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Conserved domains on  [gi|394273891|gb|EJE18318|]
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transaldolase [Staphylococcus epidermidis NIHLM031]

Protein Classification

beta/alpha barrel domain-containing protein( domain architecture ID 229392)

beta/alpha barrel domain-containing protein belongs to a large superfamily with a wide variety of enzymatic functions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TIM super family cl21457
TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate ...
 1-237 1.87e-139

TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate isomerase (TIM) which, in general, share an eight beta/alpha closed barrel structure.


The actual alignment was detected with superfamily member TIGR02134:

Pssm-ID: 473867 [Multi-domain]  Cd Length: 236  Bit Score: 390.41  E-value: 1.87e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891    1 MTKLNVKVFADGADIEEMKSAYKNQLVDGFTTNPSLMAKAGVTDYKAFAEEAVSEIPDASISFEVFADDLPTMEKEAEIL 80
Cdd:TIGR02134   1 LQKLNVKVFADGANLEEMVKFSTHPYVKGFTTNPSLMRKAGIVDYEAFAHEALAQITDLPISFEVFADDLDEMEKEARYI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891   81 KQYGDNVFVKIPIVTTTGESTLPLIKSLSSKQVRLNVTAVYTIEQVKAITDVVTEGVPTYVSVFAGRIADTGIDPLPLMK 160
Cdd:TIGR02134  81 ASWGNNVNVKIPVTNTKGESTGPLIQKLSADGITLNVTALTTIEQVEKVCQSFTDGVPGIVSVFAGRIADTGVDPEPHMR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 394273891  161 EAVKVTHSKEGVQLLWASCREVYNVIQADEIGADIITCPADVVKKVnNNLGRDIGELSVDTVKGFAKDIQSSGLSIL 237
Cdd:TIGR02134 161 EALEIVAQKPGVELLWASPRELFNIIQADRIGCDIITCAHDILAKL-PLLGKDLTQYSLETVQMFAKDAQSSGYSIL 236
 
Name Accession Description Interval E-value
transald_staph TIGR02134
transaldolase; This small family of proteins is a member of the transaldolase sybfamily ...
 1-237 1.87e-139

transaldolase; This small family of proteins is a member of the transaldolase sybfamily represented by pfam00923. Coxiella and Staphylococcus lack members of the known transaldolase equivalog families and appear to require a transaldolase activity for completion of the pentose phosphate pathway. [Energy metabolism, Pentose phosphate pathway]


Pssm-ID: 131189 [Multi-domain]  Cd Length: 236  Bit Score: 390.41  E-value: 1.87e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891    1 MTKLNVKVFADGADIEEMKSAYKNQLVDGFTTNPSLMAKAGVTDYKAFAEEAVSEIPDASISFEVFADDLPTMEKEAEIL 80
Cdd:TIGR02134   1 LQKLNVKVFADGANLEEMVKFSTHPYVKGFTTNPSLMRKAGIVDYEAFAHEALAQITDLPISFEVFADDLDEMEKEARYI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891   81 KQYGDNVFVKIPIVTTTGESTLPLIKSLSSKQVRLNVTAVYTIEQVKAITDVVTEGVPTYVSVFAGRIADTGIDPLPLMK 160
Cdd:TIGR02134  81 ASWGNNVNVKIPVTNTKGESTGPLIQKLSADGITLNVTALTTIEQVEKVCQSFTDGVPGIVSVFAGRIADTGVDPEPHMR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 394273891  161 EAVKVTHSKEGVQLLWASCREVYNVIQADEIGADIITCPADVVKKVnNNLGRDIGELSVDTVKGFAKDIQSSGLSIL 237
Cdd:TIGR02134 161 EALEIVAQKPGVELLWASPRELFNIIQADRIGCDIITCAHDILAKL-PLLGKDLTQYSLETVQMFAKDAQSSGYSIL 236
Transaldolase_FSA cd00956
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ...
 7-231 4.47e-79

