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Conserved domains on  [gi|158081751|ref|NP_036628|]
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fructose-bisphosphate aldolase B [Rattus norvegicus]

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: 693.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751   15 ELSEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFRELLFSVDNSISQSIGGVILFHETLYQKDSQGKLF 94
Cdd:pfam00274   1 ELIATAKAIVAPGKGILAADESTGTIGKRLASIGVENTEENRRAYRQLLFTTDGELGEYISGVILFHETLYQKTDDGKPF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751   95 RNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGVDFGKWRAVLRISDQCPSSLAIQENANALARY 174
Cdd:pfam00274  81 VDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQGLDGLAERCAQYYKDGARFAKWRCVLKIGENTPSELAIQENANVLARY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  175 ASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPEQVAMATV 254
Cdd:pfam00274 161 ASICQQNGLVPIVEPEILPDGDHDLERCQKVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTPGADCPKKYTPEEIAEATV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  255 TALHRTVPAAVPGICFLSGGMSEEDATLNLNAINRCPLPRPWKLSFSYGRALQASALAAWGGKAANKKATQEAFMKRAVA 334
Cdd:pfam00274 241 TALRRTVPPAVPGVTFLSGGQSEEEATVNLNAINKLPLKKPWALTFSYGRALQASVLKAWGGKKENVKAAQEELLKRAKA 320

                         330       340       350
                  ....*....|....*....|....*....|
gi 158081751  335 NCQAAQGQYVhTGSSGAASTQSLFTASYTY 364
Cdd:pfam00274 321 NSLASLGKYV-GGVEGAAASESLFVANYAY 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: 693.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751   15 ELSEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFRELLFSVDNSISQSIGGVILFHETLYQKDSQGKLF 94
Cdd:pfam00274   1 ELIATAKAIVAPGKGILAADESTGTIGKRLASIGVENTEENRRAYRQLLFTTDGELGEYISGVILFHETLYQKTDDGKPF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751   95 RNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGVDFGKWRAVLRISDQCPSSLAIQENANALARY 174
Cdd:pfam00274  81 VDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQGLDGLAERCAQYYKDGARFAKWRCVLKIGENTPSELAIQENANVLARY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  175 ASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPEQVAMATV 254
Cdd:pfam00274 161 ASICQQNGLVPIVEPEILPDGDHDLERCQKVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTPGADCPKKYTPEEIAEATV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  255 TALHRTVPAAVPGICFLSGGMSEEDATLNLNAINRCPLPRPWKLSFSYGRALQASALAAWGGKAANKKATQEAFMKRAVA 334
Cdd:pfam00274 241 TALRRTVPPAVPGVTFLSGGQSEEEATVNLNAINKLPLKKPWALTFSYGRALQASVLKAWGGKKENVKAAQEELLKRAKA 320

                         330       340       350
                  ....*....|....*....|....*....|
gi 158081751  335 NCQAAQGQYVhTGSSGAASTQSLFTASYTY 364
Cdd:pfam00274 321 NSLASLGKYV-GGVEGAAASESLFVANYAY 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: 649.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  13 KKELSEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFRELLFSVDNsISQSIGGVILFHETLYQKDSQGK 92
Cdd:cd00948    1 KEELIKTAKAIVAPGKGILAADESTGTIGKRFASIGVENTEENRRAYRELLFTTPG-LGQYISGVILFEETLYQKTDDGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  93 LFRNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGVDFGKWRAVLRISDQCPSSLAIQENANALA 172
Cdd:cd00948   80 PFVDILKEKGIVPGIKVDKGLVPLAGTDGETTTQGLDGLAERCAKYYKQGARFAKWRAVLKIGNGTPSELAIKENAHGLA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751 173 RYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPEQVAMA 252
Cdd:cd00948  160 RYAAICQENGLVPIVEPEVLMDGDHDIERCQEVTEKVLAAVYKALNDHHVLLEGTLLKPNMVTPGADCKKKASPEEVAEY 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751 253 TVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINRCPLPRPWKLSFSYGRALQASALAAWGGKAANKKATQEAFMKRA 332
Cdd:cd00948  240 TVRALRRTVPAAVPGIVFLSGGQSEEEATLNLNAMNKLPLPKPWALSFSYGRALQASALKAWGGKKENVEAAQKALLKRA 319

