|
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: 606.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 11 MESALDQLKQFTTVVADTGDFNAIDEYKPQDATTNPSLILAAAQMPAYQELVEEAIAYGKKLGGPQEEQIKNAIDKLFVL 90
Cdd:PRK05269 1 MTNKLEQLKQFTTVVADTGDIEAIKKYQPQDATTNPSLILKAAQIPEYAPLIDDAVAWAKQQSGDRAQQIDDAIDKLAVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 91 FGAEILKKIPGRVSTEVDARLSFDKDAMVARARRLIELYKEAGVGKDRILIKLSSTWEGIQAGKELEEQhGIHCNMTLLF 170
Cdd:PRK05269 81 FGLEILKLIPGRVSTEVDARLSFDTEATIAKARKLIALYEEAGISKDRILIKIASTWEGIRAAEQLEKE-GINCNLTLLF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 171 SFAQAVACAEAGVTLISPFVGRILDWHVANTDKKSYEPQEDPGVKSVTKIYNYYKKFGYKTIVMGASFRNTGEIKALAGC 250
Cdd:PRK05269 160 SFAQARACAEAGVFLISPFVGRILDWYKKNTGKKEYAPAEDPGVVSVTKIYNYYKKHGYKTVVMGASFRNTGQILELAGC 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2589166 251 DFLTISPKLLGELLKDNSKLAPALSVKAAqtSDSEKIHLDEKAFRWLHNEDQMAVEKLSDGIRKFAADAIKLERMLTER 329
Cdd:PRK05269 240 DRLTISPALLEELAASEGELERKLSPPGE--AKARPVPLTEAEFRWQHNEDAMATEKLAEGIRKFAKDQEKLEKLIAAK 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: 575.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 13 SALDQLKQFTTVVADTGDFNAIDEYKPQDATTNPSLILAAAQMPAYQELVEEAIAYGKKLGGPQEEQIKNAIDKLFVLFG 92
Cdd:cd00957 1 NQLDQLKKFTTIVADTGDFEAIKKFKPQDATTNPSLILAAAKLPEYNKLVDEAIAYAKKKGGSDEDQISNALDKLLVNFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 93 AEILKKIPGRVSTEVDARLSFDKDAMVARARRLIELYKEAGVGKDRILIKLSSTWEGIQAGKELEeQHGIHCNMTLLFSF 172
Cdd:cd00957 81 TEILKLIPGRVSTEVDARLSFDTNATIAKARKLIKLYEEAGIDKERILIKIAATWEGIQAAKQLE-KEGIHCNLTLLFSF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 173 AQAVACAEAGVTLISPFVGRILDWHVANTDKKSYEPQEDPGVKSVTKIYNYYKKFGYKTIVMGASFRNTGEIKALAGCDF 252
Cdd:cd00957 160 AQAVACAEAGVTLISPFVGRILDWYKKHSGDKAYTAEEDPGVASVKKIYNYYKKFGYKTKVMGASFRNIGQILALAGCDY 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2589166 253 LTISPKLLGELLKDNSKLAPALSVKAAQTSDSEKIHLDEKAFRWLHNEDQMAVEKLSDGIRKFAADAIKLERML 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: 528.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 13 SALDQLKQFTTVVADTGDFNAIDEYKPQDATTNPSLILAAAQMPAYQELVEEAIAYGKKLGGPQEEQIKNAIDKLFVLFG 92
Cdd:TIGR00874 1 NQLDQLKQFTVVVADTGDIEAIKKYQPQDATTNPSLILAAAQLPKYAELIDEAVAWGKKQGKDDAQQVENALDKLAVNFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 93 AEILKKIPGRVSTEVDARLSFDKDAMVARARRLIELYKEAGVGKDRILIKLSSTWEGIQAGKELEeQHGIHCNMTLLFSF 172
