|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05269 |
PRK05269 |
transaldolase B; Provisional |
11-329 |
0e+00 |
|
transaldolase B; Provisional
Pssm-ID: 235381 [Multi-domain] Cd Length: 318 Bit Score: 604.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 11 MESALDQLKQFTTVVADTGDFHAIDEYKPQDATTNPSLILAAAQMPAYQELVEEAIAYGRKLGGSQEDQIKNAIDKLFVL 90
Cdd:PRK05269 1 MTNKLEQLKQFTTVVADTGDIEAIKKYQPQDATTNPSLILKAAQIPEYAPLIDDAVAWAKQQSGDRAQQIDDAIDKLAVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 91 FGAEILKKIPGRVSTEVDARLSFDKDAMVARARRLIELYKEAGISKDRILIKLSSTWEGIQAGKELEEQhGIHCNMTLLF 170
Cdd:PRK05269 81 FGLEILKLIPGRVSTEVDARLSFDTEATIAKARKLIALYEEAGISKDRILIKIASTWEGIRAAEQLEKE-GINCNLTLLF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 171 SFAQAVACAEAGVTLISPFVGRILDWHVANTDKKSYEPLEDPGVKSVTKIYNYYKKFSYKTIVMGASFRNTGEIKALAGC 250
Cdd:PRK05269 160 SFAQARACAEAGVFLISPFVGRILDWYKKNTGKKEYAPAEDPGVVSVTKIYNYYKKHGYKTVVMGASFRNTGQILELAGC 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332368005 251 DFLTISPKLLGELLQDNAKLVPVLSAKAAQASDleKIHLDEKSFRWLHNEDQMAVEKLSDGIRKFAADAVKLERMLTER 329
Cdd:PRK05269 240 DRLTISPALLEELAASEGELERKLSPPGEAKAR--PVPLTEAEFRWQHNEDAMATEKLAEGIRKFAKDQEKLEKLIAAK 316
|
|
| Transaldolase_TalAB |
cd00957 |
Transaldolases including both TalA and TalB; Transaldolases including both TalA and TalB. The ... |
13-326 |
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: 582.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 13 SALDQLKQFTTVVADTGDFHAIDEYKPQDATTNPSLILAAAQMPAYQELVEEAIAYGRKLGGSQEDQIKNAIDKLFVLFG 92
Cdd:cd00957 1 NQLDQLKKFTTIVADTGDFEAIKKFKPQDATTNPSLILAAAKLPEYNKLVDEAIAYAKKKGGSDEDQISNALDKLLVNFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 93 AEILKKIPGRVSTEVDARLSFDKDAMVARARRLIELYKEAGISKDRILIKLSSTWEGIQAGKELEeQHGIHCNMTLLFSF 172
Cdd:cd00957 81 TEILKLIPGRVSTEVDARLSFDTNATIAKARKLIKLYEEAGIDKERILIKIAATWEGIQAAKQLE-KEGIHCNLTLLFSF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 173 AQAVACAEAGVTLISPFVGRILDWHVANTDKKSYEPLEDPGVKSVTKIYNYYKKFSYKTIVMGASFRNTGEIKALAGCDF 252
Cdd:cd00957 160 AQAVACAEAGVTLISPFVGRILDWYKKHSGDKAYTAEEDPGVASVKKIYNYYKKFGYKTKVMGASFRNIGQILALAGCDY 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332368005 253 LTISPKLLGELLQDNAKLVPVLSAKAAQASDLEKIHLDEKSFRWLHNEDQMAVEKLSDGIRKFAADAVKLERML 326
Cdd:cd00957 240 LTISPALLEELKNSTAKVERKLDPAASKALDIHPNFLDESAFRWALNEDAMAVEKLSEGIRGFAKDAVKLEKLI 313
|
|
| talAB |
TIGR00874 |
transaldolase; This family includes the majority of known and predicted transaldolase ... |
13-330 |
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: 526.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 13 SALDQLKQFTTVVADTGDFHAIDEYKPQDATTNPSLILAAAQMPAYQELVEEAIAYGRKLGGSQEDQIKNAIDKLFVLFG 92
