|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03343 |
PRK03343 |
transaldolase; Validated |
4-373 |
0e+00 |
|
transaldolase; Validated
Pssm-ID: 235117 Cd Length: 368 Bit Score: 677.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 4 QNPNLAALSAAGVSVWLDDLSRDRLRSGNLQELIDTKSVVGVTTNPSIFQKALSEGHTYDAQIAELAARGADVDATIRTV 83
Cdd:PRK03343 1 MMNPLQALSALGQSIWLDDLSRDRLTSGNLARLIDEKGVVGVTSNPAIFQKAIAGGDAYDAQIAELAAAGADVEEAYEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 84 TTDDVRSACDVLVPQWEDSDGVDGRVSIEVDPRLAHETEKTIQQAIELWKIVDRPNLFIKIPATKAGLPAISAVLAEGIS 163
Cdd:PRK03343 81 TTADVRNACDVLRPVYEATGGVDGRVSIEVSPRLAHDTEATIAEARRLWAAVDRPNLMIKIPATPEGLPAIEALIAEGIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 164 VNVTLIFSVQRYREVMDAYLTGMEKARQAGHSLSKIHSVASFFVSRVDTEIDKRLDRIGSRQALELRGQAGVANARLAYA 243
Cdd:PRK03343 161 VNVTLIFSVERYRAVADAYLRGLEKRLAAGHDLSKIHSVASFFVSRVDTEVDKRLEAIGTDEALALRGKAAIANARLAYQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 244 TYREVFeDSDRYRSLKVDGARVQRPLWASTGVKNPDYSDTLYVTELVAPHTVNTMPEKTIDAVADHGVIqGDTVTGTASD 323
Cdd:PRK03343 241 AYEEVF-ASPRWAALAAAGARPQRPLWASTGTKNPAYSDTLYVDELVAPDTVNTMPEATLDAFADHGEV-ADTLTGDYEE 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 624384300 324 AQAVFDQLGAIGIDLTDVFAVLEEEGVRKFEASWNELLQETRAHLDTAAQ 373
Cdd:PRK03343 319 AQAVLAALAALGIDLDDVTAVLEEEGVDKFEASWNELLASLEAKLDALAA 368
|
|
| tal_mycobact |
TIGR00876 |
transaldolase, mycobacterial type; This model describes one of three related but easily ... |
14-363 |
0e+00 |
|
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: 627.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 14 AGVSVWLDDLSRDRLRSGNLQELIDTKSVVGVTTNPSIFQKALSEGHTYDAQIAELAARGADVDATIRTVTTDDVRSACD 93
Cdd:TIGR00876 1 AEFSLWCDDIERDFLENGDFLELIDKGAICGATSNPSIFCEAISEGAFYDAEIAELAAKGADADAIIETLALDDILQACD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 94 VLVPQWEDSDGVDGRVSIEVDPRLAHETEKTIQQAIELWKIVDRPNLFIKIPATKAGLPAISAVLAEGISVNVTLIFSVQ 173
Cdd:TIGR00876 81 ALMPLWEDSDGNDGRISIEIDPFLADDAAKSIDEAIELFKILDRPNLFIKIPASEAGIEAISALLAAGIPVNVTLIFSPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 174 RYREVMDAYLTGMEKARQAGHSLSKIHSVASFFVSRVDTEIDKRLDRIGSRQALELRGQAGVANARLAYATYREVFEDSD 253
Cdd:TIGR00876 161 IAGEIADALAKEAEKARQAGHSLSKIHAVASFFVSRFDKEIDKLLDKIGSRQALELQAQAGIANARLAYATYREVFEDSD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 254 RYRSLKVDGARVQRPLWASTGVKNPDYSDTLYVTELVAPHTVNTMPEKTIDAVADHGVIQGDTVTGTASDAQAVFDQLGA 333
Cdd:TIGR00876 241 CYRQIKQDAAKLQRPLFASTGVKNNDLADDLYIKALCAKHSINTAPEEAIDAVADDGNIECDTPLGTASDAEAFFDELGA 320
|
330 340 350
....*....|....*....|....*....|
