|
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: 730.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 15 ELREIAQKIVAPGKGILAADESGPTMGKRLQDIGVENTEDNRRAYRQLLFSTDPKLAENISGVILFHETLYQKADDGTPF 94
Cdd:pfam00274 1 ELIATAKAIVAPGKGILAADESTGTIGKRLASIGVENTEENRRAYRQLLFTTDGELGEYISGVILFHETLYQKTDDGKPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 95 AEILKKKGIILGIKVDKGVVPLFGSEDEVTTQGLDDLAARCAQYKKDGCDFAKWRCVLKIGKNTPSYQSILENANVLARY 174
Cdd:pfam00274 81 VDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQGLDGLAERCAQYYKDGARFAKWRCVLKIGENTPSELAIQENANVLARY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 175 ASICQSQRIVPIVEPEVLPDGDHDLDRAQKVTETVLAAVYKALSDHHVYLEGTLLKPNMVTAGQSA-KKNTPEEIALATV 253
Cdd:pfam00274 161 ASICQQNGLVPIVEPEILPDGDHDLERCQKVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTPGADCpKKYTPEEIAEATV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 254 QALRRTVPAAVTGVTFLSGGQSEEEATVNLSAINNVPLIRPWALTFSYGRALQASVLRAWAGKKENIAAGQNELLKRAKA 333
Cdd:pfam00274 241 TALRRTVPPAVPGVTFLSGGQSEEEATVNLNAINKLPLKKPWALTFSYGRALQASVLKAWGGKKENVKAAQEELLKRAKA 320
|
330 340 350
....*....|....*....|....*....|
gi 111145099 334 NGEAACGNYtAGSVKGFAGKDTLHVDDHRY 363
Cdd:pfam00274 321 NSLASLGKY-VGGVEGAAASESLFVANYAY 349
|
|
| FBP_aldolase_I_a |
cd00948 |
Fructose-1,6-bisphosphate aldolase; Fructose-1,6-bisphosphate aldolase. The enzyme catalyzes ... |
14-342 |
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: 640.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 14 DELREIAQKIVAPGKGILAADESGPTMGKRLQDIGVENTEDNRRAYRQLLFSTdPKLAENISGVILFHETLYQKADDGTP 93
Cdd:cd00948 2 EELIKTAKAIVAPGKGILAADESTGTIGKRFASIGVENTEENRRAYRELLFTT-PGLGQYISGVILFEETLYQKTDDGKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 94 FAEILKKKGIILGIKVDKGVVPLFGSEDEVTTQGLDDLAARCAQYKKDGCDFAKWRCVLKIGKNTPSYQSILENANVLAR 173
Cdd:cd00948 81 FVDILKEKGIVPGIKVDKGLVPLAGTDGETTTQGLDGLAERCAKYYKQGARFAKWRAVLKIGNGTPSELAIKENAHGLAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 174 YASICQSQRIVPIVEPEVLPDGDHDLDRAQKVTETVLAAVYKALSDHHVYLEGTLLKPNMVTAGQ-SAKKNTPEEIALAT 252
Cdd:cd00948 161 YAAICQENGLVPIVEPEVLMDGDHDIERCQEVTEKVLAAVYKALNDHHVLLEGTLLKPNMVTPGAdCKKKASPEEVAEYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 253 VQALRRTVPAAVTGVTFLSGGQSEEEATVNLSAINNVPLIRPWALTFSYGRALQASVLRAWAGKKENIAAGQNELLKRAK 332
Cdd:cd00948 241 VRALRRTVPAAVPGIVFLSGGQSEEEATLNLNAMNKLPLPKPWALSFSYGRALQASALKAWGGKKENVEAAQKALLKRAK 320
|
330
....*....|
gi 111145099 333 ANGEAACGNY 342
Cdd:cd00948 321 ANSLAALGKY 330
|
|
