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Conserved domains on  [gi|1952674377|ref|XP_038508654|]
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fructose-bisphosphate aldolase B isoform X1 [Canis lupus familiaris]

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;
22-371 0e+00

Fructose-bisphosphate aldolase class-I;


:

Pssm-ID: 459742  Cd Length: 349  Bit Score: 696.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377  22 ELAEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFREILFTVDNSINQSIGGVILFHETLYQKDSQGKLF 101
Cdd:pfam00274   1 ELIATAKAIVAPGKGILAADESTGTIGKRLASIGVENTEENRRAYRQLLFTTDGELGEYISGVILFHETLYQKTDDGKPF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 102 RNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGADFGKWRAVLRIDNQCPSQLAIQENANALARY 181
Cdd:pfam00274  81 VDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQGLDGLAERCAQYYKDGARFAKWRCVLKIGENTPSELAIQENANVLARY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 182 ASICQQNGLVPIVEPEVIPDGDHDLEHCQYVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPEQVAMATV 261
Cdd:pfam00274 161 ASICQQNGLVPIVEPEILPDGDHDLERCQKVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTPGADCPKKYTPEEIAEATV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 262 TALHRTVPAAVPGICFLSGGMSEEDATLNLNAINLCPLPKPWKLSFSYGRALQASALAAWGGKAANKKATQEAFMKRALA 341
Cdd:pfam00274 241 TALRRTVPPAVPGVTFLSGGQSEEEATVNLNAINKLPLKKPWALTFSYGRALQASVLKAWGGKKENVKAAQEELLKRAKA 320

                         330       340       350
                  ....*....|....*....|....*....|
gi 1952674377 342 NCQAAKGQYVHSGSSGAAStQSLFTACYTY 371
Cdd:pfam00274 321 NSLASLGKYVGGVEGAAAS-ESLFVANYAY 349
 
Name Accession Description Interval E-value
Glycolytic pfam00274
Fructose-bisphosphate aldolase class-I;
22-371 0e+00

Fructose-bisphosphate aldolase class-I;


Pssm-ID: 459742  Cd Length: 349  Bit Score: 696.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377  22 ELAEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFREILFTVDNSINQSIGGVILFHETLYQKDSQGKLF 101
Cdd:pfam00274   1 ELIATAKAIVAPGKGILAADESTGTIGKRLASIGVENTEENRRAYRQLLFTTDGELGEYISGVILFHETLYQKTDDGKPF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 102 RNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGADFGKWRAVLRIDNQCPSQLAIQENANALARY 181
Cdd:pfam00274  81 VDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQGLDGLAERCAQYYKDGARFAKWRCVLKIGENTPSELAIQENANVLARY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 182 ASICQQNGLVPIVEPEVIPDGDHDLEHCQYVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPEQVAMATV 261
Cdd:pfam00274 161 ASICQQNGLVPIVEPEILPDGDHDLERCQKVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTPGADCPKKYTPEEIAEATV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 262 TALHRTVPAAVPGICFLSGGMSEEDATLNLNAINLCPLPKPWKLSFSYGRALQASALAAWGGKAANKKATQEAFMKRALA 341
Cdd:pfam00274 241 TALRRTVPPAVPGVTFLSGGQSEEEATVNLNAINKLPLKKPWALTFSYGRALQASVLKAWGGKKENVKAAQEELLKRAKA 320

