|
Name |
Accession |
Description |
Interval |
E-value |
| Glycolytic |
pfam00274 |
Fructose-bisphosphate aldolase class-I; |
15-357 |
0e+00 |
|
Fructose-bisphosphate aldolase class-I;
Pssm-ID: 459742 Cd Length: 349 Bit Score: 663.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 15 ELICISKALVAPGKGILAADESSAVMGKRFQLIGVENTEENRRLYRQMLFTTDPKIAENISGVIFYHETLHQRTDDGLPF 94
Cdd:pfam00274 1 ELIATAKAIVAPGKGILAADESTGTIGKRLASIGVENTEENRRAYRQLLFTTDGELGEYISGVILFHETLYQKTDDGKPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 95 VEALRKKGILTGIKVDKHFSPLFGSEDEFTTQGLDDLANRCAQYKKEGCSFAKWRCILKITKNTPSPQAILENANVMARY 174
Cdd:pfam00274 81 VDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQGLDGLAERCAQYYKDGARFAKWRCVLKIGENTPSELAIQENANVLARY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 175 AAICQSQRLVPIISPEVLATGDHDLDRCQKVNEILLAGVYKALSDHHVFLEGTLLQPSMVMPGLQSNKNHPPADIGVATV 254
Cdd:pfam00274 161 ASICQQNGLVPIVEPEILPDGDHDLERCQKVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTPGADCPKKYTPEEIAEATV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 255 LAIRRSVPPAVMGVLFCGGAQSEEEATVHLNAINNVPLCKPWAMTFAFDRALQTSILRTWGGKKEQISHAQNELIKRCRA 334
Cdd:pfam00274 241 TALRRTVPPAVPGVTFLSGGQSEEEATVNLNAINKLPLKKPWALTFSYGRALQASVLKAWGGKKENVKAAQEELLKRAKA 320
|
330 340
....*....|....*....|...
gi 386766548 335 NGLASIGKYViGSVESSAATERL 357
Cdd:pfam00274 321 NSLASLGKYV-GGVEGAAASESL 342
|
|
| FBP_aldolase_I_a |
cd00948 |
Fructose-1,6-bisphosphate aldolase; Fructose-1,6-bisphosphate aldolase. The enzyme catalyzes ... |
14-343 |
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: 534.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 14 EELICISKALVAPGKGILAADESSAVMGKRFQLIGVENTEENRRLYRQMLFTTdPKIAENISGVIFYHETLHQRTDDGLP 93
Cdd:cd00948 2 EELIKTAKAIVAPGKGILAADESTGTIGKRFASIGVENTEENRRAYRELLFTT-PGLGQYISGVILFEETLYQKTDDGKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 94 FVEALRKKGILTGIKVDKHFSPLFGSEDEFTTQGLDDLANRCAQYKKEGCSFAKWRCILKITKNTPSPQAILENANVMAR 173
Cdd:cd00948 81 FVDILKEKGIVPGIKVDKGLVPLAGTDGETTTQGLDGLAERCAKYYKQGARFAKWRAVLKIGNGTPSELAIKENAHGLAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 174 YAAICQSQRLVPIISPEVLATGDHDLDRCQKVNEILLAGVYKALSDHHVFLEGTLLQPSMVMPGLQSNKNHPPADIGVAT 253
Cdd:cd00948 161 YAAICQENGLVPIVEPEVLMDGDHDIERCQEVTEKVLAAVYKALNDHHVLLEGTLLKPNMVTPGADCKKKASPEEVAEYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 254 VLAIRRSVPPAVMGVLFCGGAQSEEEATVHLNAINNVPLCKPWAMTFAFDRALQTSILRTWGGKKEQISHAQNELIKRCR 333
Cdd:cd00948 241 VRALRRTVPAAVPGIVFLSGGQSEEEATLNLNAMNKLPLPKPWALSFSYGRALQASALKAWGGKKENVEAAQKALLKRAK 320
|
330
....*....|
