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Conserved domains on  [gi|26333165|dbj|BAC30300|]
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unnamed protein product, 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;
2-318 0e+00

Fructose-bisphosphate aldolase class-I;


:

Pssm-ID: 459742  Cd Length: 349  Bit Score: 689.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165     2 IGVENTEENRRLYRQVLFSADDRVKKCIGGVIFFHETLYQKDDNGVPFVRTIQDKGILVGIKVDKGVVPLAGTDGETTTQ 81
Cdd:pfam00274  33 IGVENTEENRRAYRQLLFTTDGELGEYISGVILFHETLYQKTDDGKPFVDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQ 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165    82 GLDGLLERCAQYKKDGADFAKWRCVLKISDRTPSALAILENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVT 161
Cdd:pfam00274 113 GLDGLAERCAQYYKDGARFAKWRCVLKIGENTPSELAIQENANVLARYASICQQNGLVPIVEPEILPDGDHDLERCQKVT 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165   162 EKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYSPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASLNLNA 241
Cdd:pfam00274 193 EKVLAAVYKALNDHHVYLEGTLLKPNMVTPGADCPKKYTPEEIAEATVTALRRTVPPAVPGVTFLSGGQSEEEATVNLNA 272

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26333165   242 INRCPLPRPWALTFSYGRALQASALNAWRGQRDNAGAATEEFIKRAEMNGLAAQGRYEGSGDGGAAAQSLYIANHAY 318
Cdd:pfam00274 273 INKLPLKKPWALTFSYGRALQASVLKAWGGKKENVKAAQEELLKRAKANSLASLGKYVGGVEGAAASESLFVANYAY 349
 
Name Accession Description Interval E-value
Glycolytic pfam00274
Fructose-bisphosphate aldolase class-I;
2-318 0e+00

Fructose-bisphosphate aldolase class-I;


Pssm-ID: 459742  Cd Length: 349  Bit Score: 689.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165     2 IGVENTEENRRLYRQVLFSADDRVKKCIGGVIFFHETLYQKDDNGVPFVRTIQDKGILVGIKVDKGVVPLAGTDGETTTQ 81
Cdd:pfam00274  33 IGVENTEENRRAYRQLLFTTDGELGEYISGVILFHETLYQKTDDGKPFVDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQ 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165    82 GLDGLLERCAQYKKDGADFAKWRCVLKISDRTPSALAILENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVT 161
Cdd:pfam00274 113 GLDGLAERCAQYYKDGARFAKWRCVLKIGENTPSELAIQENANVLARYASICQQNGLVPIVEPEILPDGDHDLERCQKVT 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165   162 EKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYSPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASLNLNA 241
Cdd:pfam00274 193 EKVLAAVYKALNDHHVYLEGTLLKPNMVTPGADCPKKYTPEEIAEATVTALRRTVPPAVPGVTFLSGGQSEEEATVNLNA 272

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26333165   242 INRCPLPRPWALTFSYGRALQASALNAWRGQRDNAGAATEEFIKRAEMNGLAAQGRYEGSGDGGAAAQSLYIANHAY 318
Cdd:pfam00274 273 INKLPLKKPWALTFSYGRALQASVLKAWGGKKENVKAAQEELLKRAKANSLASLGKYVGGVEGAAASESLFVANYAY 349
FBP_aldolase_I_a cd00948
Fructose-1,6-bisphosphate aldolase; Fructose-1,6-bisphosphate aldolase. The enzyme catalyzes ...
 2-298 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: 594.23  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165   2 IGVENTEENRRLYRQVLFSADDRVKkCIGGVIFFHETLYQKDDNGVPFVRTIQDKGILVGIKVDKGVVPLAGTDGETTTQ 81
Cdd:cd00948  35 IGVENTEENRRAYRELLFTTPGLGQ-YISGVILFEETLYQKTDDGKPFVDILKEKGIVPGIKVDKGLVPLAGTDGETTTQ 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165  82 GLDGLLERCAQYKKDGADFAKWRCVLKISDRTPSALAILENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVT 161
Cdd:cd00948 114 GLDGLAERCAKYYKQGARFAKWRAVLKIGNGTPSELAIKENAHGLARYAAICQENGLVPIVEPEVLMDGDHDIERCQEVT 193

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165 162 EKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYSPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASLNLNA 241
Cdd:cd00948 194 EKVLAAVYKALNDHHVLLEGTLLKPNMVTPGADCKKKASPEEVAEYTVRALRRTVPAAVPGIVFLSGGQSEEEATLNLNA 273