| PTZ00019 |
PTZ00019 |
fructose-bisphosphate aldolase; Provisional |
11-363 |
0e+00 |
|
fructose-bisphosphate aldolase; Provisional
Pssm-ID: 240231 Cd Length: 355 Bit Score: 543.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 11 ELQDELREIAQKIVAPGKGILAADESGPTMGKRLQDIGVENTEDNRRAYRQLLFSTdPKLAENISGVILFHETLYQKADD 90
Cdd:PTZ00019 2 EYAKELAETAKKIAAPGKGILAADESTGTIKKRFDPIGLENTEENRRAYRELLFTT-EGLEQYISGVILFEETVYQKAPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 91 GTPFAEILKKKGIILGIKVDKGVVPLFGSEDEVTTQGLDDLAARCAQYKKDGCDFAKWRCVLKIG--KNTPSYQSILENA 168
Cdd:PTZ00019 81 GKTFVELLKEKGIVPGIKVDKGLVTLPGTDGETSTQGLDGLAERAKKYYKAGARFAKWRAVLKIDpaKGKPSELAIQENA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 169 NVLARYASICQSQRIVPIVEPEVLPDGDHDLDRAQKVTETVLAAVYKALSDHHVYLEGTLLKPNMVTAG-QSAKKNTPEE 247
Cdd:PTZ00019 161 WTLARYAAICQENGLVPIVEPEILIDGSHSIEVCQKVTEKVLAEVFKALNDHGVLLEGCLLKPNMVTPGsDCGVKATPQE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 248 IALATVQALRRTVPAAVTGVTFLSGGQSEEEATVNLSAINNVPLIRPWALTFSYGRALQASVLRAWAGKKENIAAGQNEL 327
Cdd:PTZ00019 241 VAFYTVRTLSRTVPPALPGVMFLSGGQSEEEASLNLNAMNKLTLPRPWALSFSYGRALQSSALKTWKGKDENVAAAQKAL 320
|
330 340 350
....*....|....*....|....*....|....*.
gi 111145099 328 LKRAKANGEAACGNYTAGSVKGFAGkDTLHVDDHRY 363
Cdd:PTZ00019 321 LHRAKANSLAQLGKYKGGDGGAAAS-ESLYVKDYKY 355
|
|
| FrucBisAld_I |
NF033379 |
fructose-bisphosphate aldolase class I; This family consists of fructose-bisphosphate aldolase ... |
15-338 |
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: 518.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 15 ELREIAQKIVAPGKGILAADESGPTMGKRLQDIGVENTEDNRRAYRQLLFSTdPKLAENISGVILFHETLYQKADDGTPF 94
Cdd:NF033379 1 ELEETAQAMVAPGKGILAADESTGTINKRFEAIGVESTEENRRAYRELLFTT-PGLGDYISGVILFDETIRQKTADGTPF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 95 AEILKKKGIILGIKVDKGVVPLFGSEDEVTTQGLDDLAARCAQYKKDGCDFAKWRCVLKIGKNTPSYQSILENANVLARY 174
Cdd:NF033379 80 PKVLADAGIIPGIKVDKGAKPLAGFPGEKVTEGLDGLRERLAEYYELGARFAKWRAVITIGDGIPSRACIEANAHALARY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 175 ASICQSQRIVPIVEPEVLPDGDHDLDRAQKVTETVLAAVYKALSDHHVYLEGTLLKPNMVTAG-QSAKKNTPEEIALATV 253
Cdd:NF033379 160 AALCQEAGLVPIVEPEVLMDGDHSIERCAEVTEEVLKEVFEELYRQGVDLEGMILKPNMVLPGkDCPDQASPEEVAEATV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 254 QALRRTVPAAVTGVTFLSGGQSEEEATVNLSAINNVPLiRPWALTFSYGRALQASVLRAWAGKKENIAAGQNELLKRAKA 333
Cdd:NF033379 240 RCLRRTVPAAVPGIAFLSGGQSDEEATAHLNAMNKLGP-LPWPLTFSYGRALQQPALKAWGGKAENVAAAQKALLHRARM 318
|
....*