gi 386766548 334 ANGLASIGKY 343
Cdd:cd00948 321 ANSLAALGKY 330
|
|
| PTZ00019 |
PTZ00019 |
fructose-bisphosphate aldolase; Provisional |
11-357 |
1.70e-165 |
|
fructose-bisphosphate aldolase; Provisional
Pssm-ID: 240231 Cd Length: 355 Bit Score: 466.49 E-value: 1.70e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 11 ELQEELICISKALVAPGKGILAADESSAVMGKRFQLIGVENTEENRRLYRQMLFTTdPKIAENISGVIFYHETLHQRTDD 90
Cdd:PTZ00019 2 EYAKELAETAKKIAAPGKGILAADESTGTIKKRFDPIGLENTEENRRAYRELLFTT-EGLEQYISGVILFEETVYQKAPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 91 GLPFVEALRKKGILTGIKVDKHFSPLFGSEDEFTTQGLDDLANRCAQYKKEGCSFAKWRCILKI--TKNTPSPQAILENA 168
Cdd:PTZ00019 81 GKTFVELLKEKGIVPGIKVDKGLVTLPGTDGETSTQGLDGLAERAKKYYKAGARFAKWRAVLKIdpAKGKPSELAIQENA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 169 NVMARYAAICQSQRLVPIISPEVLATGDHDLDRCQKVNEILLAGVYKALSDHHVFLEGTLLQPSMVMPGLQSNKNHPPAD 248
Cdd:PTZ00019 161 WTLARYAAICQENGLVPIVEPEILIDGSHSIEVCQKVTEKVLAEVFKALNDHGVLLEGCLLKPNMVTPGSDCGVKATPQE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 249 IGVATVLAIRRSVPPAVMGVLFCGGAQSEEEATVHLNAINNVPLCKPWAMTFAFDRALQTSILRTWGGKKEQISHAQNEL 328
Cdd:PTZ00019 241 VAFYTVRTLSRTVPPALPGVMFLSGGQSEEEASLNLNAMNKLTLPRPWALSFSYGRALQSSALKTWKGKDENVAAAQKAL 320
|
330 340
....*....|....*....|....*....
gi 386766548 329 IKRCRANGLASIGKYViGSVESSAATERL 357
Cdd:PTZ00019 321 LHRAKANSLAQLGKYK-GGDGGAAASESL 348
|
|
| FrucBisAld_I |
NF033379 |
fructose-bisphosphate aldolase class I; This family consists of fructose-bisphosphate aldolase ... |
15-339 |
8.51e-160 |
|
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: 450.47 E-value: 8.51e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 15 ELICISKALVAPGKGILAADESSAVMGKRFQLIGVENTEENRRLYRQMLFTTdPKIAENISGVIFYHETLHQRTDDGLPF 94
Cdd:NF033379 1 ELEETAQAMVAPGKGILAADESTGTINKRFEAIGVESTEENRRAYRELLFTT-PGLGDYISGVILFDETIRQKTADGTPF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 95 VEALRKKGILTGIKVDKHFSPLFGSEDEFTTQGLDDLANRCAQYKKEGCSFAKWRCILKITKNTPSPQAILENANVMARY 174
Cdd:NF033379 80 PKVLADAGIIPGIKVDKGAKPLAGFPGEKVTEGLDGLRERLAEYYELGARFAKWRAVITIGDGIPSRACIEANAHALARY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 175 AAICQSQRLVPIISPEVLATGDHDLDRCQKVNEILLAGVYKALSDHHVFLEGTLLQPSMVMPGLQSNKNHPPADIGVATV 254
Cdd:NF033379 160 AALCQEAGLVPIVEPEVLMDGDHSIERCAEVTEEVLKEVFEELYRQGVDLEGMILKPNMVLPGKDCPDQASPEEVAEATV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 255 LAIRRSVPPAVMGVLFCGGAQSEEEATVHLNAINNVPLCkPWAMTFAFDRALQTSILRTWGGKKEQISHAQNELIKRCRA 334
Cdd:NF033379 240 RCLRRTVPAAVPGIAFLSGGQSDEEATAHLNAMNKLGPL-PWPLTFSYGRALQQPALKAWGGKAENVAAAQKALLHRARM 318
