|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03343 |
PRK03343 |
transaldolase; Validated |
77-434 |
0e+00 |
|
transaldolase; Validated
Pssm-ID: 235117 Cd Length: 368 Bit Score: 526.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 77 LHDLYEkEGQSPWYDNLCRpvtDLLP------LIA-RGVRGVTSNPAIFQKAISTSNAYNDQFRTLVESGKDIESAYWEL 149
Cdd:PRK03343 5 LQALSA-LGQSIWLDDLSR---DRLTsgnlarLIDeKGVVGVTSNPAIFQKAIAGGDAYDAQIAELAAAGADVEEAYEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 150 VVKDIQDACKLFEPIYDQTEGADGYVSVEVSPRLADDTQGTVEAAKYLSKVVNRRNVYIKIPATAPCIPSIRDVIAAGIS 229
Cdd:PRK03343 81 TTADVRNACDVLRPVYEATGGVDGRVSIEVSPRLAHDTEATIAEARRLWAAVDRPNLMIKIPATPEGLPAIEALIAEGIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 230 VNVTLIFSIARYEAVIDAYLDGLE---ASGLDdLSRVTSVASFFVSRVDTLMDKMLEQIGTPEALDLRGKAAVAQAALAY 306
Cdd:PRK03343 161 VNVTLIFSVERYRAVADAYLRGLEkrlAAGHD-LSKIHSVASFFVSRVDTEVDKRLEAIGTDEALALRGKAAIANARLAY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 307 KLYQQKFSGPRWEALVKKGAKKQRLLWASTSVKNPAYSDTLYVAPLIGPDTVSTMPDQALEAFADHGIVKRTIDANVSEA 386
Cdd:PRK03343 240 QAYEEVFASPRWAALAAAGARPQRPLWASTGTKNPAYSDTLYVDELVAPDTVNTMPEATLDAFADHGEVADTLTGDYEEA 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 15240625 387 EGIYSALEKLGIDWNKVGEQLEDEGVDSFKKSFESLLGTLQDKANTLK 434
Cdd:PRK03343 320 QAVLAALAALGIDLDDVTAVLEEEGVDKFEASWNELLASLEAKLDALA 367
|
|
| Transaldolase_like |
cd00955 |
Transaldolase-like proteins from plants and bacteria; Transaldolase-like proteins from plants ... |
87-421 |
0e+00 |
|
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: 524.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 87 SPWYDNLCRPVTDLLPLI----ARGVRGVTSNPAIFQKAISTSNAYNDQFRTLVESGKDIESAYWELVVKDIQDACKLFE 162
Cdd:cd00955 1 SLWLDNLSRSFIDNGFLKrlieEQGVVGVTSNPAIFEKAIAGSAAYDDQIRALKGQGLDAEAIYEALAIEDIQDACDLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 163 PIYDQTEGADGYVSVEVSPRLADDTQGTVEAAKYLSKVVNRRNVYIKIPATAPCIPSIRDVIAAGISVNVTLIFSIARYE 242
Cdd:cd00955 81 PVYEQTGGNDGYVSLEVSPRLADDTQGTIAEAKRLWKAVGRPNLMIKIPATEAGLPAIEELIAAGISVNVTLIFSLEQYE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 243 AVIDAYLDGLEAS--GLDDLSRVTSVASFFVSRVDTLMDKMLEQigtPEALDLRGKAAVAQAALAYKLYQQKFSGPRWEA 320
Cdd:cd00955 161 AVAEAYLRGLERRveGGGDLSQVASVASFFVSRVDTLIDKKLDA---PEAKALQGKVAIANAKLAYQEYQEKFSGPRWAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 321 LVKKGAKKQRLLWASTSVKNPAYSDTLYVAPLIGPDTVSTMPDQALEAFADHGIVKRTIDANVSEAEGIYSALEKLGIDW 400
Cdd:cd00955 238 LAAAGAKPQRLLWASTGVKNPAYPDVLYVEELIGPDTVNTMPDATLKAFADHGEVRPTLEEGLEEAERVLAELERLGIDL 317
|
330 340
....*....|....*....|.
