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Conserved domains on  [gi|15227981|ref|NP_181187|]
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Aldolase superfamily protein [Arabidopsis thaliana]

Protein Classification

fructose-bisphosphate aldolase( domain architecture ID 10791362)

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
PLN02455 PLN02455
fructose-bisphosphate aldolase
 1-358 0e+00

fructose-bisphosphate aldolase


:

Pssm-ID: 178074  Cd Length: 358  Bit Score: 759.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981    1 MSSFTSKFADELIANAAYIGTPGKGILAADESTGTIGKRLASINVENVESNRRALRELLFTTPGALPCLSGVILFEETLY 80
Cdd:PLN02455   1 MSAFVGKYADELIKNAKYIATPGKGILAADESTGTIGKRLASINVENVESNRQALRELLFTAPGALQYLSGVILFEETLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981   81 QKSSDGTPFVDMLKSAGVLPGIKVDKGTVELAGTNGETTTQGLDGLGDRCKKYYEAGARFAKWRAVLKIGVNEPSQLAIH 160
Cdd:PLN02455  81 QKTSDGKPFVDVLKENGVLPGIKVDKGTVELAGTNGETTTQGLDGLGARCAKYYEAGARFAKWRAVLKIGPTEPSELAIQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981  161 ENAYGLARYAVICQENGLVPIVEPEILVDGSHDIQKCAAVTERVLAACYKALSDHHVLLEGTLLKPNMVTPGSESAKVAP 240
Cdd:PLN02455 161 ENAQGLARYAIICQENGLVPIVEPEILVDGSHDIKKCAAVTERVLAACYKALNDHHVLLEGTLLKPNMVTPGSDSPKVSP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981  241 EVIAEHTVRALQRTVPAAVPAIVFLSGGQSEEEATRNLNAMNQLKTKKPWSLSFSFGRALQQSTLKTWGGKEENVKKAQE 320
Cdd:PLN02455 241 EVIAEYTVRALQRTVPPAVPGIVFLSGGQSEEEATLNLNAMNKLKTLKPWTLSFSFGRALQQSTLKAWAGKKENVAKAQA 320

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 15227981  321 AFLVRCKANSEATLGAYKGDAKLGEGAAESLHVKDYKY 358
Cdd:PLN02455 321 AFLVRCKANSEATLGKYKGDAAGGEGASESLHVKDYKY 358
 
Name Accession Description Interval E-value
PLN02455 PLN02455
fructose-bisphosphate aldolase
 1-358 0e+00

fructose-bisphosphate aldolase


Pssm-ID: 178074  Cd Length: 358  Bit Score: 759.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981    1 MSSFTSKFADELIANAAYIGTPGKGILAADESTGTIGKRLASINVENVESNRRALRELLFTTPGALPCLSGVILFEETLY 80
Cdd:PLN02455   1 MSAFVGKYADELIKNAKYIATPGKGILAADESTGTIGKRLASINVENVESNRQALRELLFTAPGALQYLSGVILFEETLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981   81 QKSSDGTPFVDMLKSAGVLPGIKVDKGTVELAGTNGETTTQGLDGLGDRCKKYYEAGARFAKWRAVLKIGVNEPSQLAIH 160
Cdd:PLN02455  81 QKTSDGKPFVDVLKENGVLPGIKVDKGTVELAGTNGETTTQGLDGLGARCAKYYEAGARFAKWRAVLKIGPTEPSELAIQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981  161 ENAYGLARYAVICQENGLVPIVEPEILVDGSHDIQKCAAVTERVLAACYKALSDHHVLLEGTLLKPNMVTPGSESAKVAP 240
Cdd:PLN02455 161 ENAQGLARYAIICQENGLVPIVEPEILVDGSHDIKKCAAVTERVLAACYKALNDHHVLLEGTLLKPNMVTPGSDSPKVSP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981  241 EVIAEHTVRALQRTVPAAVPAIVFLSGGQSEEEATRNLNAMNQLKTKKPWSLSFSFGRALQQSTLKTWGGKEENVKKAQE 320
Cdd:PLN02455 241 EVIAEYTVRALQRTVPPAVPGIVFLSGGQSEEEATLNLNAMNKLKTLKPWTLSFSFGRALQQSTLKAWAGKKENVAKAQA 320

