTRILAASFRNPLQVLeaALAGADTVTIPP 188
|
....*....
gi 490580215 246 ALLEELDKD 254
Cdd:COG0176 189 AVLEALADH 197
|
|
| |
|
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: 586.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 1 MTSKLEQLRAITTVVADTGDIEAVARLKPVDCTTNPTIVLKALGTPAFADAVKEAVAWGKKQGGQSDAVVAAVADRLAIS 80
Cdd:PRK05269 1 MTNKLEQLKQFTTVVADTGDIEAIKKYQPQDATTNPSLILKAAQIPEYAPLIDDAVAWAKQQSGDRAQQIDDAIDKLAVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 81 VGAALAGLVPGRVSTEVDADLSFDTEASITKARHIIAAYKERGIERERILIKLASTWEGIKAAEVLQSEGIDCNLTLLFS 160
Cdd:PRK05269 81 FGLEILKLIPGRVSTEVDARLSFDTEATIAKARKLIALYEEAGISKDRILIKIASTWEGIRAAEQLEKEGINCNLTLLFS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 161 QAQAIACAEAKVFLISPFVGRILDWYKKSTGE-NYTAETDPGVVSVRSIYNYYKANGISTVVMGASFRNVGEIEALAGCD 239
Cdd:PRK05269 161 FAQARACAEAGVFLISPFVGRILDWYKKNTGKkEYAPAEDPGVVSVTKIYNYYKKHGYKTVVMGASFRNTGQILELAGCD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490580215 240 RLTISPALLEELDKDTGKLERKLSADNVKAEPLQSLDEKAFRWALNEDAMATEKLSEGIRLFAKDLVTLREMVRKEL 316
Cdd:PRK05269 241 RLTISPALLEELAASEGELERKLSPPGEAKARPVPLTEAEFRWQHNEDAMATEKLAEGIRKFAKDQEKLEKLIAAKL 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: 511.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 3 SKLEQLRAITTVVADTGDIEAVARLKPVDCTTNPTIVLKALGTPAFADAVKEAVAWGKKQGGQSDAVVAAVADRLAISVG 82
Cdd:cd00957 1 NQLDQLKKFTTIVADTGDFEAIKKFKPQDATTNPSLILAAAKLPEYNKLVDEAIAYAKKKGGSDEDQISNALDKLLVNFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 83 AALAGLVPGRVSTEVDADLSFDTEASITKARHIIAAYKERGIERERILIKLASTWEGIKAAEVLQSEGIDCNLTLLFSQA 162
Cdd:cd00957 81 TEILKLIPGRVSTEVDARLSFDTNATIAKARKLIKLYEEAGIDKERILIKIAATWEGIQAAKQLEKEGIHCNLTLLFSFA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 163 QAIACAEAKVFLISPFVGRILDWYKKSTG-ENYTAETDPGVVSVRSIYNYYKANGISTVVMGASFRNVGEIEALAGCDRL 241
Cdd:cd00957 161 QAVACAEAGVTLISPFVGRILDWYKKHSGdKAYTAEEDPGVASVKKIYNYYKKFGYKTKVMGASFRNIGQILALAGCDYL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490580215 242 TISPALLEELDKDTGKLERKLSADNVKAEPLQS--LDEKAFRWALNEDAMATEKLSEGIRLFAKDLVTLREMV 312
Cdd:cd00957 241 TISPALLEELKNSTAKVERKLDPAASKALDIHPnfLDESAFRWALNEDAMAVEKLSEGIRGFAKDAVKLEKLI 313
|
|
| PRK12346 |
PRK12346 |
transaldolase A; Provisional |
2-316 |
7.85e-165 |
|
transaldolase A; Provisional
Pssm-ID: 183458 Cd Length: 316 Bit Score: 461.50 E-value: 7.85e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 2 TSKLEQLRAITTVVADTGDIEAVARLKPVDCTTNPTIVLKALGTPAFADAVKEAVAWGKKQGGQSDAVVAAVADRLAISV 81
Cdd:PRK12346 1 MNQLDGIKQFTTVVADSGDIESIRHYHPQDATTNPSLLLKAAGLPQYQHLIDDAIAWGKKQGGTQEQQVVAACDKLAVNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 82 GAALAGLVPGRVSTEVDADLSFDTEASITKARHIIAAYKERGIERERILIKLASTWEGIKAAEVLQSEGIDCNLTLLFSQ 161
Cdd:PRK12346 81 GAEILKSVPGRVSTEVDARLSFDREKSIEKARHLVDLYQQQGIDKSRILIKLASTWEGIRAAEELEKEGINCNLTLLFSF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 162 AQAIACAEAKVFLISPFVGRILDWYKKSTG-ENYTAETDPGVVSVRSIYNYYKANGISTVVMGASFRNVGEIEALAGCDR 240