                        330
                 ....*....|.
gi 158081751 333 VANCQAAQGQY 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: 547.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  10 SEQKKELSEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFRELLFSVdNSISQSIGGVILFHETLYQKDS 89
Cdd:PTZ00019   1 TEYAKELAETAKKIAAPGKGILAADESTGTIKKRFDPIGLENTEENRRAYRELLFTT-EGLEQYISGVILFEETVYQKAP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  90 QGKLFRNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGVDFGKWRAVLRI--SDQCPSSLAIQEN 167
Cdd:PTZ00019  80 SGKTFVELLKEKGIVPGIKVDKGLVTLPGTDGETSTQGLDGLAERAKKYYKAGARFAKWRAVLKIdpAKGKPSELAIQEN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751 168 ANALARYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPE 247
Cdd:PTZ00019 160 AWTLARYAAICQENGLVPIVEPEILIDGSHSIEVCQKVTEKVLAEVFKALNDHGVLLEGCLLKPNMVTPGSDCGVKATPQ 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751 248 QVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINRCPLPRPWKLSFSYGRALQASALAAWGGKAANKKATQEA 327
Cdd:PTZ00019 240 EVAFYTVRTLSRTVPPALPGVMFLSGGQSEEEASLNLNAMNKLTLPRPWALSFSYGRALQSSALKTWKGKDENVAAAQKA 319

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 158081751 328 FMKRAVANCQAAQGQYvHTGSSGAASTQSLFTASYTY 364
Cdd:PTZ00019 320 LLHRAKANSLAQLGKY-KGGDGGAAASESLYVKDYKY 355
FrucBisAld_I NF033379
fructose-bisphosphate aldolase class I; This family consists of fructose-bisphosphate aldolase ...
 15-340 5.36e-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: 494.38  E-value: 5.36e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  15 ELSEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFRELLFSVDNsISQSIGGVILFHETLYQKDSQGKLF 94
Cdd:NF033379   1 ELEETAQAMVAPGKGILAADESTGTINKRFEAIGVESTEENRRAYRELLFTTPG-LGDYISGVILFDETIRQKTADGTPF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  95 RNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGVDFGKWRAVLRISDQCPSSLAIQENANALARY 174
Cdd:NF033379  80 PKVLADAGIIPGIKVDKGAKPLAGFPGEKVTEGLDGLRERLAEYYELGARFAKWRAVITIGDGIPSRACIEANAHALARY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751 175 ASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPEQVAMATV 254
Cdd:NF033379 160 AALCQEAGLVPIVEPEVLMDGDHSIERCAEVTEEVLKEVFEELYRQGVDLEGMILKPNMVLPGKDCPDQASPEEVAEATV 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751 255 TALHRTVPAAVPGICFLSGGMSEEDATLNLNAINRCPlPRPWKLSFSYGRALQASALAAWGGKAANKKATQEAFMKRAVA 334
Cdd:NF033379 240 RCLRRTVPAAVPGIAFLSGGQSDEEATAHLNAMNKLG-PLPWPLTFSYGRALQQPALKAWGGKAENVAAAQKALLHRARM 318


                 ....*.
gi 158081751 335 NCQAAQ 340
Cdd:NF033379 319 NSLAAL 324
Fba1 COG3588
Fructose-bisphosphate aldolase class 1 [Carbohydrate transport and metabolism]; ...
 13-343 5.30e-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: 318.21  E-value: 5.30e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  13 KKELSEIAQRIVANGKGILAA-DESVGTMGNRLQRIKVENTEENRR--------QFRELLFSVDNSISQSIGGVILFHET 83
Cdd:COG3588    2 TEELNATALAMVANGKGFLAAlDQSGGSTPKALAAYGVEETEYSRReemfdlvhAMRERIITSPAFTGDKISGAILFEET 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  84 LYQKdSQGK-LFRNILKEKGIVVGIKLDQGGAPLAgtNKETTIQGLDGLSERCAQYKKDGVDFGKWRAVLRISDQcpssL 162
Cdd:COG3588   82 MDQK-IDGTpTFDYLWEKKGIVPGIKVDKGLKDLA--PGVQLMKGLDGLDERLARAKELGAFGTKWRSVIKIANA----A 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751 163 AIQENANALARYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDHhvylEGTLLKpnMVTAGHACTK 242
Cdd:COG3588  155 GIKANVHQQARYAALCQEAGLVPIVEPEVLIDGDHKIEREAELTEEILKALFDALPED----EGVMLK--MVIPGKDNLY 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751 243 KYTPEQvamatvtalhrtvpAAVPGICFLSGGMSEEDATLNLNAINrcplprpwKLSFSYGRALQASALAAWGGKAANKK 322
Cdd:COG3588  229 QALVEH--------------PAVPRVVFLSGGQSREEATAHLNANN--------GLIASFSRALQEGLLAAWSGEEFNAA 286

