|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05269 |
PRK05269 |
transaldolase B; Provisional |
1-319 |
0e+00 |
|
transaldolase B; Provisional
Pssm-ID: 235381 [Multi-domain] Cd Length: 318 Bit Score: 563.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 1 MSVLEQLKGASVVVADTGDFNAIKEFQPTDATTNPSLILAASKMEQYAALIDQSVAYAKEHASGHQEVLQAAMDRLFVVF 80
Cdd:PRK05269 2 TNKLEQLKQFTTVVADTGDIEAIKKYQPQDATTNPSLILKAAQIPEYAPLIDDAVAWAKQQSGDRAQQIDDAIDKLAVNF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 81 GKEILKTIPGRVSTEVDARLSFDTQASIDRALGLIAQYEKEGISKDRILIKLASTWEGIRAAKFLEsKHGIHCNMTLLFN 160
Cdd:PRK05269 82 GLEILKLIPGRVSTEVDARLSFDTEATIAKARKLIALYEEAGISKDRILIKIASTWEGIRAAEQLE-KEGINCNLTLLFS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 161 FEQAVACAESGVTLISPFVGRIMDWFVKNTDQKAYTRKDDPGVVSVTRIFNYYKKYDYKTQVMAASFRNTEEIKGLVGCD 240
Cdd:PRK05269 161 FAQARACAEAGVFLISPFVGRILDWYKKNTGKKEYAPAEDPGVVSVTKIYNYYKKHGYKTVVMGASFRNTGQILELAGCD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25153750 241 LLTISPALLKQLAAETelAPVVLSTSHAKTLDLPKVSIDEKAFRWALNEDAMATEKLAEGIRNFAKDARTLEKLIEAKI 319
Cdd:PRK05269 241 RLTISPALLEELAASE--GELERKLSPPGEAKARPVPLTEAEFRWQHNEDAMATEKLAEGIRKFAKDQEKLEKLIAAKL 317
|
|
| Transaldolase_TalAB |
cd00957 |
Transaldolases including both TalA and TalB; Transaldolases including both TalA and TalB. The ... |
2-315 |
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: 545.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 2 SVLEQLKGASVVVADTGDFNAIKEFQPTDATTNPSLILAASKMEQYAALIDQSVAYAKEHASGHQEVLQAAMDRLFVVFG 81
Cdd:cd00957 1 NQLDQLKKFTTIVADTGDFEAIKKFKPQDATTNPSLILAAAKLPEYNKLVDEAIAYAKKKGGSDEDQISNALDKLLVNFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 82 KEILKTIPGRVSTEVDARLSFDTQASIDRALGLIAQYEKEGISKDRILIKLASTWEGIRAAKFLEsKHGIHCNMTLLFNF 161
Cdd:cd00957 81 TEILKLIPGRVSTEVDARLSFDTNATIAKARKLIKLYEEAGIDKERILIKIAATWEGIQAAKQLE-KEGIHCNLTLLFSF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 162 EQAVACAESGVTLISPFVGRIMDWFVKNTDQKAYTRKDDPGVVSVTRIFNYYKKYDYKTQVMAASFRNTEEIKGLVGCDL 241
Cdd:cd00957 160 AQAVACAEAGVTLISPFVGRILDWYKKHSGDKAYTAEEDPGVASVKKIYNYYKKFGYKTKVMGASFRNIGQILALAGCDY 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25153750 242 LTISPALLKQLAAETELAPVVLSTSHAKTLDLPKVSIDEKAFRWALNEDAMATEKLAEGIRNFAKDARTLEKLI 315
Cdd:cd00957 240 LTISPALLEELKNSTAKVERKLDPAASKALDIHPNFLDESAFRWALNEDAMAVEKLSEGIRGFAKDAVKLEKLI 313
|
|
| talAB |
TIGR00874 |
transaldolase; This family includes the majority of known and predicted transaldolase ... |
2-319 |
2.96e-176 |
|
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: 490.04 E-value: 2.96e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 2 SVLEQLKGASVVVADTGDFNAIKEFQPTDATTNPSLILAASKMEQYAALIDQSVAYAKEHASGHQEVLQAAMDRLFVVFG 81