|
....*
gi 386766548 335 NGLAS 339
Cdd:NF033379 319 NSLAA 323
|
|
| Fba1 |
COG3588 |
Fructose-bisphosphate aldolase class 1 [Carbohydrate transport and metabolism]; ... |
13-326 |
1.68e-91 |
|
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: 276.22 E-value: 1.68e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 13 QEELICISKALVAPGKGILAA-DESSAVMGKRFQLIGVENTEENRRL--------YRQMLFTTDPKIAENISGVIFYHET 83
Cdd:COG3588 2 TEELNATALAMVANGKGFLAAlDQSGGSTPKALAAYGVEETEYSRREemfdlvhaMRERIITSPAFTGDKISGAILFEET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 84 LHQRTDDGLPFVEALRKKGILTGIKVDKHFSPLfgSEDEFTTQGLDDLANRCAQYKKEGCSFAKWRCILKItkntPSPQA 163
Cdd:COG3588 82 MDQKIDGTPTFDYLWEKKGIVPGIKVDKGLKDL--APGVQLMKGLDGLDERLARAKELGAFGTKWRSVIKI----ANAAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 164 ILENANVMARYAAICQSQRLVPIISPEVLATGDHDLDRCQKVNEILLAGVYKALSDHhvflEGTLLQpsMVMPGlqsnKN 243
Cdd:COG3588 156 IKANVHQQARYAALCQEAGLVPIVEPEVLIDGDHKIEREAELTEEILKALFDALPED----EGVMLK--MVIPG----KD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 244 HPPADiGVATvlairrsvpPAVMGVLFCGGAQSEEEATVHLNAINnvplckpwAMTFAFDRALQTSILRTWGGKKEQISH 323
Cdd:COG3588 226 NLYQA-LVEH---------PAVPRVVFLSGGQSREEATAHLNANN--------GLIASFSRALQEGLLAAWSGEEFNAAL 287
|
...
gi 386766548 324 AQN 326
Cdd:COG3588 288 AQA 290
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Glycolytic |
pfam00274 |
Fructose-bisphosphate aldolase class-I; |
15-357 |
0e+00 |
|
Fructose-bisphosphate aldolase class-I;
Pssm-ID: 459742 Cd Length: 349 Bit Score: 663.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 15 ELICISKALVAPGKGILAADESSAVMGKRFQLIGVENTEENRRLYRQMLFTTDPKIAENISGVIFYHETLHQRTDDGLPF 94
Cdd:pfam00274 1 ELIATAKAIVAPGKGILAADESTGTIGKRLASIGVENTEENRRAYRQLLFTTDGELGEYISGVILFHETLYQKTDDGKPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 95 VEALRKKGILTGIKVDKHFSPLFGSEDEFTTQGLDDLANRCAQYKKEGCSFAKWRCILKITKNTPSPQAILENANVMARY 174
Cdd:pfam00274 81 VDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQGLDGLAERCAQYYKDGARFAKWRCVLKIGENTPSELAIQENANVLARY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 175 AAICQSQRLVPIISPEVLATGDHDLDRCQKVNEILLAGVYKALSDHHVFLEGTLLQPSMVMPGLQSNKNHPPADIGVATV 254
Cdd:pfam00274 161 ASICQQNGLVPIVEPEILPDGDHDLERCQKVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTPGADCPKKYTPEEIAEATV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 255 LAIRRSVPPAVMGVLFCGGAQSEEEATVHLNAINNVPLCKPWAMTFAFDRALQTSILRTWGGKKEQISHAQNELIKRCRA 334
Cdd:pfam00274 241 TALRRTVPPAVPGVTFLSGGQSEEEATVNLNAINKLPLKKPWALTFSYGRALQASVLKAWGGKKENVKAAQEELLKRAKA 320
|
330 340
....*....|....*....|...
