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Conserved domains on  [gi|312922382|ref|NP_001186199|]
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aldolase 1 A retrogene 1 [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;
70-419 0e+00

Fructose-bisphosphate aldolase class-I;


:

Pssm-ID: 459742  Cd Length: 349  Bit Score: 764.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382   70 ELSDIAHRIVAPGKGILAADESIGSMGNRLQSIGTENTEENRRFFRQLLLTADDRVNPCIGGVILFHETLYEKADDGRPF 149
Cdd:pfam00274   1 ELIATAKAIVAPGKGILAADESTGTIGKRLASIGVENTEENRRAYRQLLFTTDGELGEYISGVILFHETLYQKTDDGKPF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382  150 PQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGKHTPSPLAIMENANVLARY 229
Cdd:pfam00274  81 VDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQGLDGLAERCAQYYKDGARFAKWRCVLKIGENTPSELAIQENANVLARY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382  230 ASICQQNGIVPIVEPEILPDGDHDLSCCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACTQKFSNEEIAMATV 309
Cdd:pfam00274 161 ASICQQNGLVPIVEPEILPDGDHDLERCQKVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTPGADCPKKYTPEEIAEATV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382  310 TALRRTVPPAVPGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKEENLKAAQEEYIKRALA 389
Cdd:pfam00274 241 TALRRTVPPAVPGVTFLSGGQSEEEATVNLNAINKLPLKKPWALTFSYGRALQASVLKAWGGKKENVKAAQEELLKRAKA 320
                         330       340       350
                  ....*....|....*....|....*....|
gi 312922382  390 NSLACQGKYTPSGKTGAtASESLFISNHAY 419
Cdd:pfam00274 321 NSLASLGKYVGGVEGAA-ASESLFVANYAY 349
 
Name Accession Description Interval E-value
Glycolytic pfam00274
Fructose-bisphosphate aldolase class-I;
70-419 0e+00

Fructose-bisphosphate aldolase class-I;


Pssm-ID: 459742  Cd Length: 349  Bit Score: 764.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382   70 ELSDIAHRIVAPGKGILAADESIGSMGNRLQSIGTENTEENRRFFRQLLLTADDRVNPCIGGVILFHETLYEKADDGRPF 149
Cdd:pfam00274   1 ELIATAKAIVAPGKGILAADESTGTIGKRLASIGVENTEENRRAYRQLLFTTDGELGEYISGVILFHETLYQKTDDGKPF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382  150 PQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGKHTPSPLAIMENANVLARY 229
Cdd:pfam00274  81 VDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQGLDGLAERCAQYYKDGARFAKWRCVLKIGENTPSELAIQENANVLARY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382  230 ASICQQNGIVPIVEPEILPDGDHDLSCCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACTQKFSNEEIAMATV 309
Cdd:pfam00274 161 ASICQQNGLVPIVEPEILPDGDHDLERCQKVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTPGADCPKKYTPEEIAEATV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382  310 TALRRTVPPAVPGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKEENLKAAQEEYIKRALA 389
Cdd:pfam00274 241 TALRRTVPPAVPGVTFLSGGQSEEEATVNLNAINKLPLKKPWALTFSYGRALQASVLKAWGGKKENVKAAQEELLKRAKA 320
                         330       340       350
                  ....*....|....*....|....*....|
gi 312922382  390 NSLACQGKYTPSGKTGAtASESLFISNHAY 419
Cdd:pfam00274 321 NSLASLGKYVGGVEGAA-ASESLFVANYAY 349
FBP_aldolase_I_a cd00948
Fructose-1,6-bisphosphate aldolase; Fructose-1,6-bisphosphate aldolase. The enzyme catalyzes ...
68-398 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: 665.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382  68 KKELSDIAHRIVAPGKGILAADESIGSMGNRLQSIGTENTEENRRFFRQLLLTADDRvNPCIGGVILFHETLYEKADDGR 147
Cdd:cd00948    1 KEELIKTAKAIVAPGKGILAADESTGTIGKRFASIGVENTEENRRAYRELLFTTPGL-GQYISGVILFEETLYQKTDDGK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 148 PFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGKHTPSPLAIMENANVLA 227
Cdd:cd00948   80 PFVDILKEKGIVPGIKVDKGLVPLAGTDGETTTQGLDGLAERCAKYYKQGARFAKWRAVLKIGNGTPSELAIKENAHGLA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 228 RYASICQQNGIVPIVEPEILPDGDHDLSCCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACTQKFSNEEIAMA 307
Cdd:cd00948  160 RYAAICQENGLVPIVEPEVLMDGDHDIERCQEVTEKVLAAVYKALNDHHVLLEGTLLKPNMVTPGADCKKKASPEEVAEY 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 308 TVTALRRTVPPAVPGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKEENLKAAQEEYIKRA 387
Cdd:cd00948  240 TVRALRRTVPAAVPGIVFLSGGQSEEEATLNLNAMNKLPLPKPWALSFSYGRALQASALKAWGGKKENVEAAQKALLKRA 319
                        330
                 ....*....|.
gi 312922382 388 LANSLACQGKY 398
Cdd:cd00948  320 KANSLAALGKY 330
PTZ00019 PTZ00019
fructose-bisphosphate aldolase; Provisional
65-419 0e+00