Cdd:PRK12346 161 AQARACAEAGVFLISPFVGRIYDWYQARKPmDPYVVEEDPGVKSVRNIYDYYKQHRYETIVMGASFRRTEQILALAGCDR 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490580215 241 LTISPALLEELDKDTGKLERKLSADNVKAEPLQSLDEKAFRWALNEDAMATEKLSEGIRLFAKDLVTLREMVRKEL 316
Cdd:PRK12346 241 LTISPNLLKELQESESPVERKLIPSSQTFPRPAPMSEAEFRWEHNQDAMAVEKLSEGIRLFAVDQRKLEDLLAAKL 316
|
|
| talAB |
TIGR00874 |
transaldolase; This family includes the majority of known and predicted transaldolase ... |
3-316 |
3.20e-163 |
|
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: 457.30 E-value: 3.20e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 3 SKLEQLRAITTVVADTGDIEAVARLKPVDCTTNPTIVLKALGTPAFADAVKEAVAWGKKQGGQSDAVVAAVADRLAISVG 82
Cdd:TIGR00874 1 NQLDQLKQFTVVVADTGDIEAIKKYQPQDATTNPSLILAAAQLPKYAELIDEAVAWGKKQGKDDAQQVENALDKLAVNFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 83 AALAGLVPGRVSTEVDADLSFDTEASITKARHIIAAYKERGIERERILIKLASTWEGIKAAEVLQSEGIDCNLTLLFSQA 162
Cdd:TIGR00874 81 LEILKIVPGRVSTEVDARLSFDTEATVEKARHLIKLYEDAGVDKKRILIKIASTWEGIRAAEELEKEGIHCNLTLLFSFV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 163 QAIACAEAKVFLISPFVGRILDWYKKSTG-ENYTAETDPGVVSVRSIYNYYKANGISTVVMGASFRNVGEIEALAGCDRL 241
Cdd:TIGR00874 161 QAIACAEAKVTLISPFVGRILDWYKAATGkKEYSIEEDPGVASVKKIYNYYKKHGYPTEVMGASFRNKEEILALAGCDRL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490580215 242 TISPALLEELDKDTGKLERKL---SADNVKAEPlQSLDEKAFRWALNEDAMATEKLSEGIRLFAKDLVTLREMVRKEL 316
Cdd:TIGR00874 241 TISPALLDELKESTGPVERKLdpeSAKKVDKQP-IILDESEFRFLHNEDAMATEKLAEGIRKFAADQEKLEKLLEEKL 317
|
|
| PTZ00411 |
PTZ00411 |
transaldolase-like protein; Provisional |
1-319 |
2.14e-157 |
|
transaldolase-like protein; Provisional
Pssm-ID: 240406 Cd Length: 333 Bit Score: 443.03 E-value: 2.14e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 1 MTSKLEQLRAITTVVADTGDIEAVARLKPVDCTTNPTIVLKALGTPAFADAVKEAVAWGKKQGGQS----------DAVV 70
Cdd:PTZ00411 1 MPNQLEALKEHTTVVADTGDFSLLKKFQPEDATTNPSLVLAAAQMPEYAHLIDDAIKYAKANVSRLrdpllsdeekEELV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 71 AAVADRLAISVGAALAGLVPGRVSTEVDADLSFDTEASITKARHIIAAYKERGIERERILIKLASTWEGIKAAEVLQSEG 150
Cdd:PTZ00411 81 ELVVDKLTVNFGVEILKIVPGRVSTEVDARLSFDKQAMVDKARKIIKMYEEAGISKDRILIKLASTWEGIQAAKALEKEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 151 IDCNLTLLFSQAQAIACAEAKVFLISPFVGRILDWYKKSTG-ENYTAETDPGVVSVRSIYNYYKANGISTVVMGASFRNV 229
Cdd:PTZ00411 161 IHCNLTLLFSFAQAVACAQAGVTLISPFVGRILDWYKKPEKaESYVGAQDPGVISVTKIYNYYKKHGYKTIVMGASFRNT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 230 GEIEALAGCDRLTISPALLEELDK-DTGKLERKLSADNVKA--EPLQSLDEKAFRWALNEDAMATEKLSEGIRLFAKDLV 306
Cdd:PTZ00411 241 GEILELAGCDKLTISPKLLEELANtEDGPVERKLDPEKLTEdtEKLPELTEKEFRWELNEDAMATEKLAEGIRNFAKDLE 320
|
330
....*....|...