gi 111145099 334 NGEAA 338
Cdd:NF033379 319 NSLAA 323
|
|
| Fba1 |
COG3588 |
Fructose-bisphosphate aldolase class 1 [Carbohydrate transport and metabolism]; ... |
13-325 |
1.37e-113 |
|
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: 334.77 E-value: 1.37e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 13 QDELREIAQKIVAPGKGILAA-DESGPTMGKRLQDIGVENTEDNRR--------AYRQLLFSTDPKLAENISGVILFHET 83
Cdd:COG3588 2 TEELNATALAMVANGKGFLAAlDQSGGSTPKALAAYGVEETEYSRReemfdlvhAMRERIITSPAFTGDKISGAILFEET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 84 LYQKADdGTP-FAEILKKKGIILGIKVDKGVVPLfgSEDEVTTQGLDDLAARCAQYKKDGCDFAKWRCVLKIGkntpSYQ 162
Cdd:COG3588 82 MDQKID-GTPtFDYLWEKKGIVPGIKVDKGLKDL--APGVQLMKGLDGLDERLARAKELGAFGTKWRSVIKIA----NAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 163 SILENANVLARYASICQSQRIVPIVEPEVLPDGDHDLDRAQKVTETVLAAVYKALSDHhvylEGTLLKpnMVTAGQ-SAK 241
Cdd:COG3588 155 GIKANVHQQARYAALCQEAGLVPIVEPEVLIDGDHKIEREAELTEEILKALFDALPED----EGVMLK--MVIPGKdNLY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 242 KNTPEEialatvqalrrtvpAAVTGVTFLSGGQSEEEATVNLSAINnvplirpwALTFSYGRALQASVLRAWAGKKENIA 321
Cdd:COG3588 229 QALVEH--------------PAVPRVVFLSGGQSREEATAHLNANN--------GLIASFSRALQEGLLAAWSGEEFNAA 286
|
....
gi 111145099 322 AGQN 325
Cdd:COG3588 287 LAQA 290
|
|
| |
|
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: 730.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 15 ELREIAQKIVAPGKGILAADESGPTMGKRLQDIGVENTEDNRRAYRQLLFSTDPKLAENISGVILFHETLYQKADDGTPF 94
Cdd:pfam00274 1 ELIATAKAIVAPGKGILAADESTGTIGKRLASIGVENTEENRRAYRQLLFTTDGELGEYISGVILFHETLYQKTDDGKPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 95 AEILKKKGIILGIKVDKGVVPLFGSEDEVTTQGLDDLAARCAQYKKDGCDFAKWRCVLKIGKNTPSYQSILENANVLARY 174
Cdd:pfam00274 81 VDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQGLDGLAERCAQYYKDGARFAKWRCVLKIGENTPSELAIQENANVLARY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 175 ASICQSQRIVPIVEPEVLPDGDHDLDRAQKVTETVLAAVYKALSDHHVYLEGTLLKPNMVTAGQSA-KKNTPEEIALATV 253
Cdd:pfam00274 161 ASICQQNGLVPIVEPEILPDGDHDLERCQKVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTPGADCpKKYTPEEIAEATV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 254 QALRRTVPAAVTGVTFLSGGQSEEEATVNLSAINNVPLIRPWALTFSYGRALQASVLRAWAGKKENIAAGQNELLKRAKA 333
Cdd:pfam00274 241 TALRRTVPPAVPGVTFLSGGQSEEEATVNLNAINKLPLKKPWALTFSYGRALQASVLKAWGGKKENVKAAQEELLKRAKA 320
|
330 340 350
....*....|....*....|....*....|
gi 111145099 334 NGEAACGNYtAGSVKGFAGKDTLHVDDHRY 363