fructose-bisphosphate aldolase; Provisional


Pssm-ID: 240231  Cd Length: 355  Bit Score: 561.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382  65 TEQKKELSDIAHRIVAPGKGILAADESIGSMGNRLQSIGTENTEENRRFFRQLLLTADDrVNPCIGGVILFHETLYEKAD 144
Cdd:PTZ00019   1 TEYAKELAETAKKIAAPGKGILAADESTGTIKKRFDPIGLENTEENRRAYRELLFTTEG-LEQYISGVILFEETVYQKAP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 145 DGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIG--KHTPSPLAIMEN 222
Cdd:PTZ00019  80 SGKTFVELLKEKGIVPGIKVDKGLVTLPGTDGETSTQGLDGLAERAKKYYKAGARFAKWRAVLKIDpaKGKPSELAIQEN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 223 ANVLARYASICQQNGIVPIVEPEILPDGDHDLSCCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACTQKFSNE 302
Cdd:PTZ00019 160 AWTLARYAAICQENGLVPIVEPEILIDGSHSIEVCQKVTEKVLAEVFKALNDHGVLLEGCLLKPNMVTPGSDCGVKATPQ 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 303 EIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKEENLKAAQEE 382
Cdd:PTZ00019 240 EVAFYTVRTLSRTVPPALPGVMFLSGGQSEEEASLNLNAMNKLTLPRPWALSFSYGRALQSSALKTWKGKDENVAAAQKA 319
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 312922382 383 YIKRALANSLACQGKYTpSGKTGATASESLFISNHAY 419
Cdd:PTZ00019 320 LLHRAKANSLAQLGKYK-GGDGGAAASESLYVKDYKY 355
FrucBisAld_I NF033379
fructose-bisphosphate aldolase class I; This family consists of fructose-bisphosphate aldolase ...
70-395 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: 519.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382  70 ELSDIAHRIVAPGKGILAADESIGSMGNRLQSIGTENTEENRRFFRQLLLTADDrVNPCIGGVILFHETLYEKADDGRPF 149
Cdd:NF033379   1 ELEETAQAMVAPGKGILAADESTGTINKRFEAIGVESTEENRRAYRELLFTTPG-LGDYISGVILFDETIRQKTADGTPF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 150 PQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGKHTPSPLAIMENANVLARY 229
Cdd:NF033379  80 PKVLADAGIIPGIKVDKGAKPLAGFPGEKVTEGLDGLRERLAEYYELGARFAKWRAVITIGDGIPSRACIEANAHALARY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 230 ASICQQNGIVPIVEPEILPDGDHDLSCCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACTQKFSNEEIAMATV 309
Cdd:NF033379 160 AALCQEAGLVPIVEPEVLMDGDHSIERCAEVTEEVLKEVFEELYRQGVDLEGMILKPNMVLPGKDCPDQASPEEVAEATV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 310 TALRRTVPPAVPGVTFLSGGQSEEEASINLNAINKCPLLkPWALTFSYGRALQASALKAWGGKEENLKAAQEEYIKRALA 389
Cdd:NF033379 240 RCLRRTVPAAVPGIAFLSGGQSDEEATAHLNAMNKLGPL-PWPLTFSYGRALQQPALKAWGGKAENVAAAQKALLHRARM 318