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 26333165 242 INRCPLPRPWALTFSYGRALQASALNAWRGQRDNAGAATEEFIKRAEMNGLAAQGRY 298
Cdd:cd00948 274 MNKLPLPKPWALSFSYGRALQASALKAWGGKKENVEAAQKALLKRAKANSLAALGKY 330
PTZ00019 PTZ00019
fructose-bisphosphate aldolase; Provisional
 2-318 0e+00

fructose-bisphosphate aldolase; Provisional


Pssm-ID: 240231  Cd Length: 355  Bit Score: 520.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165    2 IGVENTEENRRLYRQVLFSADDrVKKCIGGVIFFHETLYQKDDNGVPFVRTIQDKGILVGIKVDKGVVPLAGTDGETTTQ 81
Cdd:PTZ00019  38 IGLENTEENRRAYRELLFTTEG-LEQYISGVILFEETVYQKAPSGKTFVELLKEKGIVPGIKVDKGLVTLPGTDGETSTQ 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165   82 GLDGLLERCAQYKKDGADFAKWRCVLKI--SDRTPSALAILENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQY 159
Cdd:PTZ00019 117 GLDGLAERAKKYYKAGARFAKWRAVLKIdpAKGKPSELAIQENAWTLARYAAICQENGLVPIVEPEILIDGSHSIEVCQK 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165  160 VTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYSPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASLNL 239
Cdd:PTZ00019 197 VTEKVLAEVFKALNDHGVLLEGCLLKPNMVTPGSDCGVKATPQEVAFYTVRTLSRTVPPALPGVMFLSGGQSEEEASLNL 276

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26333165  240 NAINRCPLPRPWALTFSYGRALQASALNAWRGQRDNAGAATEEFIKRAEMNGLAAQGRYEGSGDGGAAAQSLYIANHAY 318
Cdd:PTZ00019 277 NAMNKLTLPRPWALSFSYGRALQSSALKTWKGKDENVAAAQKALLHRAKANSLAQLGKYKGGDGGAAASESLYVKDYKY 355
FrucBisAld_I NF033379
fructose-bisphosphate aldolase class I; This family consists of fructose-bisphosphate aldolase ...
 2-295 6.50e-169

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: 471.66  E-value: 6.50e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165    2 IGVENTEENRRLYRQVLFSADDrVKKCIGGVIFFHETLYQKDDNGVPFVRTIQDKGILVGIKVDKGVVPLAGTDGETTTQ 81
Cdd:NF033379  33 IGVESTEENRRAYRELLFTTPG-LGDYISGVILFDETIRQKTADGTPFPKVLADAGIIPGIKVDKGAKPLAGFPGEKVTE 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165   82 GLDGLLERCAQYKKDGADFAKWRCVLKISDRTPSALAILENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVT 161
Cdd:NF033379 112 GLDGLRERLAEYYELGARFAKWRAVITIGDGIPSRACIEANAHALARYAALCQEAGLVPIVEPEVLMDGDHSIERCAEVT 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165  162 EKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYSPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASLNLNA 241
Cdd:NF033379 192 EEVLKEVFEELYRQGVDLEGMILKPNMVLPGKDCPDQASPEEVAEATVRCLRRTVPAAVPGIAFLSGGQSDEEATAHLNA 271

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 26333165  242 INRCPlPRPWALTFSYGRALQASALNAWRGQRDNAGAATEEFIKRAEMNGLAAQ 295
Cdd:NF033379 272 MNKLG-PLPWPLTFSYGRALQQPALKAWGGKAENVAAAQKALLHRARMNSLAAL 324
Fba1 COG3588
Fructose-bisphosphate aldolase class 1 [Carbohydrate transport and metabolism]; ...
 2-301 1.41e-100

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: 297.41  E-value: 1.41e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165   2 IGVENTEENRRL--------YRQVLFSADDRVKKCIGGVIFFHETLYQKDDnGVP-FVRTIQDKGILVGIKVDKGVVPLA 72
Cdd:COG3588  37 YGVEETEYSRREemfdlvhaMRERIITSPAFTGDKISGAILFEETMDQKID-GTPtFDYLWEKKGIVPGIKVDKGLKDLA 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165  73 gtDGETTTQGLDGLLERCAQYKKDGADFAKWRCVLKISDRTpsalAILENANVLARYASICQQNGIVPIVEPEILPDGDH 152
Cdd:COG3588 116 --PGVQLMKGLDGLDERLARAKELGAFGTKWRSVIKIANAA----GIKANVHQQARYAALCQEAGLVPIVEPEVLIDGDH 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165 153 DLKRCQYVTEKVLAAVYKALSDHhvylEGTLLKpnMVTPGHACPIKYSPEEiamatvtalrrtvpPAVPGVTFLSGGQSE 232
Cdd:COG3588 190 KIEREAELTEEILKALFDALPED----EGVMLK--MVIPGKDNLYQALVEH--------------PAVPRVVFLSGGQSR 249