Cdd:pfam00274 321 NSLASLGKY-VGGVEGAAASESLFVANYAY 349
|
|
| FBP_aldolase_I_a |
cd00948 |
Fructose-1,6-bisphosphate aldolase; Fructose-1,6-bisphosphate aldolase. The enzyme catalyzes ... |
14-342 |
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: 640.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 14 DELREIAQKIVAPGKGILAADESGPTMGKRLQDIGVENTEDNRRAYRQLLFSTdPKLAENISGVILFHETLYQKADDGTP 93
Cdd:cd00948 2 EELIKTAKAIVAPGKGILAADESTGTIGKRFASIGVENTEENRRAYRELLFTT-PGLGQYISGVILFEETLYQKTDDGKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 94 FAEILKKKGIILGIKVDKGVVPLFGSEDEVTTQGLDDLAARCAQYKKDGCDFAKWRCVLKIGKNTPSYQSILENANVLAR 173
Cdd:cd00948 81 FVDILKEKGIVPGIKVDKGLVPLAGTDGETTTQGLDGLAERCAKYYKQGARFAKWRAVLKIGNGTPSELAIKENAHGLAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 174 YASICQSQRIVPIVEPEVLPDGDHDLDRAQKVTETVLAAVYKALSDHHVYLEGTLLKPNMVTAGQ-SAKKNTPEEIALAT 252
Cdd:cd00948 161 YAAICQENGLVPIVEPEVLMDGDHDIERCQEVTEKVLAAVYKALNDHHVLLEGTLLKPNMVTPGAdCKKKASPEEVAEYT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 253 VQALRRTVPAAVTGVTFLSGGQSEEEATVNLSAINNVPLIRPWALTFSYGRALQASVLRAWAGKKENIAAGQNELLKRAK 332
Cdd:cd00948 241 VRALRRTVPAAVPGIVFLSGGQSEEEATLNLNAMNKLPLPKPWALSFSYGRALQASALKAWGGKKENVEAAQKALLKRAK 320
|
330
....*....|
gi 111145099 333 ANGEAACGNY 342
Cdd:cd00948 321 ANSLAALGKY 330
|
|
| PTZ00019 |
PTZ00019 |
fructose-bisphosphate aldolase; Provisional |
11-363 |
0e+00 |
|
fructose-bisphosphate aldolase; Provisional
Pssm-ID: 240231 Cd Length: 355 Bit Score: 543.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 11 ELQDELREIAQKIVAPGKGILAADESGPTMGKRLQDIGVENTEDNRRAYRQLLFSTdPKLAENISGVILFHETLYQKADD 90
Cdd:PTZ00019 2 EYAKELAETAKKIAAPGKGILAADESTGTIKKRFDPIGLENTEENRRAYRELLFTT-EGLEQYISGVILFEETVYQKAPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 91 GTPFAEILKKKGIILGIKVDKGVVPLFGSEDEVTTQGLDDLAARCAQYKKDGCDFAKWRCVLKIG--KNTPSYQSILENA 168
Cdd:PTZ00019 81 GKTFVELLKEKGIVPGIKVDKGLVTLPGTDGETSTQGLDGLAERAKKYYKAGARFAKWRAVLKIDpaKGKPSELAIQENA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 169 NVLARYASICQSQRIVPIVEPEVLPDGDHDLDRAQKVTETVLAAVYKALSDHHVYLEGTLLKPNMVTAG-QSAKKNTPEE 247
Cdd:PTZ00019 161 WTLARYAAICQENGLVPIVEPEILIDGSHSIEVCQKVTEKVLAEVFKALNDHGVLLEGCLLKPNMVTPGsDCGVKATPQE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 248 IALATVQALRRTVPAAVTGVTFLSGGQSEEEATVNLSAINNVPLIRPWALTFSYGRALQASVLRAWAGKKENIAAGQNEL 327
Cdd:PTZ00019 241 VAFYTVRTLSRTVPPALPGVMFLSGGQSEEEASLNLNAMNKLTLPRPWALSFSYGRALQSSALKTWKGKDENVAAAQKAL 320
|
330 340 350
....*....|....*....|....*....|....*.