gi 15240625 401 NKVGEQLEDEGVDSFKKSFES 421
Cdd:cd00955 318 DAVTEKLLKEGVKKFKDSFEK 338
|
|
| tal_mycobact |
TIGR00876 |
transaldolase, mycobacterial type; This model describes one of three related but easily ... |
84-423 |
2.02e-98 |
|
transaldolase, mycobacterial type; This model describes one of three related but easily separable famiiles of known and putative transaldolases. This family and the family typified by E. coli TalA and TalB both contain experimentally verified examples. [Energy metabolism, Pentose phosphate pathway]
Pssm-ID: 129954 Cd Length: 350 Bit Score: 298.57 E-value: 2.02e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 84 EGQSPWYDNLCRPV---TDLLPLIARG-VRGVTSNPAIFQKAISTSNAYNDQFRTLVESGKDIESAYWELVVKDIQDACK 159
Cdd:TIGR00876 1 AEFSLWCDDIERDFlenGDFLELIDKGaICGATSNPSIFCEAISEGAFYDAEIAELAAKGADADAIIETLALDDILQACD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 160 LFEPIYDQTEGADGYVSVEVSPRLADDTQGTVEAAKYLSKVVNRRNVYIKIPATAPCIPSIRDVIAAGISVNVTLIFSIA 239
Cdd:TIGR00876 81 ALMPLWEDSDGNDGRISIEIDPFLADDAAKSIDEAIELFKILDRPNLFIKIPASEAGIEAISALLAAGIPVNVTLIFSPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 240 RYEAVIDAYLDGLE--ASGLDDLSRVTSVASFFVSRVDTLMDKMLEQIGTPEALDLRGKAAVAQAALAYKLYQQKFSGP- 316
Cdd:TIGR00876 161 IAGEIADALAKEAEkaRQAGHSLSKIHAVASFFVSRFDKEIDKLLDKIGSRQALELQAQAGIANARLAYATYREVFEDSd 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 317 RWEALVKKGAKKQRLLWASTSVKNPAYSDTLYVAPLIGPDTVSTMPDQALEAFADHGIVK-RTIDANVSEAEGIYSALEK 395
Cdd:TIGR00876 241 CYRQIKQDAAKLQRPLFASTGVKNNDLADDLYIKALCAKHSINTAPEEAIDAVADDGNIEcDTPLGTASDAEAFFDELGA 320
|
330 340
....*....|....*....|....*...
gi 15240625 396 LGIDWNKVGEQLEDEGVDSFKKSFESLL 423
Cdd:TIGR00876 321 HGIDLEDTAAKLEEEGLIAFEASFEELL 348
|
|
| TAL_FSA |
pfam00923 |
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ... |
106-426 |
2.81e-59 |
|
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: 193.14 E-value: 2.81e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 106 RGVRGVTSNPAIFQKAISTSNAYNDQfrtlvesgkdiesaywelvvkdIQDACKLfepiydqtegADGYVSVEVSPRLAD 185
Cdd:pfam00923 18 GGIDGVTTNPSIFLKAIEYSALYDEA----------------------IAEIKEI----------GDGPVSLEVDPRLAD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 186 DTQGTVEAAKYLSKVVNRRNVYIKIPATAPCIPSIRDVIAAGISVNVTLIFSIARYEAVIDAyldgleasglddlsrVTS 265
Cdd:pfam00923 66 DTEGTIEEARRLIALYGRPNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALAAAEA---------------GAS 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 266 VASFFVSRVDTLMDKMLEQigtpealDLRGKAAVAQAALAYKLYQQKfsgpRWealvkkgakkqrllwaSTSVKNPAYSD 345
Cdd:pfam00923 131 VISPFVGRIDDWGDKRLGA-------ALRGDDGIANAKEIYQIYKKY----GW----------------STGVLAASFRN 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 346 TLYVAPLIGPDTVsTMPDQALEAFADhgivkrtidanvseaegiysaleklgidwnkvgeqleDEGVDSFKKSFESLLGT 425
Cdd:pfam00923 184 VLYVLALAGCDTI-TIPPDTLEALAK-------------------------------------DEGVRKFAKDWEKLLGS 225
|
.