gi 490580215 307 TLREMVRKELTAA 319
Cdd:PTZ00411 321 KLENVIRAKLTEA 333
|
|
| PRK12309 |
PRK12309 |
transaldolase; |
1-317 |
1.03e-147 |
|
transaldolase;
Pssm-ID: 183426 [Multi-domain] Cd Length: 391 Bit Score: 420.68 E-value: 1.03e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 1 MTSKLEQLRAITTVVADTGDIEAVARLKPVDCTTNPTIVLKALGTPAFADAVKEAVAWGKKQGGQS---DAVVAAVADRL 77
Cdd:PRK12309 2 MASLLEQLRQMTVVVADTGDIQAIEKFTPRDATTNPSLITAAAQMPQYQSIVDETLRQARKELGSDapvEDVVALAFDRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 78 AISVGAALAGLVPGRVSTEVDADLSFDTEASITKARHIIAAYKERGIERERILIKLASTWEGIKAAEVLQSEGIDCNLTL 157
Cdd:PRK12309 82 AVAFGLKILKIVPGRVSTEVDARLSYDTEATIAKARKLISLYEDAGISRDRVLIKIASTWEGIKAAEVLEKEGIHCNLTL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 158 LFSQAQAIACAEAKVFLISPFVGRILDWYKKSTG-ENYTAETDPGVVSVRSIYNYYKANGISTVVMGASFRNVGEIEALA 236
Cdd:PRK12309 162 LFGFHQAIACAEAGVTLISPFVGRILDWYKKETGrDSYPGAEDPGVQSVTQIYNYYKKFGYKTEVMGASFRNIGEIIELA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 237 GCDRLTISPALLEELDKDTGKLERKLSADNVKAEPLQ--SLDEKAFRWALNEDAMATEKLSEGIRLFAKDLVTLREMVRK 314
Cdd:PRK12309 242 GCDLLTISPKLLEQLRSTEAELPRKLDPANAAGMEIEkiHMDRATFDKMHAEDRMASEKLDEGIKGFSKALETLEKLLAH 321
|
...
gi 490580215 315 ELT 317
Cdd:PRK12309 322 RLA 324
|
|
| TAL_FSA |
pfam00923 |
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ... |
14-256 |
5.22e-88 |
|
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: 262.86 E-value: 5.22e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 14 VVADTGDIEAVARLKP----VDCTTNPTIVLKAL-GTPAFADAVKEavawgkkqggqsdavvaavadrlaisvgaaLAGL 88
Cdd:pfam00923 1 IWLDTADRDLIKKLIEeggiDGVTTNPSIFLKAIeYSALYDEAIAE------------------------------IKEI 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 89 VPGRVSTEVDADLSFDTEASITKARHIIAAYkergiERERILIKLASTWEGIKAAEVLQSEGIDCNLTLLFSQAQAIACA 168
Cdd:pfam00923 51 GDGPVSLEVDPRLADDTEGTIEEARRLIALY-----GRPNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALAAA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 169 EAKVFLISPFVGRILDWYKKSTGEnyTAETDPGVVSVRSIYNYYKANGISTVVMGASFRNVGEIEALAGCDRLTISPALL 248
Cdd:pfam00923 126 EAGASVISPFVGRIDDWGDKRLGA--ALRGDDGIANAKEIYQIYKKYGWSTGVLAASFRNVLYVLALAGCDTITIPPDTL 203
|
....*...
