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Conserved domains on  [gi|1034111862|ref|XP_016783982|]
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fructose-bisphosphate aldolase A isoform X2 [Pan troglodytes]

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;
15-364 0e+00

Fructose-bisphosphate aldolase class-I;


:

Pssm-ID: 459742  Cd Length: 349  Bit Score: 770.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  15 ELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPF 94
Cdd:pfam00274   1 ELIATAKAIVAPGKGILAADESTGTIGKRLASIGVENTEENRRAYRQLLFTTDGELGEYISGVILFHETLYQKTDDGKPF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  95 PQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARY 174
Cdd:pfam00274  81 VDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQGLDGLAERCAQYYKDGARFAKWRCVLKIGENTPSELAIQENANVLARY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 175 ASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKFSHEEIAMATV 254
Cdd:pfam00274 161 ASICQQNGLVPIVEPEILPDGDHDLERCQKVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTPGADCPKKYTPEEIAEATV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 255 TALRRTVPPAVTGITFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALA 334
Cdd:pfam00274 241 TALRRTVPPAVPGVTFLSGGQSEEEATVNLNAINKLPLKKPWALTFSYGRALQASVLKAWGGKKENVKAAQEELLKRAKA 320

                         330       340       350
                  ....*....|....*....|....*....|
gi 1034111862 335 NSLACQGKYTPSGqAGAAASESLFVSNHAY 364
Cdd:pfam00274 321 NSLASLGKYVGGV-EGAAASESLFVANYAY 349
 
Name Accession Description Interval E-value
Glycolytic pfam00274
Fructose-bisphosphate aldolase class-I;
15-364 0e+00

Fructose-bisphosphate aldolase class-I;


Pssm-ID: 459742  Cd Length: 349  Bit Score: 770.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  15 ELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPF 94
Cdd:pfam00274   1 ELIATAKAIVAPGKGILAADESTGTIGKRLASIGVENTEENRRAYRQLLFTTDGELGEYISGVILFHETLYQKTDDGKPF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  95 PQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARY 174
Cdd:pfam00274  81 VDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQGLDGLAERCAQYYKDGARFAKWRCVLKIGENTPSELAIQENANVLARY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 175 ASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKFSHEEIAMATV 254
Cdd:pfam00274 161 ASICQQNGLVPIVEPEILPDGDHDLERCQKVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTPGADCPKKYTPEEIAEATV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 255 TALRRTVPPAVTGITFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALA 334
Cdd:pfam00274 241 TALRRTVPPAVPGVTFLSGGQSEEEATVNLNAINKLPLKKPWALTFSYGRALQASVLKAWGGKKENVKAAQEELLKRAKA 320

                         330       340       350
                  ....*....|....*....|....*....|
gi 1034111862 335 NSLACQGKYTPSGqAGAAASESLFVSNHAY 364
Cdd:pfam00274 321 NSLASLGKYVGGV-EGAAASESLFVANYAY 349
FBP_aldolase_I_a cd00948
Fructose-1,6-bisphosphate aldolase; Fructose-1,6-bisphosphate aldolase. The enzyme catalyzes ...
 13-343 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: 670.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  13 KKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRvNPCIGGVILFHETLYQKADDGR 92
Cdd:cd00948     1 KEELIKTAKAIVAPGKGILAADESTGTIGKRFASIGVENTEENRRAYRELLFTTPGL-GQYISGVILFEETLYQKTDDGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  93 PFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLA 172
Cdd:cd00948    80 PFVDILKEKGIVPGIKVDKGLVPLAGTDGETTTQGLDGLAERCAKYYKQGARFAKWRAVLKIGNGTPSELAIKENAHGLA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 173 RYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKFSHEEIAMA 252
Cdd:cd00948   160 RYAAICQENGLVPIVEPEVLMDGDHDIERCQEVTEKVLAAVYKALNDHHVLLEGTLLKPNMVTPGADCKKKASPEEVAEY 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 253 TVTALRRTVPPAVTGITFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRA 332
Cdd:cd00948   240 TVRALRRTVPAAVPGIVFLSGGQSEEEATLNLNAMNKLPLPKPWALSFSYGRALQASALKAWGGKKENVEAAQKALLKRA 319