gi 386766548 335 NGLASIGKYViGSVESSAATERL 357
Cdd:pfam00274 321 NSLASLGKYV-GGVEGAAASESL 342
|
|
| FBP_aldolase_I_a |
cd00948 |
Fructose-1,6-bisphosphate aldolase; Fructose-1,6-bisphosphate aldolase. The enzyme catalyzes ... |
14-343 |
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: 534.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 14 EELICISKALVAPGKGILAADESSAVMGKRFQLIGVENTEENRRLYRQMLFTTdPKIAENISGVIFYHETLHQRTDDGLP 93
Cdd:cd00948 2 EELIKTAKAIVAPGKGILAADESTGTIGKRFASIGVENTEENRRAYRELLFTT-PGLGQYISGVILFEETLYQKTDDGKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 94 FVEALRKKGILTGIKVDKHFSPLFGSEDEFTTQGLDDLANRCAQYKKEGCSFAKWRCILKITKNTPSPQAILENANVMAR 173
Cdd:cd00948 81 FVDILKEKGIVPGIKVDKGLVPLAGTDGETTTQGLDGLAERCAKYYKQGARFAKWRAVLKIGNGTPSELAIKENAHGLAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 174 YAAICQSQRLVPIISPEVLATGDHDLDRCQKVNEILLAGVYKALSDHHVFLEGTLLQPSMVMPGLQSNKNHPPADIGVAT 253
Cdd:cd00948 161 YAAICQENGLVPIVEPEVLMDGDHDIERCQEVTEKVLAAVYKALNDHHVLLEGTLLKPNMVTPGADCKKKASPEEVAEYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 254 VLAIRRSVPPAVMGVLFCGGAQSEEEATVHLNAINNVPLCKPWAMTFAFDRALQTSILRTWGGKKEQISHAQNELIKRCR 333
Cdd:cd00948 241 VRALRRTVPAAVPGIVFLSGGQSEEEATLNLNAMNKLPLPKPWALSFSYGRALQASALKAWGGKKENVEAAQKALLKRAK 320
|
330
....*....|
gi 386766548 334 ANGLASIGKY 343
Cdd:cd00948 321 ANSLAALGKY 330
|
|
| PTZ00019 |
PTZ00019 |
fructose-bisphosphate aldolase; Provisional |
11-357 |
1.70e-165 |
|
fructose-bisphosphate aldolase; Provisional
Pssm-ID: 240231 Cd Length: 355 Bit Score: 466.49 E-value: 1.70e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 11 ELQEELICISKALVAPGKGILAADESSAVMGKRFQLIGVENTEENRRLYRQMLFTTdPKIAENISGVIFYHETLHQRTDD 90
Cdd:PTZ00019 2 EYAKELAETAKKIAAPGKGILAADESTGTIKKRFDPIGLENTEENRRAYRELLFTT-EGLEQYISGVILFEETVYQKAPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 91 GLPFVEALRKKGILTGIKVDKHFSPLFGSEDEFTTQGLDDLANRCAQYKKEGCSFAKWRCILKI--TKNTPSPQAILENA 168
Cdd:PTZ00019 81 GKTFVELLKEKGIVPGIKVDKGLVTLPGTDGETSTQGLDGLAERAKKYYKAGARFAKWRAVLKIdpAKGKPSELAIQENA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 169 NVMARYAAICQSQRLVPIISPEVLATGDHDLDRCQKVNEILLAGVYKALSDHHVFLEGTLLQPSMVMPGLQSNKNHPPAD 248
Cdd:PTZ00019 161 WTLARYAAICQENGLVPIVEPEILIDGSHSIEVCQKVTEKVLAEVFKALNDHGVLLEGCLLKPNMVTPGSDCGVKATPQE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 249 IGVATVLAIRRSVPPAVMGVLFCGGAQSEEEATVHLNAINNVPLCKPWAMTFAFDRALQTSILRTWGGKKEQISHAQNEL 328
Cdd:PTZ00019 241 VAFYTVRTLSRTVPPALPGVMFLSGGQSEEEASLNLNAMNKLTLPRPWALSFSYGRALQSSALKTWKGKDENVAAAQKAL 320
|
330 340
....*....|....*....|....*....