Cdd:TIGR00874 81 LEILKIVPGRVSTEVDARLSFDTEATVEKARHLIKLYEDAGVDKKRILIKIASTWEGIRAAEELE-KEGIHCNLTLLFSF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 173 AQAVACAEAGVTLISPFVGRILDWHVANTDKKSYEPQEDPGVKSVTKIYNYYKKFGYKTIVMGASFRNTGEIKALAGCDF 252
Cdd:TIGR00874 160 VQAIACAEAKVTLISPFVGRILDWYKAATGKKEYSIEEDPGVASVKKIYNYYKKHGYPTEVMGASFRNKEEILALAGCDR 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2589166 253 LTISPKLLGELLKDNSKLAPALSVKAAQTSDSEKIHLDEKAFRWLHNEDQMAVEKLSDGIRKFAADAIKLERMLTERM 330
Cdd:TIGR00874 240 LTISPALLDELKESTGPVERKLDPESAKKVDKQPIILDESEFRFLHNEDAMATEKLAEGIRKFAADQEKLEKLLEEKL 317
|
|
| TAL_FSA |
pfam00923 |
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ... |
24-326 |
7.30e-95 |
|
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose phosphate pathway (PPP) found almost ubiquitously in the three domains of life (Archaea, Bacteria, and Eukarya). TAL shares a high degree of structural similarity and sequence identity with fructose-6-phosphate aldolase (FSA). They both belong to the class I aldolase family. Their protein structures have been revealed.
Pssm-ID: 395737 [Multi-domain] Cd Length: 226 Bit Score: 280.96 E-value: 7.30e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 24 VVADTGDFNAIDEYKP----QDATTNPSLILAAAQmpaYQELVEEAIAygkklggpqeeqiknaidklfvlfgaEILKKI 99
Cdd:pfam00923 1 IWLDTADRDLIKKLIEeggiDGVTTNPSIFLKAIE---YSALYDEAIA--------------------------EIKEIG 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 100 PGRVSTEVDARLSFDKDAMVARARRLIELYKeagvgKDRILIKLSSTWEGIQAGKELEeQHGIHCNMTLLFSFAQAVACA 179
Cdd:pfam00923 52 DGPVSLEVDPRLADDTEGTIEEARRLIALYG-----RPNVLIKIPATWEGIKAIKELS-AEGINVNVTLIFSLAQALAAA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 180 EAGVTLISPFVGRILDWHVANTDKksyEPQEDPGVKSVTKIYNYYKKFGYKTIVMGASFRNTGEIKALAGCDFLTISPKL 259
Cdd:pfam00923 126 EAGASVISPFVGRIDDWGDKRLGA---ALRGDDGIANAKEIYQIYKKYGWSTGVLAASFRNVLYVLALAGCDTITIPPDT 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2589166 260 LGELLKDnsklapalsvkaaqtsdsekihldekafrwlhnedqmaveklsDGIRKFAADAIKLERML 326
Cdd:pfam00923 203 LEALAKD-------------------------------------------EGVRKFAKDWEKLLGSI 226
|
|
| TalA |
COG0176 |
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ... |
22-322 |
1.67e-74 |
|
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: 228.81 E-value: 1.67e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 22 TTVVADTGDFNAIDEYK----PQDATTNPSLILAAAqmpayqelveeaiaygkklggpqeeqIKNAIDklfvlFGAEILK 97