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26333165 233 EEASLNLNAINrcplprpwALTFSYGRALQASALNAWRGQRDNAGAATeefikraemnglAAQGRYEGS 301
Cdd:COG3588 250 EEATAHLNANN--------GLIASFSRALQEGLLAAWSGEEFNAALAQ------------AIDGIYDAS 298
 
Name Accession Description Interval E-value
Glycolytic pfam00274
Fructose-bisphosphate aldolase class-I;
2-318 0e+00

Fructose-bisphosphate aldolase class-I;


Pssm-ID: 459742  Cd Length: 349  Bit Score: 689.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165     2 IGVENTEENRRLYRQVLFSADDRVKKCIGGVIFFHETLYQKDDNGVPFVRTIQDKGILVGIKVDKGVVPLAGTDGETTTQ 81
Cdd:pfam00274  33 IGVENTEENRRAYRQLLFTTDGELGEYISGVILFHETLYQKTDDGKPFVDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQ 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165    82 GLDGLLERCAQYKKDGADFAKWRCVLKISDRTPSALAILENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVT 161
Cdd:pfam00274 113 GLDGLAERCAQYYKDGARFAKWRCVLKIGENTPSELAIQENANVLARYASICQQNGLVPIVEPEILPDGDHDLERCQKVT 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165   162 EKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYSPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASLNLNA 241
Cdd:pfam00274 193 EKVLAAVYKALNDHHVYLEGTLLKPNMVTPGADCPKKYTPEEIAEATVTALRRTVPPAVPGVTFLSGGQSEEEATVNLNA 272

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26333165   242 INRCPLPRPWALTFSYGRALQASALNAWRGQRDNAGAATEEFIKRAEMNGLAAQGRYEGSGDGGAAAQSLYIANHAY 318
Cdd:pfam00274 273 INKLPLKKPWALTFSYGRALQASVLKAWGGKKENVKAAQEELLKRAKANSLASLGKYVGGVEGAAASESLFVANYAY 349
FBP_aldolase_I_a cd00948
Fructose-1,6-bisphosphate aldolase; Fructose-1,6-bisphosphate aldolase. The enzyme catalyzes ...
 2-298 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: 594.23  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165   2 IGVENTEENRRLYRQVLFSADDRVKkCIGGVIFFHETLYQKDDNGVPFVRTIQDKGILVGIKVDKGVVPLAGTDGETTTQ 81
Cdd:cd00948  35 IGVENTEENRRAYRELLFTTPGLGQ-YISGVILFEETLYQKTDDGKPFVDILKEKGIVPGIKVDKGLVPLAGTDGETTTQ 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165  82 GLDGLLERCAQYKKDGADFAKWRCVLKISDRTPSALAILENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVT 161
Cdd:cd00948 114 GLDGLAERCAKYYKQGARFAKWRAVLKIGNGTPSELAIKENAHGLARYAAICQENGLVPIVEPEVLMDGDHDIERCQEVT 193

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165 162 EKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYSPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASLNLNA 241
Cdd:cd00948 194 EKVLAAVYKALNDHHVLLEGTLLKPNMVTPGADCKKKASPEEVAEYTVRALRRTVPAAVPGIVFLSGGQSEEEATLNLNA 273

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 26333165 242 INRCPLPRPWALTFSYGRALQASALNAWRGQRDNAGAATEEFIKRAEMNGLAAQGRY 298
Cdd:cd00948 274 MNKLPLPKPWALSFSYGRALQASALKAWGGKKENVEAAQKALLKRAKANSLAALGKY 330
PTZ00019 PTZ00019
fructose-bisphosphate aldolase; Provisional
 2-318 0e+00