gi 386766548 329 IKRCRANGLASIGKYViGSVESSAATERL 357
Cdd:PTZ00019 321 LHRAKANSLAQLGKYK-GGDGGAAASESL 348
|
|
| FrucBisAld_I |
NF033379 |
fructose-bisphosphate aldolase class I; This family consists of fructose-bisphosphate aldolase ... |
15-339 |
8.51e-160 |
|
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: 450.47 E-value: 8.51e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 15 ELICISKALVAPGKGILAADESSAVMGKRFQLIGVENTEENRRLYRQMLFTTdPKIAENISGVIFYHETLHQRTDDGLPF 94
Cdd:NF033379 1 ELEETAQAMVAPGKGILAADESTGTINKRFEAIGVESTEENRRAYRELLFTT-PGLGDYISGVILFDETIRQKTADGTPF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 95 VEALRKKGILTGIKVDKHFSPLFGSEDEFTTQGLDDLANRCAQYKKEGCSFAKWRCILKITKNTPSPQAILENANVMARY 174
Cdd:NF033379 80 PKVLADAGIIPGIKVDKGAKPLAGFPGEKVTEGLDGLRERLAEYYELGARFAKWRAVITIGDGIPSRACIEANAHALARY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 175 AAICQSQRLVPIISPEVLATGDHDLDRCQKVNEILLAGVYKALSDHHVFLEGTLLQPSMVMPGLQSNKNHPPADIGVATV 254
Cdd:NF033379 160 AALCQEAGLVPIVEPEVLMDGDHSIERCAEVTEEVLKEVFEELYRQGVDLEGMILKPNMVLPGKDCPDQASPEEVAEATV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 255 LAIRRSVPPAVMGVLFCGGAQSEEEATVHLNAINNVPLCkPWAMTFAFDRALQTSILRTWGGKKEQISHAQNELIKRCRA 334
Cdd:NF033379 240 RCLRRTVPAAVPGIAFLSGGQSDEEATAHLNAMNKLGPL-PWPLTFSYGRALQQPALKAWGGKAENVAAAQKALLHRARM 318
|
....*
gi 386766548 335 NGLAS 339
Cdd:NF033379 319 NSLAA 323
|
|
| PLN02455 |
PLN02455 |
fructose-bisphosphate aldolase |
14-357 |
1.18e-153 |
|
fructose-bisphosphate aldolase
Pssm-ID: 178074 Cd Length: 358 Bit Score: 436.49 E-value: 1.18e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 14 EELICISKALVAPGKGILAADESSAVMGKRFQLIGVENTEENRRLYRQMLFTTdPKIAENISGVIFYHETLHQRTDDGLP 93
Cdd:PLN02455 10 DELIKNAKYIATPGKGILAADESTGTIGKRLASINVENVESNRQALRELLFTA-PGALQYLSGVILFEETLYQKTSDGKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 94 FVEALRKKGILTGIKVDKHFSPLFGSEDEFTTQGLDDLANRCAQYKKEGCSFAKWRCILKITKNTPSPQAILENANVMAR 173
Cdd:PLN02455 89 FVDVLKENGVLPGIKVDKGTVELAGTNGETTTQGLDGLGARCAKYYEAGARFAKWRAVLKIGPTEPSELAIQENAQGLAR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 174 YAAICQSQRLVPIISPEVLATGDHDLDRCQKVNEILLAGVYKALSDHHVFLEGTLLQPSMVMPGLQSNKNhPPADIGVAT 253
Cdd:PLN02455 169 YAIICQENGLVPIVEPEILVDGSHDIKKCAAVTERVLAACYKALNDHHVLLEGTLLKPNMVTPGSDSPKV-SPEVIAEYT 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 254 VLAIRRSVPPAVMGVLFCGGAQSEEEATVHLNAINNVPLCKPWAMTFAFDRALQTSILRTWGGKKEQISHAQNELIKRCR 333
Cdd:PLN02455 248 VRALQRTVPPAVPGIVFLSGGQSEEEATLNLNAMNKLKTLKPWTLSFSFGRALQQSTLKAWAGKKENVAKAQAAFLVRCK 327
|
330 340
....*....|....*....|....