                         330       340       350
                  ....*....|....*....|....*....|
gi 1952674377 342 NCQAAKGQYVHSGSSGAAStQSLFTACYTY 371
Cdd:pfam00274 321 NSLASLGKYVGGVEGAAAS-ESLFVANYAY 349
FBP_aldolase_I_a cd00948
Fructose-1,6-bisphosphate aldolase; Fructose-1,6-bisphosphate aldolase. The enzyme catalyzes ...
 20-350 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: 650.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377  20 KKELAEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFREILFTVDNsINQSIGGVILFHETLYQKDSQGK 99
Cdd:cd00948     1 KEELIKTAKAIVAPGKGILAADESTGTIGKRFASIGVENTEENRRAYRELLFTTPG-LGQYISGVILFEETLYQKTDDGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 100 LFRNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGADFGKWRAVLRIDNQCPSQLAIQENANALA 179
Cdd:cd00948    80 PFVDILKEKGIVPGIKVDKGLVPLAGTDGETTTQGLDGLAERCAKYYKQGARFAKWRAVLKIGNGTPSELAIKENAHGLA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 180 RYASICQQNGLVPIVEPEVIPDGDHDLEHCQYVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPEQVAMA 259
Cdd:cd00948   160 RYAAICQENGLVPIVEPEVLMDGDHDIERCQEVTEKVLAAVYKALNDHHVLLEGTLLKPNMVTPGADCKKKASPEEVAEY 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 260 TVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINLCPLPKPWKLSFSYGRALQASALAAWGGKAANKKATQEAFMKRA 339
Cdd:cd00948   240 TVRALRRTVPAAVPGIVFLSGGQSEEEATLNLNAMNKLPLPKPWALSFSYGRALQASALKAWGGKKENVEAAQKALLKRA 319

                         330
                  ....*....|.
gi 1952674377 340 LANCQAAKGQY 350
Cdd:cd00948   320 KANSLAALGKY 330
PTZ00019 PTZ00019
fructose-bisphosphate aldolase; Provisional
 17-371 0e+00

fructose-bisphosphate aldolase; Provisional


Pssm-ID: 240231  Cd Length: 355  Bit Score: 550.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377  17 SEKKKELAEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFREILFTVdNSINQSIGGVILFHETLYQKDS 96
Cdd:PTZ00019    1 TEYAKELAETAKKIAAPGKGILAADESTGTIKKRFDPIGLENTEENRRAYRELLFTT-EGLEQYISGVILFEETVYQKAP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377  97 QGKLFRNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGADFGKWRAVLRID--NQCPSQLAIQEN 174
Cdd:PTZ00019   80 SGKTFVELLKEKGIVPGIKVDKGLVTLPGTDGETSTQGLDGLAERAKKYYKAGARFAKWRAVLKIDpaKGKPSELAIQEN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 175 ANALARYASICQQNGLVPIVEPEVIPDGDHDLEHCQYVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPE 254
Cdd:PTZ00019  160 AWTLARYAAICQENGLVPIVEPEILIDGSHSIEVCQKVTEKVLAEVFKALNDHGVLLEGCLLKPNMVTPGSDCGVKATPQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 255 QVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINLCPLPKPWKLSFSYGRALQASALAAWGGKAANKKATQEA 334
Cdd:PTZ00019  240 EVAFYTVRTLSRTVPPALPGVMFLSGGQSEEEASLNLNAMNKLTLPRPWALSFSYGRALQSSALKTWKGKDENVAAAQKA 319

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1952674377 335 FMKRALANCQAAKGQYvHSGSSGAASTQSLFTACYTY 371
Cdd:PTZ00019  320 LLHRAKANSLAQLGKY-KGGDGGAAASESLYVKDYKY 355
FrucBisAld_I NF033379
fructose-bisphosphate aldolase class I; This family consists of fructose-bisphosphate aldolase ...
 22-347 3.41e-177

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: 495.15  E-value: 3.41e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377  22 ELAEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFREILFTVDNsINQSIGGVILFHETLYQKDSQGKLF 101
Cdd:NF033379    1 ELEETAQAMVAPGKGILAADESTGTINKRFEAIGVESTEENRRAYRELLFTTPG-LGDYISGVILFDETIRQKTADGTPF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 102 RNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGADFGKWRAVLRIDNQCPSQLAIQENANALARY 181
Cdd:NF033379   80 PKVLADAGIIPGIKVDKGAKPLAGFPGEKVTEGLDGLRERLAEYYELGARFAKWRAVITIGDGIPSRACIEANAHALARY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 182 ASICQQNGLVPIVEPEVIPDGDHDLEHCQYVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPEQVAMATV 261
Cdd:NF033379  160 AALCQEAGLVPIVEPEVLMDGDHSIERCAEVTEEVLKEVFEELYRQGVDLEGMILKPNMVLPGKDCPDQASPEEVAEATV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 262 TALHRTVPAAVPGICFLSGGMSEEDATLNLNAINLCPlPKPWKLSFSYGRALQASALAAWGGKAANKKATQEAFMKRALA 341
Cdd:NF033379  240 RCLRRTVPAAVPGIAFLSGGQSDEEATAHLNAMNKLG-PLPWPLTFSYGRALQQPALKAWGGKAENVAAAQKALLHRARM 318