fructose-bisphosphate aldolase; Provisional


Pssm-ID: 240231  Cd Length: 355  Bit Score: 520.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165    2 IGVENTEENRRLYRQVLFSADDrVKKCIGGVIFFHETLYQKDDNGVPFVRTIQDKGILVGIKVDKGVVPLAGTDGETTTQ 81
Cdd:PTZ00019  38 IGLENTEENRRAYRELLFTTEG-LEQYISGVILFEETVYQKAPSGKTFVELLKEKGIVPGIKVDKGLVTLPGTDGETSTQ 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165   82 GLDGLLERCAQYKKDGADFAKWRCVLKI--SDRTPSALAILENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQY 159
Cdd:PTZ00019 117 GLDGLAERAKKYYKAGARFAKWRAVLKIdpAKGKPSELAIQENAWTLARYAAICQENGLVPIVEPEILIDGSHSIEVCQK 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165  160 VTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYSPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASLNL 239
Cdd:PTZ00019 197 VTEKVLAEVFKALNDHGVLLEGCLLKPNMVTPGSDCGVKATPQEVAFYTVRTLSRTVPPALPGVMFLSGGQSEEEASLNL 276

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26333165  240 NAINRCPLPRPWALTFSYGRALQASALNAWRGQRDNAGAATEEFIKRAEMNGLAAQGRYEGSGDGGAAAQSLYIANHAY 318
Cdd:PTZ00019 277 NAMNKLTLPRPWALSFSYGRALQSSALKTWKGKDENVAAAQKALLHRAKANSLAQLGKYKGGDGGAAASESLYVKDYKY 355
FrucBisAld_I NF033379
fructose-bisphosphate aldolase class I; This family consists of fructose-bisphosphate aldolase ...
 2-295 6.50e-169

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: 471.66  E-value: 6.50e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165    2 IGVENTEENRRLYRQVLFSADDrVKKCIGGVIFFHETLYQKDDNGVPFVRTIQDKGILVGIKVDKGVVPLAGTDGETTTQ 81
Cdd:NF033379  33 IGVESTEENRRAYRELLFTTPG-LGDYISGVILFDETIRQKTADGTPFPKVLADAGIIPGIKVDKGAKPLAGFPGEKVTE 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165   82 GLDGLLERCAQYKKDGADFAKWRCVLKISDRTPSALAILENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVT 161
Cdd:NF033379 112 GLDGLRERLAEYYELGARFAKWRAVITIGDGIPSRACIEANAHALARYAALCQEAGLVPIVEPEVLMDGDHSIERCAEVT 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165  162 EKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYSPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASLNLNA 241
Cdd:NF033379 192 EEVLKEVFEELYRQGVDLEGMILKPNMVLPGKDCPDQASPEEVAEATVRCLRRTVPAAVPGIAFLSGGQSDEEATAHLNA 271

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 26333165  242 INRCPlPRPWALTFSYGRALQASALNAWRGQRDNAGAATEEFIKRAEMNGLAAQ 295
Cdd:NF033379 272 MNKLG-PLPWPLTFSYGRALQQPALKAWGGKAENVAAAQKALLHRARMNSLAAL 324
PLN02455 PLN02455
fructose-bisphosphate aldolase
 2-318 5.78e-165

fructose-bisphosphate aldolase


Pssm-ID: 178074  Cd Length: 358  Bit Score: 463.07  E-value: 5.78e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165    2 IGVENTEENRRLYRQVLFSADDrVKKCIGGVIFFHETLYQKDDNGVPFVRTIQDKGILVGIKVDKGVVPLAGTDGETTTQ 81
Cdd:PLN02455  43 INVENVESNRQALRELLFTAPG-ALQYLSGVILFEETLYQKTSDGKPFVDVLKENGVLPGIKVDKGTVELAGTNGETTTQ 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165   82 GLDGLLERCAQYKKDGADFAKWRCVLKISDRTPSALAILENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVT 161
Cdd:PLN02455 122 GLDGLGARCAKYYEAGARFAKWRAVLKIGPTEPSELAIQENAQGLARYAIICQENGLVPIVEPEILVDGSHDIKKCAAVT 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165  162 EKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPiKYSPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASLNLNA 241
Cdd:PLN02455 202 ERVLAACYKALNDHHVLLEGTLLKPNMVTPGSDSP-KVSPEVIAEYTVRALQRTVPPAVPGIVFLSGGQSEEEATLNLNA 280

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26333165  242 INRCPLPRPWALTFSYGRALQASALNAWRGQRDNAGAATEEFIKRAEMNGLAAQGRYEGSGDGG-AAAQSLYIANHAY 318
Cdd:PLN02455 281 MNKLKTLKPWTLSFSFGRALQQSTLKAWAGKKENVAKAQAAFLVRCKANSEATLGKYKGDAAGGeGASESLHVKDYKY 358
FBP_aldolase_I cd00344
Fructose-bisphosphate aldolase class I; Fructose-bisphosphate aldolase class I. Fructose-1, ...
 2-295 5.82e-164