Cdd:TIGR00874 1 NQLDQLKQFTVVVADTGDIEAIKKYQPQDATTNPSLILAAAQLPKYAELIDEAVAWGKKQGKDDAQQVENALDKLAVNFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 93 AEILKKIPGRVSTEVDARLSFDKDAMVARARRLIELYKEAGISKDRILIKLSSTWEGIQAGKELEeQHGIHCNMTLLFSF 172
Cdd:TIGR00874 81 LEILKIVPGRVSTEVDARLSFDTEATVEKARHLIKLYEDAGVDKKRILIKIASTWEGIRAAEELE-KEGIHCNLTLLFSF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 173 AQAVACAEAGVTLISPFVGRILDWHVANTDKKSYEPLEDPGVKSVTKIYNYYKKFSYKTIVMGASFRNTGEIKALAGCDF 252
Cdd:TIGR00874 160 VQAIACAEAKVTLISPFVGRILDWYKAATGKKEYSIEEDPGVASVKKIYNYYKKHGYPTEVMGASFRNKEEILALAGCDR 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332368005 253 LTISPKLLGELLQDNAKLVPVLSAKAAQASDLEKIHLDEKSFRWLHNEDQMAVEKLSDGIRKFAADAVKLERMLTERM 330
Cdd:TIGR00874 240 LTISPALLDELKESTGPVERKLDPESAKKVDKQPIILDESEFRFLHNEDAMATEKLAEGIRKFAADQEKLEKLLEEKL 317
|
|
| TAL_FSA |
pfam00923 |
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ... |
24-326 |
1.46e-93 |
|
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: 277.88 E-value: 1.46e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 24 VVADTGDFHAIDEYKP----QDATTNPSLILAAAQmpaYQELVEEAIAygrklggsqedqiknaidklfvlfgaEILKKI 99
Cdd:pfam00923 1 IWLDTADRDLIKKLIEeggiDGVTTNPSIFLKAIE---YSALYDEAIA--------------------------EIKEIG 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 100 PGRVSTEVDARLSFDKDAMVARARRLIELYKeagisKDRILIKLSSTWEGIQAGKELEeQHGIHCNMTLLFSFAQAVACA 179
Cdd:pfam00923 52 DGPVSLEVDPRLADDTEGTIEEARRLIALYG-----RPNVLIKIPATWEGIKAIKELS-AEGINVNVTLIFSLAQALAAA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 180 EAGVTLISPFVGRILDWHVANTDKksyEPLEDPGVKSVTKIYNYYKKFSYKTIVMGASFRNTGEIKALAGCDFLTISPKL 259
Cdd:pfam00923 126 EAGASVISPFVGRIDDWGDKRLGA---ALRGDDGIANAKEIYQIYKKYGWSTGVLAASFRNVLYVLALAGCDTITIPPDT 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332368005 260 LGELLQDnaklvpvlsakaaqasdlekihldeksfrwlhnedqmaveklsDGIRKFAADAVKLERML 326
Cdd:pfam00923 203 LEALAKD-------------------------------------------EGVRKFAKDWEKLLGSI 226
|
|
| TalA |
COG0176 |
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ... |
22-322 |
1.28e-72 |
|
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: 223.80 E-value: 1.28e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 22 TTVVADTGDFHAIDEYK----PQDATTNPSLILAAAqmpayqelveeaiaygrklggsqedqIKNAIDklfvlFGAEILK 97
Cdd:COG0176 1 MKLWLDTADREEIKELIdlggVDGVTTNPSLIAKAG--------------------------IKDFVE-----DIREICD 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 98 KIPGRVSTEVdarLSFDKDAMVARARRLIELYKEagiskdRILIKLSSTWEGIQAGKELEEQhGIHCNMTLLFSFAQAVA 177