                  ....*.
gi 1952674377 342 NCQAAK 347
Cdd:NF033379  319 NSLAAL 324
Fba1 COG3588
Fructose-bisphosphate aldolase class 1 [Carbohydrate transport and metabolism]; ...
 20-350 8.80e-108

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: 317.83  E-value: 8.80e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377  20 KKELAEIAQRIVANGKGILAA-DESVGTMGNRLQRIKVENTEENRR--------QFREILFTVDNSINQSIGGVILFHET 90
Cdd:COG3588     2 TEELNATALAMVANGKGFLAAlDQSGGSTPKALAAYGVEETEYSRReemfdlvhAMRERIITSPAFTGDKISGAILFEET 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377  91 LYQKdSQGK-LFRNILKEKGIVVGIKLDQGGAPLAgtNKETTIQGLDGLSERCAQYKKDGADFGKWRAVLRIDNQcpsqL 169
Cdd:COG3588    82 MDQK-IDGTpTFDYLWEKKGIVPGIKVDKGLKDLA--PGVQLMKGLDGLDERLARAKELGAFGTKWRSVIKIANA----A 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 170 AIQENANALARYASICQQNGLVPIVEPEVIPDGDHDLEHCQYVTEKVLAAVYKALNDHhvylEGTLLKpnMVTAGHACTK 249
Cdd:COG3588   155 GIKANVHQQARYAALCQEAGLVPIVEPEVLIDGDHKIEREAELTEEILKALFDALPED----EGVMLK--MVIPGKDNLY 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 250 KYTPEQvamatvtalhrtvpAAVPGICFLSGGMSEEDATLNLNAINlcplpkpwKLSFSYGRALQASALAAWGGKAANKK 329
Cdd:COG3588   229 QALVEH--------------PAVPRVVFLSGGQSREEATAHLNANN--------GLIASFSRALQEGLLAAWSGEEFNAA 286

                         330       340
                  ....*....|....*....|.
gi 1952674377 330 ATqeafmkralancQAAKGQY 350
Cdd:COG3588   287 LA------------QAIDGIY 295
 
Name Accession Description Interval E-value
Glycolytic pfam00274
Fructose-bisphosphate aldolase class-I;
22-371 0e+00

Fructose-bisphosphate aldolase class-I;


Pssm-ID: 459742  Cd Length: 349  Bit Score: 696.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377  22 ELAEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFREILFTVDNSINQSIGGVILFHETLYQKDSQGKLF 101
Cdd:pfam00274   1 ELIATAKAIVAPGKGILAADESTGTIGKRLASIGVENTEENRRAYRQLLFTTDGELGEYISGVILFHETLYQKTDDGKPF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 102 RNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGADFGKWRAVLRIDNQCPSQLAIQENANALARY 181
Cdd:pfam00274  81 VDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQGLDGLAERCAQYYKDGARFAKWRCVLKIGENTPSELAIQENANVLARY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 182 ASICQQNGLVPIVEPEVIPDGDHDLEHCQYVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPEQVAMATV 261
Cdd:pfam00274 161 ASICQQNGLVPIVEPEILPDGDHDLERCQKVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTPGADCPKKYTPEEIAEATV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 262 TALHRTVPAAVPGICFLSGGMSEEDATLNLNAINLCPLPKPWKLSFSYGRALQASALAAWGGKAANKKATQEAFMKRALA 341
Cdd:pfam00274 241 TALRRTVPPAVPGVTFLSGGQSEEEATVNLNAINKLPLKKPWALTFSYGRALQASVLKAWGGKKENVKAAQEELLKRAKA 320