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: 459.65  E-value: 5.82e-164
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165   2 IGVENTEENRRLYRQVLFSADDRVKKCIGGVIFFHETLYQKDDNGVPFVRTIQDKGILVGIKVDKGVVPLAGTDGETTTQ 81
Cdd:cd00344  35 IGTENTEENRRFYRQLLLTADDRVNPRIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQ 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165  82 GLDGLLERCAQYKKDGADFAKWRCVLKISDRTPSALAILENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVT 161
Cdd:cd00344 115 GLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVT 194

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165 162 EKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYSPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASLNLNA 241
Cdd:cd00344 195 EKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKFSHEEIAMATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNA 274

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 26333165 242 INRCPLPRPWALTFSYGRALQASALNAWRGQRDNAGAATEEFIKRAEMNGLAAQ 295
Cdd:cd00344 275 INKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALANSLAAQ 328
PLN02425 PLN02425
probable fructose-bisphosphate aldolase
 2-318 2.52e-123

probable fructose-bisphosphate aldolase


Pssm-ID: 215234  Cd Length: 390  Bit Score: 358.95  E-value: 2.52e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165    2 IGVENTEENRRLYRQVLFSADDrVKKCIGGVIFFHETLYQKDDNGVPFVRTIQDKGILVGIKVDKGVVPLAGTDGETTTQ 81
Cdd:PLN02425  78 IGLDNTETNRQAYRQLLLTTPG-LGEYISGAILFEETLYQSTTDGKKFVDCLRDQNIVPGIKVDKGLVPLPGSNNESWCQ 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165   82 GLDGLLERCAQYKKDGADFAKWRCVLKISdRTPSALAILENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVT 161
Cdd:PLN02425 157 GLDGLASRSAEYYKQGARFAKWRTVVSIP-CGPSALAVKEAAWGLARYAAISQDNGLVPIVEPEILLDGDHPIERTLEVA 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165  162 EKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYSPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASLNLNA 241
Cdd:PLN02425 236 EKVWSEVFFYLAQNNVLFEGILLKPSMVTPGAEHKEKASPETIAKYTLTMLRRRVPPAVPGIMFLSGGQSEVEATLNLNA 315

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26333165  242 INRCplPRPWALTFSYGRALQASALNAWRGQRDNAGAATEEFIKRAEMNGLAAQGRYEGSGDGGAAAQSLYIANHAY 318
Cdd:PLN02425 316 MNQS--PNPWHVSFSYARALQNSVLKTWQGRPENVEAAQKALLVRAKANSLAQLGRYSAEGESEEAKKGMFVKGYTY 390
PLN02227 PLN02227
fructose-bisphosphate aldolase I
 2-318 1.68e-102

fructose-bisphosphate aldolase I


Pssm-ID: 177872  Cd Length: 399  Bit Score: 305.95  E-value: 1.68e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165    2 IGVENTEENRRLYRQVLFSADDrVKKCIGGVIFFHETLYQKDDNGVPFVRTIQDKGILVGIKVDKGVVPLAGTDGETTTQ 81
Cdd:PLN02227  87 IGLENTEANRQAYRTLLVSAPG-LGQYISGAILFEETLYQSTTDGKKMVDVLVEQNIVPGIKVDKGLVPLVGSYDESWCQ 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165   82 GLDGLLERCAQYKKDGADFAKWRCVLKISDrTPSALAILENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVT 161
Cdd:PLN02227 166 GLDGLASRTAAYYQQGARFAKWRTVVSIPN-GPSALAVKEAAWGLARYAAISQDSGLVPIVEPEIMLDGEHGIDRTYDVA 244

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165  162 EKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYSPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASLNLNA 241
Cdd:PLN02227 245 EKVWAEVFFYLAQNNVMFEGILLKPSMVTPGAEATDRATPEQVASYTLKLLRNRIPPAVPGIMFLSGGQSELEATLNLNA 324

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26333165  242 INRCplPRPWALTFSYGRALQASALNAWRGQRDNAGAATEEFIKRAEMNGLAAQGRYEGSGDGGAAAQSLYIANHAY 318
Cdd:PLN02227 325 MNQA--PNPWHVSFSYARALQNTCLKTWGGKEENVKAAQDILLARAKANSLAQLGKYTGEGESEEAKEGMFVKGYTY 399
Fba1 COG3588
Fructose-bisphosphate aldolase class 1 [Carbohydrate transport and metabolism]; ...
 2-301 1.41e-100