Cdd:COG0176 1 MKLWLDTADREEIKELIdlggVDGVTTNPSLIAKAG--------------------------IKDFVE-----DIREICD 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 98 KIPGRVSTEVdarLSFDKDAMVARARRLIELYKEagvgkdRILIKLSSTWEGIQAGKELEEQhGIHCNMTLLFSFAQAVA 177
Cdd:COG0176 50 IVDGPVSAEV---LATDTEGMIAEARRLAALYRP------NVVIKIPATEEGLKAIEELSAE-GIKVNVTLIFSAAQALL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 178 CAEAGVTLISPFVGRILDWhvaNTDkksyepqedpGVKSVTKIYNYYKKFGYKTIVMGASFRNTGEIK--ALAGCDFLTI 255
Cdd:COG0176 120 AAEAGASYVSPFVGRIDDI---GID----------GIALVREIYQIYKNYGARTRILAASFRNPLQVLeaALAGADTVTI 186
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2589166 256 SPKLLGELLKDnsklapalsvkaaqtsdsekihldekafrwlhnedqmavEKLSDGIRKFAADAIKL 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: 606.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 11 MESALDQLKQFTTVVADTGDFNAIDEYKPQDATTNPSLILAAAQMPAYQELVEEAIAYGKKLGGPQEEQIKNAIDKLFVL 90
Cdd:PRK05269 1 MTNKLEQLKQFTTVVADTGDIEAIKKYQPQDATTNPSLILKAAQIPEYAPLIDDAVAWAKQQSGDRAQQIDDAIDKLAVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 91 FGAEILKKIPGRVSTEVDARLSFDKDAMVARARRLIELYKEAGVGKDRILIKLSSTWEGIQAGKELEEQhGIHCNMTLLF 170
Cdd:PRK05269 81 FGLEILKLIPGRVSTEVDARLSFDTEATIAKARKLIALYEEAGISKDRILIKIASTWEGIRAAEQLEKE-GINCNLTLLF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 171 SFAQAVACAEAGVTLISPFVGRILDWHVANTDKKSYEPQEDPGVKSVTKIYNYYKKFGYKTIVMGASFRNTGEIKALAGC 250
Cdd:PRK05269 160 SFAQARACAEAGVFLISPFVGRILDWYKKNTGKKEYAPAEDPGVVSVTKIYNYYKKHGYKTVVMGASFRNTGQILELAGC 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2589166 251 DFLTISPKLLGELLKDNSKLAPALSVKAAqtSDSEKIHLDEKAFRWLHNEDQMAVEKLSDGIRKFAADAIKLERMLTER 329
Cdd:PRK05269 240 DRLTISPALLEELAASEGELERKLSPPGE--AKARPVPLTEAEFRWQHNEDAMATEKLAEGIRKFAKDQEKLEKLIAAK 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: 575.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 13 SALDQLKQFTTVVADTGDFNAIDEYKPQDATTNPSLILAAAQMPAYQELVEEAIAYGKKLGGPQEEQIKNAIDKLFVLFG 92
Cdd:cd00957 1 NQLDQLKKFTTIVADTGDFEAIKKFKPQDATTNPSLILAAAKLPEYNKLVDEAIAYAKKKGGSDEDQISNALDKLLVNFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 93 AEILKKIPGRVSTEVDARLSFDKDAMVARARRLIELYKEAGVGKDRILIKLSSTWEGIQAGKELEeQHGIHCNMTLLFSF 172
Cdd:cd00957 81 TEILKLIPGRVSTEVDARLSFDTNATIAKARKLIKLYEEAGIDKERILIKIAATWEGIQAAKQLE-KEGIHCNLTLLFSF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 173 AQAVACAEAGVTLISPFVGRILDWHVANTDKKSYEPQEDPGVKSVTKIYNYYKKFGYKTIVMGASFRNTGEIKALAGCDF 252
