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Conserved domains on  [gi|148670365|gb|EDL02312|]
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aldolase 2, B isoform, isoform CRA_b, partial [Mus musculus]

Protein Classification

fructose-bisphosphate aldolase( domain architecture ID 10447203)

Fructose-1,6-bisphosphate aldolase catalyzes the cleavage of D-fructose 1,6-bisphosphate to dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde 3-phosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glycolytic pfam00274
Fructose-bisphosphate aldolase class-I;
4-275 0e+00

Fructose-bisphosphate aldolase class-I;


:

Pssm-ID: 459742  Cd Length: 349  Bit Score: 564.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365    4 ELLFSVDNSISQSIGGVILFHETLYQKDSQGNLFRNVLKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKK 83
Cdd:pfam00274  47 QLLFTTDGELGEYISGVILFHETLYQKTDDGKPFVDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQGLDGLAERCAQYYK 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365   84 DGVDFGKWRAVLRIADQCPSSLAIQENANALARYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDH 163
Cdd:pfam00274 127 DGARFAKWRCVLKIGENTPSELAIQENANVLARYASICQQNGLVPIVEPEILPDGDHDLERCQKVTEKVLAAVYKALNDH 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365  164 HVYLEGTLLKPNMVTAGHACTKKYTPEQVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINRCPLPRPWKLSF 243
Cdd:pfam00274 207 HVYLEGTLLKPNMVTPGADCPKKYTPEEIAEATVTALRRTVPPAVPGVTFLSGGQSEEEATVNLNAINKLPLKKPWALTF 286

                         250       260       270
                  ....*....|....*....|....*....|..
gi 148670365  244 SYGRALQASALAAWGGKAANKKATQEAFMKRA 275
Cdd:pfam00274 287 SYGRALQASVLKAWGGKKENVKAAQEELLKRA 318
 
Name Accession Description Interval E-value
Glycolytic pfam00274
Fructose-bisphosphate aldolase class-I;
4-275 0e+00

Fructose-bisphosphate aldolase class-I;


Pssm-ID: 459742  Cd Length: 349  Bit Score: 564.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365    4 ELLFSVDNSISQSIGGVILFHETLYQKDSQGNLFRNVLKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKK 83
Cdd:pfam00274  47 QLLFTTDGELGEYISGVILFHETLYQKTDDGKPFVDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQGLDGLAERCAQYYK 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365   84 DGVDFGKWRAVLRIADQCPSSLAIQENANALARYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDH 163
Cdd:pfam00274 127 DGARFAKWRCVLKIGENTPSELAIQENANVLARYASICQQNGLVPIVEPEILPDGDHDLERCQKVTEKVLAAVYKALNDH 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365  164 HVYLEGTLLKPNMVTAGHACTKKYTPEQVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINRCPLPRPWKLSF 243
Cdd:pfam00274 207 HVYLEGTLLKPNMVTPGADCPKKYTPEEIAEATVTALRRTVPPAVPGVTFLSGGQSEEEATVNLNAINKLPLKKPWALTF 286

                         250       260       270
                  ....*....|....*....|....*....|..
gi 148670365  244 SYGRALQASALAAWGGKAANKKATQEAFMKRA 275
Cdd:pfam00274 287 SYGRALQASVLKAWGGKKENVKAAQEELLKRA 318
FBP_aldolase_I_a cd00948
Fructose-1,6-bisphosphate aldolase; Fructose-1,6-bisphosphate aldolase. The enzyme catalyzes ...
 4-275 0e+00

Fructose-1,6-bisphosphate aldolase; Fructose-1,6-bisphosphate aldolase. The enzyme catalyzes the cleavage of fructose 1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate (DHAP). This family includes proteins found in vertebrates, plants, and bacterial plant pathogens. Mutations in the aldolase genes in humans cause hemolytic anemia and hereditary fructose intolerance. The enzyme is a member of the class I aldolase family, which utilizes covalent catalysis through a Schiff base formed between a lysine residue of the enzyme and ketose substrates.