gi 386766548 334 ANGLASIGKYVIGSVESSAATERL 357
Cdd:PLN02455 328 ANSEATLGKYKGDAAGGEGASESL 351
|
|
| FBP_aldolase_I |
cd00344 |
Fructose-bisphosphate aldolase class I; Fructose-bisphosphate aldolase class I. Fructose-1, ... |
13-338 |
1.28e-125 |
|
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: 364.12 E-value: 1.28e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 13 QEELICISKALVAPGKGILAADESSAVMGKRFQLIGVENTEENRRLYRQMLFTTDPKIAENISGVIFYHETLHQRTDDGL 92
Cdd:cd00344 1 KKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPRIGGVILFHETLYQKADDGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 93 PFVEALRKKGILTGIKVDKHFSPLFGSEDEFTTQGLDDLANRCAQYKKEGCSFAKWRCILKITKNTPSPQAILENANVMA 172
Cdd:cd00344 81 PFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 173 RYAAICQSQRLVPIISPEVLATGDHDLDRCQKVNEILLAGVYKALSDHHVFLEGTLLQPSMVMPGLQSNKNHPPADIGVA 252
Cdd:cd00344 161 RYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKFSHEEIAMA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 253 TVLAIRRSVPPAVMGVLFCGGAQSEEEATVHLNAINNVPLCKPWAMTFAFDRALQTSILRTWGGKKEQISHAQNELIKRC 332
Cdd:cd00344 241 TVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRA 320
|
....*.
gi 386766548 333 RANGLA 338
Cdd:cd00344 321 LANSLA 326
|
|
| PLN02425 |
PLN02425 |
probable fructose-bisphosphate aldolase |
14-364 |
1.25e-121 |
|
probable fructose-bisphosphate aldolase
Pssm-ID: 215234 Cd Length: 390 Bit Score: 356.25 E-value: 1.25e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 14 EELICISKALVAPGKGILAADESSAVMGKRFQLIGVENTEENRRLYRQMLFTTdPKIAENISGVIFYHETLHQRTDDGLP 93
Cdd:PLN02425 45 DELVQTAKSVASPGRGILAIDESNATCGKRLASIGLDNTETNRQAYRQLLLTT-PGLGEYISGAILFEETLYQSTTDGKK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 94 FVEALRKKGILTGIKVDKHFSPLFGSEDEFTTQGLDDLANRCAQYKKEGCSFAKWRCILKITKNtPSPQAILENANVMAR 173
Cdd:PLN02425 124 FVDCLRDQNIVPGIKVDKGLVPLPGSNNESWCQGLDGLASRSAEYYKQGARFAKWRTVVSIPCG-PSALAVKEAAWGLAR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 174 YAAICQSQRLVPIISPEVLATGDHDLDRCQKVNEILLAGVYKALSDHHVFLEGTLLQPSMVMPGLQSNKNHPPADIGVAT 253
Cdd:PLN02425 203 YAAISQDNGLVPIVEPEILLDGDHPIERTLEVAEKVWSEVFFYLAQNNVLFEGILLKPSMVTPGAEHKEKASPETIAKYT 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 254 VLAIRRSVPPAVMGVLFCGGAQSEEEATVHLNAINNVPlcKPWAMTFAFDRALQTSILRTWGGKKEQISHAQNELIKRCR 333
Cdd:PLN02425 283 LTMLRRRVPPAVPGIMFLSGGQSEVEATLNLNAMNQSP--NPWHVSFSYARALQNSVLKTWQGRPENVEAAQKALLVRAK 360
|
330 340 350
....*....|....*....|....*....|.