gi 15240625 426 L 426
Cdd:pfam00923 226 I 226
|
|
| TalA |
COG0176 |
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ... |
86-422 |
1.50e-47 |
|
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: 162.17 E-value: 1.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 86 QSPWYDNLCRP-VTDLLPLiaRGVRGVTSNPAIFQKAISTSnayndqfrtlvesgkdiesaywelVVKDIQDACKLfepi 164
Cdd:COG0176 1 MKLWLDTADREeIKELIDL--GGVDGVTTNPSLIAKAGIKD------------------------FVEDIREICDI---- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 165 ydqtegADGYVSVEVsprLADDTQGTVEAAKYLSKVVnRRNVYIKIPATAPCIPSIRDVIAAGISVNVTLIFSIARYEAV 244
Cdd:COG0176 51 ------VDGPVSAEV---LATDTEGMIAEARRLAALY-RPNVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQALLA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 245 IDAyldgleasglddlsrVTSVASFFVSRVDTL-MDKM--LEQIgtpealdlrgkaavaqaalaYKLYQQKfsgprweal 321
Cdd:COG0176 121 AEA---------------GASYVSPFVGRIDDIgIDGIalVREI--------------------YQIYKNY--------- 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 322 vkkgAKKQRLLWASTsvknpaySDTLYV--APLIGPDTVsTMPDQALEAFADHGivkrtidanvseaegiysaleklgid 399
Cdd:COG0176 157 ----GARTRILAASF-------RNPLQVleAALAGADTV-TIPPAVLEALADHP-------------------------- 198
|
330 340
....*....|....*....|...
gi 15240625 400 wnkvgeqLEDEGVDSFKKSFESL 422
Cdd:COG0176 199 -------LTDEGIEKFLADWEKL 214
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03343 |
PRK03343 |
transaldolase; Validated |
77-434 |
0e+00 |
|
transaldolase; Validated
Pssm-ID: 235117 Cd Length: 368 Bit Score: 526.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 77 LHDLYEkEGQSPWYDNLCRpvtDLLP------LIA-RGVRGVTSNPAIFQKAISTSNAYNDQFRTLVESGKDIESAYWEL 149
Cdd:PRK03343 5 LQALSA-LGQSIWLDDLSR---DRLTsgnlarLIDeKGVVGVTSNPAIFQKAIAGGDAYDAQIAELAAAGADVEEAYEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 150 VVKDIQDACKLFEPIYDQTEGADGYVSVEVSPRLADDTQGTVEAAKYLSKVVNRRNVYIKIPATAPCIPSIRDVIAAGIS 229
Cdd:PRK03343 81 TTADVRNACDVLRPVYEATGGVDGRVSIEVSPRLAHDTEATIAEARRLWAAVDRPNLMIKIPATPEGLPAIEALIAEGIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 230 VNVTLIFSIARYEAVIDAYLDGLE---ASGLDdLSRVTSVASFFVSRVDTLMDKMLEQIGTPEALDLRGKAAVAQAALAY 306
Cdd:PRK03343 161 VNVTLIFSVERYRAVADAYLRGLEkrlAAGHD-LSKIHSVASFFVSRVDTEVDKRLEAIGTDEALALRGKAAIANARLAY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 307 KLYQQKFSGPRWEALVKKGAKKQRLLWASTSVKNPAYSDTLYVAPLIGPDTVSTMPDQALEAFADHGIVKRTIDANVSEA 386
Cdd:PRK03343 240 QAYEEVFASPRWAALAAAGARPQRPLWASTGTKNPAYSDTLYVDELVAPDTVNTMPEATLDAFADHGEVADTLTGDYEEA 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 15240625 387 EGIYSALEKLGIDWNKVGEQLEDEGVDSFKKSFESLLGTLQDKANTLK 434
Cdd:PRK03343 320 QAVLAALAALGIDLDDVTAVLEEEGVDKFEASWNELLASLEAKLDALA 367
|
|