                         330       340       350
                  ....*....|....*....|....*....|
gi 1952674377 342 NCQAAKGQYVHSGSSGAAStQSLFTACYTY 371
Cdd:pfam00274 321 NSLASLGKYVGGVEGAAAS-ESLFVANYAY 349
FBP_aldolase_I_a cd00948
Fructose-1,6-bisphosphate aldolase; Fructose-1,6-bisphosphate aldolase. The enzyme catalyzes ...
 20-350 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: 650.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377  20 KKELAEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFREILFTVDNsINQSIGGVILFHETLYQKDSQGK 99
Cdd:cd00948     1 KEELIKTAKAIVAPGKGILAADESTGTIGKRFASIGVENTEENRRAYRELLFTTPG-LGQYISGVILFEETLYQKTDDGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 100 LFRNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGADFGKWRAVLRIDNQCPSQLAIQENANALA 179
Cdd:cd00948    80 PFVDILKEKGIVPGIKVDKGLVPLAGTDGETTTQGLDGLAERCAKYYKQGARFAKWRAVLKIGNGTPSELAIKENAHGLA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 180 RYASICQQNGLVPIVEPEVIPDGDHDLEHCQYVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPEQVAMA 259
Cdd:cd00948   160 RYAAICQENGLVPIVEPEVLMDGDHDIERCQEVTEKVLAAVYKALNDHHVLLEGTLLKPNMVTPGADCKKKASPEEVAEY 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 260 TVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINLCPLPKPWKLSFSYGRALQASALAAWGGKAANKKATQEAFMKRA 339
Cdd:cd00948   240 TVRALRRTVPAAVPGIVFLSGGQSEEEATLNLNAMNKLPLPKPWALSFSYGRALQASALKAWGGKKENVEAAQKALLKRA 319

                         330
                  ....*....|.
gi 1952674377 340 LANCQAAKGQY 350
Cdd:cd00948   320 KANSLAALGKY 330
PTZ00019 PTZ00019
fructose-bisphosphate aldolase; Provisional
 17-371 0e+00

fructose-bisphosphate aldolase; Provisional


Pssm-ID: 240231  Cd Length: 355  Bit Score: 550.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377  17 SEKKKELAEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFREILFTVdNSINQSIGGVILFHETLYQKDS 96
Cdd:PTZ00019    1 TEYAKELAETAKKIAAPGKGILAADESTGTIKKRFDPIGLENTEENRRAYRELLFTT-EGLEQYISGVILFEETVYQKAP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377  97 QGKLFRNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGADFGKWRAVLRID--NQCPSQLAIQEN 174
Cdd:PTZ00019   80 SGKTFVELLKEKGIVPGIKVDKGLVTLPGTDGETSTQGLDGLAERAKKYYKAGARFAKWRAVLKIDpaKGKPSELAIQEN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 175 ANALARYASICQQNGLVPIVEPEVIPDGDHDLEHCQYVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPE 254
Cdd:PTZ00019  160 AWTLARYAAICQENGLVPIVEPEILIDGSHSIEVCQKVTEKVLAEVFKALNDHGVLLEGCLLKPNMVTPGSDCGVKATPQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 255 QVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINLCPLPKPWKLSFSYGRALQASALAAWGGKAANKKATQEA 334
Cdd:PTZ00019  240 EVAFYTVRTLSRTVPPALPGVMFLSGGQSEEEASLNLNAMNKLTLPRPWALSFSYGRALQSSALKTWKGKDENVAAAQKA 319

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1952674377 335 FMKRALANCQAAKGQYvHSGSSGAASTQSLFTACYTY 371
Cdd:PTZ00019  320 LLHRAKANSLAQLGKY-KGGDGGAAASESLYVKDYKY 355
FrucBisAld_I NF033379
fructose-bisphosphate aldolase class I; This family consists of fructose-bisphosphate aldolase ...
 22-347 3.41e-177

