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Conserved domains on  [gi|1835603664|ref|XP_033777029|]
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fructose-bisphosphate aldolase C [Geotrypetes seraphini]

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: 742.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  15 ELADIAQKIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQILFSADDRVKKCIGGVIFFHETMYQKGDCGTSF 94
Cdd:pfam00274   1 ELIATAKAIVAPGKGILAADESTGTIGKRLASIGVENTEENRRAYRQLLFTTDGELGEYISGVILFHETLYQKTDDGKPF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  95 VKMIKNKGIVVGIKVDKGVVPLAGTDGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKISEHTPSSLAIMENANVLARY 174
Cdd:pfam00274  81 VDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQGLDGLAERCAQYYKDGARFAKWRCVLKIGENTPSELAIQENANVLARY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 175 ASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTAGHACSIKYSAEEIAMATV 254
Cdd:pfam00274 161 ASICQQNGLVPIVEPEILPDGDHDLERCQKVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTPGADCPKKYTPEEIAEATV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 255 TALRRTVPPAVPGITFLSGGQSEEEASINLNAINNCPLARPWALTFSYGRALQASALNAWCGQKENEGAATEEFIKRAEV 334
Cdd:pfam00274 241 TALRRTVPPAVPGVTFLSGGQSEEEATVNLNAINKLPLKKPWALTFSYGRALQASVLKAWGGKKENVKAAQEELLKRAKA 320

                         330       340       350
                  ....*....|....*....|....*....|
gi 1835603664 335 NGLAALGKFEhSGDGGGAAGKSLYVANHAY 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: 742.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  15 ELADIAQKIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQILFSADDRVKKCIGGVIFFHETMYQKGDCGTSF 94
Cdd:pfam00274   1 ELIATAKAIVAPGKGILAADESTGTIGKRLASIGVENTEENRRAYRQLLFTTDGELGEYISGVILFHETLYQKTDDGKPF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  95 VKMIKNKGIVVGIKVDKGVVPLAGTDGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKISEHTPSSLAIMENANVLARY 174
Cdd:pfam00274  81 VDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQGLDGLAERCAQYYKDGARFAKWRCVLKIGENTPSELAIQENANVLARY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 175 ASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTAGHACSIKYSAEEIAMATV 254
Cdd:pfam00274 161 ASICQQNGLVPIVEPEILPDGDHDLERCQKVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTPGADCPKKYTPEEIAEATV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 255 TALRRTVPPAVPGITFLSGGQSEEEASINLNAINNCPLARPWALTFSYGRALQASALNAWCGQKENEGAATEEFIKRAEV 334
Cdd:pfam00274 241 TALRRTVPPAVPGVTFLSGGQSEEEATVNLNAINKLPLKKPWALTFSYGRALQASVLKAWGGKKENVKAAQEELLKRAKA 320

                         330       340       350
                  ....*....|....*....|....*....|
gi 1835603664 335 NGLAALGKFEhSGDGGGAAGKSLYVANHAY 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 1835603664  13 KKELADIAQKIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQILFSADDRVKkCIGGVIFFHETMYQKGDCGT 92
Cdd:cd00948     1 KEELIKTAKAIVAPGKGILAADESTGTIGKRFASIGVENTEENRRAYRELLFTTPGLGQ-YISGVILFEETLYQKTDDGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  93 SFVKMIKNKGIVVGIKVDKGVVPLAGTDGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKISEHTPSSLAIMENANVLA 172
Cdd:cd00948    80 PFVDILKEKGIVPGIKVDKGLVPLAGTDGETTTQGLDGLAERCAKYYKQGARFAKWRAVLKIGNGTPSELAIKENAHGLA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 173 RYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTAGHACSIKYSAEEIAMA 252
Cdd:cd00948   160 RYAAICQENGLVPIVEPEVLMDGDHDIERCQEVTEKVLAAVYKALNDHHVLLEGTLLKPNMVTPGADCKKKASPEEVAEY 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 253 TVTALRRTVPPAVPGITFLSGGQSEEEASINLNAINNCPLARPWALTFSYGRALQASALNAWCGQKENEGAATEEFIKRA 332
Cdd:cd00948   240 TVRALRRTVPAAVPGIVFLSGGQSEEEATLNLNAMNKLPLPKPWALSFSYGRALQASALKAWGGKKENVEAAQKALLKRA 319