Cdd:COG0176 50 IVDGPVSAEV---LATDTEGMIAEARRLAALYRP------NVVIKIPATEEGLKAIEELSAE-GIKVNVTLIFSAAQALL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 178 CAEAGVTLISPFVGRILDWhvantdkksyepLEDpGVKSVTKIYNYYKKFSYKTIVMGASFRNTGEIK--ALAGCDFLTI 255
Cdd:COG0176 120 AAEAGASYVSPFVGRIDDI------------GID-GIALVREIYQIYKNYGARTRILAASFRNPLQVLeaALAGADTVTI 186
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332368005 256 SPKLLGELLQDnaklvpvlsakaaqasdlekihldeksfrwlhnedqmavEKLSDGIRKFAADAVKL 322
Cdd:COG0176 187 PPAVLEALADH---------------------------------------PLTDEGIEKFLADWEKL 214
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05269 |
PRK05269 |
transaldolase B; Provisional |
11-329 |
0e+00 |
|
transaldolase B; Provisional
Pssm-ID: 235381 [Multi-domain] Cd Length: 318 Bit Score: 604.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 11 MESALDQLKQFTTVVADTGDFHAIDEYKPQDATTNPSLILAAAQMPAYQELVEEAIAYGRKLGGSQEDQIKNAIDKLFVL 90
Cdd:PRK05269 1 MTNKLEQLKQFTTVVADTGDIEAIKKYQPQDATTNPSLILKAAQIPEYAPLIDDAVAWAKQQSGDRAQQIDDAIDKLAVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 91 FGAEILKKIPGRVSTEVDARLSFDKDAMVARARRLIELYKEAGISKDRILIKLSSTWEGIQAGKELEEQhGIHCNMTLLF 170
Cdd:PRK05269 81 FGLEILKLIPGRVSTEVDARLSFDTEATIAKARKLIALYEEAGISKDRILIKIASTWEGIRAAEQLEKE-GINCNLTLLF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 171 SFAQAVACAEAGVTLISPFVGRILDWHVANTDKKSYEPLEDPGVKSVTKIYNYYKKFSYKTIVMGASFRNTGEIKALAGC 250
Cdd:PRK05269 160 SFAQARACAEAGVFLISPFVGRILDWYKKNTGKKEYAPAEDPGVVSVTKIYNYYKKHGYKTVVMGASFRNTGQILELAGC 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 332368005 251 DFLTISPKLLGELLQDNAKLVPVLSAKAAQASDleKIHLDEKSFRWLHNEDQMAVEKLSDGIRKFAADAVKLERMLTER 329
Cdd:PRK05269 240 DRLTISPALLEELAASEGELERKLSPPGEAKAR--PVPLTEAEFRWQHNEDAMATEKLAEGIRKFAKDQEKLEKLIAAK 316
|
|
| Transaldolase_TalAB |
cd00957 |
Transaldolases including both TalA and TalB; Transaldolases including both TalA and TalB. The ... |
13-326 |
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: 582.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 13 SALDQLKQFTTVVADTGDFHAIDEYKPQDATTNPSLILAAAQMPAYQELVEEAIAYGRKLGGSQEDQIKNAIDKLFVLFG 92
Cdd:cd00957 1 NQLDQLKKFTTIVADTGDFEAIKKFKPQDATTNPSLILAAAKLPEYNKLVDEAIAYAKKKGGSDEDQISNALDKLLVNFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 93 AEILKKIPGRVSTEVDARLSFDKDAMVARARRLIELYKEAGISKDRILIKLSSTWEGIQAGKELEeQHGIHCNMTLLFSF 172
Cdd:cd00957 81 TEILKLIPGRVSTEVDARLSFDTNATIAKARKLIKLYEEAGIDKERILIKIAATWEGIQAAKQLE-KEGIHCNLTLLFSF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 173 AQAVACAEAGVTLISPFVGRILDWHVANTDKKSYEPLEDPGVKSVTKIYNYYKKFSYKTIVMGASFRNTGEIKALAGCDF 252