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: 495.15  E-value: 3.41e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377  22 ELAEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFREILFTVDNsINQSIGGVILFHETLYQKDSQGKLF 101
Cdd:NF033379    1 ELEETAQAMVAPGKGILAADESTGTINKRFEAIGVESTEENRRAYRELLFTTPG-LGDYISGVILFDETIRQKTADGTPF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 102 RNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGADFGKWRAVLRIDNQCPSQLAIQENANALARY 181
Cdd:NF033379   80 PKVLADAGIIPGIKVDKGAKPLAGFPGEKVTEGLDGLRERLAEYYELGARFAKWRAVITIGDGIPSRACIEANAHALARY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 182 ASICQQNGLVPIVEPEVIPDGDHDLEHCQYVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPEQVAMATV 261
Cdd:NF033379  160 AALCQEAGLVPIVEPEVLMDGDHSIERCAEVTEEVLKEVFEELYRQGVDLEGMILKPNMVLPGKDCPDQASPEEVAEATV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 262 TALHRTVPAAVPGICFLSGGMSEEDATLNLNAINLCPlPKPWKLSFSYGRALQASALAAWGGKAANKKATQEAFMKRALA 341
Cdd:NF033379  240 RCLRRTVPAAVPGIAFLSGGQSDEEATAHLNAMNKLG-PLPWPLTFSYGRALQQPALKAWGGKAENVAAAQKALLHRARM 318


                  ....*.
gi 1952674377 342 NCQAAK 347
Cdd:NF033379  319 NSLAAL 324
PLN02455 PLN02455
fructose-bisphosphate aldolase
 14-371 8.07e-175

fructose-bisphosphate aldolase


Pssm-ID: 178074  Cd Length: 358  Bit Score: 490.42  E-value: 8.07e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377  14 ALTSEKKKELAEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFREILFTVDNSInQSIGGVILFHETLYQ 93
Cdd:PLN02455    3 AFVGKYADELIKNAKYIATPGKGILAADESTGTIGKRLASINVENVESNRQALRELLFTAPGAL-QYLSGVILFEETLYQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377  94 KDSQGKLFRNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGADFGKWRAVLRIDNQCPSQLAIQE 173
Cdd:PLN02455   82 KTSDGKPFVDVLKENGVLPGIKVDKGTVELAGTNGETTTQGLDGLGARCAKYYEAGARFAKWRAVLKIGPTEPSELAIQE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 174 NANALARYASICQQNGLVPIVEPEVIPDGDHDLEHCQYVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHAcTKKYTP 253
Cdd:PLN02455  162 NAQGLARYAIICQENGLVPIVEPEILVDGSHDIKKCAAVTERVLAACYKALNDHHVLLEGTLLKPNMVTPGSD-SPKVSP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 254 EQVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINLCPLPKPWKLSFSYGRALQASALAAWGGKAANKKATQE 333
Cdd:PLN02455  241 EVIAEYTVRALQRTVPPAVPGIVFLSGGQSEEEATLNLNAMNKLKTLKPWTLSFSFGRALQQSTLKAWAGKKENVAKAQA 320

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1952674377 334 AFMKRALANCQAAKGQYVHSGSSGAASTQSLFTACYTY 371
Cdd:PLN02455  321 AFLVRCKANSEATLGKYKGDAAGGEGASESLHVKDYKY 358
FBP_aldolase_I cd00344
Fructose-bisphosphate aldolase class I; Fructose-bisphosphate aldolase class I. Fructose-1, ...
 20-347 3.82e-155

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: 439.62  E-value: 3.82e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377  20 KKELAEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFREILFTVDNSINQSIGGVILFHETLYQKDSQGK 99
Cdd:cd00344     1 KKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPRIGGVILFHETLYQKADDGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 100 LFRNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGADFGKWRAVLRIDNQCPSQLAIQENANALA 179
Cdd:cd00344    81 PFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 180 RYASICQQNGLVPIVEPEVIPDGDHDLEHCQYVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPEQVAMA 259
Cdd:cd00344   161 RYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKFSHEEIAMA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 260 TVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINLCPLPKPWKLSFSYGRALQASALAAWGGKAANKKATQEAFMKRA 339
Cdd:cd00344   241 TVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRA 320