                 ....*.
gi 312922382 390 NSLACQ 395
Cdd:NF033379 319 NSLAAL 324
Fba1 COG3588
Fructose-bisphosphate aldolase class 1 [Carbohydrate transport and metabolism]; ...
68-401 1.20e-115

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: 339.78  E-value: 1.20e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382  68 KKELSDIAHRIVAPGKGILAA-DESIGSMGNRLQSIGTENTEENRRF--------FRQLLLTADDRVNPCIGGVILFHET 138
Cdd:COG3588    2 TEELNATALAMVANGKGFLAAlDQSGGSTPKALAAYGVEETEYSRREemfdlvhaMRERIITSPAFTGDKISGAILFEET 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 139 LYEKADdGRP-FPQVIKSKGGVVGIKVDKGVVPLAgtNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGkhtpSPL 217
Cdd:COG3588   82 MDQKID-GTPtFDYLWEKKGIVPGIKVDKGLKDLA--PGVQLMKGLDGLDERLARAKELGAFGTKWRSVIKIA----NAA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 218 AIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLSCCQYVTEKVLAAVYKALSDHhvylEGTLLKpnMVTPGHACTQ 297
Cdd:COG3588  155 GIKANVHQQARYAALCQEAGLVPIVEPEVLIDGDHKIEREAELTEEILKALFDALPED----EGVMLK--MVIPGKDNLY 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 298 KFSNEEiamatvtalrrtvpPAVPGVTFLSGGQSEEEASINLNAINKcpllkpwaLTFSYGRALQASALKAWGGKEENLK 377
Cdd:COG3588  229 QALVEH--------------PAVPRVVFLSGGQSREEATAHLNANNG--------LIASFSRALQEGLLAAWSGEEFNAA 286
                        330       340
                 ....*....|....*....|....
gi 312922382 378 AAQeeyikralanslACQGKYTPS 401
Cdd:COG3588  287 LAQ------------AIDGIYDAS 298
 
Name Accession Description Interval E-value
Glycolytic pfam00274
Fructose-bisphosphate aldolase class-I;
70-419 0e+00

Fructose-bisphosphate aldolase class-I;