                        330       340
                 ....*....|....*....|.
gi 158081751 323 ATqeafmkravancQAAQGQY 343
Cdd:COG3588  287 LA------------QAIDGIY 295
 
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: 693.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751   15 ELSEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFRELLFSVDNSISQSIGGVILFHETLYQKDSQGKLF 94
Cdd:pfam00274   1 ELIATAKAIVAPGKGILAADESTGTIGKRLASIGVENTEENRRAYRQLLFTTDGELGEYISGVILFHETLYQKTDDGKPF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751   95 RNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGVDFGKWRAVLRISDQCPSSLAIQENANALARY 174
Cdd:pfam00274  81 VDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQGLDGLAERCAQYYKDGARFAKWRCVLKIGENTPSELAIQENANVLARY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  175 ASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPEQVAMATV 254
Cdd:pfam00274 161 ASICQQNGLVPIVEPEILPDGDHDLERCQKVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTPGADCPKKYTPEEIAEATV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  255 TALHRTVPAAVPGICFLSGGMSEEDATLNLNAINRCPLPRPWKLSFSYGRALQASALAAWGGKAANKKATQEAFMKRAVA 334
Cdd:pfam00274 241 TALRRTVPPAVPGVTFLSGGQSEEEATVNLNAINKLPLKKPWALTFSYGRALQASVLKAWGGKKENVKAAQEELLKRAKA 320

                         330       340       350
                  ....*....|....*....|....*....|
gi 158081751  335 NCQAAQGQYVhTGSSGAASTQSLFTASYTY 364
Cdd:pfam00274 321 NSLASLGKYV-GGVEGAAASESLFVANYAY 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: 649.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  13 KKELSEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFRELLFSVDNsISQSIGGVILFHETLYQKDSQGK 92
Cdd:cd00948    1 KEELIKTAKAIVAPGKGILAADESTGTIGKRFASIGVENTEENRRAYRELLFTTPG-LGQYISGVILFEETLYQKTDDGK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  93 LFRNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGVDFGKWRAVLRISDQCPSSLAIQENANALA 172
Cdd:cd00948   80 PFVDILKEKGIVPGIKVDKGLVPLAGTDGETTTQGLDGLAERCAKYYKQGARFAKWRAVLKIGNGTPSELAIKENAHGLA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751 173 RYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPEQVAMA 252
Cdd:cd00948  160 RYAAICQENGLVPIVEPEVLMDGDHDIERCQEVTEKVLAAVYKALNDHHVLLEGTLLKPNMVTPGADCKKKASPEEVAEY 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751 253 TVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINRCPLPRPWKLSFSYGRALQASALAAWGGKAANKKATQEAFMKRA 332
Cdd:cd00948  240 TVRALRRTVPAAVPGIVFLSGGQSEEEATLNLNAMNKLPLPKPWALSFSYGRALQASALKAWGGKKENVEAAQKALLKRA 319

                        330
                 ....*....|.
gi 158081751 333 VANCQAAQGQY 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: 547.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  10 SEQKKELSEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFRELLFSVdNSISQSIGGVILFHETLYQKDS 89
Cdd:PTZ00019   1 TEYAKELAETAKKIAAPGKGILAADESTGTIKKRFDPIGLENTEENRRAYRELLFTT-EGLEQYISGVILFEETVYQKAP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  90 QGKLFRNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGVDFGKWRAVLRI--SDQCPSSLAIQEN 167
Cdd:PTZ00019  80 SGKTFVELLKEKGIVPGIKVDKGLVTLPGTDGETSTQGLDGLAERAKKYYKAGARFAKWRAVLKIdpAKGKPSELAIQEN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751 168 ANALARYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPE 247
Cdd:PTZ00019 160 AWTLARYAAICQENGLVPIVEPEILIDGSHSIEVCQKVTEKVLAEVFKALNDHGVLLEGCLLKPNMVTPGSDCGVKATPQ 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751 248 QVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINRCPLPRPWKLSFSYGRALQASALAAWGGKAANKKATQEA 327
Cdd:PTZ00019 240 EVAFYTVRTLSRTVPPALPGVMFLSGGQSEEEASLNLNAMNKLTLPRPWALSFSYGRALQSSALKTWKGKDENVAAAQKA 319