                  ....*...
gi 1952674377 340 LANCQAAK 347
Cdd:cd00344   321 LANSLAAQ 328
PLN02425 PLN02425
probable fructose-bisphosphate aldolase
 3-371 4.45e-130

probable fructose-bisphosphate aldolase


Pssm-ID: 215234  Cd Length: 390  Bit Score: 378.21  E-value: 4.45e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377   3 SGPVTMAHQFPALTSEKKKELAEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFREILFTVDnSINQSIG 82
Cdd:PLN02425   27 SSSSTRRVSFRIRAGSYSDELVQTAKSVASPGRGILAIDESNATCGKRLASIGLDNTETNRQAYRQLLLTTP-GLGEYIS 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377  83 GVILFHETLYQKDSQGKLFRNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGADFGKWRAVLRId 162
Cdd:PLN02425  106 GAILFEETLYQSTTDGKKFVDCLRDQNIVPGIKVDKGLVPLPGSNNESWCQGLDGLASRSAEYYKQGARFAKWRTVVSI- 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 163 nQC-PSQLAIQENANALARYASICQQNGLVPIVEPEVIPDGDHDLEHCQYVTEKVLAAVYKALNDHHVYLEGTLLKPNMV 241
Cdd:PLN02425  185 -PCgPSALAVKEAAWGLARYAAISQDNGLVPIVEPEILLDGDHPIERTLEVAEKVWSEVFFYLAQNNVLFEGILLKPSMV 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 242 TAGHACTKKYTPEQVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINLCplPKPWKLSFSYGRALQASALAAW 321
Cdd:PLN02425  264 TPGAEHKEKASPETIAKYTLTMLRRRVPPAVPGIMFLSGGQSEVEATLNLNAMNQS--PNPWHVSFSYARALQNSVLKTW 341

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1952674377 322 GGKAANKKATQEAFMKRALANCQAAKGQYVHSGSSGAAStQSLFTACYTY 371
Cdd:PLN02425  342 QGRPENVEAAQKALLVRAKANSLAQLGRYSAEGESEEAK-KGMFVKGYTY 390
PLN02227 PLN02227
fructose-bisphosphate aldolase I
 22-371 1.74e-108

fructose-bisphosphate aldolase I


Pssm-ID: 177872  Cd Length: 399  Bit Score: 323.67  E-value: 1.74e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377  22 ELAEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFREILFTVDnSINQSIGGVILFHETLYQKDSQGKLF 101
Cdd:PLN02227   55 ELVKTAKTIASPGHGIMAMDESNATCGKRLASIGLENTEANRQAYRTLLVSAP-GLGQYISGAILFEETLYQSTTDGKKM 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 102 RNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGADFGKWRAVLRIDNQcPSQLAIQENANALARY 181
Cdd:PLN02227  134 VDVLVEQNIVPGIKVDKGLVPLVGSYDESWCQGLDGLASRTAAYYQQGARFAKWRTVVSIPNG-PSALAVKEAAWGLARY 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 182 ASICQQNGLVPIVEPEVIPDGDHDLEHCQYVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPEQVAMATV 261
Cdd:PLN02227  213 AAISQDSGLVPIVEPEIMLDGEHGIDRTYDVAEKVWAEVFFYLAQNNVMFEGILLKPSMVTPGAEATDRATPEQVASYTL 292

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 262 TALHRTVPAAVPGICFLSGGMSEEDATLNLNAINLCplPKPWKLSFSYGRALQASALAAWGGKAANKKATQEAFMKRALA 341
Cdd:PLN02227  293 KLLRNRIPPAVPGIMFLSGGQSELEATLNLNAMNQA--PNPWHVSFSYARALQNTCLKTWGGKEENVKAAQDILLARAKA 370

                         330       340       350
                  ....*....|....*....|....*....|
gi 1952674377 342 NCQAAKGQYVHSGSSGAAStQSLFTACYTY 371
Cdd:PLN02227  371 NSLAQLGKYTGEGESEEAK-EGMFVKGYTY 399
Fba1 COG3588
Fructose-bisphosphate aldolase class 1 [Carbohydrate transport and metabolism]; ...
 20-350 8.80e-108