                         330
                  ....*....|.
gi 1034111862 333 LANSLACQGKY 343
Cdd:cd00948   320 KANSLAALGKY 330
PTZ00019 PTZ00019
fructose-bisphosphate aldolase; Provisional
 10-364 0e+00

fructose-bisphosphate aldolase; Provisional


Pssm-ID: 240231  Cd Length: 355  Bit Score: 562.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  10 PEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDrVNPCIGGVILFHETLYQKAD 89
Cdd:PTZ00019    1 TEYAKELAETAKKIAAPGKGILAADESTGTIKKRFDPIGLENTEENRRAYRELLFTTEG-LEQYISGVILFEETVYQKAP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  90 DGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEH--TPSALAIMEN 167
Cdd:PTZ00019   80 SGKTFVELLKEKGIVPGIKVDKGLVTLPGTDGETSTQGLDGLAERAKKYYKAGARFAKWRAVLKIDPAkgKPSELAIQEN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 168 ANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKFSHE 247
Cdd:PTZ00019  160 AWTLARYAAICQENGLVPIVEPEILIDGSHSIEVCQKVTEKVLAEVFKALNDHGVLLEGCLLKPNMVTPGSDCGVKATPQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 248 EIAMATVTALRRTVPPAVTGITFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEE 327
Cdd:PTZ00019  240 EVAFYTVRTLSRTVPPALPGVMFLSGGQSEEEASLNLNAMNKLTLPRPWALSFSYGRALQSSALKTWKGKDENVAAAQKA 319

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1034111862 328 YVKRALANSLACQGKYTpSGQAGAAASESLFVSNHAY 364
Cdd:PTZ00019  320 LLHRAKANSLAQLGKYK-GGDGGAAASESLYVKDYKY 355
FrucBisAld_I NF033379
fructose-bisphosphate aldolase class I; This family consists of fructose-bisphosphate aldolase ...
 15-340 0e+00

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: 523.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  15 ELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDrVNPCIGGVILFHETLYQKADDGRPF 94
Cdd:NF033379    1 ELEETAQAMVAPGKGILAADESTGTINKRFEAIGVESTEENRRAYRELLFTTPG-LGDYISGVILFDETIRQKTADGTPF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  95 PQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARY 174
Cdd:NF033379   80 PKVLADAGIIPGIKVDKGAKPLAGFPGEKVTEGLDGLRERLAEYYELGARFAKWRAVITIGDGIPSRACIEANAHALARY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 175 ASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKFSHEEIAMATV 254
Cdd:NF033379  160 AALCQEAGLVPIVEPEVLMDGDHSIERCAEVTEEVLKEVFEELYRQGVDLEGMILKPNMVLPGKDCPDQASPEEVAEATV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 255 TALRRTVPPAVTGITFLSGGQSEEEASINLNAINKCPLLkPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALA 334
Cdd:NF033379  240 RCLRRTVPAAVPGIAFLSGGQSDEEATAHLNAMNKLGPL-PWPLTFSYGRALQQPALKAWGGKAENVAAAQKALLHRARM 318


                  ....*.
gi 1034111862 335 NSLACQ 340
Cdd:NF033379  319 NSLAAL 324
Fba1 COG3588
Fructose-bisphosphate aldolase class 1 [Carbohydrate transport and metabolism]; ...
 13-346 5.46e-120

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: 348.64  E-value: 5.46e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  13 KKELSDIAHRIVAPGKGILAA-DESTGSIAKRLQSIGTENTEENRRF--------YRQLLLTADDRVNPCIGGVILFHET 83
Cdd:COG3588     2 TEELNATALAMVANGKGFLAAlDQSGGSTPKALAAYGVEETEYSRREemfdlvhaMRERIITSPAFTGDKISGAILFEET 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  84 LYQKADdGRP-FPQVIKSKGGVVGIKVDKGVVPLAgtNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTpsal 162
Cdd:COG3588    82 MDQKID-GTPtFDYLWEKKGIVPGIKVDKGLKDLA--PGVQLMKGLDGLDERLARAKELGAFGTKWRSVIKIANAA---- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 163 AIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHhiylEGTLLKpnMVTPGHACTQ 242
Cdd:COG3588   155 GIKANVHQQARYAALCQEAGLVPIVEPEVLIDGDHKIEREAELTEEILKALFDALPED----EGVMLK--MVIPGKDNLY 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 243 KFSHEEiamatvtalrrtvpPAVTGITFLSGGQSEEEASINLNAINKcpllkpwaLTFSYGRALQASALKAWGGKKENLK 322
Cdd:COG3588   229 QALVEH--------------PAVPRVVFLSGGQSREEATAHLNANNG--------LIASFSRALQEGLLAAWSGEEFNAA 286