Cdd:cd00957 160 AQAVACAEAGVTLISPFVGRILDWYKKHSGDKAYTAEEDPGVASVKKIYNYYKKFGYKTKVMGASFRNIGQILALAGCDY 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2589166 253 LTISPKLLGELLKDNSKLAPALSVKAAQTSDSEKIHLDEKAFRWLHNEDQMAVEKLSDGIRKFAADAIKLERML 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: 528.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 13 SALDQLKQFTTVVADTGDFNAIDEYKPQDATTNPSLILAAAQMPAYQELVEEAIAYGKKLGGPQEEQIKNAIDKLFVLFG 92
Cdd:TIGR00874 1 NQLDQLKQFTVVVADTGDIEAIKKYQPQDATTNPSLILAAAQLPKYAELIDEAVAWGKKQGKDDAQQVENALDKLAVNFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 93 AEILKKIPGRVSTEVDARLSFDKDAMVARARRLIELYKEAGVGKDRILIKLSSTWEGIQAGKELEeQHGIHCNMTLLFSF 172
Cdd:TIGR00874 81 LEILKIVPGRVSTEVDARLSFDTEATVEKARHLIKLYEDAGVDKKRILIKIASTWEGIRAAEELE-KEGIHCNLTLLFSF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 173 AQAVACAEAGVTLISPFVGRILDWHVANTDKKSYEPQEDPGVKSVTKIYNYYKKFGYKTIVMGASFRNTGEIKALAGCDF 252
Cdd:TIGR00874 160 VQAIACAEAKVTLISPFVGRILDWYKAATGKKEYSIEEDPGVASVKKIYNYYKKHGYPTEVMGASFRNKEEILALAGCDR 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2589166 253 LTISPKLLGELLKDNSKLAPALSVKAAQTSDSEKIHLDEKAFRWLHNEDQMAVEKLSDGIRKFAADAIKLERMLTERM 330
Cdd:TIGR00874 240 LTISPALLDELKESTGPVERKLDPESAKKVDKQPIILDESEFRFLHNEDAMATEKLAEGIRKFAADQEKLEKLLEEKL 317
|
|
| PTZ00411 |
PTZ00411 |
transaldolase-like protein; Provisional |
11-330 |
0e+00 |
|
transaldolase-like protein; Provisional
Pssm-ID: 240406 Cd Length: 333 Bit Score: 510.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 11 MESALDQLKQFTTVVADTGDFNAIDEYKPQDATTNPSLILAAAQMPAYQELVEEAIAYGKKLGG----------PQEEQI 80
Cdd:PTZ00411 1 MPNQLEALKEHTTVVADTGDFSLLKKFQPEDATTNPSLVLAAAQMPEYAHLIDDAIKYAKANVSrlrdpllsdeEKEELV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 81 KNAIDKLFVLFGAEILKKIPGRVSTEVDARLSFDKDAMVARARRLIELYKEAGVGKDRILIKLSSTWEGIQAGKELEEQh 160
Cdd:PTZ00411 81 ELVVDKLTVNFGVEILKIVPGRVSTEVDARLSFDKQAMVDKARKIIKMYEEAGISKDRILIKLASTWEGIQAAKALEKE- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 161 GIHCNMTLLFSFAQAVACAEAGVTLISPFVGRILDWHVANTDKKSYEPQEDPGVKSVTKIYNYYKKFGYKTIVMGASFRN 240
Cdd:PTZ00411 160 GIHCNLTLLFSFAQAVACAQAGVTLISPFVGRILDWYKKPEKAESYVGAQDPGVISVTKIYNYYKKHGYKTIVMGASFRN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 241 TGEIKALAGCDFLTISPKLLGELLK-DNSKLAPALSVKAAQTSDSEKIHLDEKAFRWLHNEDQMAVEKLSDGIRKFAADA 319
Cdd:PTZ00411 240 TGEILELAGCDKLTISPKLLEELANtEDGPVERKLDPEKLTEDTEKLPELTEKEFRWELNEDAMATEKLAEGIRNFAKDL 319
|
330
....*....|.