gi 624384300 334 IGIDLTDVFAVLEEEGVRKFEASWNELLQE 363
Cdd:TIGR00876 321 HGIDLEDTAAKLEEEGLIAFEASFEELLQE 350
|
|
| Transaldolase_like |
cd00955 |
Transaldolase-like proteins from plants and bacteria; Transaldolase-like proteins from plants ... |
17-359 |
6.74e-161 |
|
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: 454.47 E-value: 6.74e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 17 SVWLDDLSRDRLRSGNLQELIDTKSVVGVTTNPSIFQKALSEGHTYDAQIAELAARGADVDATIRTVTTDDVRSACDVLV 96
Cdd:cd00955 1 SLWLDNLSRSFIDNGFLKRLIEEQGVVGVTSNPAIFEKAIAGSAAYDDQIRALKGQGLDAEAIYEALAIEDIQDACDLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 97 PQWEDSDGVDGRVSIEVDPRLAHETEKTIQQAIELWKIVDRPNLFIKIPATKAGLPAISAVLAEGISVNVTLIFSVQRYR 176
Cdd:cd00955 81 PVYEQTGGNDGYVSLEVSPRLADDTQGTIAEAKRLWKAVGRPNLMIKIPATEAGLPAIEELIAAGISVNVTLIFSLEQYE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 177 EVMDAYLTGMEKARQAGHSLSKIHSVASFFVSRVDTEIDKRLDRigsRQALELRGQAGVANARLAYATYREVFEdSDRYR 256
Cdd:cd00955 161 AVAEAYLRGLERRVEGGGDLSQVASVASFFVSRVDTLIDKKLDA---PEAKALQGKVAIANAKLAYQEYQEKFS-GPRWA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 257 SLKVDGARVQRPLWASTGVKNPDYSDTLYVTELVAPHTVNTMPEKTIDAVADHGVIQGDTVTGTaSDAQAVFDQLGAIGI 336
Cdd:cd00955 237 ALAAAGAKPQRLLWASTGVKNPAYPDVLYVEELIGPDTVNTMPDATLKAFADHGEVRPTLEEGL-EEAERVLAELERLGI 315
|
330 340
....*....|....*....|...
gi 624384300 337 DLTDVFAVLEEEGVRKFEASWNE 359
Cdd:cd00955 316 DLDAVTEKLLKEGVKKFKDSFEK 338
|
|
| TAL_FSA |
pfam00923 |
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ... |
18-363 |
5.27e-77 |
|
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: 236.67 E-value: 5.27e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 18 VWLDDLSRDRLRsgnlqELIDTKSVVGVTTNPSIFQKALSEGHTYDAQIAELAARGadvdatirtvttddvrsacdvlvp 97
Cdd:pfam00923 1 IWLDTADRDLIK-----KLIEEGGIDGVTTNPSIFLKAIEYSALYDEAIAEIKEIG------------------------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 98 qwedsdgvDGRVSIEVDPRLAHETEKTIQQAIELWKIVDRPNLFIKIPATKAGLPAISAVLAEGISVNVTLIFSVQRYRE 177
Cdd:pfam00923 52 --------DGPVSLEVDPRLADDTEGTIEEARRLIALYGRPNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 178 VMDAyltgmekarqaghslskIHSVASFFVSRVDTEIDKRLDRigsrqalELRGQAGVANARLAYATYREVfedsdryrs 257
Cdd:pfam00923 124 AAEA-----------------GASVISPFVGRIDDWGDKRLGA-------ALRGDDGIANAKEIYQIYKKY--------- 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 258 lkvdgarvqrpLWaSTGVKNPDYSDTLYVTELVAPHTVnTMPEKTIDAVADhgviqgdtvtgtasdaqavfdqlgaigid 337
Cdd:pfam00923 171 -----------GW-STGVLAASFRNVLYVLALAGCDTI-TIPPDTLEALAK----------------------------- 208
|
330 340
....*....|....*....|....*.