                         330       340
                  ....*....|....*....|....
gi 1034111862 323 AAQeeyvkralanslACQGKYTPS 346
Cdd:COG3588   287 LAQ------------AIDGIYDAS 298
 
Name Accession Description Interval E-value
Glycolytic pfam00274
Fructose-bisphosphate aldolase class-I;
15-364 0e+00

Fructose-bisphosphate aldolase class-I;


Pssm-ID: 459742  Cd Length: 349  Bit Score: 770.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  15 ELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPF 94
Cdd:pfam00274   1 ELIATAKAIVAPGKGILAADESTGTIGKRLASIGVENTEENRRAYRQLLFTTDGELGEYISGVILFHETLYQKTDDGKPF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  95 PQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARY 174
Cdd:pfam00274  81 VDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQGLDGLAERCAQYYKDGARFAKWRCVLKIGENTPSELAIQENANVLARY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 175 ASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKFSHEEIAMATV 254
Cdd:pfam00274 161 ASICQQNGLVPIVEPEILPDGDHDLERCQKVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTPGADCPKKYTPEEIAEATV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 255 TALRRTVPPAVTGITFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALA 334
Cdd:pfam00274 241 TALRRTVPPAVPGVTFLSGGQSEEEATVNLNAINKLPLKKPWALTFSYGRALQASVLKAWGGKKENVKAAQEELLKRAKA 320

                         330       340       350
                  ....*....|....*....|....*....|
gi 1034111862 335 NSLACQGKYTPSGqAGAAASESLFVSNHAY 364
Cdd:pfam00274 321 NSLASLGKYVGGV-EGAAASESLFVANYAY 349
FBP_aldolase_I_a cd00948
Fructose-1,6-bisphosphate aldolase; Fructose-1,6-bisphosphate aldolase. The enzyme catalyzes ...
 13-343 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: 670.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  13 KKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRvNPCIGGVILFHETLYQKADDGR 92
Cdd:cd00948     1 KEELIKTAKAIVAPGKGILAADESTGTIGKRFASIGVENTEENRRAYRELLFTTPGL-GQYISGVILFEETLYQKTDDGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  93 PFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLA 172
Cdd:cd00948    80 PFVDILKEKGIVPGIKVDKGLVPLAGTDGETTTQGLDGLAERCAKYYKQGARFAKWRAVLKIGNGTPSELAIKENAHGLA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 173 RYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKFSHEEIAMA 252
Cdd:cd00948   160 RYAAICQENGLVPIVEPEVLMDGDHDIERCQEVTEKVLAAVYKALNDHHVLLEGTLLKPNMVTPGADCKKKASPEEVAEY 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 253 TVTALRRTVPPAVTGITFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRA 332
Cdd:cd00948   240 TVRALRRTVPAAVPGIVFLSGGQSEEEATLNLNAMNKLPLPKPWALSFSYGRALQASALKAWGGKKENVEAAQKALLKRA 319

                         330
                  ....*....|.
gi 1034111862 333 LANSLACQGKY 343
Cdd:cd00948   320 KANSLAALGKY 330
FBP_aldolase_I cd00344
Fructose-bisphosphate aldolase class I; Fructose-bisphosphate aldolase class I. Fructose-1, ...
 13-340 0e+00

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: 594.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  13 KKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGR 92
Cdd:cd00344     1 KKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPRIGGVILFHETLYQKADDGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  93 PFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLA 172
Cdd:cd00344    81 PFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 173 RYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKFSHEEIAMA 252
Cdd:cd00344   161 RYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKFSHEEIAMA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 253 TVTALRRTVPPAVTGITFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRA 332
Cdd:cd00344   241 TVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRA 320