gi 2589166 320 IKLERMLTERM 330
Cdd:PTZ00411 320 EKLENVIRAKL 330
|
|
| PRK12346 |
PRK12346 |
transaldolase A; Provisional |
13-330 |
0e+00 |
|
transaldolase A; Provisional
Pssm-ID: 183458 Cd Length: 316 Bit Score: 506.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 13 SALDQLKQFTTVVADTGDFNAIDEYKPQDATTNPSLILAAAQMPAYQELVEEAIAYGKKLGGPQEEQIKNAIDKLFVLFG 92
Cdd:PRK12346 2 NQLDGIKQFTTVVADSGDIESIRHYHPQDATTNPSLLLKAAGLPQYQHLIDDAIAWGKKQGGTQEQQVVAACDKLAVNFG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 93 AEILKKIPGRVSTEVDARLSFDKDAMVARARRLIELYKEAGVGKDRILIKLSSTWEGIQAGKELeEQHGIHCNMTLLFSF 172
Cdd:PRK12346 82 AEILKSVPGRVSTEVDARLSFDREKSIEKARHLVDLYQQQGIDKSRILIKLASTWEGIRAAEEL-EKEGINCNLTLLFSF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 173 AQAVACAEAGVTLISPFVGRILDWHVANTDKKSYEPQEDPGVKSVTKIYNYYKKFGYKTIVMGASFRNTGEIKALAGCDF 252
Cdd:PRK12346 161 AQARACAEAGVFLISPFVGRIYDWYQARKPMDPYVVEEDPGVKSVRNIYDYYKQHRYETIVMGASFRRTEQILALAGCDR 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2589166 253 LTISPKLLGELLKDNSKLAPALSvkAAQTSDSEKIHLDEKAFRWLHNEDQMAVEKLSDGIRKFAADAIKLERMLTERM 330
Cdd:PRK12346 241 LTISPNLLKELQESESPVERKLI--PSSQTFPRPAPMSEAEFRWEHNQDAMAVEKLSEGIRLFAVDQRKLEDLLAAKL 316
|
|
| PRK12309 |
PRK12309 |
transaldolase; |
11-337 |
6.33e-176 |
|
transaldolase;
Pssm-ID: 183426 [Multi-domain] Cd Length: 391 Bit Score: 493.10 E-value: 6.33e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 11 MESALDQLKQFTTVVADTGDFNAIDEYKPQDATTNPSLILAAAQMPAYQELVEEAIAYGKKLGG---PQEEQIKNAIDKL 87
Cdd:PRK12309 2 MASLLEQLRQMTVVVADTGDIQAIEKFTPRDATTNPSLITAAAQMPQYQSIVDETLRQARKELGsdaPVEDVVALAFDRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 88 FVLFGAEILKKIPGRVSTEVDARLSFDKDAMVARARRLIELYKEAGVGKDRILIKLSSTWEGIQAGKELEeQHGIHCNMT 167
Cdd:PRK12309 82 AVAFGLKILKIVPGRVSTEVDARLSYDTEATIAKARKLISLYEDAGISRDRVLIKIASTWEGIKAAEVLE-KEGIHCNLT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 168 LLFSFAQAVACAEAGVTLISPFVGRILDWHVANTDKKSYEPQEDPGVKSVTKIYNYYKKFGYKTIVMGASFRNTGEIKAL 247
Cdd:PRK12309 161 LLFGFHQAIACAEAGVTLISPFVGRILDWYKKETGRDSYPGAEDPGVQSVTQIYNYYKKFGYKTEVMGASFRNIGEIIEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 248 AGCDFLTISPKLLGELLKDNSKLAPALSVKAAQTSDSEKIHLDEKAFRWLHNEDQMAVEKLSDGIRKFAADAIKLERMLT 327
Cdd:PRK12309 241 AGCDLLTISPKLLEQLRSTEAELPRKLDPANAAGMEIEKIHMDRATFDKMHAEDRMASEKLDEGIKGFSKALETLEKLLA 320
|
330
....*....|
gi 2589166 328 ERMFSAENGK 337
Cdd:PRK12309 321 HRLARLEGGE 330
|
|
| Transaldolase |
cd00439 |
Transaldolase; Transaldolase. Enzymes found in the non-oxidative branch of the pentose ... |
23-263 |
3.28e-116 |
|
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: 336.25 E-value: 3.28e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 23 TVVADTGDFNAIDEYK----PQDATTNPSLILAAAQMPAYQELVEEAIAYGKKLGGPQEEQIKNAIDKLFVLFGAEILKK 98
Cdd:cd00439 1 SPWYDTLDRPATDLLPlirgVRGVTTNPSIIQAAISTSNAYNDQFRTLVESGKDIESAYWELVVKDIQDACKLFEPIYDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 99 I--PGRVSTEVDARLSFDKDAMVARARRLIELYKEagvgkDRILIKLSSTWEGIQAGKELEeQHGIHCNMTLLFSFAQAV 176
Cdd:cd00439 81 TeaDGRVSVEVSARLADDTQGMVEAAKYLSKVVNR-----RNIYIKIPATAEGIPAIKDLI-AAGISVNVTLIFSIAQYE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 177 ACAEAGVTLISPFVGRILDWHVANTDKKSYEPQEDPGVKSVTKIYNYYKKFGYKTIVMGASFRNTGEIKALAGCDFLTIS 256
Cdd:cd00439 155 AVADAGTSVASPFVSRIDTLMDKMLEQIGLDLRGKAGVAQVTLAYKLYKQKFKKQRVLWASFSDTLYVAPLIGCDTVTTM 234
|
....*..