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: 317.83  E-value: 8.80e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377  20 KKELAEIAQRIVANGKGILAA-DESVGTMGNRLQRIKVENTEENRR--------QFREILFTVDNSINQSIGGVILFHET 90
Cdd:COG3588     2 TEELNATALAMVANGKGFLAAlDQSGGSTPKALAAYGVEETEYSRReemfdlvhAMRERIITSPAFTGDKISGAILFEET 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377  91 LYQKdSQGK-LFRNILKEKGIVVGIKLDQGGAPLAgtNKETTIQGLDGLSERCAQYKKDGADFGKWRAVLRIDNQcpsqL 169
Cdd:COG3588    82 MDQK-IDGTpTFDYLWEKKGIVPGIKVDKGLKDLA--PGVQLMKGLDGLDERLARAKELGAFGTKWRSVIKIANA----A 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 170 AIQENANALARYASICQQNGLVPIVEPEVIPDGDHDLEHCQYVTEKVLAAVYKALNDHhvylEGTLLKpnMVTAGHACTK 249
Cdd:COG3588   155 GIKANVHQQARYAALCQEAGLVPIVEPEVLIDGDHKIEREAELTEEILKALFDALPED----EGVMLK--MVIPGKDNLY 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377 250 KYTPEQvamatvtalhrtvpAAVPGICFLSGGMSEEDATLNLNAINlcplpkpwKLSFSYGRALQASALAAWGGKAANKK 329
Cdd:COG3588   229 QALVEH--------------PAVPRVVFLSGGQSREEATAHLNANN--------GLIASFSRALQEGLLAAWSGEEFNAA 286

                         330       340
                  ....*....|....*....|.
gi 1952674377 330 ATqeafmkralancQAAKGQY 350
Cdd:COG3588   287 LA------------QAIDGIY 295
FBP_aldolase_I_bact cd00949
Fructose-1.6-bisphosphate aldolase found in gram +/- bacteria; Fructose-1.6-bisphosphate ...
 25-198 3.44e-08

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: 54.34  E-value: 3.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377  25 EIAQRIvANGKGILAA-DESVGTMGNRLQRIKVE----NTEENR----RQFREILFTVDNSINQSIGGVILFHETLYQKd 95
Cdd:cd00949     2 EQLERM-KSGKGFIAAlDQSGGSTPKALAAYGIEedaySNEEEMfdlvHEMRTRIITSPAFDGDKILGAILFEQTMDRE- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377  96 SQGKLFRNIL-KEKGIVVGIKLDQGGAPLA-GTNKETTIQGLDGLSERCAQYKKdgadFG-KWRAVLRIDNQCPSQLAIQ 172
Cdd:cd00949    80 IEGKPTADYLwEKKQIVPFLKVDKGLAEEKnGVQLMKPIPNLDELLMRAKEKGV----FGtKMRSVIKEANPKGIAAVVD 155

                         170       180
                  ....*....|....*....|....*.
gi 1952674377 173 ENANalarYASICQQNGLVPIVEPEV 198
Cdd:cd00949   156 QQFE----LAKQILSHGLVPIIEPEV 177
PRK05377 PRK05377
fructose-1,6-bisphosphate aldolase; Reviewed
 81-198 6.68e-05

fructose-1,6-bisphosphate aldolase; Reviewed


Pssm-ID: 180045  Cd Length: 296  Bit Score: 44.09  E-value: 6.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952674377  81 IGGVILFHETLYQKdSQGKLFRNIL-KEKGIVVGIKLDQGGAPLA-GTNKETTIQGLDGLSERCAQYKKdgadFG-KWRA 157
Cdd:PRK05377   69 ILGAILFEQTMDRE-IEGKPTADYLwEKKGVVPFLKVDKGLAEEAnGVQLMKPIPNLDDLLDRAVEKGI----FGtKMRS 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1952674377 158 VlridnqcpsqlaIQEnANALARYASICQQ---------NGLVPIVEPEV 198
Cdd:PRK05377  144 V------------IKE-ANEQGIAAVVAQQfevakqilaAGLVPIIEPEV 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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