|
Name |
Accession |
Description |
Interval |
E-value |
| Glycolytic |
pfam00274 |
Fructose-bisphosphate aldolase class-I; |
15-363 |
0e+00 |
|
Fructose-bisphosphate aldolase class-I;
Pssm-ID: 459742 Cd Length: 349 Bit Score: 751.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 15 ELSDIALRIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQVLFSADDRVKKCIGGVIFFHETLYQKDDNGVPF 94
Cdd:pfam00274 1 ELIATAKAIVAPGKGILAADESTGTIGKRLASIGVENTEENRRAYRQLLFTTDGELGEYISGVILFHETLYQKTDDGKPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 95 VRTIQEKGILVGIKVDKGVVPLAGTDGETTTQGLDGLLERCAQYKKDGADFAKWRCVLKISDRTPSALAILENANVLARY 174
Cdd:pfam00274 81 VDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQGLDGLAERCAQYYKDGARFAKWRCVLKIGENTPSELAIQENANVLARY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 175 ASICQQNGIVPIVEPEILPDGDHDLKRCQFVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYSPEEIAMATV 254
Cdd:pfam00274 161 ASICQQNGLVPIVEPEILPDGDHDLERCQKVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTPGADCPKKYTPEEIAEATV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 255 TALRRTVPPAVPGVTFLSGGQSEEEASLNLNAINRCSLPRPWALTFSYGRALQASALSAWRGQRDNAGAATEEFIKRAEM 334
Cdd:pfam00274 241 TALRRTVPPAVPGVTFLSGGQSEEEATVNLNAINKLPLKKPWALTFSYGRALQASVLKAWGGKKENVKAAQEELLKRAKA 320
|
330 340
....*....|....*....|....*....
gi 6978489 335 NGLAAQGKYEGSGDGGAAAQSLYVANHAY 363
Cdd:pfam00274 321 NSLASLGKYVGGVEGAAASESLFVANYAY 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 6978489 13 KKELSDIALRIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQVLFSADDRVKkCIGGVIFFHETLYQKDDNGV 92
Cdd:cd00948 1 KEELIKTAKAIVAPGKGILAADESTGTIGKRFASIGVENTEENRRAYRELLFTTPGLGQ-YISGVILFEETLYQKTDDGK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 93 PFVRTIQEKGILVGIKVDKGVVPLAGTDGETTTQGLDGLLERCAQYKKDGADFAKWRCVLKISDRTPSALAILENANVLA 172
Cdd:cd00948 80 PFVDILKEKGIVPGIKVDKGLVPLAGTDGETTTQGLDGLAERCAKYYKQGARFAKWRAVLKIGNGTPSELAIKENAHGLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 173 RYASICQQNGIVPIVEPEILPDGDHDLKRCQFVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYSPEEIAMA 252
Cdd:cd00948 160 RYAAICQENGLVPIVEPEVLMDGDHDIERCQEVTEKVLAAVYKALNDHHVLLEGTLLKPNMVTPGADCKKKASPEEVAEY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 253 TVTALRRTVPPAVPGVTFLSGGQSEEEASLNLNAINRCSLPRPWALTFSYGRALQASALSAWRGQRDNAGAATEEFIKRA 332
Cdd:cd00948 240 TVRALRRTVPAAVPGIVFLSGGQSEEEATLNLNAMNKLPLPKPWALSFSYGRALQASALKAWGGKKENVEAAQKALLKRA 319
|
330
....*....|.