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 158081751 328 FMKRAVANCQAAQGQYvHTGSSGAASTQSLFTASYTY 364
Cdd:PTZ00019 320 LLHRAKANSLAQLGKY-KGGDGGAAASESLYVKDYKY 355
FrucBisAld_I NF033379
fructose-bisphosphate aldolase class I; This family consists of fructose-bisphosphate aldolase ...
 15-340 5.36e-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: 494.38  E-value: 5.36e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  15 ELSEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFRELLFSVDNsISQSIGGVILFHETLYQKDSQGKLF 94
Cdd:NF033379   1 ELEETAQAMVAPGKGILAADESTGTINKRFEAIGVESTEENRRAYRELLFTTPG-LGDYISGVILFDETIRQKTADGTPF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  95 RNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGVDFGKWRAVLRISDQCPSSLAIQENANALARY 174
Cdd:NF033379  80 PKVLADAGIIPGIKVDKGAKPLAGFPGEKVTEGLDGLRERLAEYYELGARFAKWRAVITIGDGIPSRACIEANAHALARY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751 175 ASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPEQVAMATV 254
Cdd:NF033379 160 AALCQEAGLVPIVEPEVLMDGDHSIERCAEVTEEVLKEVFEELYRQGVDLEGMILKPNMVLPGKDCPDQASPEEVAEATV 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751 255 TALHRTVPAAVPGICFLSGGMSEEDATLNLNAINRCPlPRPWKLSFSYGRALQASALAAWGGKAANKKATQEAFMKRAVA 334
Cdd:NF033379 240 RCLRRTVPAAVPGIAFLSGGQSDEEATAHLNAMNKLG-PLPWPLTFSYGRALQQPALKAWGGKAENVAAAQKALLHRARM 318


                 ....*.
gi 158081751 335 NCQAAQ 340
Cdd:NF033379 319 NSLAAL 324
PLN02455 PLN02455
fructose-bisphosphate aldolase
 7-364 2.11e-173

fructose-bisphosphate aldolase


Pssm-ID: 178074  Cd Length: 358  Bit Score: 486.57  E-value: 2.11e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751   7 ALTSEQKKELSEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFRELLFSVDNSIsQSIGGVILFHETLYQ 86
Cdd:PLN02455   3 AFVGKYADELIKNAKYIATPGKGILAADESTGTIGKRLASINVENVESNRQALRELLFTAPGAL-QYLSGVILFEETLYQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  87 KDSQGKLFRNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGVDFGKWRAVLRISDQCPSSLAIQE 166
Cdd:PLN02455  82 KTSDGKPFVDVLKENGVLPGIKVDKGTVELAGTNGETTTQGLDGLGARCAKYYEAGARFAKWRAVLKIGPTEPSELAIQE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751 167 NANALARYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHAcTKKYTP 246
Cdd:PLN02455 162 NAQGLARYAIICQENGLVPIVEPEILVDGSHDIKKCAAVTERVLAACYKALNDHHVLLEGTLLKPNMVTPGSD-SPKVSP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751 247 EQVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINRCPLPRPWKLSFSYGRALQASALAAWGGKAANKKATQE 326
Cdd:PLN02455 241 EVIAEYTVRALQRTVPPAVPGIVFLSGGQSEEEATLNLNAMNKLKTLKPWTLSFSFGRALQQSTLKAWAGKKENVAKAQA 320