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: 236.32  E-value: 4.47e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891   7 KVFADGADIEEMKSAYKNQLVDGFTTNPSLMAKAGVTDYKAFAEEAVSEIpDASISFEVFADDLPTMEKEAEILKQYGDN 86
Cdd:cd00956    1 KIFLDTADLEEIKKASETGLLDGVTTNPSLIAKSGRIDFEAVLKEICEII-DGPVSAQVVSTDAEGMVAEARKLASLGGN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891  87 VFVKIPiVTTTGestLPLIKSLSSKQVRLNVTAVYTIEQVKaitdVVTEGVPTYVSVFAGRIADTGIDPLPLMKEAVKVT 166
Cdd:cd00956   80 VVVKIP-VTEDG---LKAIKKLSEEGIKTNVTAIFSAAQAL----LAAKAGATYVSPFVGRIDDLGGDGMELIREIRTIF 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 394273891 167 HSKE-GVQLLWASCREVYNVIQADEIGADIITCPADVVKKVNNNlgrdigELSVDTVKGFAKDIQS 231
Cdd:cd00956  152 DNYGfDTKILAASIRNPQHVIEAALAGADAITLPPDVLEQLLKH------PLTDKGVEKFLEDWQS 211
TalA COG0176
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ...
 6-231 1.38e-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: 202.23  E-value: 1.38e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891   6 VKVFADGADIEEMKSAYKNQLVDGFTTNPSLMAKAGVTDYKAFAEEAVSEIpDASISFEVFADDLPTMEKEA-EILKQYG 84
Cdd:COG0176    1 MKLWLDTADREEIKELIDLGGVDGVTTNPSLIAKAGIKDFVEDIREICDIV-DGPVSAEVLATDTEGMIAEArRLAALYR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891  85 DNVFVKIPiVTTTGestLPLIKSLSSKQVRLNVTAVYTIEQVKAitdvVTEGVPTYVSVFAGRIADTGIDPLPLMKEAVK 164
Cdd:COG0176   80 PNVVIKIP-ATEEG---LKAIEELSAEGIKVNVTLIFSAAQALL----AAEAGASYVSPFVGRIDDIGIDGIALVREIYQ 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 394273891 165 V-THSKEGVQLLWASCREVYNVIQADEIGADIITCPADVVKKVNNNlgrdigELSVDTVKGFAKDIQS 231
Cdd:COG0176  152 IyKNYGARTRILAASFRNPLQVLEAALAGADTVTIPPAVLEALADH------PLTDEGIEKFLADWEK 213
TAL_FSA pfam00923
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ...
 8-236 5.07e-48

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: 157.70  E-value: 5.07e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891    8 VFADGADIEEMKSAYKNQLVDGFTTNPSLMAKAGVtdYKAFAEEAVSEIP---DASISFEVFA---DDLPTMEKEAEILK 81
Cdd:pfam00923   1 IWLDTADRDLIKKLIEEGGIDGVTTNPSIFLKAIE--YSALYDEAIAEIKeigDGPVSLEVDPrlaDDTEGTIEEARRLI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891   82 QYG--DNVFVKIPiVTTTGestLPLIKSLSSKQVRLNVTAVYTIEQVKAitdvVTEGVPTYVSVFAGRIADTGI------ 153
Cdd:pfam00923  79 ALYgrPNVLIKIP-ATWEG---IKAIKELSAEGINVNVTLIFSLAQALA----AAEAGASVISPFVGRIDDWGDkrlgaa 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891  154 ----DPLPLMKEAV---KVTHSKEGVqlLWASCREVYNVIqaDEIGADIITCPADVVKKVNNNlgrdigelsvDTVKGFA 226
Cdd:pfam00923 151 lrgdDGIANAKEIYqiyKKYGWSTGV--LAASFRNVLYVL--ALAGCDTITIPPDTLEALAKD----------EGVRKFA 216

                         250
                  ....*....|
gi 394273891  227 KDIQSSGLSI 236
Cdd:pfam00923 217 KDWEKLLGSI 226
PRK12656 PRK12656
fructose-6-phosphate aldolase; Reviewed
 11-204 2.26e-17

fructose-6-phosphate aldolase; Reviewed


Pssm-ID: 183656 [Multi-domain]  Cd Length: 222  Bit Score: 77.86  E-value: 2.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891  11 DGADIEEMKSAYKNQLVDGFTTNPSLMAKAGVTDYkaFAE-EAVSEI--PDASISFEVFADDLPTMEKEA-EILKQYGDN 86
Cdd:PRK12656   6 DTLNLEAIKKWHEILPLAGVTSNPSIAKKEGDIDF--FERiREVREIigDEASIHVQVVAQDYEGILKDAhEIRRQCGDD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891  87 VFVKIPiVTTTGestLPLIKSLSSKQVRLNVTAVYTIEQ-VKAItdvvtEGVPTYVSVFAGRIADTGIDPLPLMK---EA 162
Cdd:PRK12656  84 VYIKVP-VTPAG---LAAIKTLKAEGYHITATAIYTVFQgLLAI-----EAGADYLAPYYNRMENLNIDSNAVIGqlaEA 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 394273891 163 VKVTHSKEgvQLLWASCREVYNVIQADEIGADIITCPADVVK 204
Cdd:PRK12656 155 IDRENSDS--KILAASFKNVAQVNKAFALGAQAVTAGPDVFE 194
 