Cdd:TIGR00874 1 NQLDQLKQFTVVVADTGDIEAIKKYQPQDATTNPSLILAAAQLPKYAELIDEAVAWGKKQGKDDAQQVENALDKLAVNFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 82 KEILKTIPGRVSTEVDARLSFDTQASIDRALGLIAQYEKEGISKDRILIKLASTWEGIRAAKFLEsKHGIHCNMTLLFNF 161
Cdd:TIGR00874 81 LEILKIVPGRVSTEVDARLSFDTEATVEKARHLIKLYEDAGVDKKRILIKIASTWEGIRAAEELE-KEGIHCNLTLLFSF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 162 EQAVACAESGVTLISPFVGRIMDWFVKNTDQKAYTRKDDPGVVSVTRIFNYYKKYDYKTQVMAASFRNTEEIKGLVGCDL 241
Cdd:TIGR00874 160 VQAIACAEAKVTLISPFVGRILDWYKAATGKKEYSIEEDPGVASVKKIYNYYKKHGYPTEVMGASFRNKEEILALAGCDR 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25153750 242 LTISPALLKQLAAETELAPVVLSTSHAKTLDLPKVSIDEKAFRWALNEDAMATEKLAEGIRNFAKDARTLEKLIEAKI 319
Cdd:TIGR00874 240 LTISPALLDELKESTGPVERKLDPESAKKVDKQPIILDESEFRFLHNEDAMATEKLAEGIRKFAADQEKLEKLLEEKL 317
|
|
| TAL_FSA |
pfam00923 |
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ... |
13-315 |
1.04e-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: 264.79 E-value: 1.04e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 13 VVADTGDFNAIKEFQP----TDATTNPSLILAASKmeqYAALIDQSVAYAKEHAsghqevlqaamdrlfvvfgkeilkti 88
Cdd:pfam00923 1 IWLDTADRDLIKKLIEeggiDGVTTNPSIFLKAIE---YSALYDEAIAEIKEIG-------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 89 PGRVSTEVDARLSFDTQASIDRALGLIAQYEKegiskDRILIKLASTWEGIRAAKFLEsKHGIHCNMTLLFNFEQAVACA 168
Cdd:pfam00923 52 DGPVSLEVDPRLADDTEGTIEEARRLIALYGR-----PNVLIKIPATWEGIKAIKELS-AEGINVNVTLIFSLAQALAAA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 169 ESGVTLISPFVGRIMDWFVKNTDQkayTRKDDPGVVSVTRIFNYYKKYDYKTQVMAASFRNTEEIKGLVGCDLLTISPAL 248
Cdd:pfam00923 126 EAGASVISPFVGRIDDWGDKRLGA---ALRGDDGIANAKEIYQIYKKYGWSTGVLAASFRNVLYVLALAGCDTITIPPDT 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25153750 249 LKQLAAetelapvvlstshaktldlpkvsidekafrwalnedamateklAEGIRNFAKDARTLEKLI 315
Cdd:pfam00923 203 LEALAK-------------------------------------------DEGVRKFAKDWEKLLGSI 226
|
|
| TalA |
COG0176 |
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ... |
13-311 |
1.57e-67 |
|
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: 210.32 E-value: 1.57e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 13 VVADTGDFNAIKEFQ----PTDATTNPSLILAASkmeqyaalidqsvayakehasghqevlqaamDRLFVVFGKEILKTI 88
Cdd:COG0176 3 LWLDTADREEIKELIdlggVDGVTTNPSLIAKAG-------------------------------IKDFVEDIREICDIV 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 89 PGRVSTEVdarLSFDTQASIDRALGLIAqyekegISKDRILIKLASTWEGIRAAKFLESKhGIHCNMTLLFNFEQAVACA 168