gi 2589166 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 |
7.30e-95 |
|
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose phosphate pathway (PPP) found almost ubiquitously in the three domains of life (Archaea, Bacteria, and Eukarya). TAL shares a high degree of structural similarity and sequence identity with fructose-6-phosphate aldolase (FSA). They both belong to the class I aldolase family. Their protein structures have been revealed.
Pssm-ID: 395737 [Multi-domain] Cd Length: 226 Bit Score: 280.96 E-value: 7.30e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 24 VVADTGDFNAIDEYKP----QDATTNPSLILAAAQmpaYQELVEEAIAygkklggpqeeqiknaidklfvlfgaEILKKI 99
Cdd:pfam00923 1 IWLDTADRDLIKKLIEeggiDGVTTNPSIFLKAIE---YSALYDEAIA--------------------------EIKEIG 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 100 PGRVSTEVDARLSFDKDAMVARARRLIELYKeagvgKDRILIKLSSTWEGIQAGKELEeQHGIHCNMTLLFSFAQAVACA 179
Cdd:pfam00923 52 DGPVSLEVDPRLADDTEGTIEEARRLIALYG-----RPNVLIKIPATWEGIKAIKELS-AEGINVNVTLIFSLAQALAAA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 180 EAGVTLISPFVGRILDWHVANTDKksyEPQEDPGVKSVTKIYNYYKKFGYKTIVMGASFRNTGEIKALAGCDFLTISPKL 259
Cdd:pfam00923 126 EAGASVISPFVGRIDDWGDKRLGA---ALRGDDGIANAKEIYQIYKKYGWSTGVLAASFRNVLYVLALAGCDTITIPPDT 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2589166 260 LGELLKDnsklapalsvkaaqtsdsekihldekafrwlhnedqmaveklsDGIRKFAADAIKLERML 326
Cdd:pfam00923 203 LEALAKD-------------------------------------------EGVRKFAKDWEKLLGSI 226
|
|
| TalA |
COG0176 |
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ... |
22-322 |
1.67e-74 |
|
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: 228.81 E-value: 1.67e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 22 TTVVADTGDFNAIDEYK----PQDATTNPSLILAAAqmpayqelveeaiaygkklggpqeeqIKNAIDklfvlFGAEILK 97
Cdd:COG0176 1 MKLWLDTADREEIKELIdlggVDGVTTNPSLIAKAG--------------------------IKDFVE-----DIREICD 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 98 KIPGRVSTEVdarLSFDKDAMVARARRLIELYKEagvgkdRILIKLSSTWEGIQAGKELEEQhGIHCNMTLLFSFAQAVA 177
Cdd:COG0176 50 IVDGPVSAEV---LATDTEGMIAEARRLAALYRP------NVVIKIPATEEGLKAIEELSAE-GIKVNVTLIFSAAQALL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 178 CAEAGVTLISPFVGRILDWhvaNTDkksyepqedpGVKSVTKIYNYYKKFGYKTIVMGASFRNTGEIK--ALAGCDFLTI 255
Cdd:COG0176 120 AAEAGASYVSPFVGRIDDI---GID----------GIALVREIYQIYKNYGARTRILAASFRNPLQVLeaALAGADTVTI 186
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2589166 256 SPKLLGELLKDnsklapalsvkaaqtsdsekihldekafrwlhnedqmavEKLSDGIRKFAADAIKL 322
Cdd:COG0176 187 PPAVLEALADH---------------------------------------PLTDEGIEKFLADWEKL 214
|
|
| Transaldolase_FSA |
cd00956 |
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ... |
27-266 |
4.79e-33 |
|
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea, which are member of the MipB/TalC subfamily of class I aldolases. FSA catalyze an aldol cleavage of fructose 6-phosphate and do not utilize fructose, fructose 1-phosphate, fructose 1,6-phosphate, or dihydroxyacetone phosphate. The enzymes belong to the transaldolase family that serves in transfer reactions in the pentose phosphate cycle, and are more distantly related to fructose 1,6-bisphosphate aldolase.