                         330
                  ....*....|.
gi 1835603664 333 EVNGLAALGKF 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: 558.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  10 AEQKKELADIAQKIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQILFSADDrVKKCIGGVIFFHETMYQKGD 89
Cdd:PTZ00019    1 TEYAKELAETAKKIAAPGKGILAADESTGTIKKRFDPIGLENTEENRRAYRELLFTTEG-LEQYISGVILFEETVYQKAP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  90 CGTSFVKMIKNKGIVVGIKVDKGVVPLAGTDGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKI--SEHTPSSLAIMEN 167
Cdd:PTZ00019   80 SGKTFVELLKEKGIVPGIKVDKGLVTLPGTDGETSTQGLDGLAERAKKYYKAGARFAKWRAVLKIdpAKGKPSELAIQEN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 168 ANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTAGHACSIKYSAE 247
Cdd:PTZ00019  160 AWTLARYAAICQENGLVPIVEPEILIDGSHSIEVCQKVTEKVLAEVFKALNDHGVLLEGCLLKPNMVTPGSDCGVKATPQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 248 EIAMATVTALRRTVPPAVPGITFLSGGQSEEEASINLNAINNCPLARPWALTFSYGRALQASALNAWCGQKENEGAATEE 327
Cdd:PTZ00019  240 EVAFYTVRTLSRTVPPALPGVMFLSGGQSEEEASLNLNAMNKLTLPRPWALSFSYGRALQSSALKTWKGKDENVAAAQKA 319

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1835603664 328 FIKRAEVNGLAALGKFeHSGDGGGAAGKSLYVANHAY 364
Cdd:PTZ00019  320 LLHRAKANSLAQLGKY-KGGDGGAAASESLYVKDYKY 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: 511.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  15 ELADIAQKIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQILFSADDrVKKCIGGVIFFHETMYQKGDCGTSF 94
Cdd:NF033379    1 ELEETAQAMVAPGKGILAADESTGTINKRFEAIGVESTEENRRAYRELLFTTPG-LGDYISGVILFDETIRQKTADGTPF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  95 VKMIKNKGIVVGIKVDKGVVPLAGTDGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKISEHTPSSLAIMENANVLARY 174
Cdd:NF033379   80 PKVLADAGIIPGIKVDKGAKPLAGFPGEKVTEGLDGLRERLAEYYELGARFAKWRAVITIGDGIPSRACIEANAHALARY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 175 ASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTAGHACSIKYSAEEIAMATV 254
Cdd:NF033379  160 AALCQEAGLVPIVEPEVLMDGDHSIERCAEVTEEVLKEVFEELYRQGVDLEGMILKPNMVLPGKDCPDQASPEEVAEATV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 255 TALRRTVPPAVPGITFLSGGQSEEEASINLNAINNCPlARPWALTFSYGRALQASALNAWCGQKENEGAATEEFIKRAEV 334
Cdd:NF033379  240 RCLRRTVPAAVPGIAFLSGGQSDEEATAHLNAMNKLG-PLPWPLTFSYGRALQQPALKAWGGKAENVAAAQKALLHRARM 318


                  ....*.
gi 1835603664 335 NGLAAL 340
Cdd:NF033379  319 NSLAAL 324
Fba1 COG3588
Fructose-bisphosphate aldolase class 1 [Carbohydrate transport and metabolism]; ...
 13-324 8.48e-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: 335.54  E-value: 8.48e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  13 KKELADIAQKIVAPGKGILAA-DESVGSMAKRLSQIGVENTEENRRL--------YRQILFSADDRVKKCIGGVIFFHET 83
Cdd:COG3588     2 TEELNATALAMVANGKGFLAAlDQSGGSTPKALAAYGVEETEYSRREemfdlvhaMRERIITSPAFTGDKISGAILFEET 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  84 MYQKGDCGTSFVKMIKNKGIVVGIKVDKGVVPLAgtDGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKISEHTpsslA 163
Cdd:COG3588    82 MDQKIDGTPTFDYLWEKKGIVPGIKVDKGLKDLA--PGVQLMKGLDGLDERLARAKELGAFGTKWRSVIKIANAA----G 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 164 IMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHhiylEGTLLKpnMVTAGHACSIK 243
Cdd:COG3588   156 IKANVHQQARYAALCQEAGLVPIVEPEVLIDGDHKIEREAELTEEILKALFDALPED----EGVMLK--MVIPGKDNLYQ 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 244 YSAEEiamatvtalrrtvpPAVPGITFLSGGQSEEEASINLNAINncplarpwALTFSYGRALQASALNAWCGQKENEGA 323
Cdd:COG3588   230 ALVEH--------------PAVPRVVFLSGGQSREEATAHLNANN--------GLIASFSRALQEGLLAAWSGEEFNAAL 287