gi 6978489 333 EMNGLAAQGKY 343
Cdd:cd00948 320 KANSLAALGKY 330
|
|
| PTZ00019 |
PTZ00019 |
fructose-bisphosphate aldolase; Provisional |
10-363 |
0e+00 |
|
fructose-bisphosphate aldolase; Provisional
Pssm-ID: 240231 Cd Length: 355 Bit Score: 568.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 10 AEQKKELSDIALRIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQVLFSADDrVKKCIGGVIFFHETLYQKDD 89
Cdd:PTZ00019 1 TEYAKELAETAKKIAAPGKGILAADESTGTIKKRFDPIGLENTEENRRAYRELLFTTEG-LEQYISGVILFEETVYQKAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 90 NGVPFVRTIQEKGILVGIKVDKGVVPLAGTDGETTTQGLDGLLERCAQYKKDGADFAKWRCVLKI--SDRTPSALAILEN 167
Cdd:PTZ00019 80 SGKTFVELLKEKGIVPGIKVDKGLVTLPGTDGETSTQGLDGLAERAKKYYKAGARFAKWRAVLKIdpAKGKPSELAIQEN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 168 ANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQFVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYSPE 247
Cdd:PTZ00019 160 AWTLARYAAICQENGLVPIVEPEILIDGSHSIEVCQKVTEKVLAEVFKALNDHGVLLEGCLLKPNMVTPGSDCGVKATPQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 248 EIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASLNLNAINRCSLPRPWALTFSYGRALQASALSAWRGQRDNAGAATEE 327
Cdd:PTZ00019 240 EVAFYTVRTLSRTVPPALPGVMFLSGGQSEEEASLNLNAMNKLTLPRPWALSFSYGRALQSSALKTWKGKDENVAAAQKA 319
|
330 340 350
....*....|....*....|....*....|....*.
gi 6978489 328 FIKRAEMNGLAAQGKYEGSGDGGAAAQSLYVANHAY 363
Cdd:PTZ00019 320 LLHRAKANSLAQLGKYKGGDGGAAASESLYVKDYKY 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: 522.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 15 ELSDIALRIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQVLFSADDrVKKCIGGVIFFHETLYQKDDNGVPF 94
Cdd:NF033379 1 ELEETAQAMVAPGKGILAADESTGTINKRFEAIGVESTEENRRAYRELLFTTPG-LGDYISGVILFDETIRQKTADGTPF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 95 VRTIQEKGILVGIKVDKGVVPLAGTDGETTTQGLDGLLERCAQYKKDGADFAKWRCVLKISDRTPSALAILENANVLARY 174
Cdd:NF033379 80 PKVLADAGIIPGIKVDKGAKPLAGFPGEKVTEGLDGLRERLAEYYELGARFAKWRAVITIGDGIPSRACIEANAHALARY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 175 ASICQQNGIVPIVEPEILPDGDHDLKRCQFVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYSPEEIAMATV 254
Cdd:NF033379 160 AALCQEAGLVPIVEPEVLMDGDHSIERCAEVTEEVLKEVFEELYRQGVDLEGMILKPNMVLPGKDCPDQASPEEVAEATV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 255 TALRRTVPPAVPGVTFLSGGQSEEEASLNLNAINRCSlPRPWALTFSYGRALQASALSAWRGQRDNAGAATEEFIKRAEM 334
Cdd:NF033379 240 RCLRRTVPAAVPGIAFLSGGQSDEEATAHLNAMNKLG-PLPWPLTFSYGRALQQPALKAWGGKAENVAAAQKALLHRARM 318
|
....*.
gi 6978489 335 NGLAAQ 340
Cdd:NF033379 319 NSLAAL 324
|
|
| Fba1 |
COG3588 |
Fructose-bisphosphate aldolase class 1 [Carbohydrate transport and metabolism]; ... |
13-346 |
8.04e-117 |
|
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: 340.55 E-value: 8.04e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 13 KKELSDIALRIVAPGKGILAA-DESVGSMAKRLSQIGVENTEENRRL--------YRQVLFSADDRVKKCIGGVIFFHET 83
Cdd:COG3588 2 TEELNATALAMVANGKGFLAAlDQSGGSTPKALAAYGVEETEYSRREemfdlvhaMRERIITSPAFTGDKISGAILFEET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 84 LYQKDDnGVP-FVRTIQEKGILVGIKVDKGVVPLAgtDGETTTQGLDGLLERCAQYKKDGADFAKWRCVLKISDRTpsal 162
Cdd:COG3588 82 MDQKID-GTPtFDYLWEKKGIVPGIKVDKGLKDLA--PGVQLMKGLDGLDERLARAKELGAFGTKWRSVIKIANAA---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 163 AILENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQFVTEKVLAAVYKALSDHhvylEGTLLKpnMVTPGHACPI 242
Cdd:COG3588 155 GIKANVHQQARYAALCQEAGLVPIVEPEVLIDGDHKIEREAELTEEILKALFDALPED----EGVMLK--MVIPGKDNLY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 243 KYSPEEiamatvtalrrtvpPAVPGVTFLSGGQSEEEASLNLNAINrcslprpwALTFSYGRALQASALSAWRGQRDNAG 322
Cdd:COG3588 229 QALVEH--------------PAVPRVVFLSGGQSREEATAHLNANN--------GLIASFSRALQEGLLAAWSGEEFNAA 286
|
330 340
....*....|....*....|....