Cdd:COG0176 52 DGPVSAEV---LATDTEGMIAEARRLAA------LYRPNVVIKIPATEEGLKAIEELSAE-GIKVNVTLIFSAAQALLAA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 169 ESGVTLISPFVGRIMDWFVKntdqkaytrkddpGVVSVTRIFNYYKKYDYKTQVMAASFRNTEEIK--GLVGCDLLTISP 246
Cdd:COG0176 122 EAGASYVSPFVGRIDDIGID-------------GIALVREIYQIYKNYGARTRILAASFRNPLQVLeaALAGADTVTIPP 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25153750 247 ALLKQLAaetelapvvlstshaktldlpkvsidekafrwalnedamATEKLAEGIRNFAKDARTL 311
Cdd:COG0176 189 AVLEALA---------------------------------------DHPLTDEGIEKFLADWEKL 214
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05269 |
PRK05269 |
transaldolase B; Provisional |
1-319 |
0e+00 |
|
transaldolase B; Provisional
Pssm-ID: 235381 [Multi-domain] Cd Length: 318 Bit Score: 563.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 1 MSVLEQLKGASVVVADTGDFNAIKEFQPTDATTNPSLILAASKMEQYAALIDQSVAYAKEHASGHQEVLQAAMDRLFVVF 80
Cdd:PRK05269 2 TNKLEQLKQFTTVVADTGDIEAIKKYQPQDATTNPSLILKAAQIPEYAPLIDDAVAWAKQQSGDRAQQIDDAIDKLAVNF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 81 GKEILKTIPGRVSTEVDARLSFDTQASIDRALGLIAQYEKEGISKDRILIKLASTWEGIRAAKFLEsKHGIHCNMTLLFN 160
Cdd:PRK05269 82 GLEILKLIPGRVSTEVDARLSFDTEATIAKARKLIALYEEAGISKDRILIKIASTWEGIRAAEQLE-KEGINCNLTLLFS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 161 FEQAVACAESGVTLISPFVGRIMDWFVKNTDQKAYTRKDDPGVVSVTRIFNYYKKYDYKTQVMAASFRNTEEIKGLVGCD 240
Cdd:PRK05269 161 FAQARACAEAGVFLISPFVGRILDWYKKNTGKKEYAPAEDPGVVSVTKIYNYYKKHGYKTVVMGASFRNTGQILELAGCD 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25153750 241 LLTISPALLKQLAAETelAPVVLSTSHAKTLDLPKVSIDEKAFRWALNEDAMATEKLAEGIRNFAKDARTLEKLIEAKI 319
Cdd:PRK05269 241 RLTISPALLEELAASE--GELERKLSPPGEAKARPVPLTEAEFRWQHNEDAMATEKLAEGIRKFAKDQEKLEKLIAAKL 317
|
|
| Transaldolase_TalAB |
cd00957 |
Transaldolases including both TalA and TalB; Transaldolases including both TalA and TalB. The ... |
2-315 |
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: 545.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 2 SVLEQLKGASVVVADTGDFNAIKEFQPTDATTNPSLILAASKMEQYAALIDQSVAYAKEHASGHQEVLQAAMDRLFVVFG 81
Cdd:cd00957 1 NQLDQLKKFTTIVADTGDFEAIKKFKPQDATTNPSLILAAAKLPEYNKLVDEAIAYAKKKGGSDEDQISNALDKLLVNFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 82 KEILKTIPGRVSTEVDARLSFDTQASIDRALGLIAQYEKEGISKDRILIKLASTWEGIRAAKFLEsKHGIHCNMTLLFNF 161
Cdd:cd00957 81 TEILKLIPGRVSTEVDARLSFDTNATIAKARKLIKLYEEAGIDKERILIKIAATWEGIQAAKQLE-KEGIHCNLTLLFSF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 162 EQAVACAESGVTLISPFVGRIMDWFVKNTDQKAYTRKDDPGVVSVTRIFNYYKKYDYKTQVMAASFRNTEEIKGLVGCDL 241