Cdd:cd00957 160 AQAVACAEAGVTLISPFVGRILDWYKKHSGDKAYTAEEDPGVASVKKIYNYYKKFGYKTKVMGASFRNIGQILALAGCDY 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 332368005 253 LTISPKLLGELLQDNAKLVPVLSAKAAQASDLEKIHLDEKSFRWLHNEDQMAVEKLSDGIRKFAADAVKLERML 326
Cdd:cd00957 240 LTISPALLEELKNSTAKVERKLDPAASKALDIHPNFLDESAFRWALNEDAMAVEKLSEGIRGFAKDAVKLEKLI 313
|
|
| talAB |
TIGR00874 |
transaldolase; This family includes the majority of known and predicted transaldolase ... |
13-330 |
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: 526.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 13 SALDQLKQFTTVVADTGDFHAIDEYKPQDATTNPSLILAAAQMPAYQELVEEAIAYGRKLGGSQEDQIKNAIDKLFVLFG 92
Cdd:TIGR00874 1 NQLDQLKQFTVVVADTGDIEAIKKYQPQDATTNPSLILAAAQLPKYAELIDEAVAWGKKQGKDDAQQVENALDKLAVNFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 93 AEILKKIPGRVSTEVDARLSFDKDAMVARARRLIELYKEAGISKDRILIKLSSTWEGIQAGKELEeQHGIHCNMTLLFSF 172
Cdd:TIGR00874 81 LEILKIVPGRVSTEVDARLSFDTEATVEKARHLIKLYEDAGVDKKRILIKIASTWEGIRAAEELE-KEGIHCNLTLLFSF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 173 AQAVACAEAGVTLISPFVGRILDWHVANTDKKSYEPLEDPGVKSVTKIYNYYKKFSYKTIVMGASFRNTGEIKALAGCDF 252
Cdd:TIGR00874 160 VQAIACAEAKVTLISPFVGRILDWYKAATGKKEYSIEEDPGVASVKKIYNYYKKHGYPTEVMGASFRNKEEILALAGCDR 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332368005 253 LTISPKLLGELLQDNAKLVPVLSAKAAQASDLEKIHLDEKSFRWLHNEDQMAVEKLSDGIRKFAADAVKLERMLTERM 330
Cdd:TIGR00874 240 LTISPALLDELKESTGPVERKLDPESAKKVDKQPIILDESEFRFLHNEDAMATEKLAEGIRKFAADQEKLEKLLEEKL 317
|
|
| PRK12346 |
PRK12346 |
transaldolase A; Provisional |
13-330 |
0e+00 |
|
transaldolase A; Provisional
Pssm-ID: 183458 Cd Length: 316 Bit Score: 505.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 13 SALDQLKQFTTVVADTGDFHAIDEYKPQDATTNPSLILAAAQMPAYQELVEEAIAYGRKLGGSQEDQIKNAIDKLFVLFG 92
Cdd:PRK12346 2 NQLDGIKQFTTVVADSGDIESIRHYHPQDATTNPSLLLKAAGLPQYQHLIDDAIAWGKKQGGTQEQQVVAACDKLAVNFG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 93 AEILKKIPGRVSTEVDARLSFDKDAMVARARRLIELYKEAGISKDRILIKLSSTWEGIQAGKELeEQHGIHCNMTLLFSF 172
Cdd:PRK12346 82 AEILKSVPGRVSTEVDARLSFDREKSIEKARHLVDLYQQQGIDKSRILIKLASTWEGIRAAEEL-EKEGINCNLTLLFSF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 173 AQAVACAEAGVTLISPFVGRILDWHVANTDKKSYEPLEDPGVKSVTKIYNYYKKFSYKTIVMGASFRNTGEIKALAGCDF 252
Cdd:PRK12346 161 AQARACAEAGVFLISPFVGRIYDWYQARKPMDPYVVEEDPGVKSVRNIYDYYKQHRYETIVMGASFRRTEQILALAGCDR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 253 LTISPKLLGELLQDNA----KLVPVLSAKAAQASdlekihLDEKSFRWLHNEDQMAVEKLSDGIRKFAADAVKLERMLTE 328
Cdd:PRK12346 241 LTISPNLLKELQESESpverKLIPSSQTFPRPAP------MSEAEFRWEHNQDAMAVEKLSEGIRLFAVDQRKLEDLLAA 314
|
..