gi 624384300 338 ltdvfavleEEGVRKFEASWNELLQE 363
Cdd:pfam00923 209 ---------DEGVRKFAKDWEKLLGS 225
|
|
| TalA |
COG0176 |
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ... |
16-360 |
1.24e-65 |
|
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: 207.24 E-value: 1.24e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 16 VSVWLDDLSRDRLRsgnlqELIDTKSVVGVTTNPSIFQKAlseghtydaqiaelaargadvdaTIRTvTTDDVRSACDVl 95
Cdd:COG0176 1 MKLWLDTADREEIK-----ELIDLGGVDGVTTNPSLIAKA-----------------------GIKD-FVEDIREICDI- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 96 vpqwedsdgVDGRVSIEVdprLAHETEKTIQQAIELWKIVdRPNLFIKIPATKAGLPAISAVLAEGISVNVTLIFSVQRY 175
Cdd:COG0176 51 ---------VDGPVSAEV---LATDTEGMIAEARRLAALY-RPNVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 176 REVMDAyltgmekarqaghslskIHSVASFFVSRVDTEidkrldrigsrqalelrGQAGVANARLAYATYREVfedsdry 255
Cdd:COG0176 118 LLAAEA-----------------GASYVSPFVGRIDDI-----------------GIDGIALVREIYQIYKNY------- 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 256 rslkvdGARvQRPLWASTGvknpdysDTLYVTE--LVAPHTVnTMPEKTIDAVADHGviqgdtvtgtasdaqavfdqlga 333
Cdd:COG0176 157 ------GAR-TRILAASFR-------NPLQVLEaaLAGADTV-TIPPAVLEALADHP----------------------- 198
|
330 340
....*....|....*....|....*..
gi 624384300 334 igidltdvfavLEEEGVRKFEASWNEL 360
Cdd:COG0176 199 -----------LTDEGIEKFLADWEKL 214
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03343 |
PRK03343 |
transaldolase; Validated |
4-373 |
0e+00 |
|
transaldolase; Validated
Pssm-ID: 235117 Cd Length: 368 Bit Score: 677.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 4 QNPNLAALSAAGVSVWLDDLSRDRLRSGNLQELIDTKSVVGVTTNPSIFQKALSEGHTYDAQIAELAARGADVDATIRTV 83
Cdd:PRK03343 1 MMNPLQALSALGQSIWLDDLSRDRLTSGNLARLIDEKGVVGVTSNPAIFQKAIAGGDAYDAQIAELAAAGADVEEAYEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 84 TTDDVRSACDVLVPQWEDSDGVDGRVSIEVDPRLAHETEKTIQQAIELWKIVDRPNLFIKIPATKAGLPAISAVLAEGIS 163
Cdd:PRK03343 81 TTADVRNACDVLRPVYEATGGVDGRVSIEVSPRLAHDTEATIAEARRLWAAVDRPNLMIKIPATPEGLPAIEALIAEGIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 164 VNVTLIFSVQRYREVMDAYLTGMEKARQAGHSLSKIHSVASFFVSRVDTEIDKRLDRIGSRQALELRGQAGVANARLAYA 243
Cdd:PRK03343 161 VNVTLIFSVERYRAVADAYLRGLEKRLAAGHDLSKIHSVASFFVSRVDTEVDKRLEAIGTDEALALRGKAAIANARLAYQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 244 TYREVFeDSDRYRSLKVDGARVQRPLWASTGVKNPDYSDTLYVTELVAPHTVNTMPEKTIDAVADHGVIqGDTVTGTASD 323
Cdd:PRK03343 241 AYEEVF-ASPRWAALAAAGARPQRPLWASTGTKNPAYSDTLYVDELVAPDTVNTMPEATLDAFADHGEV-ADTLTGDYEE 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 624384300 324 AQAVFDQLGAIGIDLTDVFAVLEEEGVRKFEASWNELLQETRAHLDTAAQ 373