Cdd:cd00957 160 AQAVACAEAGVTLISPFVGRILDWYKKHSGDKAYTAEEDPGVASVKKIYNYYKKFGYKTKVMGASFRNIGQILALAGCDY 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25153750 242 LTISPALLKQLAAETELAPVVLSTSHAKTLDLPKVSIDEKAFRWALNEDAMATEKLAEGIRNFAKDARTLEKLI 315
Cdd:cd00957 240 LTISPALLEELKNSTAKVERKLDPAASKALDIHPNFLDESAFRWALNEDAMAVEKLSEGIRGFAKDAVKLEKLI 313
|
|
| talAB |
TIGR00874 |
transaldolase; This family includes the majority of known and predicted transaldolase ... |
2-319 |
2.96e-176 |
|
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: 490.04 E-value: 2.96e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 2 SVLEQLKGASVVVADTGDFNAIKEFQPTDATTNPSLILAASKMEQYAALIDQSVAYAKEHASGHQEVLQAAMDRLFVVFG 81
Cdd:TIGR00874 1 NQLDQLKQFTVVVADTGDIEAIKKYQPQDATTNPSLILAAAQLPKYAELIDEAVAWGKKQGKDDAQQVENALDKLAVNFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 82 KEILKTIPGRVSTEVDARLSFDTQASIDRALGLIAQYEKEGISKDRILIKLASTWEGIRAAKFLEsKHGIHCNMTLLFNF 161
Cdd:TIGR00874 81 LEILKIVPGRVSTEVDARLSFDTEATVEKARHLIKLYEDAGVDKKRILIKIASTWEGIRAAEELE-KEGIHCNLTLLFSF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 162 EQAVACAESGVTLISPFVGRIMDWFVKNTDQKAYTRKDDPGVVSVTRIFNYYKKYDYKTQVMAASFRNTEEIKGLVGCDL 241
Cdd:TIGR00874 160 VQAIACAEAKVTLISPFVGRILDWYKAATGKKEYSIEEDPGVASVKKIYNYYKKHGYPTEVMGASFRNKEEILALAGCDR 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25153750 242 LTISPALLKQLAAETELAPVVLSTSHAKTLDLPKVSIDEKAFRWALNEDAMATEKLAEGIRNFAKDARTLEKLIEAKI 319
Cdd:TIGR00874 240 LTISPALLDELKESTGPVERKLDPESAKKVDKQPIILDESEFRFLHNEDAMATEKLAEGIRKFAADQEKLEKLLEEKL 317
|
|
| PTZ00411 |
PTZ00411 |
transaldolase-like protein; Provisional |
1-319 |
3.60e-170 |
|
transaldolase-like protein; Provisional
Pssm-ID: 240406 Cd Length: 333 Bit Score: 475.38 E-value: 3.60e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 1 MSVLEQLKGASVVVADTGDFNAIKEFQPTDATTNPSLILAASKMEQYAALIDQSVAYAKEHASGH----------QEVLQ 70
Cdd:PTZ00411 2 PNQLEALKEHTTVVADTGDFSLLKKFQPEDATTNPSLVLAAAQMPEYAHLIDDAIKYAKANVSRLrdpllsdeekEELVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 71 AAMDRLFVVFGKEILKTIPGRVSTEVDARLSFDTQASIDRALGLIAQYEKEGISKDRILIKLASTWEGIRAAKFLEsKHG 150
Cdd:PTZ00411 82 LVVDKLTVNFGVEILKIVPGRVSTEVDARLSFDKQAMVDKARKIIKMYEEAGISKDRILIKLASTWEGIQAAKALE-KEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 151 IHCNMTLLFNFEQAVACAESGVTLISPFVGRIMDWFVKNTDQKAYTRKDDPGVVSVTRIFNYYKKYDYKTQVMAASFRNT 230
Cdd:PTZ00411 161 IHCNLTLLFSFAQAVACAQAGVTLISPFVGRILDWYKKPEKAESYVGAQDPGVISVTKIYNYYKKHGYKTIVMGASFRNT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 231 EEIKGLVGCDLLTISPALLKQLAAeTELAPV--VLSTSHAKTLDLPKVSIDEKAFRWALNEDAMATEKLAEGIRNFAKDA 308
Cdd:PTZ00411 241 GEILELAGCDKLTISPKLLEELAN-TEDGPVerKLDPEKLTEDTEKLPELTEKEFRWELNEDAMATEKLAEGIRNFAKDL 319
|
330
....*....|.