| Transaldolase_like |
cd00955 |
Transaldolase-like proteins from plants and bacteria; Transaldolase-like proteins from plants ... |
87-421 |
0e+00 |
|
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: 524.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 87 SPWYDNLCRPVTDLLPLI----ARGVRGVTSNPAIFQKAISTSNAYNDQFRTLVESGKDIESAYWELVVKDIQDACKLFE 162
Cdd:cd00955 1 SLWLDNLSRSFIDNGFLKrlieEQGVVGVTSNPAIFEKAIAGSAAYDDQIRALKGQGLDAEAIYEALAIEDIQDACDLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 163 PIYDQTEGADGYVSVEVSPRLADDTQGTVEAAKYLSKVVNRRNVYIKIPATAPCIPSIRDVIAAGISVNVTLIFSIARYE 242
Cdd:cd00955 81 PVYEQTGGNDGYVSLEVSPRLADDTQGTIAEAKRLWKAVGRPNLMIKIPATEAGLPAIEELIAAGISVNVTLIFSLEQYE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 243 AVIDAYLDGLEAS--GLDDLSRVTSVASFFVSRVDTLMDKMLEQigtPEALDLRGKAAVAQAALAYKLYQQKFSGPRWEA 320
Cdd:cd00955 161 AVAEAYLRGLERRveGGGDLSQVASVASFFVSRVDTLIDKKLDA---PEAKALQGKVAIANAKLAYQEYQEKFSGPRWAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 321 LVKKGAKKQRLLWASTSVKNPAYSDTLYVAPLIGPDTVSTMPDQALEAFADHGIVKRTIDANVSEAEGIYSALEKLGIDW 400
Cdd:cd00955 238 LAAAGAKPQRLLWASTGVKNPAYPDVLYVEELIGPDTVNTMPDATLKAFADHGEVRPTLEEGLEEAERVLAELERLGIDL 317
|
330 340
....*....|....*....|.
gi 15240625 401 NKVGEQLEDEGVDSFKKSFES 421
Cdd:cd00955 318 DAVTEKLLKEGVKKFKDSFEK 338
|
|
| PRK09533 |
PRK09533 |
bifunctional transaldolase/phosoglucose isomerase; Validated |
82-433 |
1.67e-142 |
|
bifunctional transaldolase/phosoglucose isomerase; Validated
Pssm-ID: 236551 [Multi-domain] Cd Length: 948 Bit Score: 430.55 E-value: 1.67e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 82 EKEGQSPWYDNLCRPVT---DLLPLIAR-GVRGVTSNPAIFQKAISTSNAYNDQFRTLVESG-KDIESAYWELVVKDIQD 156
Cdd:PRK09533 8 AQHGQSVWLDFLARGFIakgELKRLVEEdGLRGVTSNPAIFEKAIGSSDEYDDAIKAALAEGdRSVIELYETLAIEDIQA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 157 ACKLFEPIYDQTEGADGYVSVEVSPRLADDTQGTVEAAKYLSKVVNRRNVYIKIPATAPCIPSIRDVIAAGISVNVTLIF 236
Cdd:PRK09533 88 AADVLRPVYDATDGADGFVSLEVSPYLALDTEGTIAEARRLWAAVDRPNLMIKVPATPEGLPAIRQLIAEGINVNVTLLF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 237 SIARYEAVIDAYLDGLE---ASGlDDLSRVTSVASFFVSRVDTLMDKMLEQ-------IGTPEALD-LRGKAAVAQAALA 305
Cdd:PRK09533 168 SQDVYEEVAEAYISGLEaraAKG-GDPSHVASVASFFVSRIDSAVDKRLDEkiaaandPAEKAALEaLKGKVAIANAKLA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 306 YKLYQQKFSGPRWEALVKKGAKKQRLLWASTSVKNPAYSDTLYVAPLIGPDTVSTMPDQALEAFADHGIVKRTIDANVSE 385
Cdd:PRK09533 247 YQRYKRLFAGPRWEALAAKGAKPQRLLWASTGTKNKAYSDVLYVEELIGPDTVNTMPPATLDAFRDHGKVRATLEEDVDE 326
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 15240625 386 AEGIYSALEKLGIDWNKVGEQLEDEGVDSFKKSFESLLGTLQDKANTL 433
Cdd:PRK09533 327 ARAVLADLAEAGISLDAVTDKLVAEGVQLFADAFDKLLGAVAEKREAL 374