gi 386766548 334 ANGLASIGKYViGSVESSAATERLIQEAVEF 364
Cdd:PLN02425 361 ANSLAQLGRYS-AEGESEEAKKGMFVKGYTY 390
|
|
| PLN02227 |
PLN02227 |
fructose-bisphosphate aldolase I |
14-355 |
4.25e-105 |
|
fructose-bisphosphate aldolase I
Pssm-ID: 177872 Cd Length: 399 Bit Score: 314.43 E-value: 4.25e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 14 EELICISKALVAPGKGILAADESSAVMGKRFQLIGVENTEENRRLYRQMLFTTdPKIAENISGVIFYHETLHQRTDDGLP 93
Cdd:PLN02227 54 DELVKTAKTIASPGHGIMAMDESNATCGKRLASIGLENTEANRQAYRTLLVSA-PGLGQYISGAILFEETLYQSTTDGKK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 94 FVEALRKKGILTGIKVDKHFSPLFGSEDEFTTQGLDDLANRCAQYKKEGCSFAKWRCILKItKNTPSPQAILENANVMAR 173
Cdd:PLN02227 133 MVDVLVEQNIVPGIKVDKGLVPLVGSYDESWCQGLDGLASRTAAYYQQGARFAKWRTVVSI-PNGPSALAVKEAAWGLAR 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 174 YAAICQSQRLVPIISPEVLATGDHDLDRCQKVNEILLAGVYKALSDHHVFLEGTLLQPSMVMPGLQSNKNHPPADIGVAT 253
Cdd:PLN02227 212 YAAISQDSGLVPIVEPEIMLDGEHGIDRTYDVAEKVWAEVFFYLAQNNVMFEGILLKPSMVTPGAEATDRATPEQVASYT 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 254 VLAIRRSVPPAVMGVLFCGGAQSEEEATVHLNAINNVPlcKPWAMTFAFDRALQTSILRTWGGKKEQISHAQNELIKRCR 333
Cdd:PLN02227 292 LKLLRNRIPPAVPGIMFLSGGQSELEATLNLNAMNQAP--NPWHVSFSYARALQNTCLKTWGGKEENVKAAQDILLARAK 369
|
330 340
....*....|....*....|..
gi 386766548 334 ANGLASIGKYViGSVESSAATE 355
Cdd:PLN02227 370 ANSLAQLGKYT-GEGESEEAKE 390
|
|
| Fba1 |
COG3588 |
Fructose-bisphosphate aldolase class 1 [Carbohydrate transport and metabolism]; ... |
13-326 |
1.68e-91 |
|
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: 276.22 E-value: 1.68e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 13 QEELICISKALVAPGKGILAA-DESSAVMGKRFQLIGVENTEENRRL--------YRQMLFTTDPKIAENISGVIFYHET 83
Cdd:COG3588 2 TEELNATALAMVANGKGFLAAlDQSGGSTPKALAAYGVEETEYSRREemfdlvhaMRERIITSPAFTGDKISGAILFEET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 84 LHQRTDDGLPFVEALRKKGILTGIKVDKHFSPLfgSEDEFTTQGLDDLANRCAQYKKEGCSFAKWRCILKItkntPSPQA 163
Cdd:COG3588 82 MDQKIDGTPTFDYLWEKKGIVPGIKVDKGLKDL--APGVQLMKGLDGLDERLARAKELGAFGTKWRSVIKI----ANAAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 164 ILENANVMARYAAICQSQRLVPIISPEVLATGDHDLDRCQKVNEILLAGVYKALSDHhvflEGTLLQpsMVMPGlqsnKN 243
Cdd:COG3588 156 IKANVHQQARYAALCQEAGLVPIVEPEVLIDGDHKIEREAELTEEILKALFDALPED----EGVMLK--MVIPG----KD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 244 HPPADiGVATvlairrsvpPAVMGVLFCGGAQSEEEATVHLNAINnvplckpwAMTFAFDRALQTSILRTWGGKKEQISH 323
Cdd:COG3588 226 NLYQA-LVEH---------PAVPRVVFLSGGQSREEATAHLNANN--------GLIASFSRALQEGLLAAWSGEEFNAAL 287
|
...