                  .
gi 1835603664 324 A 324
Cdd:COG3588   288 A 288
 
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: 742.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  15 ELADIAQKIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQILFSADDRVKKCIGGVIFFHETMYQKGDCGTSF 94
Cdd:pfam00274   1 ELIATAKAIVAPGKGILAADESTGTIGKRLASIGVENTEENRRAYRQLLFTTDGELGEYISGVILFHETLYQKTDDGKPF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  95 VKMIKNKGIVVGIKVDKGVVPLAGTDGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKISEHTPSSLAIMENANVLARY 174
Cdd:pfam00274  81 VDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQGLDGLAERCAQYYKDGARFAKWRCVLKIGENTPSELAIQENANVLARY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 175 ASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTAGHACSIKYSAEEIAMATV 254
Cdd:pfam00274 161 ASICQQNGLVPIVEPEILPDGDHDLERCQKVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTPGADCPKKYTPEEIAEATV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 255 TALRRTVPPAVPGITFLSGGQSEEEASINLNAINNCPLARPWALTFSYGRALQASALNAWCGQKENEGAATEEFIKRAEV 334
Cdd:pfam00274 241 TALRRTVPPAVPGVTFLSGGQSEEEATVNLNAINKLPLKKPWALTFSYGRALQASVLKAWGGKKENVKAAQEELLKRAKA 320

                         330       340       350
                  ....*....|....*....|....*....|
gi 1835603664 335 NGLAALGKFEhSGDGGGAAGKSLYVANHAY 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 1835603664  13 KKELADIAQKIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQILFSADDRVKkCIGGVIFFHETMYQKGDCGT 92
Cdd:cd00948     1 KEELIKTAKAIVAPGKGILAADESTGTIGKRFASIGVENTEENRRAYRELLFTTPGLGQ-YISGVILFEETLYQKTDDGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  93 SFVKMIKNKGIVVGIKVDKGVVPLAGTDGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKISEHTPSSLAIMENANVLA 172
Cdd:cd00948    80 PFVDILKEKGIVPGIKVDKGLVPLAGTDGETTTQGLDGLAERCAKYYKQGARFAKWRAVLKIGNGTPSELAIKENAHGLA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 173 RYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTAGHACSIKYSAEEIAMA 252
Cdd:cd00948   160 RYAAICQENGLVPIVEPEVLMDGDHDIERCQEVTEKVLAAVYKALNDHHVLLEGTLLKPNMVTPGADCKKKASPEEVAEY 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 253 TVTALRRTVPPAVPGITFLSGGQSEEEASINLNAINNCPLARPWALTFSYGRALQASALNAWCGQKENEGAATEEFIKRA 332
Cdd:cd00948   240 TVRALRRTVPAAVPGIVFLSGGQSEEEATLNLNAMNKLPLPKPWALSFSYGRALQASALKAWGGKKENVEAAQKALLKRA 319

                         330
                  ....*....|.
gi 1835603664 333 EVNGLAALGKF 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: 558.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  10 AEQKKELADIAQKIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQILFSADDrVKKCIGGVIFFHETMYQKGD 89
Cdd:PTZ00019    1 TEYAKELAETAKKIAAPGKGILAADESTGTIKKRFDPIGLENTEENRRAYRELLFTTEG-LEQYISGVILFEETVYQKAP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  90 CGTSFVKMIKNKGIVVGIKVDKGVVPLAGTDGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKI--SEHTPSSLAIMEN 167
Cdd:PTZ00019   80 SGKTFVELLKEKGIVPGIKVDKGLVTLPGTDGETSTQGLDGLAERAKKYYKAGARFAKWRAVLKIdpAKGKPSELAIQEN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 168 ANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTAGHACSIKYSAE 247
Cdd:PTZ00019  160 AWTLARYAAICQENGLVPIVEPEILIDGSHSIEVCQKVTEKVLAEVFKALNDHGVLLEGCLLKPNMVTPGSDCGVKATPQ 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 248 EIAMATVTALRRTVPPAVPGITFLSGGQSEEEASINLNAINNCPLARPWALTFSYGRALQASALNAWCGQKENEGAATEE 327
Cdd:PTZ00019  240 EVAFYTVRTLSRTVPPALPGVMFLSGGQSEEEASLNLNAMNKLTLPRPWALSFSYGRALQSSALKTWKGKDENVAAAQKA 319