gi 6978489 323 AATeefikraemnglAAQGKYEGS 346
Cdd:COG3588 287 LAQ------------AIDGIYDAS 298
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Glycolytic |
pfam00274 |
Fructose-bisphosphate aldolase class-I; |
15-363 |
0e+00 |
|
Fructose-bisphosphate aldolase class-I;
Pssm-ID: 459742 Cd Length: 349 Bit Score: 751.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 15 ELSDIALRIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQVLFSADDRVKKCIGGVIFFHETLYQKDDNGVPF 94
Cdd:pfam00274 1 ELIATAKAIVAPGKGILAADESTGTIGKRLASIGVENTEENRRAYRQLLFTTDGELGEYISGVILFHETLYQKTDDGKPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 95 VRTIQEKGILVGIKVDKGVVPLAGTDGETTTQGLDGLLERCAQYKKDGADFAKWRCVLKISDRTPSALAILENANVLARY 174
Cdd:pfam00274 81 VDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQGLDGLAERCAQYYKDGARFAKWRCVLKIGENTPSELAIQENANVLARY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 175 ASICQQNGIVPIVEPEILPDGDHDLKRCQFVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYSPEEIAMATV 254
Cdd:pfam00274 161 ASICQQNGLVPIVEPEILPDGDHDLERCQKVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTPGADCPKKYTPEEIAEATV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 255 TALRRTVPPAVPGVTFLSGGQSEEEASLNLNAINRCSLPRPWALTFSYGRALQASALSAWRGQRDNAGAATEEFIKRAEM 334
Cdd:pfam00274 241 TALRRTVPPAVPGVTFLSGGQSEEEATVNLNAINKLPLKKPWALTFSYGRALQASVLKAWGGKKENVKAAQEELLKRAKA 320
|
330 340
....*....|....*....|....*....
gi 6978489 335 NGLAAQGKYEGSGDGGAAAQSLYVANHAY 363
Cdd:pfam00274 321 NSLASLGKYVGGVEGAAASESLFVANYAY 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 6978489 13 KKELSDIALRIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQVLFSADDRVKkCIGGVIFFHETLYQKDDNGV 92
Cdd:cd00948 1 KEELIKTAKAIVAPGKGILAADESTGTIGKRFASIGVENTEENRRAYRELLFTTPGLGQ-YISGVILFEETLYQKTDDGK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 93 PFVRTIQEKGILVGIKVDKGVVPLAGTDGETTTQGLDGLLERCAQYKKDGADFAKWRCVLKISDRTPSALAILENANVLA 172
Cdd:cd00948 80 PFVDILKEKGIVPGIKVDKGLVPLAGTDGETTTQGLDGLAERCAKYYKQGARFAKWRAVLKIGNGTPSELAIKENAHGLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 173 RYASICQQNGIVPIVEPEILPDGDHDLKRCQFVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYSPEEIAMA 252
Cdd:cd00948 160 RYAAICQENGLVPIVEPEVLMDGDHDIERCQEVTEKVLAAVYKALNDHHVLLEGTLLKPNMVTPGADCKKKASPEEVAEY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 253 TVTALRRTVPPAVPGVTFLSGGQSEEEASLNLNAINRCSLPRPWALTFSYGRALQASALSAWRGQRDNAGAATEEFIKRA 332
Cdd:cd00948 240 TVRALRRTVPAAVPGIVFLSGGQSEEEATLNLNAMNKLPLPKPWALSFSYGRALQASALKAWGGKKENVEAAQKALLKRA 319
|
330
....*....|.