                  ....*...
gi 1034111862 333 LANSLACQ 340
Cdd:cd00344   321 LANSLAAQ 328
PTZ00019 PTZ00019
fructose-bisphosphate aldolase; Provisional
 10-364 0e+00

fructose-bisphosphate aldolase; Provisional


Pssm-ID: 240231  Cd Length: 355  Bit Score: 562.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  10 PEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDrVNPCIGGVILFHETLYQKAD 89
Cdd:PTZ00019    1 TEYAKELAETAKKIAAPGKGILAADESTGTIKKRFDPIGLENTEENRRAYRELLFTTEG-LEQYISGVILFEETVYQKAP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  90 DGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEH--TPSALAIMEN 167
Cdd:PTZ00019   80 SGKTFVELLKEKGIVPGIKVDKGLVTLPGTDGETSTQGLDGLAERAKKYYKAGARFAKWRAVLKIDPAkgKPSELAIQEN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 168 ANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKFSHE 247
Cdd:PTZ00019  160 AWTLARYAAICQENGLVPIVEPEILIDGSHSIEVCQKVTEKVLAEVFKALNDHGVLLEGCLLKPNMVTPGSDCGVKATPQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 248 EIAMATVTALRRTVPPAVTGITFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEE 327
Cdd:PTZ00019  240 EVAFYTVRTLSRTVPPALPGVMFLSGGQSEEEASLNLNAMNKLTLPRPWALSFSYGRALQSSALKTWKGKDENVAAAQKA 319

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1034111862 328 YVKRALANSLACQGKYTpSGQAGAAASESLFVSNHAY 364
Cdd:PTZ00019  320 LLHRAKANSLAQLGKYK-GGDGGAAASESLYVKDYKY 355
PLN02455 PLN02455
fructose-bisphosphate aldolase
 13-364 0e+00

fructose-bisphosphate aldolase


Pssm-ID: 178074  Cd Length: 358  Bit Score: 527.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  13 KKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDrVNPCIGGVILFHETLYQKADDGR 92
Cdd:PLN02455    9 ADELIKNAKYIATPGKGILAADESTGTIGKRLASINVENVESNRQALRELLFTAPG-ALQYLSGVILFEETLYQKTSDGK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  93 PFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLA 172
Cdd:PLN02455   88 PFVDVLKENGVLPGIKVDKGTVELAGTNGETTTQGLDGLGARCAKYYEAGARFAKWRAVLKIGPTEPSELAIQENAQGLA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 173 RYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHAcTQKFSHEEIAMA 252
Cdd:PLN02455  168 RYAIICQENGLVPIVEPEILVDGSHDIKKCAAVTERVLAACYKALNDHHVLLEGTLLKPNMVTPGSD-SPKVSPEVIAEY 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 253 TVTALRRTVPPAVTGITFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRA 332
Cdd:PLN02455  247 TVRALQRTVPPAVPGIVFLSGGQSEEEATLNLNAMNKLKTLKPWTLSFSFGRALQQSTLKAWAGKKENVAKAQAAFLVRC 326

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1034111862 333 LANSLACQGKYTPSGQAGAAASESLFVSNHAY 364
Cdd:PLN02455  327 KANSEATLGKYKGDAAGGEGASESLHVKDYKY 358
FrucBisAld_I NF033379
fructose-bisphosphate aldolase class I; This family consists of fructose-bisphosphate aldolase ...
 15-340 0e+00

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: 523.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  15 ELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDrVNPCIGGVILFHETLYQKADDGRPF 94
Cdd:NF033379    1 ELEETAQAMVAPGKGILAADESTGTINKRFEAIGVESTEENRRAYRELLFTTPG-LGDYISGVILFDETIRQKTADGTPF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  95 PQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARY 174
Cdd:NF033379   80 PKVLADAGIIPGIKVDKGAKPLAGFPGEKVTEGLDGLRERLAEYYELGARFAKWRAVITIGDGIPSRACIEANAHALARY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 175 ASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKFSHEEIAMATV 254
Cdd:NF033379  160 AALCQEAGLVPIVEPEVLMDGDHSIERCAEVTEEVLKEVFEELYRQGVDLEGMILKPNMVLPGKDCPDQASPEEVAEATV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 255 TALRRTVPPAVTGITFLSGGQSEEEASINLNAINKCPLLkPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALA 334
Cdd:NF033379  240 RCLRRTVPAAVPGIAFLSGGQSDEEATAHLNAMNKLGPL-PWPLTFSYGRALQQPALKAWGGKAENVAAAQKALLHRARM 318