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1835603664 328 FIKRAEVNGLAALGKFeHSGDGGGAAGKSLYVANHAY 364
Cdd:PTZ00019  320 LLHRAKANSLAQLGKY-KGGDGGAAASESLYVKDYKY 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: 511.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  15 ELADIAQKIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQILFSADDrVKKCIGGVIFFHETMYQKGDCGTSF 94
Cdd:NF033379    1 ELEETAQAMVAPGKGILAADESTGTINKRFEAIGVESTEENRRAYRELLFTTPG-LGDYISGVILFDETIRQKTADGTPF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  95 VKMIKNKGIVVGIKVDKGVVPLAGTDGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKISEHTPSSLAIMENANVLARY 174
Cdd:NF033379   80 PKVLADAGIIPGIKVDKGAKPLAGFPGEKVTEGLDGLRERLAEYYELGARFAKWRAVITIGDGIPSRACIEANAHALARY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 175 ASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTAGHACSIKYSAEEIAMATV 254
Cdd:NF033379  160 AALCQEAGLVPIVEPEVLMDGDHSIERCAEVTEEVLKEVFEELYRQGVDLEGMILKPNMVLPGKDCPDQASPEEVAEATV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 255 TALRRTVPPAVPGITFLSGGQSEEEASINLNAINNCPlARPWALTFSYGRALQASALNAWCGQKENEGAATEEFIKRAEV 334
Cdd:NF033379  240 RCLRRTVPAAVPGIAFLSGGQSDEEATAHLNAMNKLG-PLPWPLTFSYGRALQQPALKAWGGKAENVAAAQKALLHRARM 318


                  ....*.
gi 1835603664 335 NGLAAL 340
Cdd:NF033379  319 NSLAAL 324
FBP_aldolase_I cd00344
Fructose-bisphosphate aldolase class I; Fructose-bisphosphate aldolase class I. Fructose-1, ...
 13-339 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: 507.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  13 KKELADIAQKIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQILFSADDRVKKCIGGVIFFHETMYQKGDCGT 92
Cdd:cd00344     1 KKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPRIGGVILFHETLYQKADDGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  93 SFVKMIKNKGIVVGIKVDKGVVPLAGTDGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKISEHTPSSLAIMENANVLA 172
Cdd:cd00344    81 PFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 173 RYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTAGHACSIKYSAEEIAMA 252
Cdd:cd00344   161 RYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKFSHEEIAMA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 253 TVTALRRTVPPAVPGITFLSGGQSEEEASINLNAINNCPLARPWALTFSYGRALQASALNAWCGQKENEGAATEEFIKRA 332
Cdd:cd00344   241 TVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRA 320


                  ....*..
gi 1835603664 333 EVNGLAA 339
Cdd:cd00344   321 LANSLAA 327
PLN02455 PLN02455
fructose-bisphosphate aldolase
 7-364 9.13e-177

fructose-bisphosphate aldolase


Pssm-ID: 178074  Cd Length: 358  Bit Score: 495.04  E-value: 9.13e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664   7 ALSAEQKKELADIAQKIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQILFSADDrVKKCIGGVIFFHETMYQ 86
Cdd:PLN02455    3 AFVGKYADELIKNAKYIATPGKGILAADESTGTIGKRLASINVENVESNRQALRELLFTAPG-ALQYLSGVILFEETLYQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  87 KGDCGTSFVKMIKNKGIVVGIKVDKGVVPLAGTDGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKISEHTPSSLAIME 166
Cdd:PLN02455   82 KTSDGKPFVDVLKENGVLPGIKVDKGTVELAGTNGETTTQGLDGLGARCAKYYEAGARFAKWRAVLKIGPTEPSELAIQE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 167 NANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTAGHAcSIKYSA 246
Cdd:PLN02455  162 NAQGLARYAIICQENGLVPIVEPEILVDGSHDIKKCAAVTERVLAACYKALNDHHVLLEGTLLKPNMVTPGSD-SPKVSP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 247 EEIAMATVTALRRTVPPAVPGITFLSGGQSEEEASINLNAINNCPLARPWALTFSYGRALQASALNAWCGQKENEGAATE 326
Cdd:PLN02455  241 EVIAEYTVRALQRTVPPAVPGIVFLSGGQSEEEATLNLNAMNKLKTLKPWTLSFSFGRALQQSTLKAWAGKKENVAKAQA 320