Pssm-ID: 188635  Cd Length: 330  Bit Score: 536.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365   4 ELLFSVDNsISQSIGGVILFHETLYQKDSQGNLFRNVLKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKK 83
Cdd:cd00948   49 ELLFTTPG-LGQYISGVILFEETLYQKTDDGKPFVDILKEKGIVPGIKVDKGLVPLAGTDGETTTQGLDGLAERCAKYYK 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365  84 DGVDFGKWRAVLRIADQCPSSLAIQENANALARYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDH 163
Cdd:cd00948  128 QGARFAKWRAVLKIGNGTPSELAIKENAHGLARYAAICQENGLVPIVEPEVLMDGDHDIERCQEVTEKVLAAVYKALNDH 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365 164 HVYLEGTLLKPNMVTAGHACTKKYTPEQVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINRCPLPRPWKLSF 243
Cdd:cd00948  208 HVLLEGTLLKPNMVTPGADCKKKASPEEVAEYTVRALRRTVPAAVPGIVFLSGGQSEEEATLNLNAMNKLPLPKPWALSF 287

                        250       260       270
                 ....*....|....*....|....*....|..
gi 148670365 244 SYGRALQASALAAWGGKAANKKATQEAFMKRA 275
Cdd:cd00948  288 SYGRALQASALKAWGGKKENVEAAQKALLKRA 319
PTZ00019 PTZ00019
fructose-bisphosphate aldolase; Provisional
 4-275 1.91e-157

fructose-bisphosphate aldolase; Provisional


Pssm-ID: 240231  Cd Length: 355  Bit Score: 442.23  E-value: 1.91e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365   4 ELLFSVdNSISQSIGGVILFHETLYQKDSQGNLFRNVLKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKK 83
Cdd:PTZ00019  52 ELLFTT-EGLEQYISGVILFEETVYQKAPSGKTFVELLKEKGIVPGIKVDKGLVTLPGTDGETSTQGLDGLAERAKKYYK 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365  84 DGVDFGKWRAVLRI--ADQCPSSLAIQENANALARYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALN 161
Cdd:PTZ00019 131 AGARFAKWRAVLKIdpAKGKPSELAIQENAWTLARYAAICQENGLVPIVEPEILIDGSHSIEVCQKVTEKVLAEVFKALN 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365 162 DHHVYLEGTLLKPNMVTAGHACTKKYTPEQVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINRCPLPRPWKL 241
Cdd:PTZ00019 211 DHGVLLEGCLLKPNMVTPGSDCGVKATPQEVAFYTVRTLSRTVPPALPGVMFLSGGQSEEEASLNLNAMNKLTLPRPWAL 290

                        250       260       270
                 ....*....|....*....|....*....|....
gi 148670365 242 SFSYGRALQASALAAWGGKAANKKATQEAFMKRA 275
Cdd:PTZ00019 291 SFSYGRALQSSALKTWKGKDENVAAAQKALLHRA 324
FrucBisAld_I NF033379
fructose-bisphosphate aldolase class I; This family consists of fructose-bisphosphate aldolase ...
 4-275 1.96e-144

fructose-bisphosphate aldolase class I; This family consists of fructose-bisphosphate aldolase class I. All members of the seed alignment are from prokaryotes, although class I is the common form in plants and animals. The common form in prokaryotes is class II.


Pssm-ID: 380231  Cd Length: 324  Bit Score: 408.10  E-value: 1.96e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365   4 ELLFSVDNsISQSIGGVILFHETLYQKDSQGNLFRNVLKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKK 83
Cdd:NF033379  47 ELLFTTPG-LGDYISGVILFDETIRQKTADGTPFPKVLADAGIIPGIKVDKGAKPLAGFPGEKVTEGLDGLRERLAEYYE 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365  84 DGVDFGKWRAVLRIADQCPSSLAIQENANALARYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDH 163
Cdd:NF033379 126 LGARFAKWRAVITIGDGIPSRACIEANAHALARYAALCQEAGLVPIVEPEVLMDGDHSIERCAEVTEEVLKEVFEELYRQ 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365 164 HVYLEGTLLKPNMVTAGHACTKKYTPEQVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINRCPlPRPWKLSF 243
Cdd:NF033379 206 GVDLEGMILKPNMVLPGKDCPDQASPEEVAEATVRCLRRTVPAAVPGIAFLSGGQSDEEATAHLNAMNKLG-PLPWPLTF 284