Cdd:PRK03343 319 AQAVLAALAALGIDLDDVTAVLEEEGVDKFEASWNELLASLEAKLDALAA 368
|
|
| tal_mycobact |
TIGR00876 |
transaldolase, mycobacterial type; This model describes one of three related but easily ... |
14-363 |
0e+00 |
|
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: 627.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 14 AGVSVWLDDLSRDRLRSGNLQELIDTKSVVGVTTNPSIFQKALSEGHTYDAQIAELAARGADVDATIRTVTTDDVRSACD 93
Cdd:TIGR00876 1 AEFSLWCDDIERDFLENGDFLELIDKGAICGATSNPSIFCEAISEGAFYDAEIAELAAKGADADAIIETLALDDILQACD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 94 VLVPQWEDSDGVDGRVSIEVDPRLAHETEKTIQQAIELWKIVDRPNLFIKIPATKAGLPAISAVLAEGISVNVTLIFSVQ 173
Cdd:TIGR00876 81 ALMPLWEDSDGNDGRISIEIDPFLADDAAKSIDEAIELFKILDRPNLFIKIPASEAGIEAISALLAAGIPVNVTLIFSPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 174 RYREVMDAYLTGMEKARQAGHSLSKIHSVASFFVSRVDTEIDKRLDRIGSRQALELRGQAGVANARLAYATYREVFEDSD 253
Cdd:TIGR00876 161 IAGEIADALAKEAEKARQAGHSLSKIHAVASFFVSRFDKEIDKLLDKIGSRQALELQAQAGIANARLAYATYREVFEDSD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 254 RYRSLKVDGARVQRPLWASTGVKNPDYSDTLYVTELVAPHTVNTMPEKTIDAVADHGVIQGDTVTGTASDAQAVFDQLGA 333
Cdd:TIGR00876 241 CYRQIKQDAAKLQRPLFASTGVKNNDLADDLYIKALCAKHSINTAPEEAIDAVADDGNIECDTPLGTASDAEAFFDELGA 320
|
330 340 350
....*....|....*....|....*....|
gi 624384300 334 IGIDLTDVFAVLEEEGVRKFEASWNELLQE 363
Cdd:TIGR00876 321 HGIDLEDTAAKLEEEGLIAFEASFEELLQE 350
|
|
| Transaldolase_like |
cd00955 |
Transaldolase-like proteins from plants and bacteria; Transaldolase-like proteins from plants ... |
17-359 |
6.74e-161 |
|
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: 454.47 E-value: 6.74e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 17 SVWLDDLSRDRLRSGNLQELIDTKSVVGVTTNPSIFQKALSEGHTYDAQIAELAARGADVDATIRTVTTDDVRSACDVLV 96
Cdd:cd00955 1 SLWLDNLSRSFIDNGFLKRLIEEQGVVGVTSNPAIFEKAIAGSAAYDDQIRALKGQGLDAEAIYEALAIEDIQDACDLLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 97 PQWEDSDGVDGRVSIEVDPRLAHETEKTIQQAIELWKIVDRPNLFIKIPATKAGLPAISAVLAEGISVNVTLIFSVQRYR 176
Cdd:cd00955 81 PVYEQTGGNDGYVSLEVSPRLADDTQGTIAEAKRLWKAVGRPNLMIKIPATEAGLPAIEELIAAGISVNVTLIFSLEQYE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 177 EVMDAYLTGMEKARQAGHSLSKIHSVASFFVSRVDTEIDKRLDRigsRQALELRGQAGVANARLAYATYREVFEdSDRYR 256
Cdd:cd00955 161 AVAEAYLRGLERRVEGGGDLSQVASVASFFVSRVDTLIDKKLDA---PEAKALQGKVAIANAKLAYQEYQEKFS-GPRWA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 257 SLKVDGARVQRPLWASTGVKNPDYSDTLYVTELVAPHTVNTMPEKTIDAVADHGVIQGDTVTGTaSDAQAVFDQLGAIGI 336
Cdd:cd00955 237 ALAAAGAKPQRLLWASTGVKNPAYPDVLYVEELIGPDTVNTMPDATLKAFADHGEVRPTLEEGL-EEAERVLAELERLGI 315
|
330 340
....*....|....*....|...