gi 25153750 309 RTLEKLIEAKI 319
Cdd:PTZ00411 320 EKLENVIRAKL 330
|
|
| PRK12309 |
PRK12309 |
transaldolase; |
1-315 |
4.28e-166 |
|
transaldolase;
Pssm-ID: 183426 [Multi-domain] Cd Length: 391 Bit Score: 467.29 E-value: 4.28e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 1 MSVLEQLKGASVVVADTGDFNAIKEFQPTDATTNPSLILAASKMEQYAALIDQSVAYAKEHA---SGHQEVLQAAMDRLF 77
Cdd:PRK12309 3 ASLLEQLRQMTVVVADTGDIQAIEKFTPRDATTNPSLITAAAQMPQYQSIVDETLRQARKELgsdAPVEDVVALAFDRLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 78 VVFGKEILKTIPGRVSTEVDARLSFDTQASIDRALGLIAQYEKEGISKDRILIKLASTWEGIRAAKFLEsKHGIHCNMTL 157
Cdd:PRK12309 83 VAFGLKILKIVPGRVSTEVDARLSYDTEATIAKARKLISLYEDAGISRDRVLIKIASTWEGIKAAEVLE-KEGIHCNLTL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 158 LFNFEQAVACAESGVTLISPFVGRIMDWFVKNTDQKAYTRKDDPGVVSVTRIFNYYKKYDYKTQVMAASFRNTEEIKGLV 237
Cdd:PRK12309 162 LFGFHQAIACAEAGVTLISPFVGRILDWYKKETGRDSYPGAEDPGVQSVTQIYNYYKKFGYKTEVMGASFRNIGEIIELA 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 25153750 238 GCDLLTISPALLKQLAAETELAPVVLSTSHAKTLDLPKVSIDEKAFRWALNEDAMATEKLAEGIRNFAKDARTLEKLI 315
Cdd:PRK12309 242 GCDLLTISPKLLEQLRSTEAELPRKLDPANAAGMEIEKIHMDRATFDKMHAEDRMASEKLDEGIKGFSKALETLEKLL 319
|
|
| PRK12346 |
PRK12346 |
transaldolase A; Provisional |
1-319 |
8.42e-160 |
|
transaldolase A; Provisional
Pssm-ID: 183458 Cd Length: 316 Bit Score: 448.40 E-value: 8.42e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 1 MSVLEQLKGASVVVADTGDFNAIKEFQPTDATTNPSLILAASKMEQYAALIDQSVAYAKEHASGHQEVLQAAMDRLFVVF 80
Cdd:PRK12346 1 MNQLDGIKQFTTVVADSGDIESIRHYHPQDATTNPSLLLKAAGLPQYQHLIDDAIAWGKKQGGTQEQQVVAACDKLAVNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 81 GKEILKTIPGRVSTEVDARLSFDTQASIDRALGLIAQYEKEGISKDRILIKLASTWEGIRAAKFLEsKHGIHCNMTLLFN 160
Cdd:PRK12346 81 GAEILKSVPGRVSTEVDARLSFDREKSIEKARHLVDLYQQQGIDKSRILIKLASTWEGIRAAEELE-KEGINCNLTLLFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 161 FEQAVACAESGVTLISPFVGRIMDWFVKNTDQKAYTRKDDPGVVSVTRIFNYYKKYDYKTQVMAASFRNTEEIKGLVGCD 240
Cdd:PRK12346 160 FAQARACAEAGVFLISPFVGRIYDWYQARKPMDPYVVEEDPGVKSVRNIYDYYKQHRYETIVMGASFRRTEQILALAGCD 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 25153750 241 LLTISPALLKQLAAETElaPVVLSTSHAKTLDLPKVSIDEKAFRWALNEDAMATEKLAEGIRNFAKDARTLEKLIEAKI 319