gi 6978489 333 EMNGLAAQGKY 343
Cdd:cd00948 320 KANSLAALGKY 330
|
|
| PTZ00019 |
PTZ00019 |
fructose-bisphosphate aldolase; Provisional |
10-363 |
0e+00 |
|
fructose-bisphosphate aldolase; Provisional
Pssm-ID: 240231 Cd Length: 355 Bit Score: 568.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 10 AEQKKELSDIALRIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQVLFSADDrVKKCIGGVIFFHETLYQKDD 89
Cdd:PTZ00019 1 TEYAKELAETAKKIAAPGKGILAADESTGTIKKRFDPIGLENTEENRRAYRELLFTTEG-LEQYISGVILFEETVYQKAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 90 NGVPFVRTIQEKGILVGIKVDKGVVPLAGTDGETTTQGLDGLLERCAQYKKDGADFAKWRCVLKI--SDRTPSALAILEN 167
Cdd:PTZ00019 80 SGKTFVELLKEKGIVPGIKVDKGLVTLPGTDGETSTQGLDGLAERAKKYYKAGARFAKWRAVLKIdpAKGKPSELAIQEN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 168 ANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQFVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYSPE 247
Cdd:PTZ00019 160 AWTLARYAAICQENGLVPIVEPEILIDGSHSIEVCQKVTEKVLAEVFKALNDHGVLLEGCLLKPNMVTPGSDCGVKATPQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 248 EIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASLNLNAINRCSLPRPWALTFSYGRALQASALSAWRGQRDNAGAATEE 327
Cdd:PTZ00019 240 EVAFYTVRTLSRTVPPALPGVMFLSGGQSEEEASLNLNAMNKLTLPRPWALSFSYGRALQSSALKTWKGKDENVAAAQKA 319
|
330 340 350
....*....|....*....|....*....|....*.
gi 6978489 328 FIKRAEMNGLAAQGKYEGSGDGGAAAQSLYVANHAY 363
Cdd:PTZ00019 320 LLHRAKANSLAQLGKYKGGDGGAAASESLYVKDYKY 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: 522.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 15 ELSDIALRIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQVLFSADDrVKKCIGGVIFFHETLYQKDDNGVPF 94
Cdd:NF033379 1 ELEETAQAMVAPGKGILAADESTGTINKRFEAIGVESTEENRRAYRELLFTTPG-LGDYISGVILFDETIRQKTADGTPF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 95 VRTIQEKGILVGIKVDKGVVPLAGTDGETTTQGLDGLLERCAQYKKDGADFAKWRCVLKISDRTPSALAILENANVLARY 174
Cdd:NF033379 80 PKVLADAGIIPGIKVDKGAKPLAGFPGEKVTEGLDGLRERLAEYYELGARFAKWRAVITIGDGIPSRACIEANAHALARY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 175 ASICQQNGIVPIVEPEILPDGDHDLKRCQFVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYSPEEIAMATV 254
Cdd:NF033379 160 AALCQEAGLVPIVEPEVLMDGDHSIERCAEVTEEVLKEVFEELYRQGVDLEGMILKPNMVLPGKDCPDQASPEEVAEATV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 255 TALRRTVPPAVPGVTFLSGGQSEEEASLNLNAINRCSlPRPWALTFSYGRALQASALSAWRGQRDNAGAATEEFIKRAEM 334
Cdd:NF033379 240 RCLRRTVPAAVPGIAFLSGGQSDEEATAHLNAMNKLG-PLPWPLTFSYGRALQQPALKAWGGKAENVAAAQKALLHRARM 318
|
....*.