Pssm-ID: 459742  Cd Length: 349  Bit Score: 764.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382   70 ELSDIAHRIVAPGKGILAADESIGSMGNRLQSIGTENTEENRRFFRQLLLTADDRVNPCIGGVILFHETLYEKADDGRPF 149
Cdd:pfam00274   1 ELIATAKAIVAPGKGILAADESTGTIGKRLASIGVENTEENRRAYRQLLFTTDGELGEYISGVILFHETLYQKTDDGKPF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382  150 PQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGKHTPSPLAIMENANVLARY 229
Cdd:pfam00274  81 VDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQGLDGLAERCAQYYKDGARFAKWRCVLKIGENTPSELAIQENANVLARY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382  230 ASICQQNGIVPIVEPEILPDGDHDLSCCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACTQKFSNEEIAMATV 309
Cdd:pfam00274 161 ASICQQNGLVPIVEPEILPDGDHDLERCQKVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTPGADCPKKYTPEEIAEATV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382  310 TALRRTVPPAVPGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKEENLKAAQEEYIKRALA 389
Cdd:pfam00274 241 TALRRTVPPAVPGVTFLSGGQSEEEATVNLNAINKLPLKKPWALTFSYGRALQASVLKAWGGKKENVKAAQEELLKRAKA 320
                         330       340       350
                  ....*....|....*....|....*....|
gi 312922382  390 NSLACQGKYTPSGKTGAtASESLFISNHAY 419
Cdd:pfam00274 321 NSLASLGKYVGGVEGAA-ASESLFVANYAY 349
FBP_aldolase_I_a cd00948
Fructose-1,6-bisphosphate aldolase; Fructose-1,6-bisphosphate aldolase. The enzyme catalyzes ...
68-398 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: 665.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382  68 KKELSDIAHRIVAPGKGILAADESIGSMGNRLQSIGTENTEENRRFFRQLLLTADDRvNPCIGGVILFHETLYEKADDGR 147
Cdd:cd00948    1 KEELIKTAKAIVAPGKGILAADESTGTIGKRFASIGVENTEENRRAYRELLFTTPGL-GQYISGVILFEETLYQKTDDGK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 148 PFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGKHTPSPLAIMENANVLA 227
Cdd:cd00948   80 PFVDILKEKGIVPGIKVDKGLVPLAGTDGETTTQGLDGLAERCAKYYKQGARFAKWRAVLKIGNGTPSELAIKENAHGLA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 228 RYASICQQNGIVPIVEPEILPDGDHDLSCCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACTQKFSNEEIAMA 307
Cdd:cd00948  160 RYAAICQENGLVPIVEPEVLMDGDHDIERCQEVTEKVLAAVYKALNDHHVLLEGTLLKPNMVTPGADCKKKASPEEVAEY 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 308 TVTALRRTVPPAVPGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKEENLKAAQEEYIKRA 387
Cdd:cd00948  240 TVRALRRTVPAAVPGIVFLSGGQSEEEATLNLNAMNKLPLPKPWALSFSYGRALQASALKAWGGKKENVEAAQKALLKRA 319
                        330
                 ....*....|.
gi 312922382 388 LANSLACQGKY 398
Cdd:cd00948  320 KANSLAALGKY 330
FBP_aldolase_I cd00344
Fructose-bisphosphate aldolase class I; Fructose-bisphosphate aldolase class I. Fructose-1, ...
68-395 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: 572.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382  68 KKELSDIAHRIVAPGKGILAADESIGSMGNRLQSIGTENTEENRRFFRQLLLTADDRVNPCIGGVILFHETLYEKADDGR 147
Cdd:cd00344    1 KKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPRIGGVILFHETLYQKADDGR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 148 PFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGKHTPSPLAIMENANVLA 227
Cdd:cd00344   81 PFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 228 RYASICQQNGIVPIVEPEILPDGDHDLSCCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACTQKFSNEEIAMA 307
Cdd:cd00344  161 RYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKFSHEEIAMA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 308 TVTALRRTVPPAVPGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKEENLKAAQEEYIKRA 387
Cdd:cd00344  241 TVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRA 320

                 ....*...
gi 312922382 388 LANSLACQ 395
Cdd:cd00344  321 LANSLAAQ 328
PTZ00019 PTZ00019
fructose-bisphosphate aldolase; Provisional
65-419 0e+00

fructose-bisphosphate aldolase; Provisional


Pssm-ID: 240231  Cd Length: 355  Bit Score: 561.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382  65 TEQKKELSDIAHRIVAPGKGILAADESIGSMGNRLQSIGTENTEENRRFFRQLLLTADDrVNPCIGGVILFHETLYEKAD 144
Cdd:PTZ00019   1 TEYAKELAETAKKIAAPGKGILAADESTGTIKKRFDPIGLENTEENRRAYRELLFTTEG-LEQYISGVILFEETVYQKAP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 145 DGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIG--KHTPSPLAIMEN 222
Cdd:PTZ00019  80 SGKTFVELLKEKGIVPGIKVDKGLVTLPGTDGETSTQGLDGLAERAKKYYKAGARFAKWRAVLKIDpaKGKPSELAIQEN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 223 ANVLARYASICQQNGIVPIVEPEILPDGDHDLSCCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACTQKFSNE 302
Cdd:PTZ00019 160 AWTLARYAAICQENGLVPIVEPEILIDGSHSIEVCQKVTEKVLAEVFKALNDHGVLLEGCLLKPNMVTPGSDCGVKATPQ 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 303 EIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKEENLKAAQEE 382
Cdd:PTZ00019 240 EVAFYTVRTLSRTVPPALPGVMFLSGGQSEEEASLNLNAMNKLTLPRPWALSFSYGRALQSSALKTWKGKDENVAAAQKA 319
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 312922382 383 YIKRALANSLACQGKYTpSGKTGATASESLFISNHAY 419
Cdd:PTZ00019 320 LLHRAKANSLAQLGKYK-GGDGGAAASESLYVKDYKY 355
PLN02455 PLN02455
fructose-bisphosphate aldolase
62-419 0e+00