|
|
| Transaldolase |
cd00439 |
Transaldolase; Transaldolase. Enzymes found in the non-oxidative branch of the pentose ... |
87-368 |
8.23e-109 |
|
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: 321.61 E-value: 8.23e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 87 SPWYDNLCRPVTDLLPLIaRGVRGVTSNPAIFQKAISTSNAYNDQFRTLVESGKDIESAYWELVVKDIQDACKLFEPIYD 166
Cdd:cd00439 1 SPWYDTLDRPATDLLPLI-RGVRGVTTNPSIIQAAISTSNAYNDQFRTLVESGKDIESAYWELVVKDIQDACKLFEPIYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 167 QTEGaDGYVSVEVSPRLADDTQGTVEAAKYLSKVVNRRNVYIKIPATAPCIPSIRDVIAAGISVNVTLIFSIARYEAVID 246
Cdd:cd00439 80 QTEA-DGRVSVEVSARLADDTQGMVEAAKYLSKVVNRRNIYIKIPATAEGIPAIKDLIAAGISVNVTLIFSIAQYEAVAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 247 AYldgleasglddlsrvTSVASFFVSRVDTLMDKMLEQIGtpeaLDLRGKAAVAQAALAYKLYQQKFsgprwealvkkga 326
Cdd:cd00439 159 AG---------------TSVASPFVSRIDTLMDKMLEQIG----LDLRGKAGVAQVTLAYKLYKQKF------------- 206
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 15240625 327 KKQRLLWASTsvknpaySDTLYVAPLIGPDTVSTMPDQALEA 368
Cdd:cd00439 207 KKQRVLWASF-------SDTLYVAPLIGCDTVTTMPDQALEA 241
|
|
| tal_mycobact |
TIGR00876 |
transaldolase, mycobacterial type; This model describes one of three related but easily ... |
84-423 |
2.02e-98 |
|
transaldolase, mycobacterial type; This model describes one of three related but easily separable famiiles of known and putative transaldolases. This family and the family typified by E. coli TalA and TalB both contain experimentally verified examples. [Energy metabolism, Pentose phosphate pathway]
Pssm-ID: 129954 Cd Length: 350 Bit Score: 298.57 E-value: 2.02e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 84 EGQSPWYDNLCRPV---TDLLPLIARG-VRGVTSNPAIFQKAISTSNAYNDQFRTLVESGKDIESAYWELVVKDIQDACK 159
Cdd:TIGR00876 1 AEFSLWCDDIERDFlenGDFLELIDKGaICGATSNPSIFCEAISEGAFYDAEIAELAAKGADADAIIETLALDDILQACD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 160 LFEPIYDQTEGADGYVSVEVSPRLADDTQGTVEAAKYLSKVVNRRNVYIKIPATAPCIPSIRDVIAAGISVNVTLIFSIA 239
Cdd:TIGR00876 81 ALMPLWEDSDGNDGRISIEIDPFLADDAAKSIDEAIELFKILDRPNLFIKIPASEAGIEAISALLAAGIPVNVTLIFSPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 240 RYEAVIDAYLDGLE--ASGLDDLSRVTSVASFFVSRVDTLMDKMLEQIGTPEALDLRGKAAVAQAALAYKLYQQKFSGP- 316
Cdd:TIGR00876 161 IAGEIADALAKEAEkaRQAGHSLSKIHAVASFFVSRFDKEIDKLLDKIGSRQALELQAQAGIANARLAYATYREVFEDSd 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 317 RWEALVKKGAKKQRLLWASTSVKNPAYSDTLYVAPLIGPDTVSTMPDQALEAFADHGIVK-RTIDANVSEAEGIYSALEK 395
Cdd:TIGR00876 241 CYRQIKQDAAKLQRPLFASTGVKNNDLADDLYIKALCAKHSINTAPEEAIDAVADDGNIEcDTPLGTASDAEAFFDELGA 320
|
330 340
....*....|....*....|....*...