Cdd:PRK12346 240 RLTISPNLLKELQESES--PVERKLIPSSQTFPRPAPMSEAEFRWEHNQDAMAVEKLSEGIRLFAVDQRKLEDLLAAKL 316
|
|
| TAL_FSA |
pfam00923 |
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ... |
13-315 |
1.04e-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: 264.79 E-value: 1.04e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 13 VVADTGDFNAIKEFQP----TDATTNPSLILAASKmeqYAALIDQSVAYAKEHAsghqevlqaamdrlfvvfgkeilkti 88
Cdd:pfam00923 1 IWLDTADRDLIKKLIEeggiDGVTTNPSIFLKAIE---YSALYDEAIAEIKEIG-------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 89 PGRVSTEVDARLSFDTQASIDRALGLIAQYEKegiskDRILIKLASTWEGIRAAKFLEsKHGIHCNMTLLFNFEQAVACA 168
Cdd:pfam00923 52 DGPVSLEVDPRLADDTEGTIEEARRLIALYGR-----PNVLIKIPATWEGIKAIKELS-AEGINVNVTLIFSLAQALAAA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 169 ESGVTLISPFVGRIMDWFVKNTDQkayTRKDDPGVVSVTRIFNYYKKYDYKTQVMAASFRNTEEIKGLVGCDLLTISPAL 248
Cdd:pfam00923 126 EAGASVISPFVGRIDDWGDKRLGA---ALRGDDGIANAKEIYQIYKKYGWSTGVLAASFRNVLYVLALAGCDTITIPPDT 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25153750 249 LKQLAAetelapvvlstshaktldlpkvsidekafrwalnedamateklAEGIRNFAKDARTLEKLI 315
Cdd:pfam00923 203 LEALAK-------------------------------------------DEGVRKFAKDWEKLLGSI 226
|
|
| Transaldolase |
cd00439 |
Transaldolase; Transaldolase. Enzymes found in the non-oxidative branch of the pentose ... |
13-253 |
3.23e-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: 3.23e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 13 VVADTGDFNAIKE----FQPTDATTNPSLILAASKMEQYAALIDQSVAYAKEHASGHQEVLQAAMDRLFVVFGKEILKTI 88
Cdd:cd00439 2 PWYDTLDRPATDLlpliRGVRGVTTNPSIIQAAISTSNAYNDQFRTLVESGKDIESAYWELVVKDIQDACKLFEPIYDQT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 89 --PGRVSTEVDARLSFDTQASIDRALGLIaqyekEGISKDRILIKLASTWEGIRAAKFLESkHGIHCNMTLLFNFEQAVA 166
Cdd:cd00439 82 eaDGRVSVEVSARLADDTQGMVEAAKYLS-----KVVNRRNIYIKIPATAEGIPAIKDLIA-AGISVNVTLIFSIAQYEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 167 CAESGVTLISPFVGRIMDWFVKNTDQKAYTRKDDPGVVSVTRIFNYYKKYDYKTQVMAASFRNTEEIKGLVGCDLLTISP 246
Cdd:cd00439 156 VADAGTSVASPFVSRIDTLMDKMLEQIGLDLRGKAGVAQVTLAYKLYKQKFKKQRVLWASFSDTLYVAPLIGCDTVTTMP 235
|
....*..