gi 111145099 328 LKRAKANGEAACGNYTAGSVKGFAGkDTLHVDDHRY 363
Cdd:PTZ00019 321 LHRAKANSLAQLGKYKGGDGGAAAS-ESLYVKDYKY 355
|
|
| FrucBisAld_I |
NF033379 |
fructose-bisphosphate aldolase class I; This family consists of fructose-bisphosphate aldolase ... |
15-338 |
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: 518.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 15 ELREIAQKIVAPGKGILAADESGPTMGKRLQDIGVENTEDNRRAYRQLLFSTdPKLAENISGVILFHETLYQKADDGTPF 94
Cdd:NF033379 1 ELEETAQAMVAPGKGILAADESTGTINKRFEAIGVESTEENRRAYRELLFTT-PGLGDYISGVILFDETIRQKTADGTPF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 95 AEILKKKGIILGIKVDKGVVPLFGSEDEVTTQGLDDLAARCAQYKKDGCDFAKWRCVLKIGKNTPSYQSILENANVLARY 174
Cdd:NF033379 80 PKVLADAGIIPGIKVDKGAKPLAGFPGEKVTEGLDGLRERLAEYYELGARFAKWRAVITIGDGIPSRACIEANAHALARY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 175 ASICQSQRIVPIVEPEVLPDGDHDLDRAQKVTETVLAAVYKALSDHHVYLEGTLLKPNMVTAG-QSAKKNTPEEIALATV 253
Cdd:NF033379 160 AALCQEAGLVPIVEPEVLMDGDHSIERCAEVTEEVLKEVFEELYRQGVDLEGMILKPNMVLPGkDCPDQASPEEVAEATV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 254 QALRRTVPAAVTGVTFLSGGQSEEEATVNLSAINNVPLiRPWALTFSYGRALQASVLRAWAGKKENIAAGQNELLKRAKA 333
Cdd:NF033379 240 RCLRRTVPAAVPGIAFLSGGQSDEEATAHLNAMNKLGP-LPWPLTFSYGRALQQPALKAWGGKAENVAAAQKALLHRARM 318
|
....*
gi 111145099 334 NGEAA 338
Cdd:NF033379 319 NSLAA 323
|
|
| PLN02455 |
PLN02455 |
fructose-bisphosphate aldolase |
14-363 |
1.92e-178 |
|
fructose-bisphosphate aldolase
Pssm-ID: 178074 Cd Length: 358 Bit Score: 501.59 E-value: 1.92e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 14 DELREIAQKIVAPGKGILAADESGPTMGKRLQDIGVENTEDNRRAYRQLLFSTdPKLAENISGVILFHETLYQKADDGTP 93
Cdd:PLN02455 10 DELIKNAKYIATPGKGILAADESTGTIGKRLASINVENVESNRQALRELLFTA-PGALQYLSGVILFEETLYQKTSDGKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 94 FAEILKKKGIILGIKVDKGVVPLFGSEDEVTTQGLDDLAARCAQYKKDGCDFAKWRCVLKIGKNTPSYQSILENANVLAR 173
Cdd:PLN02455 89 FVDVLKENGVLPGIKVDKGTVELAGTNGETTTQGLDGLGARCAKYYEAGARFAKWRAVLKIGPTEPSELAIQENAQGLAR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 174 YASICQSQRIVPIVEPEVLPDGDHDLDRAQKVTETVLAAVYKALSDHHVYLEGTLLKPNMVTAGQSAKKNTPEEIALATV 253
Cdd:PLN02455 169 YAIICQENGLVPIVEPEILVDGSHDIKKCAAVTERVLAACYKALNDHHVLLEGTLLKPNMVTPGSDSPKVSPEVIAEYTV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 254 QALRRTVPAAVTGVTFLSGGQSEEEATVNLSAINNVPLIRPWALTFSYGRALQASVLRAWAGKKENIAAGQNELLKRAKA 333
Cdd:PLN02455 249 RALQRTVPPAVPGIVFLSGGQSEEEATLNLNAMNKLKTLKPWTLSFSFGRALQQSTLKAWAGKKENVAKAQAAFLVRCKA 328
|
330 340 350
....*....|....*....|....*....|
gi 111145099 334 NGEAACGNYTAGSVKGFAGKDTLHVDDHRY 363
Cdd:PLN02455 329 NSEATLGKYKGDAAGGEGASESLHVKDYKY 358
|
|
| FBP_aldolase_I |
cd00344 |
Fructose-bisphosphate aldolase class I; Fructose-bisphosphate aldolase class I. Fructose-1, ... |
13-338 |
2.67e-150 |
|
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: 429.22 E-value: 2.67e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 13 QDELREIAQKIVAPGKGILAADESGPTMGKRLQDIGVENTEDNRRAYRQLLFSTDPKLAENISGVILFHETLYQKADDGT 92
Cdd:cd00344 1 KKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPRIGGVILFHETLYQKADDGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 93 PFAEILKKKGIILGIKVDKGVVPLFGSEDEVTTQGLDDLAARCAQYKKDGCDFAKWRCVLKIGKNTPSYQSILENANVLA 172
Cdd:cd00344 81 PFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 173 RYASICQSQRIVPIVEPEVLPDGDHDLDRAQKVTETVLAAVYKALSDHHVYLEGTLLKPNMVTAGQS-AKKNTPEEIALA 251
Cdd:cd00344 161 RYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHAcTQKFSHEEIAMA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 252 TVQALRRTVPAAVTGVTFLSGGQSEEEATVNLSAINNVPLIRPWALTFSYGRALQASVLRAWAGKKENIAAGQNELLKRA 331
Cdd:cd00344 241 TVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRA 320
|
....*..