                  ....*.
gi 1034111862 335 NSLACQ 340
Cdd:NF033379  319 NSLAAL 324
PLN02425 PLN02425
probable fructose-bisphosphate aldolase
 5-364 2.87e-140

probable fructose-bisphosphate aldolase


Pssm-ID: 215234  Cd Length: 390  Bit Score: 403.63  E-value: 2.87e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862   5 YPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDrVNPCIGGVILFHETL 84
Cdd:PLN02425   36 FRIRAGSYSDELVQTAKSVASPGRGILAIDESNATCGKRLASIGLDNTETNRQAYRQLLLTTPG-LGEYISGAILFEETL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  85 YQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIgEHTPSALAI 164
Cdd:PLN02425  115 YQSTTDGKKFVDCLRDQNIVPGIKVDKGLVPLPGSNNESWCQGLDGLASRSAEYYKQGARFAKWRTVVSI-PCGPSALAV 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 165 MENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKF 244
Cdd:PLN02425  194 KEAAWGLARYAAISQDNGLVPIVEPEILLDGDHPIERTLEVAEKVWSEVFFYLAQNNVLFEGILLKPSMVTPGAEHKEKA 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 245 SHEEIAMATVTALRRTVPPAVTGITFLSGGQSEEEASINLNAINKCPllKPWALTFSYGRALQASALKAWGGKKENLKAA 324
Cdd:PLN02425  274 SPETIAKYTLTMLRRRVPPAVPGIMFLSGGQSEVEATLNLNAMNQSP--NPWHVSFSYARALQNSVLKTWQGRPENVEAA 351

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1034111862 325 QEEYVKRALANSLACQGKYTPSGQAgAAASESLFVSNHAY 364
Cdd:PLN02425  352 QKALLVRAKANSLAQLGRYSAEGES-EEAKKGMFVKGYTY 390
Fba1 COG3588
Fructose-bisphosphate aldolase class 1 [Carbohydrate transport and metabolism]; ...
 13-346 5.46e-120

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: 348.64  E-value: 5.46e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  13 KKELSDIAHRIVAPGKGILAA-DESTGSIAKRLQSIGTENTEENRRF--------YRQLLLTADDRVNPCIGGVILFHET 83
Cdd:COG3588     2 TEELNATALAMVANGKGFLAAlDQSGGSTPKALAAYGVEETEYSRREemfdlvhaMRERIITSPAFTGDKISGAILFEET 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  84 LYQKADdGRP-FPQVIKSKGGVVGIKVDKGVVPLAgtNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTpsal 162
Cdd:COG3588    82 MDQKID-GTPtFDYLWEKKGIVPGIKVDKGLKDLA--PGVQLMKGLDGLDERLARAKELGAFGTKWRSVIKIANAA---- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 163 AIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHhiylEGTLLKpnMVTPGHACTQ 242
Cdd:COG3588   155 GIKANVHQQARYAALCQEAGLVPIVEPEVLIDGDHKIEREAELTEEILKALFDALPED----EGVMLK--MVIPGKDNLY 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 243 KFSHEEiamatvtalrrtvpPAVTGITFLSGGQSEEEASINLNAINKcpllkpwaLTFSYGRALQASALKAWGGKKENLK 322
Cdd:COG3588   229 QALVEH--------------PAVPRVVFLSGGQSREEATAHLNANNG--------LIASFSRALQEGLLAAWSGEEFNAA 286