gi 25153750 247 ALLKQLA 253
Cdd:cd00439 236 DQALEAG 242
|
|
| TalA |
COG0176 |
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ... |
13-311 |
1.57e-67 |
|
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: 210.32 E-value: 1.57e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 13 VVADTGDFNAIKEFQ----PTDATTNPSLILAASkmeqyaalidqsvayakehasghqevlqaamDRLFVVFGKEILKTI 88
Cdd:COG0176 3 LWLDTADREEIKELIdlggVDGVTTNPSLIAKAG-------------------------------IKDFVEDIREICDIV 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 89 PGRVSTEVdarLSFDTQASIDRALGLIAqyekegISKDRILIKLASTWEGIRAAKFLESKhGIHCNMTLLFNFEQAVACA 168
Cdd:COG0176 52 DGPVSAEV---LATDTEGMIAEARRLAA------LYRPNVVIKIPATEEGLKAIEELSAE-GIKVNVTLIFSAAQALLAA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 169 ESGVTLISPFVGRIMDWFVKntdqkaytrkddpGVVSVTRIFNYYKKYDYKTQVMAASFRNTEEIK--GLVGCDLLTISP 246
Cdd:COG0176 122 EAGASYVSPFVGRIDDIGID-------------GIALVREIYQIYKNYGARTRILAASFRNPLQVLeaALAGADTVTIPP 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25153750 247 ALLKQLAaetelapvvlstshaktldlpkvsidekafrwalnedamATEKLAEGIRNFAKDARTL 311
Cdd:COG0176 189 AVLEALA---------------------------------------DHPLTDEGIEKFLADWEKL 214
|
|
| Transaldolase_FSA |
cd00956 |
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ... |
16-254 |
9.66e-32 |
|
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: 117.68 E-value: 9.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 16 DTGDFNAIKEFQPT----DATTNPSLIlAASKMEQYAALIdqsvayakehasghqevlqaamdrlfvvfgKEILKTIPGR 91
Cdd:cd00956 5 DTADLEEIKKASETglldGVTTNPSLI-AKSGRIDFEAVL------------------------------KEICEIIDGP 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 92 VSTEVDARlSFDtqasidralGLIAQYEKegISK--DRILIKLASTWEGIRAAKFLeSKHGIHCNMTLLFNFEQAVACAE 169
Cdd:cd00956 54 VSAQVVST-DAE---------GMVAEARK--LASlgGNVVVKIPVTEDGLKAIKKL-SEEGIKTNVTAIFSAAQALLAAK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 170 SGVTLISPFVGRImdwfvkntdqkaytrkDDPGVVS---VTRIFNYYKKYDYKTQVMAASFRNTEEIK--GLVGCDLLTI 244
Cdd:cd00956 121 AGATYVSPFVGRI----------------DDLGGDGmelIREIRTIFDNYGFDTKILAASIRNPQHVIeaALAGADAITL 184
|
250
....*....|
gi 25153750 245 SPALLKQLAA 254
Cdd:cd00956 185 PPDVLEQLLK 194
|
|
| PRK03903 |
PRK03903 |
transaldolase; Provisional |
90-226 |
3.66e-11 |
|
transaldolase; Provisional
Pssm-ID: 235171 Cd Length: 274 Bit Score: 62.69 E-value: 3.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 90 GRVSTEVDARLSFDTQASIDRALGLIAQyekegISKDRILIKLASTWEGIRAAKFLESKhGIHCNMTLLFNFEQAVACAE 169
Cdd:PRK03903 43 GFISIEIDPFLEDDAAGSIEEGKRLYKT-----IGRPNVMIKVPATKAGYEAMSALMKK-GISVNATLIFSPEQAKECAE 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25153750 170 -----------SGVTLISPFVGRI---MDWFVKNTDQKAYTrkddpGVVSVTRIFNYYKKYD-YKTQVMAAS 226
Cdd:PRK03903 117 alneglkkntkDPKAVISVFVSRFdrlLDPKLAPKNLQAKS-----GIMNATKCYNQIEQHAnKNIRTLFAS 183
|
|
| Transaldolase_like |
cd00955 |