gi 490580215 249 EELDKDTG 256
Cdd:pfam00923 204 EALAKDEG 211
|
|
| TalA |
COG0176 |
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ... |
12-254 |
7.52e-69 |
|
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: 213.78 E-value: 7.52e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 12 TTVVADTGDIEAVARLK----PVDCTTNPTIVLKALGTPAFADavkeavawgkkqggqsdavvaavadrlaisvGAALAG 87
Cdd:COG0176 1 MKLWLDTADREEIKELIdlggVDGVTTNPSLIAKAGIKDFVED-------------------------------IREICD 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 88 LVPGRVSTEVdadLSFDTEASITKARHIIAAYkergieRERILIKLASTWEGIKAAEVLQSEGIDCNLTLLFSQAQAIAC 167
Cdd:COG0176 50 IVDGPVSAEV---LATDTEGMIAEARRLAALY------RPNVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQALLA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 168 AEAKVFLISPFVGRILDWykkstGENytaetdpGVVSVRSIYNYYKANGISTVVMGASFRNVGEIE--ALAGCDRLTISP 245
Cdd:COG0176 121 AEAGASYVSPFVGRIDDI-----GID-------GIALVREIYQIYKNYGARTRILAASFRNPLQVLeaALAGADTVTIPP 188
|
....*....
gi 490580215 246 ALLEELDKD 254
Cdd:COG0176 189 AVLEALADH 197
|
|
| Transaldolase |
cd00439 |
Transaldolase; Transaldolase. Enzymes found in the non-oxidative branch of the pentose ... |
13-251 |
6.57e-60 |
|
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: 192.18 E-value: 6.57e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 13 TVVADTGDIEAVARLK----PVDCTTNPTIVLKALGTPAFADAVKEAVAWGKKQGGQSDAVVAAVADRLAISVGAAL--A 86
Cdd:cd00439 1 SPWYDTLDRPATDLLPlirgVRGVTTNPSIIQAAISTSNAYNDQFRTLVESGKDIESAYWELVVKDIQDACKLFEPIydQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 87 GLVPGRVSTEVDADLSFDTEASITKARHIIAAYKERgiereRILIKLASTWEGIKAAEVLQSEGIDCNLTLLFSQAQAIA 166
Cdd:cd00439 81 TEADGRVSVEVSARLADDTQGMVEAAKYLSKVVNRR-----NIYIKIPATAEGIPAIKDLIAAGISVNVTLIFSIAQYEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 167 CAEAKVFLISPFVGRILDWYKKSTGE-NYTAETDPGVVSVRSIYNYYKANGISTVVMGASFRNVGEIEALAGCDRLTISP 245
Cdd:cd00439 156 VADAGTSVASPFVSRIDTLMDKMLEQiGLDLRGKAGVAQVTLAYKLYKQKFKKQRVLWASFSDTLYVAPLIGCDTVTTMP 235
|
....*.
gi 490580215 246 ALLEEL 251
Cdd:cd00439 236 DQALEA 241
|
|
| Transaldolase_FSA |
cd00956 |
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ... |
16-254 |
2.92e-27 |
|
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: 105.74 E-value: 2.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 16 ADTGDIEAVARLKPVD-CTTNPTIVLKAlGTPAFADAVKEAVAwgkkqggqsdavvaavadrlaisvgaalagLVPGRVS 94
Cdd:cd00956 7 ADLEEIKKASETGLLDgVTTNPSLIAKS-GRIDFEAVLKEICE------------------------------IIDGPVS 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 95 TEVDADlsfDTEASITKARHIIAaykergiERERILIKLASTWEGIKAAEVLQSEGIDCNLTLLFSQAQAIACAEAKVFL 174
Cdd:cd00956 56 AQVVST---DAEGMVAEARKLAS-------LGGNVVVKIPVTEDGLKAIKKLSEEGIKTNVTAIFSAAQALLAAKAGATY 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 175 ISPFVGRILDwykksTGENytaetdpGVVSVRSIYNYYKANGISTVVMGASFRNVGEI--EALAGCDRLTISPALLEELD 252
Cdd:cd00956 126 VSPFVGRIDD-----LGGD-------GMELIREIRTIFDNYGFDTKILAASIRNPQHVieAALAGADAITLPPDVLEQLL 193
|
..