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: 297.41  E-value: 1.41e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165   2 IGVENTEENRRL--------YRQVLFSADDRVKKCIGGVIFFHETLYQKDDnGVP-FVRTIQDKGILVGIKVDKGVVPLA 72
Cdd:COG3588  37 YGVEETEYSRREemfdlvhaMRERIITSPAFTGDKISGAILFEETMDQKID-GTPtFDYLWEKKGIVPGIKVDKGLKDLA 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165  73 gtDGETTTQGLDGLLERCAQYKKDGADFAKWRCVLKISDRTpsalAILENANVLARYASICQQNGIVPIVEPEILPDGDH 152
Cdd:COG3588 116 --PGVQLMKGLDGLDERLARAKELGAFGTKWRSVIKIANAA----GIKANVHQQARYAALCQEAGLVPIVEPEVLIDGDH 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165 153 DLKRCQYVTEKVLAAVYKALSDHhvylEGTLLKpnMVTPGHACPIKYSPEEiamatvtalrrtvpPAVPGVTFLSGGQSE 232
Cdd:COG3588 190 KIEREAELTEEILKALFDALPED----EGVMLK--MVIPGKDNLYQALVEH--------------PAVPRVVFLSGGQSR 249

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26333165 233 EEASLNLNAINrcplprpwALTFSYGRALQASALNAWRGQRDNAGAATeefikraemnglAAQGRYEGS 301
Cdd:COG3588 250 EEATAHLNANN--------GLIASFSRALQEGLLAAWSGEEFNAALAQ------------AIDGIYDAS 298
FBP_aldolase_I_bact cd00949
Fructose-1.6-bisphosphate aldolase found in gram +/- bacteria; Fructose-1.6-bisphosphate ...
 29-301 3.73e-05

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: 44.71  E-value: 3.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165  29 IGGVIFFHETLYQKDDnGVPFVR-TIQDKGILVGIKVDKGVVPLA-GTDGETTTQGLDGLLERCAQYKKDGAdfaKWRCV 106
Cdd:cd00949  66 ILGAILFEQTMDREIE-GKPTADyLWEKKQIVPFLKVDKGLAEEKnGVQLMKPIPNLDELLMRAKEKGVFGT---KMRSV 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165 107 LKisdrtpsalaileNANVLARYASICQQ---------NGIVPIVEPEIlpdgdhDLKRCQyvTEKVLAAVYKALSDHhv 177
Cdd:cd00949 142 IK-------------EANPKGIAAVVDQQfelakqilsHGLVPIIEPEV------DIHSAD--KAKCEAILKAEILKH-- 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165 178 yLEgTLLKPNMVTPGHACPIK---YSPeeiamatvtalrRTVPPAVPGVTFLSGGQSEEEASlNLNAINRcplprpwALT 254
Cdd:cd00949 199 -LD-KLPEGQQVMLKLTLPTEanfYSE------------LIEHPKVLRVVALSGGYSREEAN-ELLAKNN-------GVI 256

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 26333165 255 FSYGRALqASALNAwrGQRDnagaatEEFikrAEMNGLAAQGRYEGS 301
Cdd:cd00949 257 ASFSRAL-TEGLSA--DQSD------AEF---NATLEKSIDEIYQAS 291
PRK05377 PRK05377
fructose-1,6-bisphosphate aldolase; Reviewed
 29-146 3.88e-04

fructose-1,6-bisphosphate aldolase; Reviewed


Pssm-ID: 180045  Cd Length: 296  Bit Score: 41.40  E-value: 3.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26333165   29 IGGVIFFHETLYQKDDnGVPFV-RTIQDKGILVGIKVDKGVVPLAgtDGettTQ------GLDGLLERCAQYKKDGAdfa 101
Cdd:PRK05377  69 ILGAILFEQTMDREIE-GKPTAdYLWEKKGVVPFLKVDKGLAEEA--NG---VQlmkpipNLDDLLDRAVEKGIFGT--- 139

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 26333165  102 KWRCVLKISDRTpsalAIlenANVLARYASICQQ---NGIVPIVEPEI 146
Cdd:PRK05377 140 KMRSVIKEANEQ----GI---AAVVAQQFEVAKQilaAGLVPIIEPEV 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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