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 15227981  321 AFLVRCKANSEATLGAYKGDAKLGEGAAESLHVKDYKY 358
Cdd:PLN02455 321 AFLVRCKANSEATLGKYKGDAAGGEGASESLHVKDYKY 358
Glycolytic pfam00274
Fructose-bisphosphate aldolase class-I;
11-358 0e+00

Fructose-bisphosphate aldolase class-I;


Pssm-ID: 459742  Cd Length: 349  Bit Score: 695.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981    11 ELIANAAYIGTPGKGILAADESTGTIGKRLASINVENVESNRRALRELLFTTPGAL-PCLSGVILFEETLYQKSSDGTPF 89
Cdd:pfam00274   1 ELIATAKAIVAPGKGILAADESTGTIGKRLASIGVENTEENRRAYRQLLFTTDGELgEYISGVILFHETLYQKTDDGKPF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981    90 VDMLKSAGVLPGIKVDKGTVELAGTNGETTTQGLDGLGDRCKKYYEAGARFAKWRAVLKIGVNEPSQLAIHENAYGLARY 169
Cdd:pfam00274  81 VDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQGLDGLAERCAQYYKDGARFAKWRCVLKIGENTPSELAIQENANVLARY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981   170 AVICQENGLVPIVEPEILVDGSHDIQKCAAVTERVLAACYKALSDHHVLLEGTLLKPNMVTPGSES-AKVAPEVIAEHTV 248
Cdd:pfam00274 161 ASICQQNGLVPIVEPEILPDGDHDLERCQKVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTPGADCpKKYTPEEIAEATV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981   249 RALQRTVPAAVPAIVFLSGGQSEEEATRNLNAMNQLKTKKPWSLSFSFGRALQQSTLKTWGGKEENVKKAQEAFLVRCKA 328
Cdd:pfam00274 241 TALRRTVPPAVPGVTFLSGGQSEEEATVNLNAINKLPLKKPWALTFSYGRALQASVLKAWGGKKENVKAAQEELLKRAKA 320

                         330       340       350
                  ....*....|....*....|....*....|
gi 15227981   329 NSEATLGAYKGDAKlGEGAAESLHVKDYKY 358
Cdd:pfam00274 321 NSLASLGKYVGGVE-GAAASESLFVANYAY 349
FBP_aldolase_I_a cd00948
Fructose-1,6-bisphosphate aldolase; Fructose-1,6-bisphosphate aldolase. The enzyme catalyzes ...
 9-337 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: 647.00  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981   9 ADELIANAAYIGTPGKGILAADESTGTIGKRLASINVENVESNRRALRELLFTTPGALPCLSGVILFEETLYQKSSDGTP 88
Cdd:cd00948   1 KEELIKTAKAIVAPGKGILAADESTGTIGKRFASIGVENTEENRRAYRELLFTTPGLGQYISGVILFEETLYQKTDDGKP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981  89 FVDMLKSAGVLPGIKVDKGTVELAGTNGETTTQGLDGLGDRCKKYYEAGARFAKWRAVLKIGVNEPSQLAIHENAYGLAR 168
Cdd:cd00948  81 FVDILKEKGIVPGIKVDKGLVPLAGTDGETTTQGLDGLAERCAKYYKQGARFAKWRAVLKIGNGTPSELAIKENAHGLAR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981 169 YAVICQENGLVPIVEPEILVDGSHDIQKCAAVTERVLAACYKALSDHHVLLEGTLLKPNMVTPGSESA-KVAPEVIAEHT 247
Cdd:cd00948 161 YAAICQENGLVPIVEPEVLMDGDHDIERCQEVTEKVLAAVYKALNDHHVLLEGTLLKPNMVTPGADCKkKASPEEVAEYT 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981 248 VRALQRTVPAAVPAIVFLSGGQSEEEATRNLNAMNQLKTKKPWSLSFSFGRALQQSTLKTWGGKEENVKKAQEAFLVRCK 327
Cdd:cd00948 241 VRALRRTVPAAVPGIVFLSGGQSEEEATLNLNAMNKLPLPKPWALSFSYGRALQASALKAWGGKKENVEAAQKALLKRAK 320