                        250       260       270
                 ....*....|....*....|....*....|..
gi 148670365 244 SYGRALQASALAAWGGKAANKKATQEAFMKRA 275
Cdd:NF033379 285 SYGRALQQPALKAWGGKAENVAAAQKALLHRA 316
Fba1 COG3588
Fructose-bisphosphate aldolase class 1 [Carbohydrate transport and metabolism]; ...
 4-270 3.33e-87

Fructose-bisphosphate aldolase class 1 [Carbohydrate transport and metabolism]; Fructose-bisphosphate aldolase class 1 is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 442807  Cd Length: 302  Bit Score: 261.97  E-value: 3.33e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365   4 ELLFSVDNSISQSIGGVILFHETLYQKDSQGNLFRNVLKEKGIVVGIKLDQGGAPLAgtNKETTIQGLDGLSERCAQYKK 83
Cdd:COG3588   59 ERIITSPAFTGDKISGAILFEETMDQKIDGTPTFDYLWEKKGIVPGIKVDKGLKDLA--PGVQLMKGLDGLDERLARAKE 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365  84 DGVDFGKWRAVLRIADQcpssLAIQENANALARYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDH 163
Cdd:COG3588  137 LGAFGTKWRSVIKIANA----AGIKANVHQQARYAALCQEAGLVPIVEPEVLIDGDHKIEREAELTEEILKALFDALPED 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365 164 hvylEGTLLKpnMVTAGHACTKKYTPEQvamatvtalhrtvpAAVPGICFLSGGMSEEDATLNLNAINrcplprpwKLSF 243
Cdd:COG3588  213 ----EGVMLK--MVIPGKDNLYQALVEH--------------PAVPRVVFLSGGQSREEATAHLNANN--------GLIA 264

                        250       260
                 ....*....|....*....|....*..
gi 148670365 244 SYGRALQASALAAWGGKAANKKATQEA 270
Cdd:COG3588  265 SFSRALQEGLLAAWSGEEFNAALAQAI 291
 
Name Accession Description Interval E-value
Glycolytic pfam00274
Fructose-bisphosphate aldolase class-I;
4-275 0e+00

Fructose-bisphosphate aldolase class-I;


Pssm-ID: 459742  Cd Length: 349  Bit Score: 564.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365    4 ELLFSVDNSISQSIGGVILFHETLYQKDSQGNLFRNVLKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKK 83
Cdd:pfam00274  47 QLLFTTDGELGEYISGVILFHETLYQKTDDGKPFVDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQGLDGLAERCAQYYK 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365   84 DGVDFGKWRAVLRIADQCPSSLAIQENANALARYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDH 163
Cdd:pfam00274 127 DGARFAKWRCVLKIGENTPSELAIQENANVLARYASICQQNGLVPIVEPEILPDGDHDLERCQKVTEKVLAAVYKALNDH 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365  164 HVYLEGTLLKPNMVTAGHACTKKYTPEQVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINRCPLPRPWKLSF 243
Cdd:pfam00274 207 HVYLEGTLLKPNMVTPGADCPKKYTPEEIAEATVTALRRTVPPAVPGVTFLSGGQSEEEATVNLNAINKLPLKKPWALTF 286

                         250       260       270
                  ....*....|....*....|....*....|..
gi 148670365  244 SYGRALQASALAAWGGKAANKKATQEAFMKRA 275
Cdd:pfam00274 287 SYGRALQASVLKAWGGKKENVKAAQEELLKRA 318
FBP_aldolase_I_a cd00948
Fructose-1,6-bisphosphate aldolase; Fructose-1,6-bisphosphate aldolase. The enzyme catalyzes ...
 4-275 0e+00