gi 332368005 329 RM 330
Cdd:PRK12346 315 KL 316
|
|
| PTZ00411 |
PTZ00411 |
transaldolase-like protein; Provisional |
11-330 |
0e+00 |
|
transaldolase-like protein; Provisional
Pssm-ID: 240406 Cd Length: 333 Bit Score: 505.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 11 MESALDQLKQFTTVVADTGDFHAIDEYKPQDATTNPSLILAAAQMPAYQELVEEAIAYGRKLGG----------SQEDQI 80
Cdd:PTZ00411 1 MPNQLEALKEHTTVVADTGDFSLLKKFQPEDATTNPSLVLAAAQMPEYAHLIDDAIKYAKANVSrlrdpllsdeEKEELV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 81 KNAIDKLFVLFGAEILKKIPGRVSTEVDARLSFDKDAMVARARRLIELYKEAGISKDRILIKLSSTWEGIQAGKELEEQh 160
Cdd:PTZ00411 81 ELVVDKLTVNFGVEILKIVPGRVSTEVDARLSFDKQAMVDKARKIIKMYEEAGISKDRILIKLASTWEGIQAAKALEKE- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 161 GIHCNMTLLFSFAQAVACAEAGVTLISPFVGRILDWHVANTDKKSYEPLEDPGVKSVTKIYNYYKKFSYKTIVMGASFRN 240
Cdd:PTZ00411 160 GIHCNLTLLFSFAQAVACAQAGVTLISPFVGRILDWYKKPEKAESYVGAQDPGVISVTKIYNYYKKHGYKTIVMGASFRN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 241 TGEIKALAGCDFLTISPKLLGELLQDNAKLV-PVLSAKAAQASDLEKIHLDEKSFRWLHNEDQMAVEKLSDGIRKFAADA 319
Cdd:PTZ00411 240 TGEILELAGCDKLTISPKLLEELANTEDGPVeRKLDPEKLTEDTEKLPELTEKEFRWELNEDAMATEKLAEGIRNFAKDL 319
|
330
....*....|.