                       330
                ....*....|
gi 15227981 328 ANSEATLGAY 337
Cdd:cd00948 321 ANSLAALGKY 330
FrucBisAld_I NF033379
fructose-bisphosphate aldolase class I; This family consists of fructose-bisphosphate aldolase ...
 11-334 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: 549.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981   11 ELIANAAYIGTPGKGILAADESTGTIGKRLASINVENVESNRRALRELLFTTPGALPCLSGVILFEETLYQKSSDGTPFV 90
Cdd:NF033379   1 ELEETAQAMVAPGKGILAADESTGTINKRFEAIGVESTEENRRAYRELLFTTPGLGDYISGVILFDETIRQKTADGTPFP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981   91 DMLKSAGVLPGIKVDKGTVELAGTNGETTTQGLDGLGDRCKKYYEAGARFAKWRAVLKIGVNEPSQLAIHENAYGLARYA 170
Cdd:NF033379  81 KVLADAGIIPGIKVDKGAKPLAGFPGEKVTEGLDGLRERLAEYYELGARFAKWRAVITIGDGIPSRACIEANAHALARYA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981  171 VICQENGLVPIVEPEILVDGSHDIQKCAAVTERVLAACYKALSDHHVLLEGTLLKPNMVTPGSESA-KVAPEVIAEHTVR 249
Cdd:NF033379 161 ALCQEAGLVPIVEPEVLMDGDHSIERCAEVTEEVLKEVFEELYRQGVDLEGMILKPNMVLPGKDCPdQASPEEVAEATVR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981  250 ALQRTVPAAVPAIVFLSGGQSEEEATRNLNAMNQLKtKKPWSLSFSFGRALQQSTLKTWGGKEENVKKAQEAFLVRCKAN 329
Cdd:NF033379 241 CLRRTVPAAVPGIAFLSGGQSDEEATAHLNAMNKLG-PLPWPLTFSYGRALQQPALKAWGGKAENVAAAQKALLHRARMN 319


                 ....*
gi 15227981  330 SEATL 334
Cdd:NF033379 320 SLAAL 324
Fba1 COG3588
Fructose-bisphosphate aldolase class 1 [Carbohydrate transport and metabolism]; ...
 9-321 3.77e-125

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: 361.74  E-value: 3.77e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981   9 ADELIANAAYIGTPGKGILAA-DESTGTIGKRLASINVENVESNRR--------ALRELLFTTPGALP-CLSGVILFEET 78
Cdd:COG3588   2 TEELNATALAMVANGKGFLAAlDQSGGSTPKALAAYGVEETEYSRReemfdlvhAMRERIITSPAFTGdKISGAILFEET 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981  79 LYQKSsDGTP-FVDMLKSAGVLPGIKVDKGTVELAgtNGETTTQGLDGLGDRCKKYYEAGARFAKWRAVLKIGvnepSQL 157
Cdd:COG3588  82 MDQKI-DGTPtFDYLWEKKGIVPGIKVDKGLKDLA--PGVQLMKGLDGLDERLARAKELGAFGTKWRSVIKIA----NAA 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981 158 AIHENAYGLARYAVICQENGLVPIVEPEILVDGSHDIQKCAAVTERVLAACYKALSDHhvllEGTLLKpnMVTPGSESAK 237
Cdd:COG3588 155 GIKANVHQQARYAALCQEAGLVPIVEPEVLIDGDHKIEREAELTEEILKALFDALPED----EGVMLK--MVIPGKDNLY 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981 238 VApevIAEHtvralqrtvpAAVPAIVFLSGGQSEEEATRNLNAMNQlktkkpwsLSFSFGRALQQSTLKTWGGKEENVKK 317
Cdd:COG3588 229 QA---LVEH----------PAVPRVVFLSGGQSREEATAHLNANNG--------LIASFSRALQEGLLAAWSGEEFNAAL 287