fructose-bisphosphate aldolase


Pssm-ID: 178074  Cd Length: 358  Bit Score: 523.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382  62 ALTTEQKKELSDIAHRIVAPGKGILAADESIGSMGNRLQSIGTENTEENRRFFRQLLLTADDrVNPCIGGVILFHETLYE 141
Cdd:PLN02455   3 AFVGKYADELIKNAKYIATPGKGILAADESTGTIGKRLASINVENVESNRQALRELLFTAPG-ALQYLSGVILFEETLYQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 142 KADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGKHTPSPLAIME 221
Cdd:PLN02455  82 KTSDGKPFVDVLKENGVLPGIKVDKGTVELAGTNGETTTQGLDGLGARCAKYYEAGARFAKWRAVLKIGPTEPSELAIQE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 222 NANVLARYASICQQNGIVPIVEPEILPDGDHDLSCCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHAcTQKFSN 301
Cdd:PLN02455 162 NAQGLARYAIICQENGLVPIVEPEILVDGSHDIKKCAAVTERVLAACYKALNDHHVLLEGTLLKPNMVTPGSD-SPKVSP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 302 EEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKEENLKAAQE 381
Cdd:PLN02455 241 EVIAEYTVRALQRTVPPAVPGIVFLSGGQSEEEATLNLNAMNKLKTLKPWTLSFSFGRALQQSTLKAWAGKKENVAKAQA 320
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 312922382 382 EYIKRALANSLACQGKYTPSGKTGATASESLFISNHAY 419
Cdd:PLN02455 321 AFLVRCKANSEATLGKYKGDAAGGEGASESLHVKDYKY 358
FrucBisAld_I NF033379
fructose-bisphosphate aldolase class I; This family consists of fructose-bisphosphate aldolase ...
70-395 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: 519.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382  70 ELSDIAHRIVAPGKGILAADESIGSMGNRLQSIGTENTEENRRFFRQLLLTADDrVNPCIGGVILFHETLYEKADDGRPF 149
Cdd:NF033379   1 ELEETAQAMVAPGKGILAADESTGTINKRFEAIGVESTEENRRAYRELLFTTPG-LGDYISGVILFDETIRQKTADGTPF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 150 PQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGKHTPSPLAIMENANVLARY 229
Cdd:NF033379  80 PKVLADAGIIPGIKVDKGAKPLAGFPGEKVTEGLDGLRERLAEYYELGARFAKWRAVITIGDGIPSRACIEANAHALARY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 230 ASICQQNGIVPIVEPEILPDGDHDLSCCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACTQKFSNEEIAMATV 309
Cdd:NF033379 160 AALCQEAGLVPIVEPEVLMDGDHSIERCAEVTEEVLKEVFEELYRQGVDLEGMILKPNMVLPGKDCPDQASPEEVAEATV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 310 TALRRTVPPAVPGVTFLSGGQSEEEASINLNAINKCPLLkPWALTFSYGRALQASALKAWGGKEENLKAAQEEYIKRALA 389
Cdd:NF033379 240 RCLRRTVPAAVPGIAFLSGGQSDEEATAHLNAMNKLGPL-PWPLTFSYGRALQQPALKAWGGKAENVAAAQKALLHRARM 318