gi 490580215 253 KD 254
Cdd:cd00956 194 KH 195
|
|
| Transaldolase_like |
cd00955 |
Transaldolase-like proteins from plants and bacteria; Transaldolase-like proteins from plants ... |
33-303 |
4.22e-21 |
|
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: 92.00 E-value: 4.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 33 TTNPTIVLKALGTpafADAVKEAVAWGKKQGGQSDAVVAAVADRLAISVGAALA------GLVPGRVSTEVDADLSFDTE 106
Cdd:cd00955 30 TSNPAIFEKAIAG---SAAYDDQIRALKGQGLDAEAIYEALAIEDIQDACDLLApvyeqtGGNDGYVSLEVSPRLADDTQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 107 ASITKARHIIAAykergIERERILIKLASTWEGIKAAEVLQSEGIDCNLTLLFSQAQAIACAEA---------------- 170
Cdd:cd00955 107 GTIAEAKRLWKA-----VGRPNLMIKIPATEAGLPAIEELIAAGISVNVTLIFSLEQYEAVAEAylrglerrvegggdls 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 171 -KVFLISPFVGRIlDWYKKSTGENYTAETDPGVVSV---RSIYNYYK---------------ANGI-----STVVMGASF 226
Cdd:cd00955 182 qVASVASFFVSRV-DTLIDKKLDAPEAKALQGKVAIanaKLAYQEYQekfsgprwaalaaagAKPQrllwaSTGVKNPAY 260
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490580215 227 RNVGEIEALAGCDRLTISPALLEELDKDTGKLERKLSADNVKAEPLQSLDEKAfrwALNEDAMATEKLSEGIRLFAK 303
Cdd:cd00955 261 PDVLYVEELIGPDTVNTMPDATLKAFADHGEVRPTLEEGLEEAERVLAELERL---GIDLDAVTEKLLKEGVKKFKD 334
|
|
| fsa_talC_mipB |
TIGR00875 |
fructose-6-phosphate aldolase, TalC/MipB family; This model represents a family that includes ... |
16-251 |
2.73e-17 |
|
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: 79.13 E-value: 2.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 16 ADTGDIEAVARLKPVD-CTTNPTIVLKAlgTPAFADAVKEavawgkkqggqsdavvaavadrlaisvgaaLAGLVPGRVS 94
Cdd:TIGR00875 8 ANVEEIKKAAELGILAgVTTNPSLIAKE--GRSFWEVLKE------------------------------IQEAVEGPVS 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 95 TEVdadLSFDTEASITKARHIIAAYkergierERILIKLASTWEGIKAAEVLQSEGIDCNLTLLFSQAQAIACAEAKVFL 174
Cdd:TIGR00875 56 AET---ISLDAEGMVEEAKELAKLA-------PNIVVKIPMTSEGLKAVKILKKEGIKTNVTLVFSAAQALLAAKAGATY 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490580215 175 ISPFVGRILDwykksTGENytaetdpGVVSVRSIYNYYKANGISTVVMGASFRNVGEI--EALAGCDRLTISPALLEEL 251
Cdd:TIGR00875 126 VSPFVGRLDD-----IGGD-------GMKLIEEVKTIFENHAPDTEVIAASVRHPRHVleAALIGADIATMPLDVMQQL 192
|
|
| PRK03343 |
PRK03343 |
transaldolase; Validated |
33-170 |
3.74e-17 |
|
transaldolase; Validated
Pssm-ID: 235117 Cd Length: 368 Bit Score: 81.02 E-value: 3.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 33 TTNPTIVLKAL-GTPAFADAVKEAVAWGKkqgGQSDAV-------VAAVADRLAiSVGAALAGlVPGRVSTEVDADLSFD 104