gi 15240625 396 LGIDWNKVGEQLEDEGVDSFKKSFESLL 423
Cdd:TIGR00876 321 HGIDLEDTAAKLEEEGLIAFEASFEELL 348
|
|
| TAL_FSA |
pfam00923 |
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ... |
106-426 |
2.81e-59 |
|
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: 193.14 E-value: 2.81e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 106 RGVRGVTSNPAIFQKAISTSNAYNDQfrtlvesgkdiesaywelvvkdIQDACKLfepiydqtegADGYVSVEVSPRLAD 185
Cdd:pfam00923 18 GGIDGVTTNPSIFLKAIEYSALYDEA----------------------IAEIKEI----------GDGPVSLEVDPRLAD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 186 DTQGTVEAAKYLSKVVNRRNVYIKIPATAPCIPSIRDVIAAGISVNVTLIFSIARYEAVIDAyldgleasglddlsrVTS 265
Cdd:pfam00923 66 DTEGTIEEARRLIALYGRPNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALAAAEA---------------GAS 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 266 VASFFVSRVDTLMDKMLEQigtpealDLRGKAAVAQAALAYKLYQQKfsgpRWealvkkgakkqrllwaSTSVKNPAYSD 345
Cdd:pfam00923 131 VISPFVGRIDDWGDKRLGA-------ALRGDDGIANAKEIYQIYKKY----GW----------------STGVLAASFRN 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 346 TLYVAPLIGPDTVsTMPDQALEAFADhgivkrtidanvseaegiysaleklgidwnkvgeqleDEGVDSFKKSFESLLGT 425
Cdd:pfam00923 184 VLYVLALAGCDTI-TIPPDTLEALAK-------------------------------------DEGVRKFAKDWEKLLGS 225
|
.
gi 15240625 426 L 426
Cdd:pfam00923 226 I 226
|
|
| PRK03903 |
PRK03903 |
transaldolase; Provisional |
127-426 |
7.15e-52 |
|
transaldolase; Provisional
Pssm-ID: 235171 Cd Length: 274 Bit Score: 175.55 E-value: 7.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 127 AYNDQFRTLveSGKDIESAYWELVVKDIQDACKLFEPIYDQteGADGYVSVEVSPRLADDTQGTVEAAKYLSKVVNRRNV 206
Cdd:PRK03903 1 AYKDEIAKL--KGKKAKEIYEELAIKDIKKAADKLLPLYEK--PDDGFISIEIDPFLEDDAAGSIEEGKRLYKTIGRPNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 207 YIKIPATAPCIPSIRDVIAAGISVNVTLIFSIARYEAVIDAYLDGLEASGLDdlsrVTSVASFFVSRVDTLMDKMLEQIG 286
Cdd:PRK03903 77 MIKVPATKAGYEAMSALMKKGISVNATLIFSPEQAKECAEALNEGLKKNTKD----PKAVISVFVSRFDRLLDPKLAPKN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 287 tpealdLRGKAAVAQAALAYKLYQqkfsgprwealvKKGAKKQRLLWASTSVKNPAYSDTLYVAPLIGPDTVSTMPDQAL 366
Cdd:PRK03903 153 ------LQAKSGIMNATKCYNQIE------------QHANKNIRTLFASTGVKGDDLPKDYYIKELLFKNSINTAPLDTI 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 367 EAFADHGIVKRTIDANVSEAEGIYSALEKLGIDWNKVGEQLEDEGVDSFKKSFESLLGTL 426
Cdd:PRK03903 215 EAFLKDGNTEPKKPLKIEEIEAFFKELKSHNIDLENTYQKLLKDGLEAFKQAFEDILKSL 274
|
|
| TalA |
COG0176 |
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ... |
86-422 |
1.50e-47 |
|
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: 162.17 E-value: 1.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 86 QSPWYDNLCRP-VTDLLPLiaRGVRGVTSNPAIFQKAISTSnayndqfrtlvesgkdiesaywelVVKDIQDACKLfepi 164
Cdd:COG0176 1 MKLWLDTADREeIKELIDL--GGVDGVTTNPSLIAKAGIKD------------------------FVEDIREICDI---- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 165 ydqtegADGYVSVEVsprLADDTQGTVEAAKYLSKVVnRRNVYIKIPATAPCIPSIRDVIAAGISVNVTLIFSIARYEAV 244
Cdd:COG0176 51 ------VDGPVSAEV---LATDTEGMIAEARRLAALY-RPNVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQALLA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 245 IDAyldgleasglddlsrVTSVASFFVSRVDTL-MDKM--LEQIgtpealdlrgkaavaqaalaYKLYQQKfsgprweal 321
Cdd:COG0176 121 AEA---------------GASYVSPFVGRIDDIgIDGIalVREI--------------------YQIYKNY--------- 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 322 vkkgAKKQRLLWASTsvknpaySDTLYV--APLIGPDTVsTMPDQALEAFADHGivkrtidanvseaegiysaleklgid 399
Cdd:COG0176 157 ----GARTRILAASF-------RNPLQVleAALAGADTV-TIPPAVLEALADHP-------------------------- 198
|
330 340
....*....|....*....|...