gi 624384300 337 DLTDVFAVLEEEGVRKFEASWNE 359
Cdd:cd00955 316 DLDAVTEKLLKEGVKKFKDSFEK 338
|
|
| PRK09533 |
PRK09533 |
bifunctional transaldolase/phosoglucose isomerase; Validated |
5-361 |
9.10e-144 |
|
bifunctional transaldolase/phosoglucose isomerase; Validated
Pssm-ID: 236551 [Multi-domain] Cd Length: 948 Bit Score: 430.93 E-value: 9.10e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 5 NPnLAALSAAGVSVWLDDLSRDRLRSGNLQELIDTKSVVGVTTNPSIFQKALSEGHTYDAQIAELAARGADVDATI-RTV 83
Cdd:PRK09533 2 NP-LKALAQHGQSVWLDFLARGFIAKGELKRLVEEDGLRGVTSNPAIFEKAIGSSDEYDDAIKAALAEGDRSVIELyETL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 84 TTDDVRSACDVLVPQWEDSDGVDGRVSIEVDPRLAHETEKTIQQAIELWKIVDRPNLFIKIPATKAGLPAISAVLAEGIS 163
Cdd:PRK09533 81 AIEDIQAAADVLRPVYDATDGADGFVSLEVSPYLALDTEGTIAEARRLWAAVDRPNLMIKVPATPEGLPAIRQLIAEGIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 164 VNVTLIFSVQRYREVMDAYLTGMEKARQAGHSLSKIHSVASFFVSRVDTEIDKRLDR-------IGSRQALE-LRGQAGV 235
Cdd:PRK09533 161 VNVTLLFSQDVYEEVAEAYISGLEARAAKGGDPSHVASVASFFVSRIDSAVDKRLDEkiaaandPAEKAALEaLKGKVAI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 236 ANARLAYATYREVFEdSDRYRSLKVDGARVQRPLWASTGVKNPDYSDTLYVTELVAPHTVNTMPEKTIDAVADHGVIqGD 315
Cdd:PRK09533 241 ANAKLAYQRYKRLFA-GPRWEALAAKGAKPQRLLWASTGTKNKAYSDVLYVEELIGPDTVNTMPPATLDAFRDHGKV-RA 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 624384300 316 TVTGTASDAQAVFDQLGAIGIDLTDVFAVLEEEGVRKFEASWNELL 361
Cdd:PRK09533 319 TLEEDVDEARAVLADLAEAGISLDAVTDKLVAEGVQLFADAFDKLL 364
|
|
| TAL_FSA |
pfam00923 |
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ... |
18-363 |
5.27e-77 |
|
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: 236.67 E-value: 5.27e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 18 VWLDDLSRDRLRsgnlqELIDTKSVVGVTTNPSIFQKALSEGHTYDAQIAELAARGadvdatirtvttddvrsacdvlvp 97
Cdd:pfam00923 1 IWLDTADRDLIK-----KLIEEGGIDGVTTNPSIFLKAIEYSALYDEAIAEIKEIG------------------------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 98 qwedsdgvDGRVSIEVDPRLAHETEKTIQQAIELWKIVDRPNLFIKIPATKAGLPAISAVLAEGISVNVTLIFSVQRYRE 177
Cdd:pfam00923 52 --------DGPVSLEVDPRLADDTEGTIEEARRLIALYGRPNVLIKIPATWEGIKAIKELSAEGINVNVTLIFSLAQALA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 178 VMDAyltgmekarqaghslskIHSVASFFVSRVDTEIDKRLDRigsrqalELRGQAGVANARLAYATYREVfedsdryrs 257
Cdd:pfam00923 124 AAEA-----------------GASVISPFVGRIDDWGDKRLGA-------ALRGDDGIANAKEIYQIYKKY--------- 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 258 lkvdgarvqrpLWaSTGVKNPDYSDTLYVTELVAPHTVnTMPEKTIDAVADhgviqgdtvtgtasdaqavfdqlgaigid 337
Cdd:pfam00923 171 -----------GW-STGVLAASFRNVLYVLALAGCDTI-TIPPDTLEALAK----------------------------- 208
|
330 340
....*....|....*....|....*.
gi 624384300 338 ltdvfavleEEGVRKFEASWNELLQE 363
Cdd:pfam00923 209 ---------DEGVRKFAKDWEKLLGS 225
|
|
| TalA |
COG0176 |
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ... |
16-360 |
1.24e-65 |
|
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: 207.24 E-value: 1.24e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 16 VSVWLDDLSRDRLRsgnlqELIDTKSVVGVTTNPSIFQKAlseghtydaqiaelaargadvdaTIRTvTTDDVRSACDVl 95
Cdd:COG0176 1 MKLWLDTADREEIK-----ELIDLGGVDGVTTNPSLIAKA-----------------------GIKD-FVEDIREICDI- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 96 vpqwedsdgVDGRVSIEVdprLAHETEKTIQQAIELWKIVdRPNLFIKIPATKAGLPAISAVLAEGISVNVTLIFSVQRY 175
Cdd:COG0176 51 ---------VDGPVSAEV---LATDTEGMIAEARRLAALY-RPNVVIKIPATEEGLKAIEELSAEGIKVNVTLIFSAAQA 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 176 REVMDAyltgmekarqaghslskIHSVASFFVSRVDTEidkrldrigsrqalelrGQAGVANARLAYATYREVfedsdry 255
Cdd:COG0176 118 LLAAEA-----------------GASYVSPFVGRIDDI-----------------GIDGIALVREIYQIYKNY------- 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 256 rslkvdGARvQRPLWASTGvknpdysDTLYVTE--LVAPHTVnTMPEKTIDAVADHGviqgdtvtgtasdaqavfdqlga 333
Cdd:COG0176 157 ------GAR-TRILAASFR-------NPLQVLEaaLAGADTV-TIPPAVLEALADHP----------------------- 198
|
330 340
....*....|....*....|....*..