Cdd:PRK03343 43 TSNPAIFQKAIaGGDAYDAQIAELAAAGA---DVEEAYeelttadVRNACDVLR-PVYEATGG-VDGRVSIEVSPRLAHD 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490580215 105 TEASITKARHIIAAykergIERERILIKLASTWEGIKAAEVLQSEGIDCNLTLLFSQAQAIACAEA 170
Cdd:PRK03343 118 TEATIAEARRLWAA-----VDRPNLMIKIPATPEGLPAIEALIAEGISVNVTLIFSVERYRAVADA 178
|
|
| PRK09533 |
PRK09533 |
bifunctional transaldolase/phosoglucose isomerase; Validated |
33-170 |
8.00e-15 |
|
bifunctional transaldolase/phosoglucose isomerase; Validated
Pssm-ID: 236551 [Multi-domain] Cd Length: 948 Bit Score: 75.01 E-value: 8.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 33 TTNPTIVLKALG-TPAFADAVKEAVAWGkkqggqsDAVVAAVADRLAIS-VGAALAGLVP---------GRVSTEVDADL 101
Cdd:PRK09533 42 TSNPAIFEKAIGsSDEYDDAIKAALAEG-------DRSVIELYETLAIEdIQAAADVLRPvydatdgadGFVSLEVSPYL 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490580215 102 SFDTEASITKARHIIAAykergIERERILIKLASTWEGIKAAEVLQSEGIDCNLTLLFSQAQAIACAEA 170
Cdd:PRK09533 115 ALDTEGTIAEARRLWAA-----VDRPNLMIKVPATPEGLPAIRQLIAEGINVNVTLLFSQDVYEEVAEA 178
|
|
| PRK03903 |
PRK03903 |
transaldolase; Provisional |
91-182 |
1.25e-10 |
|
transaldolase; Provisional
Pssm-ID: 235171 Cd Length: 274 Bit Score: 61.15 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 91 GRVSTEVDADLSFDTEASITKARHIiaaYKerGIERERILIKLASTWEGIKAAEVLQSEGIDCNLTLLFSQAQAIACAEA 170
Cdd:PRK03903 43 GFISIEIDPFLEDDAAGSIEEGKRL---YK--TIGRPNVMIKVPATKAGYEAMSALMKKGISVNATLIFSPEQAKECAEA 117
|
90 100
....*....|....*....|...
gi 490580215 171 -----KVF------LISPFVGRI 182
Cdd:PRK03903 118 lneglKKNtkdpkaVISVFVSRF 140
|
|
| PRK12653 |
PRK12653 |
fructose-6-phosphate aldolase; Reviewed |
17-243 |
3.26e-04 |
|
fructose-6-phosphate aldolase; Reviewed
Pssm-ID: 183653 [Multi-domain] Cd Length: 220 Bit Score: 41.30 E-value: 3.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 17 DTGDIEAVARLKPV----DCTTNPTIVLKalgtpafadavkeavawgkkqGGQSDAVVAAvadrlaiSVGAALAGlvPGR 92
Cdd:PRK12653 6 DTSDVVAVKALSRIfplaGVTTNPSIIAA---------------------GKKPLEVVLP-------QLHEAMGG--QGR 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490580215 93 VSTEVDADlsfDTEASITKARHIiaaykeRGIERErILIKLASTWEGIKAAEVLQSEGIDCNLTLLFSQAQAIACAEAKV 172
Cdd:PRK12653 56 LFAQVMAT---TAEGMVNDARKL------RSIIAD-IVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQGLLSALAGA 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490580215 173 FLISPFVGRIldwykkstgenyTAETDPGVVSVRSIYNYYKANGISTVVMGASFRNVGEIEA--LAGCDRLTI 243
Cdd:PRK12653 126 EYVAPYVNRI------------DAQGGSGIQTVTDLQQLLKMHAPQAKVLAASFKTPRQALDclLAGCESITL 186
|
|
| |