gi 332368005 320 VKLERMLTERM 330
Cdd:PTZ00411 320 EKLENVIRAKL 330
|
|
| PRK12309 |
PRK12309 |
transaldolase; |
11-337 |
2.41e-178 |
|
transaldolase;
Pssm-ID: 183426 [Multi-domain] Cd Length: 391 Bit Score: 499.26 E-value: 2.41e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 11 MESALDQLKQFTTVVADTGDFHAIDEYKPQDATTNPSLILAAAQMPAYQELVEEAIAYGRKLGGSQ---EDQIKNAIDKL 87
Cdd:PRK12309 2 MASLLEQLRQMTVVVADTGDIQAIEKFTPRDATTNPSLITAAAQMPQYQSIVDETLRQARKELGSDapvEDVVALAFDRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 88 FVLFGAEILKKIPGRVSTEVDARLSFDKDAMVARARRLIELYKEAGISKDRILIKLSSTWEGIQAGKELEeQHGIHCNMT 167
Cdd:PRK12309 82 AVAFGLKILKIVPGRVSTEVDARLSYDTEATIAKARKLISLYEDAGISRDRVLIKIASTWEGIKAAEVLE-KEGIHCNLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 168 LLFSFAQAVACAEAGVTLISPFVGRILDWHVANTDKKSYEPLEDPGVKSVTKIYNYYKKFSYKTIVMGASFRNTGEIKAL 247
Cdd:PRK12309 161 LLFGFHQAIACAEAGVTLISPFVGRILDWYKKETGRDSYPGAEDPGVQSVTQIYNYYKKFGYKTEVMGASFRNIGEIIEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 248 AGCDFLTISPKLLGELLQDNAKLVPVLSAKAAQASDLEKIHLDEKSFRWLHNEDQMAVEKLSDGIRKFAADAVKLERMLT 327
Cdd:PRK12309 241 AGCDLLTISPKLLEQLRSTEAELPRKLDPANAAGMEIEKIHMDRATFDKMHAEDRMASEKLDEGIKGFSKALETLEKLLA 320
|
330
....*....|
gi 332368005 328 ERMFNAENGK 337
Cdd:PRK12309 321 HRLARLEGGE 330
|
|
| Transaldolase |
cd00439 |
Transaldolase; Transaldolase. Enzymes found in the non-oxidative branch of the pentose ... |
23-263 |
2.39e-120 |
|
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: 347.03 E-value: 2.39e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 23 TVVADTGDFHAIDEYK----PQDATTNPSLILAAAQMPAYQELVEEAIAYGRKLGGSQEDQIKNAIDKLFVLFGAEILKK 98
Cdd:cd00439 1 SPWYDTLDRPATDLLPlirgVRGVTTNPSIIQAAISTSNAYNDQFRTLVESGKDIESAYWELVVKDIQDACKLFEPIYDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 99 I--PGRVSTEVDARLSFDKDAMVARARRLIELYKEagiskDRILIKLSSTWEGIQAGKELEeQHGIHCNMTLLFSFAQAV 176
Cdd:cd00439 81 TeaDGRVSVEVSARLADDTQGMVEAAKYLSKVVNR-----RNIYIKIPATAEGIPAIKDLI-AAGISVNVTLIFSIAQYE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 177 ACAEAGVTLISPFVGRILDWHVANTDKKSYEPLEDPGVKSVTKIYNYYKKFSYKTIVMGASFRNTGEIKALAGCDFLTIS 256
Cdd:cd00439 155 AVADAGTSVASPFVSRIDTLMDKMLEQIGLDLRGKAGVAQVTLAYKLYKQKFKKQRVLWASFSDTLYVAPLIGCDTVTTM 234
|
....*..
gi 332368005 257 PKLLGEL 263
Cdd:cd00439 235 PDQALEA 241
|
|
| TAL_FSA |
pfam00923 |
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ... |
24-326 |
1.46e-93 |
|
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: 277.88 E-value: 1.46e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 24 VVADTGDFHAIDEYKP----QDATTNPSLILAAAQmpaYQELVEEAIAygrklggsqedqiknaidklfvlfgaEILKKI 99
Cdd:pfam00923 1 IWLDTADRDLIKKLIEeggiDGVTTNPSIFLKAIE---YSALYDEAIA--------------------------EIKEIG 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 100 PGRVSTEVDARLSFDKDAMVARARRLIELYKeagisKDRILIKLSSTWEGIQAGKELEeQHGIHCNMTLLFSFAQAVACA 179