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1835603664 327 EFIKRAEVNGLAALGKFEHSGDGGGAAGKSLYVANHAY 364
Cdd:PLN02455  321 AFLVRCKANSEATLGKYKGDAAGGEGASESLHVKDYKY 358
PLN02425 PLN02425
probable fructose-bisphosphate aldolase
 5-364 2.90e-131

probable fructose-bisphosphate aldolase


Pssm-ID: 215234  Cd Length: 390  Bit Score: 380.90  E-value: 2.90e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664   5 YPALSAEQKKELADIAQKIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQILFSADDrVKKCIGGVIFFHETM 84
Cdd:PLN02425   36 FRIRAGSYSDELVQTAKSVASPGRGILAIDESNATCGKRLASIGLDNTETNRQAYRQLLLTTPG-LGEYISGAILFEETL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  85 YQKGDCGTSFVKMIKNKGIVVGIKVDKGVVPLAGTDGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKISeHTPSSLAI 164
Cdd:PLN02425  115 YQSTTDGKKFVDCLRDQNIVPGIKVDKGLVPLPGSNNESWCQGLDGLASRSAEYYKQGARFAKWRTVVSIP-CGPSALAV 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 165 MENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTAGHACSIKY 244
Cdd:PLN02425  194 KEAAWGLARYAAISQDNGLVPIVEPEILLDGDHPIERTLEVAEKVWSEVFFYLAQNNVLFEGILLKPSMVTPGAEHKEKA 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 245 SAEEIAMATVTALRRTVPPAVPGITFLSGGQSEEEASINLNAINNCPlaRPWALTFSYGRALQASALNAWCGQKENEGAA 324
Cdd:PLN02425  274 SPETIAKYTLTMLRRRVPPAVPGIMFLSGGQSEVEATLNLNAMNQSP--NPWHVSFSYARALQNSVLKTWQGRPENVEAA 351

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1835603664 325 TEEFIKRAEVNGLAALGKFEHSGDgGGAAGKSLYVANHAY 364
Cdd:PLN02425  352 QKALLVRAKANSLAQLGRYSAEGE-SEEAKKGMFVKGYTY 390
Fba1 COG3588
Fructose-bisphosphate aldolase class 1 [Carbohydrate transport and metabolism]; ...
 13-324 8.48e-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: 335.54  E-value: 8.48e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  13 KKELADIAQKIVAPGKGILAA-DESVGSMAKRLSQIGVENTEENRRL--------YRQILFSADDRVKKCIGGVIFFHET 83
Cdd:COG3588     2 TEELNATALAMVANGKGFLAAlDQSGGSTPKALAAYGVEETEYSRREemfdlvhaMRERIITSPAFTGDKISGAILFEET 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  84 MYQKGDCGTSFVKMIKNKGIVVGIKVDKGVVPLAgtDGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKISEHTpsslA 163
Cdd:COG3588    82 MDQKIDGTPTFDYLWEKKGIVPGIKVDKGLKDLA--PGVQLMKGLDGLDERLARAKELGAFGTKWRSVIKIANAA----G 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 164 IMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHhiylEGTLLKpnMVTAGHACSIK 243
Cdd:COG3588   156 IKANVHQQARYAALCQEAGLVPIVEPEVLIDGDHKIEREAELTEEILKALFDALPED----EGVMLK--MVIPGKDNLYQ 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 244 YSAEEiamatvtalrrtvpPAVPGITFLSGGQSEEEASINLNAINncplarpwALTFSYGRALQASALNAWCGQKENEGA 323
Cdd:COG3588   230 ALVEH--------------PAVPRVVFLSGGQSREEATAHLNANN--------GLIASFSRALQEGLLAAWSGEEFNAAL 287