                ....
gi 15227981 318 AQEA 321
Cdd:COG3588 288 AQAI 291
 
Name Accession Description Interval E-value
PLN02455 PLN02455
fructose-bisphosphate aldolase
 1-358 0e+00

fructose-bisphosphate aldolase


Pssm-ID: 178074  Cd Length: 358  Bit Score: 759.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981    1 MSSFTSKFADELIANAAYIGTPGKGILAADESTGTIGKRLASINVENVESNRRALRELLFTTPGALPCLSGVILFEETLY 80
Cdd:PLN02455   1 MSAFVGKYADELIKNAKYIATPGKGILAADESTGTIGKRLASINVENVESNRQALRELLFTAPGALQYLSGVILFEETLY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981   81 QKSSDGTPFVDMLKSAGVLPGIKVDKGTVELAGTNGETTTQGLDGLGDRCKKYYEAGARFAKWRAVLKIGVNEPSQLAIH 160
Cdd:PLN02455  81 QKTSDGKPFVDVLKENGVLPGIKVDKGTVELAGTNGETTTQGLDGLGARCAKYYEAGARFAKWRAVLKIGPTEPSELAIQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981  161 ENAYGLARYAVICQENGLVPIVEPEILVDGSHDIQKCAAVTERVLAACYKALSDHHVLLEGTLLKPNMVTPGSESAKVAP 240
Cdd:PLN02455 161 ENAQGLARYAIICQENGLVPIVEPEILVDGSHDIKKCAAVTERVLAACYKALNDHHVLLEGTLLKPNMVTPGSDSPKVSP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981  241 EVIAEHTVRALQRTVPAAVPAIVFLSGGQSEEEATRNLNAMNQLKTKKPWSLSFSFGRALQQSTLKTWGGKEENVKKAQE 320
Cdd:PLN02455 241 EVIAEYTVRALQRTVPPAVPGIVFLSGGQSEEEATLNLNAMNKLKTLKPWTLSFSFGRALQQSTLKAWAGKKENVAKAQA 320

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 15227981  321 AFLVRCKANSEATLGAYKGDAKLGEGAAESLHVKDYKY 358
Cdd:PLN02455 321 AFLVRCKANSEATLGKYKGDAAGGEGASESLHVKDYKY 358
Glycolytic pfam00274
Fructose-bisphosphate aldolase class-I;
11-358 0e+00

Fructose-bisphosphate aldolase class-I;


Pssm-ID: 459742  Cd Length: 349  Bit Score: 695.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981    11 ELIANAAYIGTPGKGILAADESTGTIGKRLASINVENVESNRRALRELLFTTPGAL-PCLSGVILFEETLYQKSSDGTPF 89
Cdd:pfam00274   1 ELIATAKAIVAPGKGILAADESTGTIGKRLASIGVENTEENRRAYRQLLFTTDGELgEYISGVILFHETLYQKTDDGKPF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981    90 VDMLKSAGVLPGIKVDKGTVELAGTNGETTTQGLDGLGDRCKKYYEAGARFAKWRAVLKIGVNEPSQLAIHENAYGLARY 169
Cdd:pfam00274  81 VDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQGLDGLAERCAQYYKDGARFAKWRCVLKIGENTPSELAIQENANVLARY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981   170 AVICQENGLVPIVEPEILVDGSHDIQKCAAVTERVLAACYKALSDHHVLLEGTLLKPNMVTPGSES-AKVAPEVIAEHTV 248
Cdd:pfam00274 161 ASICQQNGLVPIVEPEILPDGDHDLERCQKVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTPGADCpKKYTPEEIAEATV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981   249 RALQRTVPAAVPAIVFLSGGQSEEEATRNLNAMNQLKTKKPWSLSFSFGRALQQSTLKTWGGKEENVKKAQEAFLVRCKA 328
Cdd:pfam00274 241 TALRRTVPPAVPGVTFLSGGQSEEEATVNLNAINKLPLKKPWALTFSYGRALQASVLKAWGGKKENVKAAQEELLKRAKA 320