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 158081751 327 AFMKRAVANCQAAQGQYVHTGSSGAASTQSLFTASYTY 364
Cdd:PLN02455 321 AFLVRCKANSEATLGKYKGDAAGGEGASESLHVKDYKY 358
FBP_aldolase_I cd00344
Fructose-bisphosphate aldolase class I; Fructose-bisphosphate aldolase class I. Fructose-1, ...
 13-340 1.83e-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: 440.01  E-value: 1.83e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  13 KKELSEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFRELLFSVDNSISQSIGGVILFHETLYQKDSQGK 92
Cdd:cd00344    1 KKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPRIGGVILFHETLYQKADDGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  93 LFRNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGVDFGKWRAVLRISDQCPSSLAIQENANALA 172
Cdd:cd00344   81 PFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751 173 RYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPEQVAMA 252
Cdd:cd00344  161 RYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKFSHEEIAMA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751 253 TVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINRCPLPRPWKLSFSYGRALQASALAAWGGKAANKKATQEAFMKRA 332
Cdd:cd00344  241 TVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRA 320


                 ....*...
gi 158081751 333 VANCQAAQ 340
Cdd:cd00344  321 LANSLAAQ 328
PLN02425 PLN02425
probable fructose-bisphosphate aldolase
 5-364 6.63e-130

probable fructose-bisphosphate aldolase


Pssm-ID: 215234  Cd Length: 390  Bit Score: 377.44  E-value: 6.63e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751   5 FPALTSEQKKELSEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFRELLFSVDnSISQSIGGVILFHETL 84
Cdd:PLN02425  36 FRIRAGSYSDELVQTAKSVASPGRGILAIDESNATCGKRLASIGLDNTETNRQAYRQLLLTTP-GLGEYISGAILFEETL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  85 YQKDSQGKLFRNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGVDFGKWRAVLRISdqC-PSSLA 163
Cdd:PLN02425 115 YQSTTDGKKFVDCLRDQNIVPGIKVDKGLVPLPGSNNESWCQGLDGLASRSAEYYKQGARFAKWRTVVSIP--CgPSALA 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751 164 IQENANALARYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKK 243
Cdd:PLN02425 193 VKEAAWGLARYAAISQDNGLVPIVEPEILLDGDHPIERTLEVAEKVWSEVFFYLAQNNVLFEGILLKPSMVTPGAEHKEK 272

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751 244 YTPEQVAMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINRCplPRPWKLSFSYGRALQASALAAWGGKAANKKA 323
Cdd:PLN02425 273 ASPETIAKYTLTMLRRRVPPAVPGIMFLSGGQSEVEATLNLNAMNQS--PNPWHVSFSYARALQNSVLKTWQGRPENVEA 350

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 158081751 324 TQEAFMKRAVANCQAAQGQYVHTGSSGAAStQSLFTASYTY 364
Cdd:PLN02425 351 AQKALLVRAKANSLAQLGRYSAEGESEEAK-KGMFVKGYTY 390
PLN02227 PLN02227
fructose-bisphosphate aldolase I
 10-364 5.58e-109

fructose-bisphosphate aldolase I


Pssm-ID: 177872  Cd Length: 399  Bit Score: 324.44  E-value: 5.58e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  10 SEQKKELSEIAQRIVANGKGILAADESVGTMGNRLQRIKVENTEENRRQFRELLFSVDnSISQSIGGVILFHETLYQKDS 89
Cdd:PLN02227  50 SAYADELVKTAKTIASPGHGIMAMDESNATCGKRLASIGLENTEANRQAYRTLLVSAP-GLGQYISGAILFEETLYQSTT 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  90 QGKLFRNILKEKGIVVGIKLDQGGAPLAGTNKETTIQGLDGLSERCAQYKKDGVDFGKWRAVLRISDQcPSSLAIQENAN 169
Cdd:PLN02227 129 DGKKMVDVLVEQNIVPGIKVDKGLVPLVGSYDESWCQGLDGLASRTAAYYQQGARFAKWRTVVSIPNG-PSALAVKEAAW 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751 170 ALARYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDHHVYLEGTLLKPNMVTAGHACTKKYTPEQV 249
Cdd:PLN02227 208 GLARYAAISQDSGLVPIVEPEIMLDGEHGIDRTYDVAEKVWAEVFFYLAQNNVMFEGILLKPSMVTPGAEATDRATPEQV 287

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751 250 AMATVTALHRTVPAAVPGICFLSGGMSEEDATLNLNAINRCplPRPWKLSFSYGRALQASALAAWGGKAANKKATQEAFM 329
Cdd:PLN02227 288 ASYTLKLLRNRIPPAVPGIMFLSGGQSELEATLNLNAMNQA--PNPWHVSFSYARALQNTCLKTWGGKEENVKAAQDILL 365