Name Accession Description Interval E-value
transald_staph TIGR02134
transaldolase; This small family of proteins is a member of the transaldolase sybfamily ...
 1-237 1.87e-139

transaldolase; This small family of proteins is a member of the transaldolase sybfamily represented by pfam00923. Coxiella and Staphylococcus lack members of the known transaldolase equivalog families and appear to require a transaldolase activity for completion of the pentose phosphate pathway. [Energy metabolism, Pentose phosphate pathway]


Pssm-ID: 131189 [Multi-domain]  Cd Length: 236  Bit Score: 390.41  E-value: 1.87e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891    1 MTKLNVKVFADGADIEEMKSAYKNQLVDGFTTNPSLMAKAGVTDYKAFAEEAVSEIPDASISFEVFADDLPTMEKEAEIL 80
Cdd:TIGR02134   1 LQKLNVKVFADGANLEEMVKFSTHPYVKGFTTNPSLMRKAGIVDYEAFAHEALAQITDLPISFEVFADDLDEMEKEARYI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891   81 KQYGDNVFVKIPIVTTTGESTLPLIKSLSSKQVRLNVTAVYTIEQVKAITDVVTEGVPTYVSVFAGRIADTGIDPLPLMK 160
Cdd:TIGR02134  81 ASWGNNVNVKIPVTNTKGESTGPLIQKLSADGITLNVTALTTIEQVEKVCQSFTDGVPGIVSVFAGRIADTGVDPEPHMR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 394273891  161 EAVKVTHSKEGVQLLWASCREVYNVIQADEIGADIITCPADVVKKVnNNLGRDIGELSVDTVKGFAKDIQSSGLSIL 237
Cdd:TIGR02134 161 EALEIVAQKPGVELLWASPRELFNIIQADRIGCDIITCAHDILAKL-PLLGKDLTQYSLETVQMFAKDAQSSGYSIL 236
Transaldolase_FSA cd00956
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ...
 7-231 4.47e-79

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: 236.32  E-value: 4.47e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891   7 KVFADGADIEEMKSAYKNQLVDGFTTNPSLMAKAGVTDYKAFAEEAVSEIpDASISFEVFADDLPTMEKEAEILKQYGDN 86
Cdd:cd00956    1 KIFLDTADLEEIKKASETGLLDGVTTNPSLIAKSGRIDFEAVLKEICEII-DGPVSAQVVSTDAEGMVAEARKLASLGGN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891  87 VFVKIPiVTTTGestLPLIKSLSSKQVRLNVTAVYTIEQVKaitdVVTEGVPTYVSVFAGRIADTGIDPLPLMKEAVKVT 166
Cdd:cd00956   80 VVVKIP-VTEDG---LKAIKKLSEEGIKTNVTAIFSAAQAL----LAAKAGATYVSPFVGRIDDLGGDGMELIREIRTIF 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 394273891 167 HSKE-GVQLLWASCREVYNVIQADEIGADIITCPADVVKKVNNNlgrdigELSVDTVKGFAKDIQS 231
Cdd:cd00956  152 DNYGfDTKILAASIRNPQHVIEAALAGADAITLPPDVLEQLLKH------PLTDKGVEKFLEDWQS 211
TalA COG0176
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ...
 6-231 1.38e-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: 202.23  E-value: 1.38e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891   6 VKVFADGADIEEMKSAYKNQLVDGFTTNPSLMAKAGVTDYKAFAEEAVSEIpDASISFEVFADDLPTMEKEA-EILKQYG 84
Cdd:COG0176    1 MKLWLDTADREEIKELIDLGGVDGVTTNPSLIAKAGIKDFVEDIREICDIV-DGPVSAEVLATDTEGMIAEArRLAALYR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891  85 DNVFVKIPiVTTTGestLPLIKSLSSKQVRLNVTAVYTIEQVKAitdvVTEGVPTYVSVFAGRIADTGIDPLPLMKEAVK 164
Cdd:COG0176   80 PNVVIKIP-ATEEG---LKAIEELSAEGIKVNVTLIFSAAQALL----AAEAGASYVSPFVGRIDDIGIDGIALVREIYQ 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 394273891 165 V-THSKEGVQLLWASCREVYNVIQADEIGADIITCPADVVKKVNNNlgrdigELSVDTVKGFAKDIQS 231
Cdd:COG0176  152 IyKNYGARTRILAASFRNPLQVLEAALAGADTVTIPPAVLEALADH------PLTDEGIEKFLADWEK 213
TAL_FSA pfam00923
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ...
 8-236 5.07e-48