gi 624384300 334 igidltdvfavLEEEGVRKFEASWNEL 360
Cdd:COG0176 199 -----------LTDEGIEKFLADWEKL 214
|
|
| PRK03903 |
PRK03903 |
transaldolase; Provisional |
62-363 |
9.41e-59 |
|
transaldolase; Provisional
Pssm-ID: 235171 Cd Length: 274 Bit Score: 191.73 E-value: 9.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 62 YDAQIAELAARGADvdaTI-RTVTTDDVRSACDVLVPQWEDSDgvDGRVSIEVDPRLAHETEKTIQQAIELWKIVDRPNL 140
Cdd:PRK03903 2 YKDEIAKLKGKKAK---EIyEELAIKDIKKAADKLLPLYEKPD--DGFISIEIDPFLEDDAAGSIEEGKRLYKTIGRPNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 141 FIKIPATKAGLPAISAVLAEGISVNVTLIFSVQRYREVMDAyltgMEKARQAGHSLSKihSVASFFVSRVDTEIDKRLdr 220
Cdd:PRK03903 77 MIKVPATKAGYEAMSALMKKGISVNATLIFSPEQAKECAEA----LNEGLKKNTKDPK--AVISVFVSRFDRLLDPKL-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 221 igsrQALELRGQAGVANARLAYatyrEVFEDSDRYRSlkvdgarvqRPLWASTGVKNPDYSDTLYVTELVAPHTVNTMPE 300
Cdd:PRK03903 149 ----APKNLQAKSGIMNATKCY----NQIEQHANKNI---------RTLFASTGVKGDDLPKDYYIKELLFKNSINTAPL 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 624384300 301 KTIDA-VADHGVIQGDTVTGTASDAQavFDQLGAIGIDLTDVFAVLEEEGVRKFEASWNELLQE 363
Cdd:PRK03903 212 DTIEAfLKDGNTEPKKPLKIEEIEAF--FKELKSHNIDLENTYQKLLKDGLEAFKQAFEDILKS 273
|
|
| Transaldolase |
cd00439 |
Transaldolase; Transaldolase. Enzymes found in the non-oxidative branch of the pentose ... |
17-300 |
6.49e-45 |
|
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: 155.20 E-value: 6.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 17 SVWLDDLSRDRLrsgnlQELIDTKSVVGVTTNPSIFQKALSEGHTYDAQIAELAARGADVDATIRTVTTDDVRSACdVLV 96
Cdd:cd00439 1 SPWYDTLDRPAT-----DLLPLIRGVRGVTTNPSIIQAAISTSNAYNDQFRTLVESGKDIESAYWELVVKDIQDAC-KLF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 97 PQWEDSDGVDGRVSIEVDPRLAHETEKTIQQAIELWKIVDRPNLFIKIPATKAGLPAISAVLAEGISVNVTLIFSVQRYR 176
Cdd:cd00439 75 EPIYDQTEADGRVSVEVSARLADDTQGMVEAAKYLSKVVNRRNIYIKIPATAEGIPAIKDLIAAGISVNVTLIFSIAQYE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 177 EVMDAYLTgmekarqaghslskihsVASFFVSRVDTEIDKRLDRIGsrqaLELRGQAGVANARLAYATYREVFEDsdryr 256
Cdd:cd00439 155 AVADAGTS-----------------VASPFVSRIDTLMDKMLEQIG----LDLRGKAGVAQVTLAYKLYKQKFKK----- 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 624384300 257 slkvdgarvQRPLWASTgvknpdySDTLYVTELVAPHTVNTMPE 300
Cdd:cd00439 209 ---------QRVLWASF-------SDTLYVAPLIGCDTVTTMPD 236
|
|
| Transaldolase_FSA |
cd00956 |
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ... |
18-211 |
8.09e-17 |
|
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: 78.39 E-value: 8.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 18 VWLDDLSRDRLRSGNLQELIDtksvvGVTTNPSIFQKalSEGHTYDAQIAELAARgadvdatirtvttddvrsacdvlvp 97
Cdd:cd00956 2 IFLDTADLEEIKKASETGLLD-----GVTTNPSLIAK--SGRIDFEAVLKEICEI------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 98 qwedsdgVDGRVSIEVdprLAHETEKTIQQAIELWKIVdrPNLFIKIPATKAGLPAISAVLAEGISVNVTLIFSvqryre 177
Cdd:cd00956 50 -------IDGPVSAQV---VSTDAEGMVAEARKLASLG--GNVVVKIPVTEDGLKAIKKLSEEGIKTNVTAIFS------ 111
|
170 180 190
....*....|....*....|....*....|....