gi 111145099 332 KANGEAA 338
Cdd:cd00344 321 LANSLAA 327
|
|
| PLN02425 |
PLN02425 |
probable fructose-bisphosphate aldolase |
14-344 |
4.36e-134 |
|
probable fructose-bisphosphate aldolase
Pssm-ID: 215234 Cd Length: 390 Bit Score: 390.53 E-value: 4.36e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 14 DELREIAQKIVAPGKGILAADESGPTMGKRLQDIGVENTEDNRRAYRQLLFSTdPKLAENISGVILFHETLYQKADDGTP 93
Cdd:PLN02425 45 DELVQTAKSVASPGRGILAIDESNATCGKRLASIGLDNTETNRQAYRQLLLTT-PGLGEYISGAILFEETLYQSTTDGKK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 94 FAEILKKKGIILGIKVDKGVVPLFGSEDEVTTQGLDDLAARCAQYKKDGCDFAKWRCVLKIgKNTPSYQSILENANVLAR 173
Cdd:PLN02425 124 FVDCLRDQNIVPGIKVDKGLVPLPGSNNESWCQGLDGLASRSAEYYKQGARFAKWRTVVSI-PCGPSALAVKEAAWGLAR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 174 YASICQSQRIVPIVEPEVLPDGDHDLDRAQKVTETVLAAVYKALSDHHVYLEGTLLKPNMVTAGQSAK-KNTPEEIALAT 252
Cdd:PLN02425 203 YAAISQDNGLVPIVEPEILLDGDHPIERTLEVAEKVWSEVFFYLAQNNVLFEGILLKPSMVTPGAEHKeKASPETIAKYT 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 253 VQALRRTVPAAVTGVTFLSGGQSEEEATVNLSAINNVPliRPWALTFSYGRALQASVLRAWAGKKENIAAGQNELLKRAK 332
Cdd:PLN02425 283 LTMLRRRVPPAVPGIMFLSGGQSEVEATLNLNAMNQSP--NPWHVSFSYARALQNSVLKTWQGRPENVEAAQKALLVRAK 360
|
330
....*....|..
gi 111145099 333 ANGEAACGNYTA 344
Cdd:PLN02425 361 ANSLAQLGRYSA 372
|
|
| Fba1 |
COG3588 |
Fructose-bisphosphate aldolase class 1 [Carbohydrate transport and metabolism]; ... |
13-325 |
1.37e-113 |
|
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: 334.77 E-value: 1.37e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 13 QDELREIAQKIVAPGKGILAA-DESGPTMGKRLQDIGVENTEDNRR--------AYRQLLFSTDPKLAENISGVILFHET 83
Cdd:COG3588 2 TEELNATALAMVANGKGFLAAlDQSGGSTPKALAAYGVEETEYSRReemfdlvhAMRERIITSPAFTGDKISGAILFEET 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 84 LYQKADdGTP-FAEILKKKGIILGIKVDKGVVPLfgSEDEVTTQGLDDLAARCAQYKKDGCDFAKWRCVLKIGkntpSYQ 162
Cdd:COG3588 82 MDQKID-GTPtFDYLWEKKGIVPGIKVDKGLKDL--APGVQLMKGLDGLDERLARAKELGAFGTKWRSVIKIA----NAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 163 SILENANVLARYASICQSQRIVPIVEPEVLPDGDHDLDRAQKVTETVLAAVYKALSDHhvylEGTLLKpnMVTAGQ-SAK 241
Cdd:COG3588 155 GIKANVHQQARYAALCQEAGLVPIVEPEVLIDGDHKIEREAELTEEILKALFDALPED----EGVMLK--MVIPGKdNLY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 242 KNTPEEialatvqalrrtvpAAVTGVTFLSGGQSEEEATVNLSAINnvplirpwALTFSYGRALQASVLRAWAGKKENIA 321
Cdd:COG3588 229 QALVEH--------------PAVPRVVFLSGGQSREEATAHLNANN--------GLIASFSRALQEGLLAAWSGEEFNAA 286
|
....