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: 157.70  E-value: 5.07e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891    8 VFADGADIEEMKSAYKNQLVDGFTTNPSLMAKAGVtdYKAFAEEAVSEIP---DASISFEVFA---DDLPTMEKEAEILK 81
Cdd:pfam00923   1 IWLDTADRDLIKKLIEEGGIDGVTTNPSIFLKAIE--YSALYDEAIAEIKeigDGPVSLEVDPrlaDDTEGTIEEARRLI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891   82 QYG--DNVFVKIPiVTTTGestLPLIKSLSSKQVRLNVTAVYTIEQVKAitdvVTEGVPTYVSVFAGRIADTGI------ 153
Cdd:pfam00923  79 ALYgrPNVLIKIP-ATWEG---IKAIKELSAEGINVNVTLIFSLAQALA----AAEAGASVISPFVGRIDDWGDkrlgaa 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891  154 ----DPLPLMKEAV---KVTHSKEGVqlLWASCREVYNVIqaDEIGADIITCPADVVKKVNNNlgrdigelsvDTVKGFA 226
Cdd:pfam00923 151 lrgdDGIANAKEIYqiyKKYGWSTGV--LAASFRNVLYVL--ALAGCDTITIPPDTLEALAKD----------EGVRKFA 216

                         250
                  ....*....|
gi 394273891  227 KDIQSSGLSI 236
Cdd:pfam00923 217 KDWEKLLGSI 226
PRK12656 PRK12656
fructose-6-phosphate aldolase; Reviewed
 11-204 2.26e-17

fructose-6-phosphate aldolase; Reviewed


Pssm-ID: 183656 [Multi-domain]  Cd Length: 222  Bit Score: 77.86  E-value: 2.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891  11 DGADIEEMKSAYKNQLVDGFTTNPSLMAKAGVTDYkaFAE-EAVSEI--PDASISFEVFADDLPTMEKEA-EILKQYGDN 86
Cdd:PRK12656   6 DTLNLEAIKKWHEILPLAGVTSNPSIAKKEGDIDF--FERiREVREIigDEASIHVQVVAQDYEGILKDAhEIRRQCGDD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891  87 VFVKIPiVTTTGestLPLIKSLSSKQVRLNVTAVYTIEQ-VKAItdvvtEGVPTYVSVFAGRIADTGIDPLPLMK---EA 162
Cdd:PRK12656  84 VYIKVP-VTPAG---LAAIKTLKAEGYHITATAIYTVFQgLLAI-----EAGADYLAPYYNRMENLNIDSNAVIGqlaEA 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 394273891 163 VKVTHSKEgvQLLWASCREVYNVIQADEIGADIITCPADVVK 204
Cdd:PRK12656 155 IDRENSDS--KILAASFKNVAQVNKAFALGAQAVTAGPDVFE 194
Transaldolase cd00439
Transaldolase; Transaldolase. Enzymes found in the non-oxidative branch of the pentose ...
 8-231 7.79e-08

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: 51.58  E-value: 7.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891   8 VFADGADIEEMKSAYKNQLVDGFTTNPSLMAKAGVT-DYKAFAEEAVSEIPDASISFE---VFADDLPTMEKEAEILKQY 83
Cdd:cd00439    2 PWYDTLDRPATDLLPLIRGVRGVTTNPSIIQAAISTsNAYNDQFRTLVESGKDIESAYwelVVKDIQDACKLFEPIYDQT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891  84 G---------------------------------DNVFVKIPiVTTTGestLPLIKSLSSKQVRLNVTAVYTIEQVKAIT 130
Cdd:cd00439   82 EadgrvsvevsarladdtqgmveaakylskvvnrRNIYIKIP-ATAEG---IPAIKDLIAAGISVNVTLIFSIAQYEAVA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891 131 DVVTegvpTYVSVFAGRIADTGIDPL------PLMKEAVK-VT--------HSKEgVQLLWASCREVYNViqADEIGADI 195
Cdd:cd00439  158 DAGT----SVASPFVSRIDTLMDKMLeqigldLRGKAGVAqVTlayklykqKFKK-QRVLWASFSDTLYV--APLIGCDT 230