Fructose-1,6-bisphosphate aldolase; Fructose-1,6-bisphosphate aldolase. The enzyme catalyzes the cleavage of fructose 1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate (DHAP). This family includes proteins found in vertebrates, plants, and bacterial plant pathogens. Mutations in the aldolase genes in humans cause hemolytic anemia and hereditary fructose intolerance. The enzyme is a member of the class I aldolase family, which utilizes covalent catalysis through a Schiff base formed between a lysine residue of the enzyme and ketose substrates.


Pssm-ID: 188635  Cd Length: 330  Bit Score: 536.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365   4 ELLFSVDNsISQSIGGVILFHETLYQKDSQGNLFRNVLKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKK 83
Cdd:cd00948   49 ELLFTTPG-LGQYISGVILFEETLYQKTDDGKPFVDILKEKGIVPGIKVDKGLVPLAGTDGETTTQGLDGLAERCAKYYK 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365  84 DGVDFGKWRAVLRIADQCPSSLAIQENANALARYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDH 163
Cdd:cd00948  128 QGARFAKWRAVLKIGNGTPSELAIKENAHGLARYAAICQENGLVPIVEPEVLMDGDHDIERCQEVTEKVLAAVYKALNDH 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365 164 HVYLEGTLLKPNMVTAGHACTKKYTPEQVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINRCPLPRPWKLSF 243
Cdd:cd00948  208 HVLLEGTLLKPNMVTPGADCKKKASPEEVAEYTVRALRRTVPAAVPGIVFLSGGQSEEEATLNLNAMNKLPLPKPWALSF 287

                        250       260       270
                 ....*....|....*....|....*....|..
gi 148670365 244 SYGRALQASALAAWGGKAANKKATQEAFMKRA 275
Cdd:cd00948  288 SYGRALQASALKAWGGKKENVEAAQKALLKRA 319
PTZ00019 PTZ00019
fructose-bisphosphate aldolase; Provisional
 4-275 1.91e-157

fructose-bisphosphate aldolase; Provisional


Pssm-ID: 240231  Cd Length: 355  Bit Score: 442.23  E-value: 1.91e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365   4 ELLFSVdNSISQSIGGVILFHETLYQKDSQGNLFRNVLKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKK 83
Cdd:PTZ00019  52 ELLFTT-EGLEQYISGVILFEETVYQKAPSGKTFVELLKEKGIVPGIKVDKGLVTLPGTDGETSTQGLDGLAERAKKYYK 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365  84 DGVDFGKWRAVLRI--ADQCPSSLAIQENANALARYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALN 161
Cdd:PTZ00019 131 AGARFAKWRAVLKIdpAKGKPSELAIQENAWTLARYAAICQENGLVPIVEPEILIDGSHSIEVCQKVTEKVLAEVFKALN 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365 162 DHHVYLEGTLLKPNMVTAGHACTKKYTPEQVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINRCPLPRPWKL 241
Cdd:PTZ00019 211 DHGVLLEGCLLKPNMVTPGSDCGVKATPQEVAFYTVRTLSRTVPPALPGVMFLSGGQSEEEASLNLNAMNKLTLPRPWAL 290

                        250       260       270
                 ....*....|....*....|....*....|....
gi 148670365 242 SFSYGRALQASALAAWGGKAANKKATQEAFMKRA 275
Cdd:PTZ00019 291 SFSYGRALQSSALKTWKGKDENVAAAQKALLHRA 324
FrucBisAld_I NF033379
fructose-bisphosphate aldolase class I; This family consists of fructose-bisphosphate aldolase ...
 4-275 1.96e-144

fructose-bisphosphate aldolase class I; This family consists of fructose-bisphosphate aldolase class I. All members of the seed alignment are from prokaryotes, although class I is the common form in plants and animals. The common form in prokaryotes is class II.