                         330       340       350
                  ....*....|....*....|....*....|
gi 15227981   329 NSEATLGAYKGDAKlGEGAAESLHVKDYKY 358
Cdd:pfam00274 321 NSLASLGKYVGGVE-GAAASESLFVANYAY 349
FBP_aldolase_I_a cd00948
Fructose-1,6-bisphosphate aldolase; Fructose-1,6-bisphosphate aldolase. The enzyme catalyzes ...
 9-337 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: 647.00  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981   9 ADELIANAAYIGTPGKGILAADESTGTIGKRLASINVENVESNRRALRELLFTTPGALPCLSGVILFEETLYQKSSDGTP 88
Cdd:cd00948   1 KEELIKTAKAIVAPGKGILAADESTGTIGKRFASIGVENTEENRRAYRELLFTTPGLGQYISGVILFEETLYQKTDDGKP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981  89 FVDMLKSAGVLPGIKVDKGTVELAGTNGETTTQGLDGLGDRCKKYYEAGARFAKWRAVLKIGVNEPSQLAIHENAYGLAR 168
Cdd:cd00948  81 FVDILKEKGIVPGIKVDKGLVPLAGTDGETTTQGLDGLAERCAKYYKQGARFAKWRAVLKIGNGTPSELAIKENAHGLAR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981 169 YAVICQENGLVPIVEPEILVDGSHDIQKCAAVTERVLAACYKALSDHHVLLEGTLLKPNMVTPGSESA-KVAPEVIAEHT 247
Cdd:cd00948 161 YAAICQENGLVPIVEPEVLMDGDHDIERCQEVTEKVLAAVYKALNDHHVLLEGTLLKPNMVTPGADCKkKASPEEVAEYT 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981 248 VRALQRTVPAAVPAIVFLSGGQSEEEATRNLNAMNQLKTKKPWSLSFSFGRALQQSTLKTWGGKEENVKKAQEAFLVRCK 327
Cdd:cd00948 241 VRALRRTVPAAVPGIVFLSGGQSEEEATLNLNAMNKLPLPKPWALSFSYGRALQASALKAWGGKKENVEAAQKALLKRAK 320

                       330
                ....*....|
gi 15227981 328 ANSEATLGAY 337
Cdd:cd00948 321 ANSLAALGKY 330
PTZ00019 PTZ00019
fructose-bisphosphate aldolase; Provisional
 6-358 0e+00

fructose-bisphosphate aldolase; Provisional


Pssm-ID: 240231  Cd Length: 355  Bit Score: 595.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981    6 SKFADELIANAAYIGTPGKGILAADESTGTIGKRLASINVENVESNRRALRELLFTTPGALPCLSGVILFEETLYQKSSD 85
Cdd:PTZ00019   1 TEYAKELAETAKKIAAPGKGILAADESTGTIKKRFDPIGLENTEENRRAYRELLFTTEGLEQYISGVILFEETVYQKAPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981   86 GTPFVDMLKSAGVLPGIKVDKGTVELAGTNGETTTQGLDGLGDRCKKYYEAGARFAKWRAVLKIGV--NEPSQLAIHENA 163
Cdd:PTZ00019  81 GKTFVELLKEKGIVPGIKVDKGLVTLPGTDGETSTQGLDGLAERAKKYYKAGARFAKWRAVLKIDPakGKPSELAIQENA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981  164 YGLARYAVICQENGLVPIVEPEILVDGSHDIQKCAAVTERVLAACYKALSDHHVLLEGTLLKPNMVTPGSESA-KVAPEV 242
Cdd:PTZ00019 161 WTLARYAAICQENGLVPIVEPEILIDGSHSIEVCQKVTEKVLAEVFKALNDHGVLLEGCLLKPNMVTPGSDCGvKATPQE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981  243 IAEHTVRALQRTVPAAVPAIVFLSGGQSEEEATRNLNAMNQLKTKKPWSLSFSFGRALQQSTLKTWGGKEENVKKAQEAF 322
Cdd:PTZ00019 241 VAFYTVRTLSRTVPPALPGVMFLSGGQSEEEASLNLNAMNKLTLPRPWALSFSYGRALQSSALKTWKGKDENVAAAQKAL 320