gi 6978489 335 NGLAAQ 340
Cdd:NF033379 319 NSLAAL 324
|
|
| PLN02455 |
PLN02455 |
fructose-bisphosphate aldolase |
7-363 |
9.40e-180 |
|
fructose-bisphosphate aldolase
Pssm-ID: 178074 Cd Length: 358 Bit Score: 502.36 E-value: 9.40e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 7 ALSAEQKKELSDIALRIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQVLFSADDrVKKCIGGVIFFHETLYQ 86
Cdd:PLN02455 3 AFVGKYADELIKNAKYIATPGKGILAADESTGTIGKRLASINVENVESNRQALRELLFTAPG-ALQYLSGVILFEETLYQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 87 KDDNGVPFVRTIQEKGILVGIKVDKGVVPLAGTDGETTTQGLDGLLERCAQYKKDGADFAKWRCVLKISDRTPSALAILE 166
Cdd:PLN02455 82 KTSDGKPFVDVLKENGVLPGIKVDKGTVELAGTNGETTTQGLDGLGARCAKYYEAGARFAKWRAVLKIGPTEPSELAIQE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 167 NANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQFVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPiKYSP 246
Cdd:PLN02455 162 NAQGLARYAIICQENGLVPIVEPEILVDGSHDIKKCAAVTERVLAACYKALNDHHVLLEGTLLKPNMVTPGSDSP-KVSP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 247 EEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASLNLNAINRCSLPRPWALTFSYGRALQASALSAWRGQRDNAGAATE 326
Cdd:PLN02455 241 EVIAEYTVRALQRTVPPAVPGIVFLSGGQSEEEATLNLNAMNKLKTLKPWTLSFSFGRALQQSTLKAWAGKKENVAKAQA 320
|
330 340 350
....*....|....*....|....*....|....*...
gi 6978489 327 EFIKRAEMNGLAAQGKYEGSGDGG-AAAQSLYVANHAY 363
Cdd:PLN02455 321 AFLVRCKANSEATLGKYKGDAAGGeGASESLHVKDYKY 358
|
|
| FBP_aldolase_I |
cd00344 |
Fructose-bisphosphate aldolase class I; Fructose-bisphosphate aldolase class I. Fructose-1, ... |
13-340 |
1.65e-178 |
|
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: 498.17 E-value: 1.65e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 13 KKELSDIALRIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQVLFSADDRVKKCIGGVIFFHETLYQKDDNGV 92
Cdd:cd00344 1 KKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPRIGGVILFHETLYQKADDGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 93 PFVRTIQEKGILVGIKVDKGVVPLAGTDGETTTQGLDGLLERCAQYKKDGADFAKWRCVLKISDRTPSALAILENANVLA 172
Cdd:cd00344 81 PFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 173 RYASICQQNGIVPIVEPEILPDGDHDLKRCQFVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYSPEEIAMA 252
Cdd:cd00344 161 RYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKFSHEEIAMA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 253 TVTALRRTVPPAVPGVTFLSGGQSEEEASLNLNAINRCSLPRPWALTFSYGRALQASALSAWRGQRDNAGAATEEFIKRA 332
Cdd:cd00344 241 TVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRA 320
|
....*...
gi 6978489 333 EMNGLAAQ 340
Cdd:cd00344 321 LANSLAAQ 328
|
|
| PLN02425 |
PLN02425 |
probable fructose-bisphosphate aldolase |
4-363 |
4.23e-136 |
|
probable fructose-bisphosphate aldolase
Pssm-ID: 215234 Cd Length: 390 Bit Score: 393.23 E-value: 4.23e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 4 SYPALSAEQKKELSDIALRIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQVLFSADDrVKKCIGGVIFFHET 83
Cdd:PLN02425 35 SFRIRAGSYSDELVQTAKSVASPGRGILAIDESNATCGKRLASIGLDNTETNRQAYRQLLLTTPG-LGEYISGAILFEET 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 84 LYQKDDNGVPFVRTIQEKGILVGIKVDKGVVPLAGTDGETTTQGLDGLLERCAQYKKDGADFAKWRCVLKISdRTPSALA 163