                         330       340
                  ....*....|....*....|....
gi 1034111862 323 AAQeeyvkralanslACQGKYTPS 346
Cdd:COG3588   287 LAQ------------AIDGIYDAS 298
PLN02227 PLN02227
fructose-bisphosphate aldolase I
 15-364 1.01e-116

fructose-bisphosphate aldolase I


Pssm-ID: 177872  Cd Length: 399  Bit Score: 344.09  E-value: 1.01e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  15 ELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDrVNPCIGGVILFHETLYQKADDGRPF 94
Cdd:PLN02227   55 ELVKTAKTIASPGHGIMAMDESNATCGKRLASIGLENTEANRQAYRTLLVSAPG-LGQYISGAILFEETLYQSTTDGKKM 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  95 PQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIgEHTPSALAIMENANVLARY 174
Cdd:PLN02227  134 VDVLVEQNIVPGIKVDKGLVPLVGSYDESWCQGLDGLASRTAAYYQQGARFAKWRTVVSI-PNGPSALAVKEAAWGLARY 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 175 ASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKFSHEEIAMATV 254
Cdd:PLN02227  213 AAISQDSGLVPIVEPEIMLDGEHGIDRTYDVAEKVWAEVFFYLAQNNVMFEGILLKPSMVTPGAEATDRATPEQVASYTL 292

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862 255 TALRRTVPPAVTGITFLSGGQSEEEASINLNAINKCPllKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALA 334
Cdd:PLN02227  293 KLLRNRIPPAVPGIMFLSGGQSELEATLNLNAMNQAP--NPWHVSFSYARALQNTCLKTWGGKEENVKAAQDILLARAKA 370

                         330       340       350
                  ....*....|....*....|....*....|
gi 1034111862 335 NSLACQGKYTPSGQAgAAASESLFVSNHAY 364
Cdd:PLN02227  371 NSLAQLGKYTGEGES-EEAKEGMFVKGYTY 399
FBP_aldolase_I_bact cd00949
Fructose-1.6-bisphosphate aldolase found in gram +/- bacteria; Fructose-1.6-bisphosphate ...
 27-191 3.24e-10

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: 60.50  E-value: 3.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  27 GKGILAA-DESTGSIAKRLQSIGTENT---EENRRF-----YRQLLLTADDRVNPCIGGVILFHETLYQKADdGRPFPQV 97
Cdd:cd00949    10 GKGFIAAlDQSGGSTPKALAAYGIEEDaysNEEEMFdlvheMRTRIITSPAFDGDKILGAILFEQTMDREIE-GKPTADY 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  98 IKSKGGVVGI-KVDKGVVPLAgtNGETTTQGLDGLSERCAQYKKDGADFAKWRCVlkIGEHTPSALAImenanVLARYAS 176
Cdd:cd00949    89 LWEKKQIVPFlKVDKGLAEEK--NGVQLMKPIPNLDELLMRAKEKGVFGTKMRSV--IKEANPKGIAA-----VVDQQFE 159

                         170
                  ....*....|....*...
gi 1034111862 177 ICQQ---NGIVPIVEPEI 191
Cdd:cd00949   160 LAKQilsHGLVPIIEPEV 177
PRK05377 PRK05377
fructose-1,6-bisphosphate aldolase; Reviewed
 24-191 4.85e-08

fructose-1,6-bisphosphate aldolase; Reviewed


Pssm-ID: 180045  Cd Length: 296  Bit Score: 53.72  E-value: 4.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  24 VAPGKGILAA-DESTGSIAKRLQSIGTENTE---ENRRF-----YRQLLLTADDRVNPCIGGVILFHETLYQKADdGRPF 94
Cdd:PRK05377   10 MKNGKGFIAAlDQSGGSTPKALKLYGVEEDAysnEEEMFdlvheMRTRIITSPAFTGDKILGAILFEQTMDREIE-GKPT 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034111862  95 PQVIKSKGGVVG-IKVDKGVVPLAgtNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKigehTPSALAImenANVLAR 173
Cdd:PRK05377   89 ADYLWEKKGVVPfLKVDKGLAEEA--NGVQLMKPIPNLDDLLDRAVEKGIFGTKMRSVIK----EANEQGI---AAVVAQ 159

                         170       180
                  ....*....|....*....|.
gi 1034111862 174 YASICQQ---NGIVPIVEPEI 191
Cdd:PRK05377  160 QFEVAKQilaAGLVPIIEPEV 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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