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 15227981  323 LVRCKANSEATLGAYKGdAKLGEGAAESLHVKDYKY 358
Cdd:PTZ00019 321 LHRAKANSLAQLGKYKG-GDGGAAASESLYVKDYKY 355
FrucBisAld_I NF033379
fructose-bisphosphate aldolase class I; This family consists of fructose-bisphosphate aldolase ...
 11-334 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: 549.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981   11 ELIANAAYIGTPGKGILAADESTGTIGKRLASINVENVESNRRALRELLFTTPGALPCLSGVILFEETLYQKSSDGTPFV 90
Cdd:NF033379   1 ELEETAQAMVAPGKGILAADESTGTINKRFEAIGVESTEENRRAYRELLFTTPGLGDYISGVILFDETIRQKTADGTPFP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981   91 DMLKSAGVLPGIKVDKGTVELAGTNGETTTQGLDGLGDRCKKYYEAGARFAKWRAVLKIGVNEPSQLAIHENAYGLARYA 170
Cdd:NF033379  81 KVLADAGIIPGIKVDKGAKPLAGFPGEKVTEGLDGLRERLAEYYELGARFAKWRAVITIGDGIPSRACIEANAHALARYA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981  171 VICQENGLVPIVEPEILVDGSHDIQKCAAVTERVLAACYKALSDHHVLLEGTLLKPNMVTPGSESA-KVAPEVIAEHTVR 249
Cdd:NF033379 161 ALCQEAGLVPIVEPEVLMDGDHSIERCAEVTEEVLKEVFEELYRQGVDLEGMILKPNMVLPGKDCPdQASPEEVAEATVR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981  250 ALQRTVPAAVPAIVFLSGGQSEEEATRNLNAMNQLKtKKPWSLSFSFGRALQQSTLKTWGGKEENVKKAQEAFLVRCKAN 329
Cdd:NF033379 241 CLRRTVPAAVPGIAFLSGGQSDEEATAHLNAMNKLG-PLPWPLTFSYGRALQQPALKAWGGKAENVAAAQKALLHRARMN 319


                 ....*
gi 15227981  330 SEATL 334
Cdd:NF033379 320 SLAAL 324
PLN02425 PLN02425
probable fructose-bisphosphate aldolase
 6-358 1.32e-157

probable fructose-bisphosphate aldolase


Pssm-ID: 215234  Cd Length: 390  Bit Score: 447.54  E-value: 1.32e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981    6 SKFADELIANAAYIGTPGKGILAADESTGTIGKRLASINVENVESNRRALRELLFTTPGALPCLSGVILFEETLYQKSSD 85
Cdd:PLN02425  41 GSYSDELVQTAKSVASPGRGILAIDESNATCGKRLASIGLDNTETNRQAYRQLLLTTPGLGEYISGAILFEETLYQSTTD 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981   86 GTPFVDMLKSAGVLPGIKVDKGTVELAGTNGETTTQGLDGLGDRCKKYYEAGARFAKWRAVLKIGVNePSQLAIHENAYG 165
Cdd:PLN02425 121 GKKFVDCLRDQNIVPGIKVDKGLVPLPGSNNESWCQGLDGLASRSAEYYKQGARFAKWRTVVSIPCG-PSALAVKEAAWG 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981  166 LARYAVICQENGLVPIVEPEILVDGSHDIQKCAAVTERVLAACYKALSDHHVLLEGTLLKPNMVTPGSE-SAKVAPEVIA 244
Cdd:PLN02425 200 LARYAAISQDNGLVPIVEPEILLDGDHPIERTLEVAEKVWSEVFFYLAQNNVLFEGILLKPSMVTPGAEhKEKASPETIA 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981  245 EHTVRALQRTVPAAVPAIVFLSGGQSEEEATRNLNAMNQlkTKKPWSLSFSFGRALQQSTLKTWGGKEENVKKAQEAFLV 324
Cdd:PLN02425 280 KYTLTMLRRRVPPAVPGIMFLSGGQSEVEATLNLNAMNQ--SPNPWHVSFSYARALQNSVLKTWQGRPENVEAAQKALLV 357

                        330       340       350
                 ....*....|....*....|....*....|....
gi 15227981  325 RCKANSEATLGAYKGDAKlGEGAAESLHVKDYKY 358
Cdd:PLN02425 358 RAKANSLAQLGRYSAEGE-SEEAKKGMFVKGYTY 390
PLN02227 PLN02227
fructose-bisphosphate aldolase I
 6-358 5.18e-132