gi 624384300 178 VMDAYLtgmekARQAGhslskiHSVASFFVSRVD 211
Cdd:cd00956 112 AAQALL-----AAKAG------ATYVSPFVGRID 134
|
|
| Transaldolase_TalAB |
cd00957 |
Transaldolases including both TalA and TalB; Transaldolases including both TalA and TalB. The ... |
30-171 |
2.65e-14 |
|
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: 72.65 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 30 SGNLqELIDTKSVVGVTTNPSIFQKALSEGHTY---DAQIAELAARGADVDATIRTVTtdD---VRSACDVLvpqwedsD 103
Cdd:cd00957 16 TGDF-EAIKKFKPQDATTNPSLILAAAKLPEYNklvDEAIAYAKKKGGSDEDQISNAL--DkllVNFGTEIL-------K 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 624384300 104 GVDGRVSIEVDPRLAHETEKTIQQAIELWKI-----VDRPNLFIKIPATKAGLPAISAVLAEGISVNVTLIFS 171
Cdd:cd00957 86 LIPGRVSTEVDARLSFDTNATIAKARKLIKLyeeagIDKERILIKIAATWEGIQAAKQLEKEGIHCNLTLLFS 158
|
|
| PRK05269 |
PRK05269 |
transaldolase B; Provisional |
45-171 |
1.80e-13 |
|
transaldolase B; Provisional
Pssm-ID: 235381 [Multi-domain] Cd Length: 318 Bit Score: 70.57 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 45 VTTNPSIFQKALSEGHtYDAQIAELAARGADVDATIRTVTTDdvrsACD---VLVPQwEDSDGVDGRVSIEVDPRLAHET 121
Cdd:PRK05269 32 ATTNPSLILKAAQIPE-YAPLIDDAVAWAKQQSGDRAQQIDD----AIDklaVNFGL-EILKLIPGRVSTEVDARLSFDT 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 624384300 122 EKTIQQAIELWKI-----VDRPNLFIKIPATKAGlpaISA--VL-AEGISVNVTLIFS 171
Cdd:PRK05269 106 EATIAKARKLIALyeeagISKDRILIKIASTWEG---IRAaeQLeKEGINCNLTLLFS 160
|
|
| PRK12346 |
PRK12346 |
transaldolase A; Provisional |
46-181 |
1.80e-11 |
|
transaldolase A; Provisional
Pssm-ID: 183458 Cd Length: 316 Bit Score: 64.36 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 46 TTNPSIFQKALSEGHtYDAQIAELAARGADVDATIRTvttdDVRSACDVLVPQW--EDSDGVDGRVSIEVDPRLAHETEK 123
Cdd:PRK12346 32 TTNPSLLLKAAGLPQ-YQHLIDDAIAWGKKQGGTQEQ----QVVAACDKLAVNFgaEILKSVPGRVSTEVDARLSFDREK 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 624384300 124 TIQQA---IELW--KIVDRPNLFIKIPATKAGLPAISAVLAEGISVNVTLIFSVQRYREVMDA 181
Cdd:PRK12346 107 SIEKArhlVDLYqqQGIDKSRILIKLASTWEGIRAAEELEKEGINCNLTLLFSFAQARACAEA 169
|
|
| PTZ00411 |
PTZ00411 |
transaldolase-like protein; Provisional |
105-171 |
1.74e-10 |
|
transaldolase-like protein; Provisional
Pssm-ID: 240406 Cd Length: 333 Bit Score: 61.68 E-value: 1.74e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 624384300 105 VDGRVSIEVDPRLAHETEKTIQQAIELWKI-----VDRPNLFIKIPATKAGLPAISAVLAEGISVNVTLIFS 171
Cdd:PTZ00411 99 VPGRVSTEVDARLSFDKQAMVDKARKIIKMyeeagISKDRILIKLASTWEGIQAAKALEKEGIHCNLTLLFS 170
|
|
| PRK12309 |
PRK12309 |
transaldolase; |
105-170 |
1.62e-09 |
|
transaldolase;