Pssm-ID: 380231  Cd Length: 324  Bit Score: 408.10  E-value: 1.96e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365   4 ELLFSVDNsISQSIGGVILFHETLYQKDSQGNLFRNVLKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKK 83
Cdd:NF033379  47 ELLFTTPG-LGDYISGVILFDETIRQKTADGTPFPKVLADAGIIPGIKVDKGAKPLAGFPGEKVTEGLDGLRERLAEYYE 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365  84 DGVDFGKWRAVLRIADQCPSSLAIQENANALARYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDH 163
Cdd:NF033379 126 LGARFAKWRAVITIGDGIPSRACIEANAHALARYAALCQEAGLVPIVEPEVLMDGDHSIERCAEVTEEVLKEVFEELYRQ 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365 164 HVYLEGTLLKPNMVTAGHACTKKYTPEQVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINRCPlPRPWKLSF 243
Cdd:NF033379 206 GVDLEGMILKPNMVLPGKDCPDQASPEEVAEATVRCLRRTVPAAVPGIAFLSGGQSDEEATAHLNAMNKLG-PLPWPLTF 284

                        250       260       270
                 ....*....|....*....|....*....|..
gi 148670365 244 SYGRALQASALAAWGGKAANKKATQEAFMKRA 275
Cdd:NF033379 285 SYGRALQQPALKAWGGKAENVAAAQKALLHRA 316
PLN02455 PLN02455
fructose-bisphosphate aldolase
 2-275 4.18e-141

fructose-bisphosphate aldolase


Pssm-ID: 178074  Cd Length: 358  Bit Score: 401.05  E-value: 4.18e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365   2 LGELLFSVDNSIsQSIGGVILFHETLYQKDSQGNLFRNVLKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQY 81
Cdd:PLN02455  55 LRELLFTAPGAL-QYLSGVILFEETLYQKTSDGKPFVDVLKENGVLPGIKVDKGTVELAGTNGETTTQGLDGLGARCAKY 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365  82 KKDGVDFGKWRAVLRIADQCPSSLAIQENANALARYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALN 161
Cdd:PLN02455 134 YEAGARFAKWRAVLKIGPTEPSELAIQENAQGLARYAIICQENGLVPIVEPEILVDGSHDIKKCAAVTERVLAACYKALN 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365 162 DHHVYLEGTLLKPNMVTAGHAcTKKYTPEQVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINRCPLPRPWKL 241
Cdd:PLN02455 214 DHHVLLEGTLLKPNMVTPGSD-SPKVSPEVIAEYTVRALQRTVPPAVPGIVFLSGGQSEEEATLNLNAMNKLKTLKPWTL 292

                        250       260       270
                 ....*....|....*....|....*....|....
gi 148670365 242 SFSYGRALQASALAAWGGKAANKKATQEAFMKRA 275
Cdd:PLN02455 293 SFSFGRALQQSTLKAWAGKKENVAKAQAAFLVRC 326
FBP_aldolase_I cd00344
Fructose-bisphosphate aldolase class I; Fructose-bisphosphate aldolase class I. Fructose-1, ...
 4-276 1.21e-133

Fructose-bisphosphate aldolase class I; Fructose-bisphosphate aldolase class I. Fructose-1,6-bisphosphate aldolase is an enzyme of the glycolytic and gluconeogenic pathways found in vertebrates, plants, and bacteria. The enzyme catalyzes the cleavage of fructose 1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate (DHAP). Mutations in the aldolase genes in humans cause hemolytic anemia and hereditary fructose intolerance. The enzyme is a member of the class I aldolase family, which utilizes covalent catalysis through a Schiff base formed between a lysine residue of the enzyme and ketose substrates. Although structurally similar, the class II aldolases use a different mechanism and are believed to have an independent evolutionary origin.