                  .
gi 1835603664 324 A 324
Cdd:COG3588   288 A 288
PLN02227 PLN02227
fructose-bisphosphate aldolase I
 15-364 1.88e-107

fructose-bisphosphate aldolase I


Pssm-ID: 177872  Cd Length: 399  Bit Score: 320.59  E-value: 1.88e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  15 ELADIAQKIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQILFSADDrVKKCIGGVIFFHETMYQKGDCGTSF 94
Cdd:PLN02227   55 ELVKTAKTIASPGHGIMAMDESNATCGKRLASIGLENTEANRQAYRTLLVSAPG-LGQYISGAILFEETLYQSTTDGKKM 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  95 VKMIKNKGIVVGIKVDKGVVPLAGTDGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKISeHTPSSLAIMENANVLARY 174
Cdd:PLN02227  134 VDVLVEQNIVPGIKVDKGLVPLVGSYDESWCQGLDGLASRTAAYYQQGARFAKWRTVVSIP-NGPSALAVKEAAWGLARY 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 175 ASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTAGHACSIKYSAEEIAMATV 254
Cdd:PLN02227  213 AAISQDSGLVPIVEPEIMLDGEHGIDRTYDVAEKVWAEVFFYLAQNNVMFEGILLKPSMVTPGAEATDRATPEQVASYTL 292

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 255 TALRRTVPPAVPGITFLSGGQSEEEASINLNAINNCPlaRPWALTFSYGRALQASALNAWCGQKENEGAATEEFIKRAEV 334
Cdd:PLN02227  293 KLLRNRIPPAVPGIMFLSGGQSELEATLNLNAMNQAP--NPWHVSFSYARALQNTCLKTWGGKEENVKAAQDILLARAKA 370

                         330       340       350
                  ....*....|....*....|....*....|
gi 1835603664 335 NGLAALGKFEHSGDgGGAAGKSLYVANHAY 364
Cdd:PLN02227  371 NSLAQLGKYTGEGE-SEEAKEGMFVKGYTY 399
FBP_aldolase_I_bact cd00949
Fructose-1.6-bisphosphate aldolase found in gram +/- bacteria; Fructose-1.6-bisphosphate ...
 13-306 1.21e-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: 61.66  E-value: 1.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  13 KKELADIAQkivapGKGILAA-DESVGSMAKRLSQIGVE-----NTEENRRLYRQ----ILFSADDRVKKCIGgVIFFHE 82
Cdd:cd00949     1 QEQLERMKS-----GKGFIAAlDQSGGSTPKALAAYGIEedaysNEEEMFDLVHEmrtrIITSPAFDGDKILG-AILFEQ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  83 TMYQKGDCGTSFVKMIKNKGIVVGIKVDKGVVPLAgtDGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKisehtpssl 162
Cdd:cd00949    75 TMDREIEGKPTADYLWEKKQIVPFLKVDKGLAEEK--NGVQLMKPIPNLDELLMRAKEKGVFGTKMRSVIK--------- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664 163 aimeNANVLARYASICQQ---------NGIVPIVEPEIlpdgdhDLKRCQyvTEKVLAAVYKALSDHHiylegtllkpNM 233
Cdd:cd00949   144 ----EANPKGIAAVVDQQfelakqilsHGLVPIIEPEV------DIHSAD--KAKCEAILKAEILKHL----------DK 201

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835603664 234 VTAGHACSIKYSaeeiaMATVTALRR--TVPPAVPGITFLSGGQSEEEAsinlnainNCPLARPWALTFSYGRAL 306
Cdd:cd00949   202 LPEGQQVMLKLT-----LPTEANFYSelIEHPKVLRVVALSGGYSREEA--------NELLAKNNGVIASFSRAL 263
PRK05377 PRK05377
fructose-1,6-bisphosphate aldolase; Reviewed
 24-191 7.95e-07

fructose-1,6-bisphosphate aldolase; Reviewed


Pssm-ID: 180045  Cd Length: 296  Bit Score: 49.87  E-value: 7.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  24 VAPGKGILAA-DESVGSMAKRLSQIGVENTEenrrlyrqilFSADD-----------RVKKC-------IGGVIFFHETM 84
Cdd:PRK05377   10 MKNGKGFIAAlDQSGGSTPKALKLYGVEEDA----------YSNEEemfdlvhemrtRIITSpaftgdkILGAILFEQTM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835603664  85 YQKGDcGTSFVK-MIKNKGIVVGIKVDKGVVPLAgtDGETTTQGLDGLSERCAQYKKDGADFAKWRCVlkISEHTPSSLA 163
Cdd:PRK05377   80 DREIE-GKPTADyLWEKKGVVPFLKVDKGLAEEA--NGVQLMKPIPNLDDLLDRAVEKGIFGTKMRSV--IKEANEQGIA 154

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1835603664 164 imenaNVLARYASICQQ---NGIVPIVEPEI 191
Cdd:PRK05377  155 -----AVVAQQFEVAKQilaAGLVPIIEPEV 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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