fructose-bisphosphate aldolase I


Pssm-ID: 177872  Cd Length: 399  Bit Score: 382.99  E-value: 5.18e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981    6 SKFADELIANAAYIGTPGKGILAADESTGTIGKRLASINVENVESNRRALRELLFTTPGALPCLSGVILFEETLYQKSSD 85
Cdd:PLN02227  50 SAYADELVKTAKTIASPGHGIMAMDESNATCGKRLASIGLENTEANRQAYRTLLVSAPGLGQYISGAILFEETLYQSTTD 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981   86 GTPFVDMLKSAGVLPGIKVDKGTVELAGTNGETTTQGLDGLGDRCKKYYEAGARFAKWRAVLKIGvNEPSQLAIHENAYG 165
Cdd:PLN02227 130 GKKMVDVLVEQNIVPGIKVDKGLVPLVGSYDESWCQGLDGLASRTAAYYQQGARFAKWRTVVSIP-NGPSALAVKEAAWG 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981  166 LARYAVICQENGLVPIVEPEILVDGSHDIQKCAAVTERVLAACYKALSDHHVLLEGTLLKPNMVTPGSESA-KVAPEVIA 244
Cdd:PLN02227 209 LARYAAISQDSGLVPIVEPEIMLDGEHGIDRTYDVAEKVWAEVFFYLAQNNVMFEGILLKPSMVTPGAEATdRATPEQVA 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981  245 EHTVRALQRTVPAAVPAIVFLSGGQSEEEATRNLNAMNQlkTKKPWSLSFSFGRALQQSTLKTWGGKEENVKKAQEAFLV 324
Cdd:PLN02227 289 SYTLKLLRNRIPPAVPGIMFLSGGQSELEATLNLNAMNQ--APNPWHVSFSYARALQNTCLKTWGGKEENVKAAQDILLA 366

                        330       340       350
                 ....*....|....*....|....*....|....
gi 15227981  325 RCKANSEATLGAYKGDAKlGEGAAESLHVKDYKY 358
Cdd:PLN02227 367 RAKANSLAQLGKYTGEGE-SEEAKEGMFVKGYTY 399
FBP_aldolase_I cd00344
Fructose-bisphosphate aldolase class I; Fructose-bisphosphate aldolase class I. Fructose-1, ...
 10-332 3.70e-128

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: 370.29  E-value: 3.70e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981  10 DELIANAAYIGTPGKGILAADESTGTIGKRLASINVENVESNRRALRELLFTTPGAL-PCLSGVILFEETLYQKSSDGTP 88
Cdd:cd00344   2 KELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVnPRIGGVILFHETLYQKADDGRP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981  89 FVDMLKSAGVLPGIKVDKGTVELAGTNGETTTQGLDGLGDRCKKYYEAGARFAKWRAVLKIGVNEPSQLAIHENAYGLAR 168
Cdd:cd00344  82 FPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLAR 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981 169 YAVICQENGLVPIVEPEILVDGSHDIQKCAAVTERVLAACYKALSDHHVLLEGTLLKPNMVTPG-SESAKVAPEVIAEHT 247
Cdd:cd00344 162 YASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGhACTQKFSHEEIAMAT 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981 248 VRALQRTVPAAVPAIVFLSGGQSEEEATRNLNAMNQLKTKKPWSLSFSFGRALQQSTLKTWGGKEENVKKAQEAFLVRCK 327
Cdd:cd00344 242 VTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRAL 321


                ....*
gi 15227981 328 ANSEA 332
Cdd:cd00344 322 ANSLA 326
Fba1 COG3588
Fructose-bisphosphate aldolase class 1 [Carbohydrate transport and metabolism]; ...
 9-321 3.77e-125

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: 361.74  E-value: 3.77e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981   9 ADELIANAAYIGTPGKGILAA-DESTGTIGKRLASINVENVESNRR--------ALRELLFTTPGALP-CLSGVILFEET 78
Cdd:COG3588   2 TEELNATALAMVANGKGFLAAlDQSGGSTPKALAAYGVEETEYSRReemfdlvhAMRERIITSPAFTGdKISGAILFEET 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981  79 LYQKSsDGTP-FVDMLKSAGVLPGIKVDKGTVELAgtNGETTTQGLDGLGDRCKKYYEAGARFAKWRAVLKIGvnepSQL 157
Cdd:COG3588  82 MDQKI-DGTPtFDYLWEKKGIVPGIKVDKGLKDLA--PGVQLMKGLDGLDERLARAKELGAFGTKWRSVIKIA----NAA 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981 158 AIHENAYGLARYAVICQENGLVPIVEPEILVDGSHDIQKCAAVTERVLAACYKALSDHhvllEGTLLKpnMVTPGSESAK 237
Cdd:COG3588 155 GIKANVHQQARYAALCQEAGLVPIVEPEVLIDGDHKIEREAELTEEILKALFDALPED----EGVMLK--MVIPGKDNLY 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981 238 VApevIAEHtvralqrtvpAAVPAIVFLSGGQSEEEATRNLNAMNQlktkkpwsLSFSFGRALQQSTLKTWGGKEENVKK 317
Cdd:COG3588 229 QA---LVEH----------PAVPRVVFLSGGQSREEATAHLNANNG--------LIASFSRALQEGLLAAWSGEEFNAAL 287