Pssm-ID: 188629  Cd Length: 328  Bit Score: 381.07  E-value: 1.21e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365   4 ELLFSVDNSISQSIGGVILFHETLYQKDSQGNLFRNVLKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKK 83
Cdd:cd00344   49 QLLLTADDRVNPRIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKK 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365  84 DGVDFGKWRAVLRIADQCPSSLAIQENANALARYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDH 163
Cdd:cd00344  129 DGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDH 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365 164 HVYLEGTLLKPNMVTAGHACTKKYTPEQVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINRCPLPRPWKLSF 243
Cdd:cd00344  209 HIYLEGTLLKPNMVTPGHACTQKFSHEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTF 288

                        250       260       270
                 ....*....|....*....|....*....|...
gi 148670365 244 SYGRALQASALAAWGGKAANKKATQEAFMKRAM 276
Cdd:cd00344  289 SYGRALQASALKAWGGKKENLKAAQEEYVKRAL 321
PLN02425 PLN02425
probable fructose-bisphosphate aldolase
 13-275 1.32e-103

probable fructose-bisphosphate aldolase


Pssm-ID: 215234  Cd Length: 390  Bit Score: 306.95  E-value: 1.32e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365  13 ISQSIGGVILFHETLYQKDSQGNLFRNVLKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGVDFGKWR 92
Cdd:PLN02425 100 LGEYISGAILFEETLYQSTTDGKKFVDCLRDQNIVPGIKVDKGLVPLPGSNNESWCQGLDGLASRSAEYYKQGARFAKWR 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365  93 AVLRIAdqC-PSSLAIQENANALARYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDHHVYLEGTL 171
Cdd:PLN02425 180 TVVSIP--CgPSALAVKEAAWGLARYAAISQDNGLVPIVEPEILLDGDHPIERTLEVAEKVWSEVFFYLAQNNVLFEGIL 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365 172 LKPNMVTAGHACTKKYTPEQVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINRCplPRPWKLSFSYGRALQA 251
Cdd:PLN02425 258 LKPSMVTPGAEHKEKASPETIAKYTLTMLRRRVPPAVPGIMFLSGGQSEVEATLNLNAMNQS--PNPWHVSFSYARALQN 335

                        250       260
                 ....*....|....*....|....
gi 148670365 252 SALAAWGGKAANKKATQEAFMKRA 275
Cdd:PLN02425 336 SVLKTWQGRPENVEAAQKALLVRA 359
PLN02227 PLN02227
fructose-bisphosphate aldolase I
 13-275 4.70e-88

fructose-bisphosphate aldolase I


Pssm-ID: 177872  Cd Length: 399  Bit Score: 267.44  E-value: 4.70e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365  13 ISQSIGGVILFHETLYQKDSQGNLFRNVLKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGVDFGKWR 92
Cdd:PLN02227 109 LGQYISGAILFEETLYQSTTDGKKMVDVLVEQNIVPGIKVDKGLVPLVGSYDESWCQGLDGLASRTAAYYQQGARFAKWR 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365  93 AVLRIADQcPSSLAIQENANALARYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDHHVYLEGTLL 172
Cdd:PLN02227 189 TVVSIPNG-PSALAVKEAAWGLARYAAISQDSGLVPIVEPEIMLDGEHGIDRTYDVAEKVWAEVFFYLAQNNVMFEGILL 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365 173 KPNMVTAGHACTKKYTPEQVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINRCplPRPWKLSFSYGRALQAS 252
Cdd:PLN02227 268 KPSMVTPGAEATDRATPEQVASYTLKLLRNRIPPAVPGIMFLSGGQSELEATLNLNAMNQA--PNPWHVSFSYARALQNT 345

                        250       260
                 ....*....|....*....|...
gi 148670365 253 ALAAWGGKAANKKATQEAFMKRA 275
Cdd:PLN02227 346 CLKTWGGKEENVKAAQDILLARA 368
Fba1 COG3588
Fructose-bisphosphate aldolase class 1 [Carbohydrate transport and metabolism]; ...
 4-270 3.33e-87