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 158081751 330 KRAVANCQAAQGQYVHTGSSGAAStQSLFTASYTY 364
Cdd:PLN02227 366 ARAKANSLAQLGKYTGEGESEEAK-EGMFVKGYTY 399
Fba1 COG3588
Fructose-bisphosphate aldolase class 1 [Carbohydrate transport and metabolism]; ...
 13-343 5.30e-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: 318.21  E-value: 5.30e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  13 KKELSEIAQRIVANGKGILAA-DESVGTMGNRLQRIKVENTEENRR--------QFRELLFSVDNSISQSIGGVILFHET 83
Cdd:COG3588    2 TEELNATALAMVANGKGFLAAlDQSGGSTPKALAAYGVEETEYSRReemfdlvhAMRERIITSPAFTGDKISGAILFEET 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  84 LYQKdSQGK-LFRNILKEKGIVVGIKLDQGGAPLAgtNKETTIQGLDGLSERCAQYKKDGVDFGKWRAVLRISDQcpssL 162
Cdd:COG3588   82 MDQK-IDGTpTFDYLWEKKGIVPGIKVDKGLKDLA--PGVQLMKGLDGLDERLARAKELGAFGTKWRSVIKIANA----A 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751 163 AIQENANALARYASICQQNGLVPIVEPEVLPDGDHDLEHCQYVSEKVLAAVYKALNDHhvylEGTLLKpnMVTAGHACTK 242
Cdd:COG3588  155 GIKANVHQQARYAALCQEAGLVPIVEPEVLIDGDHKIEREAELTEEILKALFDALPED----EGVMLK--MVIPGKDNLY 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751 243 KYTPEQvamatvtalhrtvpAAVPGICFLSGGMSEEDATLNLNAINrcplprpwKLSFSYGRALQASALAAWGGKAANKK 322
Cdd:COG3588  229 QALVEH--------------PAVPRVVFLSGGQSREEATAHLNANN--------GLIASFSRALQEGLLAAWSGEEFNAA 286

                        330       340
                 ....*....|....*....|.
gi 158081751 323 ATqeafmkravancQAAQGQY 343
Cdd:COG3588  287 LA------------QAIDGIY 295
FBP_aldolase_I_bact cd00949
Fructose-1.6-bisphosphate aldolase found in gram +/- bacteria; Fructose-1.6-bisphosphate ...
 18-191 2.52e-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: 54.72  E-value: 2.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  18 EIAQRIvANGKGILAA-DESVGTMGNRLQRIKV-ENTEENRRQFRELLFSVDNSI-------SQSIGGVILFHETLYQKd 88
Cdd:cd00949    2 EQLERM-KSGKGFIAAlDQSGGSTPKALAAYGIeEDAYSNEEEMFDLVHEMRTRIitspafdGDKILGAILFEQTMDRE- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  89 SQGKLFRNIL-KEKGIVVGIKLDQGGAPLA-GTNKETTIQGLDGLSERCaqyKKDGVdFG-KWRAVLRisdqcpsslaiq 165
Cdd:cd00949   80 IEGKPTADYLwEKKQIVPFLKVDKGLAEEKnGVQLMKPIPNLDELLMRA---KEKGV-FGtKMRSVIK------------ 143

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 158081751 166 eNANALARYASICQQ---------NGLVPIVEPEV 191
Cdd:cd00949  144 -EANPKGIAAVVDQQfelakqilsHGLVPIIEPEV 177
PRK05377 PRK05377
fructose-1,6-bisphosphate aldolase; Reviewed
 71-191 4.63e-06

fructose-1,6-bisphosphate aldolase; Reviewed


Pssm-ID: 180045  Cd Length: 296  Bit Score: 47.56  E-value: 4.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158081751  71 SQSIGGVILFHETLYQKdSQGKLFRNIL-KEKGIVVGIKLDQGGAPLA-GTNKETTIQGLDGLSERCaqyKKDGVdFG-K 147
Cdd:PRK05377  66 GDKILGAILFEQTMDRE-IEGKPTADYLwEKKGVVPFLKVDKGLAEEAnGVQLMKPIPNLDDLLDRA---VEKGI-FGtK 140

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 158081751 148 WRAVlrisdqcpsslaIQEnANALARYASICQQ---------NGLVPIVEPEV 191
Cdd:PRK05377 141 MRSV------------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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