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 394273891 196 ITCPADVVkkvnnnlgrdiGELSVDTvkgFAKDIQS 231
Cdd:cd00439  231 VTTMPDQA-----------LEAGVDK---FKKDFES 252
PRK12653 PRK12653
fructose-6-phosphate aldolase; Reviewed
 6-125 8.41e-08

fructose-6-phosphate aldolase; Reviewed


Pssm-ID: 183653 [Multi-domain]  Cd Length: 220  Bit Score: 51.32  E-value: 8.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891   6 VKVFADGADIEEMKSAYKNQLVDGFTTNPSLMAKAGVTDYKAFAE--EAVSeiPDASISFEVFADDLPTMEKEAEILKQY 83
Cdd:PRK12653   1 MELYLDTSDVVAVKALSRIFPLAGVTTNPSIIAAGKKPLEVVLPQlhEAMG--GQGRLFAQVMATTAEGMVNDARKLRSI 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 394273891  84 GDNVFVKIPiVTTTGestLPLIKSLSSKQVRLNVTAVYTIEQ 125
Cdd:PRK12653  79 IADIVVKVP-VTAEG---LAAIKMLKAEGIPTLGTAVYGAAQ 116
Transaldolase_like cd00955
Transaldolase-like proteins from plants and bacteria; Transaldolase-like proteins from plants ...
 24-187 1.56e-06

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: 48.09  E-value: 1.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891  24 NQLVDGFTTNPSLMAKA-----------------GVTDYKAFAEEAVSEIPDAS----------------ISFEV---FA 67
Cdd:cd00955   23 EQGVVGVTSNPAIFEKAiagsaayddqiralkgqGLDAEAIYEALAIEDIQDACdllapvyeqtggndgyVSLEVsprLA 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891  68 DDLP-TMEKEAEILKQYG-DNVFVKIPivttTGESTLPLIKSLSSKQVRLNVTAVYTIEQVKAITDVVTEGVPTYV---- 141
Cdd:cd00955  103 DDTQgTIAEAKRLWKAVGrPNLMIKIP----ATEAGLPAIEELIAAGISVNVTLIFSLEQYEAVAEAYLRGLERRVeggg 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 394273891 142 ---------SVFAGRIaDTGIDPLpLMKEAVKVTHSKEGVqllwASCREVYNVIQ 187
Cdd:cd00955  179 dlsqvasvaSFFVSRV-DTLIDKK-LDAPEAKALQGKVAI----ANAKLAYQEYQ 227
PRK03343 PRK03343
transaldolase; Validated
 27-156 2.49e-04

transaldolase; Validated


Pssm-ID: 235117  Cd Length: 368  Bit Score: 41.34  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891  27 VDGFTTNPSLMAKA--GVTDY----------KAFAEEAVSEI-------------P--DAS------ISFEV---FADDL 70
Cdd:PRK03343  39 VVGVTSNPAIFQKAiaGGDAYdaqiaelaaaGADVEEAYEELttadvrnacdvlrPvyEATggvdgrVSIEVsprLAHDT 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891  71 PTMEKEAEILKQYGD--NVFVKIPiVTTTGestLPLIKSLSSKQVRLNVTAVYTIEQVKAITDVVTEG------------ 136
Cdd:PRK03343 119 EATIAEARRLWAAVDrpNLMIKIP-ATPEG---LPAIEALIAEGISVNVTLIFSVERYRAVADAYLRGlekrlaaghdls 194

                        170       180
                 ....*....|....*....|.
gi 394273891 137 -VPTYVSVFAGRIaDTGIDPL 156
Cdd:PRK03343 195 kIHSVASFFVSRV-DTEVDKR 214
PRK12346 PRK12346
transaldolase A; Provisional
 8-82 2.32e-03

transaldolase A; Provisional


Pssm-ID: 183458  Cd Length: 316  Bit Score: 38.55  E-value: 2.32e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 394273891   8 VFADGADIEEMKSaYKNQlvDGfTTNPSLMAKA-GVTDYKAFAEEAVSEIPDASISFE---VFADDLPTMEKEAEILKQ 82
Cdd:PRK12346  13 VVADSGDIESIRH-YHPQ--DA-TTNPSLLLKAaGLPQYQHLIDDAIAWGKKQGGTQEqqvVAACDKLAVNFGAEILKS 87
PRK05269 PRK05269
transaldolase B; Provisional
 8-81 7.53e-03

transaldolase B; Provisional


Pssm-ID: 235381 [Multi-domain]  Cd Length: 318  Bit Score: 36.68  E-value: 7.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 394273891   8 VFADGADIEEMKsayKNQLVDGfTTNPSLMAKA-GVTDYKAFAEEAVSEIPDASISFEVFADDlpTMEKEA-----EILK 81
Cdd:PRK05269  14 VVADTGDIEAIK---KYQPQDA-TTNPSLILKAaQIPEYAPLIDDAVAWAKQQSGDRAQQIDD--AIDKLAvnfglEILK 87
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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