Pssm-ID: 183426 [Multi-domain] Cd Length: 391 Bit Score: 58.98 E-value: 1.62e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 624384300 105 VDGRVSIEVDPRLAHETEKTIQQA---IELWKI--VDRPNLFIKIPATKAGLPAISAVLAEGISVNVTLIF 170
Cdd:PRK12309 93 VPGRVSTEVDARLSYDTEATIAKArklISLYEDagISRDRVLIKIASTWEGIKAAEVLEKEGIHCNLTLLF 163
|
|
| fsa_talC_mipB |
TIGR00875 |
fructose-6-phosphate aldolase, TalC/MipB family; This model represents a family that includes ... |
42-171 |
2.03e-09 |
|
fructose-6-phosphate aldolase, TalC/MipB family; This model represents a family that includes the E. coli transaldolase homologs TalC and MipB, both shown to be fructose-6-phosphate aldolases rather than transaldolases as previously thought. It is related to but distinct from the transaldolase family of E. coli TalA and TalB. The member from Bacillus subtilis becomes phosphorylated during early stationary phase but not during exponential growth. [Energy metabolism, Pentose phosphate pathway]
Pssm-ID: 129953 [Multi-domain] Cd Length: 213 Bit Score: 57.18 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 42 VVGVTTNPSIfqkalseghtydaqiaeLAARGADVDATIRTVTtddvrsacdvlvpqwedsDGVDGRVSIEVdprLAHET 121
Cdd:TIGR00875 22 LAGVTTNPSL-----------------IAKEGRSFWEVLKEIQ------------------EAVEGPVSAET---ISLDA 63
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 624384300 122 EKTIQQAIELWKIVdrPNLFIKIPATKAGLPAISAVLAEGISVNVTLIFS 171
Cdd:TIGR00875 64 EGMVEEAKELAKLA--PNIVVKIPMTSEGLKAVKILKKEGIKTNVTLVFS 111
|
|
| PRK12653 |
PRK12653 |
fructose-6-phosphate aldolase; Reviewed |
44-174 |
1.16e-04 |
|
fructose-6-phosphate aldolase; Reviewed
Pssm-ID: 183653 [Multi-domain] Cd Length: 220 Bit Score: 42.84 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 44 GVTTNPSIfqkalseghtydaqiaeLAARGADVDatirtvttddvrsacdVLVPQWEDSDGVDGRVSIEVdprLAHETEK 123
Cdd:PRK12653 24 GVTTNPSI-----------------IAAGKKPLE----------------VVLPQLHEAMGGQGRLFAQV---MATTAEG 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 624384300 124 TIQQAIELWKIVdrPNLFIKIPATKAGLPAISAVLAEGISVNVTLIFSVQR 174
Cdd:PRK12653 68 MVNDARKLRSII--ADIVVKVPVTAEGLAAIKMLKAEGIPTLGTAVYGAAQ 116
|
|
| PRK12656 |
PRK12656 |
fructose-6-phosphate aldolase; Reviewed |
41-172 |
1.18e-04 |
|
fructose-6-phosphate aldolase; Reviewed
Pssm-ID: 183656 [Multi-domain] Cd Length: 222 Bit Score: 42.80 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384300 41 SVVGVTTNPSIFQKalsEGHTydaqiaELAARGADVDATIrtvttddvrsacdvlvpqwedsdGVDGRVSIEVdprLAHE 120
Cdd:PRK12656 21 PLAGVTSNPSIAKK---EGDI------DFFERIREVREII-----------------------GDEASIHVQV---VAQD 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 624384300 121 TEKTIQQAIELWKIVDRpNLFIKIPATKAGLPAISAVLAEGISVNVTLIFSV 172
Cdd:PRK12656 66 YEGILKDAHEIRRQCGD-DVYIKVPVTPAGLAAIKTLKAEGYHITATAIYTV 116
|
|
| |