Cdd:PLN02425 114 LYQSTTDGKKFVDCLRDQNIVPGIKVDKGLVPLPGSNNESWCQGLDGLASRSAEYYKQGARFAKWRTVVSIP-CGPSALA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 164 ILENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQFVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIK 243
Cdd:PLN02425 193 VKEAAWGLARYAAISQDNGLVPIVEPEILLDGDHPIERTLEVAEKVWSEVFFYLAQNNVLFEGILLKPSMVTPGAEHKEK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 244 YSPEEIAMATVTALRRTVPPAVPGVTFLSGGQSEEEASLNLNAINRCslPRPWALTFSYGRALQASALSAWRGQRDNAGA 323
Cdd:PLN02425 273 ASPETIAKYTLTMLRRRVPPAVPGIMFLSGGQSEVEATLNLNAMNQS--PNPWHVSFSYARALQNSVLKTWQGRPENVEA 350
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 6978489 324 ATEEFIKRAEMNGLAAQGKYEGSGDGGAAAQSLYVANHAY 363
Cdd:PLN02425 351 AQKALLVRAKANSLAQLGRYSAEGESEEAKKGMFVKGYTY 390
|
|
| Fba1 |
COG3588 |
Fructose-bisphosphate aldolase class 1 [Carbohydrate transport and metabolism]; ... |
13-346 |
8.04e-117 |
|
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: 340.55 E-value: 8.04e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 13 KKELSDIALRIVAPGKGILAA-DESVGSMAKRLSQIGVENTEENRRL--------YRQVLFSADDRVKKCIGGVIFFHET 83
Cdd:COG3588 2 TEELNATALAMVANGKGFLAAlDQSGGSTPKALAAYGVEETEYSRREemfdlvhaMRERIITSPAFTGDKISGAILFEET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 84 LYQKDDnGVP-FVRTIQEKGILVGIKVDKGVVPLAgtDGETTTQGLDGLLERCAQYKKDGADFAKWRCVLKISDRTpsal 162
Cdd:COG3588 82 MDQKID-GTPtFDYLWEKKGIVPGIKVDKGLKDLA--PGVQLMKGLDGLDERLARAKELGAFGTKWRSVIKIANAA---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 163 AILENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQFVTEKVLAAVYKALSDHhvylEGTLLKpnMVTPGHACPI 242
Cdd:COG3588 155 GIKANVHQQARYAALCQEAGLVPIVEPEVLIDGDHKIEREAELTEEILKALFDALPED----EGVMLK--MVIPGKDNLY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 243 KYSPEEiamatvtalrrtvpPAVPGVTFLSGGQSEEEASLNLNAINrcslprpwALTFSYGRALQASALSAWRGQRDNAG 322
Cdd:COG3588 229 QALVEH--------------PAVPRVVFLSGGQSREEATAHLNANN--------GLIASFSRALQEGLLAAWSGEEFNAA 286
|
330 340
....*....|....*....|....
gi 6978489 323 AATeefikraemnglAAQGKYEGS 346
Cdd:COG3588 287 LAQ------------AIDGIYDAS 298
|
|
| PLN02227 |
PLN02227 |
fructose-bisphosphate aldolase I |
15-363 |
5.86e-112 |
|
fructose-bisphosphate aldolase I
Pssm-ID: 177872 Cd Length: 399 Bit Score: 332.15 E-value: 5.86e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 15 ELSDIALRIVAPGKGILAADESVGSMAKRLSQIGVENTEENRRLYRQVLFSADDrVKKCIGGVIFFHETLYQKDDNGVPF 94
Cdd:PLN02227 55 ELVKTAKTIASPGHGIMAMDESNATCGKRLASIGLENTEANRQAYRTLLVSAPG-LGQYISGAILFEETLYQSTTDGKKM 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 95 VRTIQEKGILVGIKVDKGVVPLAGTDGETTTQGLDGLLERCAQYKKDGADFAKWRCVLKISDrTPSALAILENANVLARY 174
Cdd:PLN02227 134 VDVLVEQNIVPGIKVDKGLVPLVGSYDESWCQGLDGLASRTAAYYQQGARFAKWRTVVSIPN-GPSALAVKEAAWGLARY 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 175 ASICQQNGIVPIVEPEILPDGDHDLKRCQFVTEKVLAAVYKALSDHHVYLEGTLLKPNMVTPGHACPIKYSPEEIAMATV 254
Cdd:PLN02227 213 AAISQDSGLVPIVEPEIMLDGEHGIDRTYDVAEKVWAEVFFYLAQNNVMFEGILLKPSMVTPGAEATDRATPEQVASYTL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 255 TALRRTVPPAVPGVTFLSGGQSEEEASLNLNAINRCslPRPWALTFSYGRALQASALSAWRGQRDNAGAATEEFIKRAEM 334
Cdd:PLN02227 293 KLLRNRIPPAVPGIMFLSGGQSELEATLNLNAMNQA--PNPWHVSFSYARALQNTCLKTWGGKEENVKAAQDILLARAKA 370
|
330 340
....*....|....*....|....*....