                 ....*.
gi 312922382 390 NSLACQ 395
Cdd:NF033379 319 NSLAAL 324
PLN02425 PLN02425
probable fructose-bisphosphate aldolase
44-419 7.20e-137

probable fructose-bisphosphate aldolase


Pssm-ID: 215234  Cd Length: 390  Bit Score: 397.47  E-value: 7.20e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382  44 KELGKESTTTGTMPCPYPALTTEQKKELSDIAHRIVAPGKGILAADESIGSMGNRLQSIGTENTEENRRFFRQLLLTADD 123
Cdd:PLN02425  20 RSFGQRSSSSSTRRVSFRIRAGSYSDELVQTAKSVASPGRGILAIDESNATCGKRLASIGLDNTETNRQAYRQLLLTTPG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 124 rVNPCIGGVILFHETLYEKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKW 203
Cdd:PLN02425 100 -LGEYISGAILFEETLYQSTTDGKKFVDCLRDQNIVPGIKVDKGLVPLPGSNNESWCQGLDGLASRSAEYYKQGARFAKW 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 204 RCVLKIgKHTPSPLAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLSCCQYVTEKVLAAVYKALSDHHVYLEGTL 283
Cdd:PLN02425 179 RTVVSI-PCGPSALAVKEAAWGLARYAAISQDNGLVPIVEPEILLDGDHPIERTLEVAEKVWSEVFFYLAQNNVLFEGIL 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 284 LKPNMVTPGHACTQKFSNEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASINLNAINKCPllKPWALTFSYGRALQA 363
Cdd:PLN02425 258 LKPSMVTPGAEHKEKASPETIAKYTLTMLRRRVPPAVPGIMFLSGGQSEVEATLNLNAMNQSP--NPWHVSFSYARALQN 335
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 312922382 364 SALKAWGGKEENLKAAQEEYIKRALANSLACQGKYTPSGKTgATASESLFISNHAY 419
Cdd:PLN02425 336 SVLKTWQGRPENVEAAQKALLVRAKANSLAQLGRYSAEGES-EEAKKGMFVKGYTY 390
Fba1 COG3588
Fructose-bisphosphate aldolase class 1 [Carbohydrate transport and metabolism]; ...
68-401 1.20e-115

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: 339.78  E-value: 1.20e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382  68 KKELSDIAHRIVAPGKGILAA-DESIGSMGNRLQSIGTENTEENRRF--------FRQLLLTADDRVNPCIGGVILFHET 138
Cdd:COG3588    2 TEELNATALAMVANGKGFLAAlDQSGGSTPKALAAYGVEETEYSRREemfdlvhaMRERIITSPAFTGDKISGAILFEET 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 139 LYEKADdGRP-FPQVIKSKGGVVGIKVDKGVVPLAgtNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGkhtpSPL 217
Cdd:COG3588   82 MDQKID-GTPtFDYLWEKKGIVPGIKVDKGLKDLA--PGVQLMKGLDGLDERLARAKELGAFGTKWRSVIKIA----NAA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 218 AIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLSCCQYVTEKVLAAVYKALSDHhvylEGTLLKpnMVTPGHACTQ 297
Cdd:COG3588  155 GIKANVHQQARYAALCQEAGLVPIVEPEVLIDGDHKIEREAELTEEILKALFDALPED----EGVMLK--MVIPGKDNLY 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 298 KFSNEEiamatvtalrrtvpPAVPGVTFLSGGQSEEEASINLNAINKcpllkpwaLTFSYGRALQASALKAWGGKEENLK 377
Cdd:COG3588  229 QALVEH--------------PAVPRVVFLSGGQSREEATAHLNANNG--------LIASFSRALQEGLLAAWSGEEFNAA 286
                        330       340
                 ....*....|....*....|....
gi 312922382 378 AAQeeyikralanslACQGKYTPS 401
Cdd:COG3588  287 LAQ------------AIDGIYDAS 298
PLN02227 PLN02227
fructose-bisphosphate aldolase I
70-419 6.58e-115