Pssm-ID: 188643 [Multi-domain] Cd Length: 211 Bit Score: 121.53 E-value: 4.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 27 DTGDFNAIDEYKPQ----DATTNPSLILAAAQmpayqelveeaiaygkklgGPQEEQIKnaidklfvlfgaEILKKIPGR 102
Cdd:cd00956 5 DTADLEEIKKASETglldGVTTNPSLIAKSGR-------------------IDFEAVLK------------EICEIIDGP 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 103 VSTEVDARlsfDKDAMVARARRLIELYkeagvgkDRILIKLSSTWEGIQAGKELEEqHGIHCNMTLLFSFAQAVACAEAG 182
Cdd:cd00956 54 VSAQVVST---DAEGMVAEARKLASLG-------GNVVVKIPVTEDGLKAIKKLSE-EGIKTNVTAIFSAAQALLAAKAG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 183 VTLISPFVGRIldwhvantDKKSYEPQEDpgVKSVTKIYNYYkkfGYKTIVMGASFRNTGEIK--ALAGCDFLTISPKLL 260
Cdd:cd00956 123 ATYVSPFVGRI--------DDLGGDGMEL--IREIRTIFDNY---GFDTKILAASIRNPQHVIeaALAGADAITLPPDVL 189
|
....*.
gi 2589166 261 GELLKD 266
Cdd:cd00956 190 EQLLKH 195
|
|
| Transaldolase_like |
cd00955 |
Transaldolase-like proteins from plants and bacteria; Transaldolase-like proteins from plants ... |
42-227 |
1.02e-16 |
|
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: 79.68 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 42 ATTNPSLILAA-AQMPAYQELVEEAIAYGKKLGGPQE----EQIKNAIDKLFVLFgaEILKKIPGRVSTEVDARLSFDKD 116
Cdd:cd00955 29 VTSNPAIFEKAiAGSAAYDDQIRALKGQGLDAEAIYEalaiEDIQDACDLLAPVY--EQTGGNDGYVSLEVSPRLADDTQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 117 AMVARARRlieLYKEagVGKDRILIKLSSTWEGIQAGKELeEQHGIHCNMTLLFSFAQAVACAEAGVT------------ 184
Cdd:cd00955 107 GTIAEAKR---LWKA--VGRPNLMIKIPATEAGLPAIEEL-IAAGISVNVTLIFSLEQYEAVAEAYLRglerrvegggdl 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2589166 185 -----LISPFVGRIlDwhvANTDKKSYEPQEDP-----GVKSVTKIYNYYKKF 227
Cdd:cd00955 181 sqvasVASFFVSRV-D---TLIDKKLDAPEAKAlqgkvAIANAKLAYQEYQEK 229
|
|
| PRK03343 |
PRK03343 |
transaldolase; Validated |
43-181 |
9.02e-14 |
|
transaldolase; Validated
Pssm-ID: 235117 Cd Length: 368 Bit Score: 71.39 E-value: 9.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 43 TTNPSlILAAA--QMPAYQELVEEAIAYGKklgGPQE-------EQIKNAIDKLFVLFGAEilKKIPGRVSTEVDARLSF 113
Cdd:PRK03343 43 TSNPA-IFQKAiaGGDAYDAQIAELAAAGA---DVEEayeelttADVRNACDVLRPVYEAT--GGVDGRVSIEVSPRLAH 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 114 DKDAMVARARRLIELykeagVGKDRILIKLSSTWEGIQAgkeLEE--QHGIHCNMTLLFSFAQAVACAEA 181