Transaldolase-like proteins from plants and bacteria; Transaldolase-like proteins from plants ... |
31-169 |
4.17e-10 |
|
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: 60.03 E-value: 4.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 31 ATTNPSLILAA-SKMEQYAALIDQSVAYAKEHASGHQEV----LQAAMDRLFVVFgkEILKTIPGRVSTEVDARLSFDTQ 105
Cdd:cd00955 29 VTSNPAIFEKAiAGSAAYDDQIRALKGQGLDAEAIYEALaiedIQDACDLLAPVY--EQTGGNDGYVSLEVSPRLADDTQ 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25153750 106 ASIDRALGLiaqYEKEGisKDRILIKLASTWEGIRAAKFLESKhGIHCNMTLLFNFEQAVACAE 169
Cdd:cd00955 107 GTIAEAKRL---WKAVG--RPNLMIKIPATEAGLPAIEELIAA-GISVNVTLIFSLEQYEAVAE 164
|
|
| PRK03343 |
PRK03343 |
transaldolase; Validated |
32-169 |
4.53e-07 |
|
transaldolase; Validated
Pssm-ID: 235117 Cd Length: 368 Bit Score: 50.59 E-value: 4.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 32 TTNPSLILAA-SKMEQYAALIDqsvAYAKEHASGHQEV-------LQAAMDRLFVVFgkEILKTIPGRVSTEVDARLSFD 103
Cdd:PRK03343 43 TSNPAIFQKAiAGGDAYDAQIA---ELAAAGADVEEAYeelttadVRNACDVLRPVY--EATGGVDGRVSIEVSPRLAHD 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 25153750 104 TQASIDRALGLIAQyekegISKDRILIKLASTWEGIRAAKFLESKhGIHCNMTLLFNFEQAVACAE 169
Cdd:PRK03343 118 TEATIAEARRLWAA-----VDRPNLMIKIPATPEGLPAIEALIAE-GISVNVTLIFSVERYRAVAD 177
|
|
| PRK09533 |
PRK09533 |
bifunctional transaldolase/phosoglucose isomerase; Validated |
70-169 |
1.03e-06 |
|
bifunctional transaldolase/phosoglucose isomerase; Validated
Pssm-ID: 236551 [Multi-domain] Cd Length: 948 Bit Score: 50.35 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 70 QAAMDRLFVVFgkEILKTIPGRVSTEVDARLSFDTQASIDRALGLIAQyekegISKDRILIKLASTWEGIRAAKFLESKh 149
Cdd:PRK09533 86 QAAADVLRPVY--DATDGADGFVSLEVSPYLALDTEGTIAEARRLWAA-----VDRPNLMIKVPATPEGLPAIRQLIAE- 157
|
90 100
....*....|....*....|
gi 25153750 150 GIHCNMTLLFNFEQAVACAE 169
Cdd:PRK09533 158 GINVNVTLLFSQDVYEEVAE 177
|
|
| PRK12653 |
PRK12653 |
fructose-6-phosphate aldolase; Reviewed |
16-262 |
8.73e-03 |
|
fructose-6-phosphate aldolase; Reviewed
Pssm-ID: 183653 [Multi-domain] Cd Length: 220 Bit Score: 37.07 E-value: 8.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 16 DTGDFNAIKE----FQPTDATTNPSlILAASKMEqyaalIDQSVAYAKEHASGHQevlqaamdRLFvvfgkeilktipgr 91
Cdd:PRK12653 6 DTSDVVAVKAlsriFPLAGVTTNPS-IIAAGKKP-----LEVVLPQLHEAMGGQG--------RLF-------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 92 vstevdarlsfdTQASIDRALGLIAQYEKEGISKDRILIKLASTWEGIRAAKFLEsKHGIHCNMTLLFNFEQAVACAESG 171
Cdd:PRK12653 58 ------------AQVMATTAEGMVNDARKLRSIIADIVVKVPVTAEGLAAIKMLK-AEGIPTLGTAVYGAAQGLLSALAG 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25153750 172 VTLISPFVGRImdwfvkntdqkayTRKDDPGVVSVTRIFNYYKKYDYKTQVMAASFRNTEEIKG--LVGCDLLTISPALL 249
Cdd:PRK12653 125 AEYVAPYVNRI-------------DAQGGSGIQTVTDLQQLLKMHAPQAKVLAASFKTPRQALDclLAGCESITLPLDVA 191
|
250
....*....|...
gi 25153750 250 KQLAAETELAPVV 262
Cdd:PRK12653 192 QQMISYPAVDAAV 204
|
|
| |