fructose-bisphosphate aldolase I


Pssm-ID: 177872  Cd Length: 399  Bit Score: 341.78  E-value: 6.58e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382  70 ELSDIAHRIVAPGKGILAADESIGSMGNRLQSIGTENTEENRRFFRQLLLTADDrVNPCIGGVILFHETLYEKADDGRPF 149
Cdd:PLN02227  55 ELVKTAKTIASPGHGIMAMDESNATCGKRLASIGLENTEANRQAYRTLLVSAPG-LGQYISGAILFEETLYQSTTDGKKM 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 150 PQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIgKHTPSPLAIMENANVLARY 229
Cdd:PLN02227 134 VDVLVEQNIVPGIKVDKGLVPLVGSYDESWCQGLDGLASRTAAYYQQGARFAKWRTVVSI-PNGPSALAVKEAAWGLARY 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 230 ASICQQNGIVPIVEPEILPDGDHDLSCCQYVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACTQKFSNEEIAMATV 309
Cdd:PLN02227 213 AAISQDSGLVPIVEPEIMLDGEHGIDRTYDVAEKVWAEVFFYLAQNNVMFEGILLKPSMVTPGAEATDRATPEQVASYTL 292
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 310 TALRRTVPPAVPGVTFLSGGQSEEEASINLNAINKCPllKPWALTFSYGRALQASALKAWGGKEENLKAAQEEYIKRALA 389
Cdd:PLN02227 293 KLLRNRIPPAVPGIMFLSGGQSELEATLNLNAMNQAP--NPWHVSFSYARALQNTCLKTWGGKEENVKAAQDILLARAKA 370
                        330       340       350
                 ....*....|....*....|....*....|
gi 312922382 390 NSLACQGKYTPSGKTgATASESLFISNHAY 419
Cdd:PLN02227 371 NSLAQLGKYTGEGES-EEAKEGMFVKGYTY 399
FBP_aldolase_I_bact cd00949
Fructose-1.6-bisphosphate aldolase found in gram +/- bacteria; Fructose-1.6-bisphosphate ...
82-361 2.58e-09

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: 57.80  E-value: 2.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382  82 GKGILAA-DESIGSMGNRLQSIGTENT---EENRRF-----FRQLLLTADDRVNPCIGGVILFHETLYEKADdGRPFPQV 152
Cdd:cd00949   10 GKGFIAAlDQSGGSTPKALAAYGIEEDaysNEEEMFdlvheMRTRIITSPAFDGDKILGAILFEQTMDREIE-GKPTADY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 153 IKSKGGVVGI-KVDKGVVPLAgtNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKigkhTPSPLAImenANVLARYAS 231
Cdd:cd00949   89 LWEKKQIVPFlKVDKGLAEEK--NGVQLMKPIPNLDELLMRAKEKGVFGTKMRSVIK----EANPKGI---AAVVDQQFE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 232 ICQQ---NGIVPIVEPEIlpdgdhDLSCCQyvTEKVLAAVYKALSDHhvylegtllkpnmvtpghacTQKFSNEEIAMat 308
Cdd:cd00949  160 LAKQilsHGLVPIIEPEV------DIHSAD--KAKCEAILKAEILKH--------------------LDKLPEGQQVM-- 209
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312922382 309 vtaLRRTVP------------PAVPGVTFLSGGQSEEEASINLnAINKcpllkpwALTFSYGRAL 361
Cdd:cd00949  210 ---LKLTLPteanfyseliehPKVLRVVALSGGYSREEANELL-AKNN-------GVIASFSRAL 263
PRK05377 PRK05377
fructose-1,6-bisphosphate aldolase; Reviewed
79-246 5.99e-07

fructose-1,6-bisphosphate aldolase; Reviewed


Pssm-ID: 180045  Cd Length: 296  Bit Score: 50.64  E-value: 5.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382  79 VAPGKGILAA-DESIGSMGNRLQSIGTENTE---ENRRF-----FRQLLLTADDRVNPCIGGVILFHETLYEKADdGRPF 149
Cdd:PRK05377  10 MKNGKGFIAAlDQSGGSTPKALKLYGVEEDAysnEEEMFdlvheMRTRIITSPAFTGDKILGAILFEQTMDREIE-GKPT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312922382 150 PQVIKSKGGVVG-IKVDKGVVPLAgtNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKigkhTPSPLAImenANVLAR 228
Cdd:PRK05377  89 ADYLWEKKGVVPfLKVDKGLAEEA--NGVQLMKPIPNLDDLLDRAVEKGIFGTKMRSVIK----EANEQGI---AAVVAQ 159
                        170       180
                 ....*....|....*....|.
gi 312922382 229 YASICQQ---NGIVPIVEPEI 246
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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