gi 386766548 324 AQN 326
Cdd:COG3588 288 AQA 290
|
|
| FBP_aldolase_I_bact |
cd00949 |
Fructose-1.6-bisphosphate aldolase found in gram +/- bacteria; Fructose-1.6-bisphosphate ... |
27-306 |
2.07e-07 |
|
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: 52.03 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 27 GKGILAA-DESSAVMGKRFQLIGVE-----NTEENRRLYRQM---LFTTDPKIAENISGVIFYHETLhQRTDDGLPFVEA 97
Cdd:cd00949 10 GKGFIAAlDQSGGSTPKALAAYGIEedaysNEEEMFDLVHEMrtrIITSPAFDGDKILGAILFEQTM-DREIEGKPTADY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 98 L-RKKGILTGIKVDKhfsplfGSEDEFT-TQ------GLDDLANRCaqyKKEGCSFAKWRCILKitknTPSPQAILENAN 169
Cdd:cd00949 89 LwEKKQIVPFLKVDK------GLAEEKNgVQlmkpipNLDELLMRA---KEKGVFGTKMRSVIK----EANPKGIAAVVD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 170 VMARYAAICQSQRLVPIISPEVlatgD-HDLDRcQKVNEILLAGVYKALSDhhvflegtLLQPSMVMPGLQSnknhpPAD 248
Cdd:cd00949 156 QQFELAKQILSHGLVPIIEPEV----DiHSADK-AKCEAILKAEILKHLDK--------LPEGQQVMLKLTL-----PTE 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 386766548 249 IGVATVLAIRrsvpPAVMGVLFCGGAQSEEEATVHLnAINNvplckpwAMTFAFDRAL 306
Cdd:cd00949 218 ANFYSELIEH----PKVLRVVALSGGYSREEANELL-AKNN-------GVIASFSRAL 263
|
|
| PRK05377 |
PRK05377 |
fructose-1,6-bisphosphate aldolase; Reviewed |
24-228 |
8.95e-06 |
|
fructose-1,6-bisphosphate aldolase; Reviewed
Pssm-ID: 180045 Cd Length: 296 Bit Score: 46.79 E-value: 8.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 24 VAPGKGILAA-DESSAVMGKRFQLIGVE-----NTEENRRLYRQM---LFTTDPKIAENISGVIFYHETLHqRTDDGLPF 94
Cdd:PRK05377 10 MKNGKGFIAAlDQSGGSTPKALKLYGVEedaysNEEEMFDLVHEMrtrIITSPAFTGDKILGAILFEQTMD-REIEGKPT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386766548 95 VEAL-RKKGILTGIKVDKhfsplfGSEDEFT-TQ------GLDDLANRCAQYKKEGcsfAKWRCILKitknTPSPQAIle 166
Cdd:PRK05377 89 ADYLwEKKGVVPFLKVDK------GLAEEANgVQlmkpipNLDDLLDRAVEKGIFG---TKMRSVIK----EANEQGI-- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386766548 167 nANVMAR---YAAICQSQRLVPIISPEVLAtgdHDLDRcQKVNEILLAGVYKALS----DHHVFLEGTL 228
Cdd:PRK05377 154 -AAVVAQqfeVAKQILAAGLVPIIEPEVDI---NSPDK-AEAEAILKAEILKQLDalpeDQQVMLKLTI 217
|
|
| |