Cdd:pfam00923 52 DGPVSLEVDPRLADDTEGTIEEARRLIALYG-----RPNVLIKIPATWEGIKAIKELS-AEGINVNVTLIFSLAQALAAA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 180 EAGVTLISPFVGRILDWHVANTDKksyEPLEDPGVKSVTKIYNYYKKFSYKTIVMGASFRNTGEIKALAGCDFLTISPKL 259
Cdd:pfam00923 126 EAGASVISPFVGRIDDWGDKRLGA---ALRGDDGIANAKEIYQIYKKYGWSTGVLAASFRNVLYVLALAGCDTITIPPDT 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332368005 260 LGELLQDnaklvpvlsakaaqasdlekihldeksfrwlhnedqmaveklsDGIRKFAADAVKLERML 326
Cdd:pfam00923 203 LEALAKD-------------------------------------------EGVRKFAKDWEKLLGSI 226
|
|
| TalA |
COG0176 |
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ... |
22-322 |
1.28e-72 |
|
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: 223.80 E-value: 1.28e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 22 TTVVADTGDFHAIDEYK----PQDATTNPSLILAAAqmpayqelveeaiaygrklggsqedqIKNAIDklfvlFGAEILK 97
Cdd:COG0176 1 MKLWLDTADREEIKELIdlggVDGVTTNPSLIAKAG--------------------------IKDFVE-----DIREICD 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 98 KIPGRVSTEVdarLSFDKDAMVARARRLIELYKEagiskdRILIKLSSTWEGIQAGKELEEQhGIHCNMTLLFSFAQAVA 177
Cdd:COG0176 50 IVDGPVSAEV---LATDTEGMIAEARRLAALYRP------NVVIKIPATEEGLKAIEELSAE-GIKVNVTLIFSAAQALL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 178 CAEAGVTLISPFVGRILDWhvantdkksyepLEDpGVKSVTKIYNYYKKFSYKTIVMGASFRNTGEIK--ALAGCDFLTI 255
Cdd:COG0176 120 AAEAGASYVSPFVGRIDDI------------GID-GIALVREIYQIYKNYGARTRILAASFRNPLQVLeaALAGADTVTI 186
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 332368005 256 SPKLLGELLQDnaklvpvlsakaaqasdlekihldeksfrwlhnedqmavEKLSDGIRKFAADAVKL 322
Cdd:COG0176 187 PPAVLEALADH---------------------------------------PLTDEGIEKFLADWEKL 214
|
|
| Transaldolase_FSA |
cd00956 |
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ... |
43-266 |
1.20e-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: 118.06 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 43 TTNPSLILAAAQmpayqelveeaiaygrklgGSQEDQIKnaidklfvlfgaEILKKIPGRVSTEVDARlsfDKDAMVARA 122
Cdd:cd00956 25 TTNPSLIAKSGR-------------------IDFEAVLK------------EICEIIDGPVSAQVVST---DAEGMVAEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 123 RRLIELYkeagiskDRILIKLSSTWEGIQAGKELEEqHGIHCNMTLLFSFAQAVACAEAGVTLISPFVGRIldwhvantD 202
Cdd:cd00956 71 RKLASLG-------GNVVVKIPVTEDGLKAIKKLSE-EGIKTNVTAIFSAAQALLAAKAGATYVSPFVGRI--------D 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332368005 203 KKSYEPLEDpgVKSVTKIYNYYkkfSYKTIVMGASFRNTGEIK--ALAGCDFLTISPKLLGELLQD 266
Cdd:cd00956 135 DLGGDGMEL--IREIRTIFDNY---GFDTKILAASIRNPQHVIeaALAGADAITLPPDVLEQLLKH 195
|
|
| Transaldolase_like |
cd00955 |
Transaldolase-like proteins from plants and bacteria; Transaldolase-like proteins from plants ... |
42-227 |
2.01e-15 |
|