Fructose-bisphosphate aldolase class 1 [Carbohydrate transport and metabolism]; Fructose-bisphosphate aldolase class 1 is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 442807  Cd Length: 302  Bit Score: 261.97  E-value: 3.33e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365   4 ELLFSVDNSISQSIGGVILFHETLYQKDSQGNLFRNVLKEKGIVVGIKLDQGGAPLAgtNKETTIQGLDGLSERCAQYKK 83
Cdd:COG3588   59 ERIITSPAFTGDKISGAILFEETMDQKIDGTPTFDYLWEKKGIVPGIKVDKGLKDLA--PGVQLMKGLDGLDERLARAKE 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365  84 DGVDFGKWRAVLRIADQcpssLAIQENANALARYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDH 163
Cdd:COG3588  137 LGAFGTKWRSVIKIANA----AGIKANVHQQARYAALCQEAGLVPIVEPEVLIDGDHKIEREAELTEEILKALFDALPED 212

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365 164 hvylEGTLLKpnMVTAGHACTKKYTPEQvamatvtalhrtvpAAVPGICFLSGGMSEEDATLNLNAINrcplprpwKLSF 243
Cdd:COG3588  213 ----EGVMLK--MVIPGKDNLYQALVEH--------------PAVPRVVFLSGGQSREEATAHLNANN--------GLIA 264

                        250       260
                 ....*....|....*....|....*..
gi 148670365 244 SYGRALQASALAAWGGKAANKKATQEA 270
Cdd:COG3588  265 SFSRALQEGLLAAWSGEEFNAALAQAI 291
FBP_aldolase_I_bact cd00949
Fructose-1.6-bisphosphate aldolase found in gram +/- bacteria; Fructose-1.6-bisphosphate ...
 14-134 1.52e-06

Fructose-1.6-bisphosphate aldolase found in gram +/- bacteria; Fructose-1.6-bisphosphate aldolase found in gram +/- bacteria. The enzyme catalyzes the cleavage of fructose 1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate (DHAP). The enzyme is member of the class I aldolase family, which utilizes covalent catalysis through a Schiff base formed between a lysine residue of the enzyme and ketose substrates.


Pssm-ID: 188636  Cd Length: 292  Bit Score: 48.56  E-value: 1.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365  14 SQSIGGVILFHETLYQKdSQGNLFRNVL-KEKGIVVGIKLDQGGAPLA-GTNKETTIQGLDGLSERCaqyKKDGVdFG-K 90
Cdd:cd00949   63 GDKILGAILFEQTMDRE-IEGKPTADYLwEKKQIVPFLKVDKGLAEEKnGVQLMKPIPNLDELLMRA---KEKGV-FGtK 137

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 148670365  91 WRAVLRIADQCPSSLAIQENANalarYASICQQNGLVPIVEPEV 134
Cdd:cd00949  138 MRSVIKEANPKGIAAVVDQQFE----LAKQILSHGLVPIIEPEV 177
PRK05377 PRK05377
fructose-1,6-bisphosphate aldolase; Reviewed
 14-134 1.16e-05

fructose-1,6-bisphosphate aldolase; Reviewed


Pssm-ID: 180045  Cd Length: 296  Bit Score: 45.64  E-value: 1.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148670365  14 SQSIGGVILFHETLYQKdSQGNLFRNVL-KEKGIVVGIKLDQGGAPLA-GTNKETTIQGLDGLSERCaqyKKDGVdFG-K 90
Cdd:PRK05377  66 GDKILGAILFEQTMDRE-IEGKPTADYLwEKKGVVPFLKVDKGLAEEAnGVQLMKPIPNLDDLLDRA---VEKGI-FGtK 140

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 148670365  91 WRAVLRIAdqcpsslaiqeNANALAryASICQQ---------NGLVPIVEPEV 134
Cdd:PRK05377 141 MRSVIKEA-----------NEQGIA--AVVAQQfevakqilaAGLVPIIEPEV 180
 
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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