                ....
gi 15227981 318 AQEA 321
Cdd:COG3588 288 AQAI 291
FBP_aldolase_I_bact cd00949
Fructose-1.6-bisphosphate aldolase found in gram +/- bacteria; Fructose-1.6-bisphosphate ...
 23-304 4.55e-18

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: 83.23  E-value: 4.55e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981  23 GKGILAA-DESTGTIGKRLASINV-ENVESNRRALRELL------------FTTPGALpclsGVILFEETLYQKSsDGTP 88
Cdd:cd00949  10 GKGFIAAlDQSGGSTPKALAAYGIeEDAYSNEEEMFDLVhemrtriitspaFDGDKIL----GAILFEQTMDREI-EGKP 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981  89 FVDML-KSAGVLPGIKVDKGTVELAgtNGETTTQGLDGLGDRCKKYYEAGARFAKWRAVLKiGVNEPSQLAIHENAYGLA 167
Cdd:cd00949  85 TADYLwEKKQIVPFLKVDKGLAEEK--NGVQLMKPIPNLDELLMRAKEKGVFGTKMRSVIK-EANPKGIAAVVDQQFELA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981 168 RYAVicqENGLVPIVEPEilVD-GSHDIQKCAAVTERVLAACYKALSD-HHVLLEGTL-LKPNMVTPGSESAKVapevia 244
Cdd:cd00949 162 KQIL---SHGLVPIIEPE--VDiHSADKAKCEAILKAEILKHLDKLPEgQQVMLKLTLpTEANFYSELIEHPKV------ 230

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15227981 245 ehtVRalqrtvpaavpaIVFLSGGQSEEEATRNLnamnqlktKKPWSLSFSFGRAL------QQST 304
Cdd:cd00949 231 ---LR------------VVALSGGYSREEANELL--------AKNNGVIASFSRALteglsaDQSD 273
PRK05377 PRK05377
fructose-1,6-bisphosphate aldolase; Reviewed
 71-303 7.67e-13

fructose-1,6-bisphosphate aldolase; Reviewed


Pssm-ID: 180045  Cd Length: 296  Bit Score: 67.98  E-value: 7.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981   71 GVILFEETLYQKSsDGTPFVDML-KSAGVLPGIKVDKGTVELAgtNGETTTQGLDGLGDRCKKYYEAGARFAKWRAVLKi 149
Cdd:PRK05377  71 GAILFEQTMDREI-EGKPTADYLwEKKGVVPFLKVDKGLAEEA--NGVQLMKPIPNLDDLLDRAVEKGIFGTKMRSVIK- 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981  150 gvnepsqlaiHENAYGLAryAVICQ---------ENGLVPIVEPEILVDgSHDIQKCAAVTERVLAACYKALS-DHHVLL 219
Cdd:PRK05377 147 ----------EANEQGIA--AVVAQqfevakqilAAGLVPIIEPEVDIN-SPDKAEAEAILKAEILKQLDALPeDQQVML 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15227981  220 EGTL-LKPNMVTPGSESAKVapeviaehtVRalqrtvpaavpaIVFLSGGQSEEEATRNLnAMNQlktkkpwSLSFSFGR 298
Cdd:PRK05377 214 KLTIpTEANLYKELIDHPRV---------LR------------VVALSGGYSRDEANELL-ARNH-------GLIASFSR 264

                        250
                 ....*....|.
gi 15227981  299 AL------QQS 303
Cdd:PRK05377 265 ALteglsaQQS 275
 
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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