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: 75.82 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 42 ATTNPSLILAA-AQMPAYQELVEEAIAYGRKLGGSQED----QIKNAIDKLFVLFgaEILKKIPGRVSTEVDARLSFDKD 116
Cdd:cd00955 29 VTSNPAIFEKAiAGSAAYDDQIRALKGQGLDAEAIYEAlaieDIQDACDLLAPVY--EQTGGNDGYVSLEVSPRLADDTQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 117 AMVARARRlieLYKEAGisKDRILIKLSSTWEGIQAGKELeEQHGIHCNMTLLFSFAQAVACAEAGVT------------ 184
Cdd:cd00955 107 GTIAEAKR---LWKAVG--RPNLMIKIPATEAGLPAIEEL-IAAGISVNVTLIFSLEQYEAVAEAYLRglerrvegggdl 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 332368005 185 -----LISPFVGRIlDwhvANTDKKSYEPLEDP-----GVKSVTKIYNYYKKF 227
Cdd:cd00955 181 sqvasVASFFVSRV-D---TLIDKKLDAPEAKAlqgkvAIANAKLAYQEYQEK 229
|
|
| PRK03903 |
PRK03903 |
transaldolase; Provisional |
80-232 |
2.77e-13 |
|
transaldolase; Provisional
Pssm-ID: 235171 Cd Length: 274 Bit Score: 68.85 E-value: 2.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 80 IKNAIDKLFVLFGaeilKKIPGRVSTEVDARLSFDKDAMVARARRLielYKeaGISKDRILIKLSSTWEGIQAGKELEEQ 159
Cdd:PRK03903 26 IKKAADKLLPLYE----KPDDGFISIEIDPFLEDDAAGSIEEGKRL---YK--TIGRPNVMIKVPATKAGYEAMSALMKK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 160 hGIHCNMTLLFSFAQAVACAEA-----------GVTLISPFVGRI---LDWHVANTDKKSyepleDPGVKSVTKIYNYYK 225
Cdd:PRK03903 97 -GISVNATLIFSPEQAKECAEAlneglkkntkdPKAVISVFVSRFdrlLDPKLAPKNLQA-----KSGIMNATKCYNQIE 170
|
....*..
gi 332368005 226 KFSYKTI 232
Cdd:PRK03903 171 QHANKNI 177
|
|
| PRK03343 |
PRK03343 |
transaldolase; Validated |
43-181 |
7.88e-13 |
|
transaldolase; Validated
Pssm-ID: 235117 Cd Length: 368 Bit Score: 68.31 E-value: 7.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 43 TTNPSlILAAA--QMPAYQELVEEAIAYGRklggSQE--------DQIKNAIDKLFVLFGAEilKKIPGRVSTEVDARLS 112
Cdd:PRK03343 43 TSNPA-IFQKAiaGGDAYDAQIAELAAAGA----DVEeayeelttADVRNACDVLRPVYEAT--GGVDGRVSIEVSPRLA 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 332368005 113 FDKDAMVARARRlieLYKEAGisKDRILIKLSSTWEGIQAgkeLEE--QHGIHCNMTLLFSFAQAVACAEA 181
Cdd:PRK03343 116 HDTEATIAEARR---LWAAVD--RPNLMIKIPATPEGLPA---IEAliAEGISVNVTLIFSVERYRAVADA 178
|
|
| PRK09533 |
PRK09533 |
bifunctional transaldolase/phosoglucose isomerase; Validated |
43-181 |
7.14e-09 |
|
bifunctional transaldolase/phosoglucose isomerase; Validated
Pssm-ID: 236551 [Multi-domain] Cd Length: 948 Bit Score: 57.29 E-value: 7.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332368005 43 TTNPSLILAA-AQMPAYQELVEEAIAYGRKLGG------SQEDqIKNAIDKLFVLFgaEILKKIPGRVSTEVDARLSFDK 115
Cdd:PRK09533 42 TSNPAIFEKAiGSSDEYDDAIKAALAEGDRSVIelyetlAIED-IQAAADVLRPVY--DATDGADGFVSLEVSPYLALDT 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 332368005 116 DAMVARARRLIelykeAGISKDRILIKLSSTWEGIQAGKELEEQhGIHCNMTLLFSFAQAVACAEA 181
Cdd:PRK09533 119 EGTIAEARRLW-----AAVDRPNLMIKVPATPEGLPAIRQLIAE-GINVNVTLLFSQDVYEEVAEA 178
|
|
| |