gi 6978489 335 NGLAAQGKYEGSGDGGAAAQSLYVANHAY 363
Cdd:PLN02227 371 NSLAQLGKYTGEGESEEAKEGMFVKGYTY 399
|
|
| FBP_aldolase_I_bact |
cd00949 |
Fructose-1.6-bisphosphate aldolase found in gram +/- bacteria; Fructose-1.6-bisphosphate ... |
21-346 |
4.84e-09 |
|
Fructose-1.6-bisphosphate aldolase found in gram +/- bacteria; Fructose-1.6-bisphosphate aldolase found in gram +/- bacteria. The enzyme catalyzes the cleavage of fructose 1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate (DHAP). The enzyme is member of the class I aldolase family, which utilizes covalent catalysis through a Schiff base formed between a lysine residue of the enzyme and ketose substrates.
Pssm-ID: 188636 Cd Length: 292 Bit Score: 56.65 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 21 LRIVAPGKGILAA-DESVGSMAKRLSQIGVE-----NTEE--------NRRLYRQVLFSADDrvkkcIGGVIFFHETLYQ 86
Cdd:cd00949 4 LERMKSGKGFIAAlDQSGGSTPKALAAYGIEedaysNEEEmfdlvhemRTRIITSPAFDGDK-----ILGAILFEQTMDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 87 KDDnGVPFVR-TIQEKGILVGIKVDKGVVPLA-GTDGETTTQGLDGLLERCAQYKKDGAdfaKWRCVLKisdrtpsalai 164
Cdd:cd00949 79 EIE-GKPTADyLWEKKQIVPFLKVDKGLAEEKnGVQLMKPIPNLDELLMRAKEKGVFGT---KMRSVIK----------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 165 leNANVLARYASICQQ---------NGIVPIVEPEIlpdgdhDLKRCQfvTEKVLAAVYKALSDHhvyLEgTLLKPNMVT 235
Cdd:cd00949 144 --EANPKGIAAVVDQQfelakqilsHGLVPIIEPEV------DIHSAD--KAKCEAILKAEILKH---LD-KLPEGQQVM 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 236 PGHACPIK---YSPeeiamatvtalrRTVPPAVPGVTFLSGGQSEEEASlNLNAINRcslprpwALTFSYGRALqASALS 312
Cdd:cd00949 210 LKLTLPTEanfYSE------------LIEHPKVLRVVALSGGYSREEAN-ELLAKNN-------GVIASFSRAL-TEGLS 268
|
330 340 350
....*....|....*....|....*....|....
gi 6978489 313 AwrGQRDnagaatEEFikrAEMNGLAAQGKYEGS 346
Cdd:cd00949 269 A--DQSD------AEF---NATLEKSIDEIYQAS 291
|
|
| PRK05377 |
PRK05377 |
fructose-1,6-bisphosphate aldolase; Reviewed |
24-191 |
6.84e-07 |
|
fructose-1,6-bisphosphate aldolase; Reviewed
Pssm-ID: 180045 Cd Length: 296 Bit Score: 50.26 E-value: 6.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 24 VAPGKGILAA-DESVGSMAKRLSQIGVENTEenrrlyrqvlFSADD-----------RVKKC-------IGGVIFFHETL 84
Cdd:PRK05377 10 MKNGKGFIAAlDQSGGSTPKALKLYGVEEDA----------YSNEEemfdlvhemrtRIITSpaftgdkILGAILFEQTM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6978489 85 YQKDDnGVPFV-RTIQEKGILVGIKVDKGVVPLAgtDGettTQ------GLDGLLERCAQYKKDGAdfaKWRCVLKISDR 157
Cdd:PRK05377 80 DREIE-GKPTAdYLWEKKGVVPFLKVDKGLAEEA--NG---VQlmkpipNLDDLLDRAVEKGIFGT---KMRSVIKEANE 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 6978489 158 TpsalAIlenANVLARYASICQQ---NGIVPIVEPEI 191
Cdd:PRK05377 151 Q----GI---AAVVAQQFEVAKQilaAGLVPIIEPEV 180
|
|
| |