gi 15240625 400 wnkvgeqLEDEGVDSFKKSFESL 422
Cdd:COG0176 199 -------LTDEGIEKFLADWEKL 214
|
|
| Transaldolase_FSA |
cd00956 |
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ... |
108-372 |
3.28e-12 |
|
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: 65.29 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 108 VRGVTSNPAIFQKAISTSnayndqfrtlvesgkdiesayWELVVKDIQDAcklfepiydqtegADGYVSVEVsprLADDT 187
Cdd:cd00956 21 LDGVTTNPSLIAKSGRID---------------------FEAVLKEICEI-------------IDGPVSAQV---VSTDA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 188 QGTVEAAKYLSKVVNrrNVYIKIPATAPCIPSIRDVIAAGISVNVTLIFSIARYEAVIDAYLDgleasglddlsrvtsVA 267
Cdd:cd00956 64 EGMVAEARKLASLGG--NVVVKIPVTEDGLKAIKKLSEEGIKTNVTAIFSAAQALLAAKAGAT---------------YV 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 268 SFFVSRV-DTLMD--KMLEQIgtpealdlrgkaavaqaALAYKLYQQkfsgprwealvkkgakKQRLLWAstSVKNPAYs 344
Cdd:cd00956 127 SPFVGRIdDLGGDgmELIREI-----------------RTIFDNYGF----------------DTKILAA--SIRNPQH- 170
|
250 260
....*....|....*....|....*...
gi 15240625 345 dtLYVAPLIGPDTVsTMPDQALEAFADH 372
Cdd:cd00956 171 --VIEAALAGADAI-TLPPDVLEQLLKH 195
|
|
| Transaldolase_TalAB |
cd00957 |
Transaldolases including both TalA and TalB; Transaldolases including both TalA and TalB. The ... |
111-239 |
1.97e-09 |
|
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: 58.78 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240625 111 VTSNPAIFQKAIStSNAYNDQFRTLVESGKD--------IESAYWELVVKDIQDACKLFEpiydqtegadGYVSVEVSPR 182
Cdd:cd00957 30 ATTNPSLILAAAK-LPEYNKLVDEAIAYAKKkggsdedqISNALDKLLVNFGTEILKLIP----------GRVSTEVDAR 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15240625 183 LADDTQGTVEAAKYLSKV-----VNRRNVYIKIPATAPCIPSIRDVIAAGISVNVTLIFSIA 239
Cdd:cd00957 99 LSFDTNATIAKARKLIKLyeeagIDKERILIKIAATWEGIQAAKQLEKEGIHCNLTLLFSFA 160
|
|
| PTZ00411 |
PTZ00411 |
transaldolase-like protein; Provisional |
172-239 |
2.41e-09 |
|
transaldolase-like protein; Provisional
Pssm-ID: 240406 Cd Length: 333 Bit Score: 58.60 E-value: 2.41e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15240625 172 DGYVSVEVSPRLADDTQGTVEAAK-----YLSKVVNRRNVYIKIPATAPCIPSIRDVIAAGISVNVTLIFSIA 239
Cdd:PTZ00411 100 PGRVSTEVDARLSFDKQAMVDKARkiikmYEEAGISKDRILIKLASTWEGIQAAKALEKEGIHCNLTLLFSFA 172
|
|
| PRK05269 |
PRK05269 |
transaldolase B; Provisional |
173-239 |
2.99e-07 |
|
transaldolase B; Provisional
Pssm-ID: 235381 [Multi-domain] Cd Length: 318 Bit Score: 52.08 E-value: 2.99e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15240625 173 GYVSVEVSPRLADDTQGTVEAAKYLSKVVNRRN-----VYIKIPATAPCIPSIRDVIAAGISVNVTLIFSIA 239
Cdd:PRK05269 91 GRVSTEVDARLSFDTEATIAKARKLIALYEEAGiskdrILIKIASTWEGIRAAEQLEKEGINCNLTLLFSFA 162
|
|
| |