Cdd:PRK03343 117 DTEATIAEARRLWAA-----VDRPNLMIKIPATPEGLPA---IEAliAEGISVNVTLIFSVERYRAVADA 178
|
|
| PRK03903 |
PRK03903 |
transaldolase; Provisional |
78-232 |
2.85e-13 |
|
transaldolase; Provisional
Pssm-ID: 235171 Cd Length: 274 Bit Score: 68.85 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 78 EQIKNAIDKLFVLFGaeilKKIPGRVSTEVDARLSFDKDAMVARARRLielYKeaGVGKDRILIKLSSTWEGIQAGKELE 157
Cdd:PRK03903 24 KDIKKAADKLLPLYE----KPDDGFISIEIDPFLEDDAAGSIEEGKRL---YK--TIGRPNVMIKVPATKAGYEAMSALM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 158 EQhGIHCNMTLLFSFAQAVACAEA-----------GVTLISPFVGRI---LDWHVANtdkKSYEPQEdpGVKSVTKIYNY 223
Cdd:PRK03903 95 KK-GISVNATLIFSPEQAKECAEAlneglkkntkdPKAVISVFVSRFdrlLDPKLAP---KNLQAKS--GIMNATKCYNQ 168
|
....*....
gi 2589166 224 YKKFGYKTI 232
Cdd:PRK03903 169 IEQHANKNI 177
|
|
| PRK09533 |
PRK09533 |
bifunctional transaldolase/phosoglucose isomerase; Validated |
43-181 |
3.13e-10 |
|
bifunctional transaldolase/phosoglucose isomerase; Validated
Pssm-ID: 236551 [Multi-domain] Cd Length: 948 Bit Score: 61.53 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 43 TTNPSLILAA-AQMPAYQELVEEAIAYGKKLGGPQEEQ-----IKNAIDKLFVLFgaEILKKIPGRVSTEVDARLSFDKD 116
Cdd:PRK09533 42 TSNPAIFEKAiGSSDEYDDAIKAALAEGDRSVIELYETlaiedIQAAADVLRPVY--DATDGADGFVSLEVSPYLALDTE 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2589166 117 AMVARARRLIelykeAGVGKDRILIKLSSTWEGIQAGKELEEQhGIHCNMTLLFSFAQAVACAEA 181
Cdd:PRK09533 120 GTIAEARRLW-----AAVDRPNLMIKVPATPEGLPAIRQLIAE-GINVNVTLLFSQDVYEEVAEA 178
|
|
| PRK12656 |
PRK12656 |
fructose-6-phosphate aldolase; Reviewed |
114-260 |
9.66e-03 |
|
fructose-6-phosphate aldolase; Reviewed
Pssm-ID: 183656 [Multi-domain] Cd Length: 222 Bit Score: 37.03 E-value: 9.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2589166 114 DKDAMVARARRLIElykEAGvgkDRILIKLSSTWEGIQAGKELEEQhGIHCNMTLLFSFAQAVACAEAGVTLISPFVGRI 193
Cdd:PRK12656 65 DYEGILKDAHEIRR---QCG---DDVYIKVPVTPAGLAAIKTLKAE-GYHITATAIYTVFQGLLAIEAGADYLAPYYNRM 137
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2589166 194 LDWHVANTDKKSYEPQEDPGVKSVTKIynyykkfgyktivMGASFRNTGEI-KALA-GCDFLTISPKLL 260
Cdd:PRK12656 138 ENLNIDSNAVIGQLAEAIDRENSDSKI-------------LAASFKNVAQVnKAFAlGAQAVTAGPDVF 193
|
|
| |