gi 111145099 322 AGQN 325
Cdd:COG3588 287 LAQA 290
|
|
| PLN02227 |
PLN02227 |
fructose-bisphosphate aldolase I |
14-363 |
2.80e-112 |
|
fructose-bisphosphate aldolase I
Pssm-ID: 177872 Cd Length: 399 Bit Score: 335.23 E-value: 2.80e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 14 DELREIAQKIVAPGKGILAADESGPTMGKRLQDIGVENTEDNRRAYRQLLFSTdPKLAENISGVILFHETLYQKADDGTP 93
Cdd:PLN02227 54 DELVKTAKTIASPGHGIMAMDESNATCGKRLASIGLENTEANRQAYRTLLVSA-PGLGQYISGAILFEETLYQSTTDGKK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 94 FAEILKKKGIILGIKVDKGVVPLFGSEDEVTTQGLDDLAARCAQYKKDGCDFAKWRCVLKIgKNTPSYQSILENANVLAR 173
Cdd:PLN02227 133 MVDVLVEQNIVPGIKVDKGLVPLVGSYDESWCQGLDGLASRTAAYYQQGARFAKWRTVVSI-PNGPSALAVKEAAWGLAR 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 174 YASICQSQRIVPIVEPEVLPDGDHDLDRAQKVTETVLAAVYKALSDHHVYLEGTLLKPNMVTAGQSAK-KNTPEEIALAT 252
Cdd:PLN02227 212 YAAISQDSGLVPIVEPEIMLDGEHGIDRTYDVAEKVWAEVFFYLAQNNVMFEGILLKPSMVTPGAEATdRATPEQVASYT 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 253 VQALRRTVPAAVTGVTFLSGGQSEEEATVNLSAINNVPliRPWALTFSYGRALQASVLRAWAGKKENIAAGQNELLKRAK 332
Cdd:PLN02227 292 LKLLRNRIPPAVPGIMFLSGGQSELEATLNLNAMNQAP--NPWHVSFSYARALQNTCLKTWGGKEENVKAAQDILLARAK 369
|
330 340 350
....*....|....*....|....*....|.
gi 111145099 333 ANGEAACGNYTaGSVKGFAGKDTLHVDDHRY 363
Cdd:PLN02227 370 ANSLAQLGKYT-GEGESEEAKEGMFVKGYTY 399
|
|
| FBP_aldolase_I_bact |
cd00949 |
Fructose-1.6-bisphosphate aldolase found in gram +/- bacteria; Fructose-1.6-bisphosphate ... |
13-305 |
4.42e-14 |
|
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: 72.44 E-value: 4.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 13 QDELREIAQkivapGKGILAA-DESGPTMGKRLQDIGV-ENTEDNRRAYRQLLFS------TDPKLA-ENISGVILFHET 83
Cdd:cd00949 1 QEQLERMKS-----GKGFIAAlDQSGGSTPKALAAYGIeEDAYSNEEEMFDLVHEmrtriiTSPAFDgDKILGAILFEQT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 84 LYQKADdGTPFAEIL-KKKGIILGIKVDKGVvplfgSEDEVTTQ------GLDDLAARCAQYKKDGcdfAKWRCVLKiGK 156
Cdd:cd00949 76 MDREIE-GKPTADYLwEKKQIVPFLKVDKGL-----AEEKNGVQlmkpipNLDELLMRAKEKGVFG---TKMRSVIK-EA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 157 NTPSYQSILENANVLARyasICQSQRIVPIVEPEVlpdgD-HDLDRAqKVTETVLAAVYKALS----DHHVYLEGTLlkp 231
Cdd:cd00949 146 NPKGIAAVVDQQFELAK---QILSHGLVPIIEPEV----DiHSADKA-KCEAILKAEILKHLDklpeGQQVMLKLTL--- 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 111145099 232 nmvtagqSAKKNTPEEIalatvqalrrTVPAAVTGVTFLSGGQSEEEATVNLSaiNNVPLIRpwaltfSYGRAL 305
Cdd:cd00949 215 -------PTEANFYSEL----------IEHPKVLRVVALSGGYSREEANELLA--KNNGVIA------SFSRAL 263
|
|
| PRK05377 |
PRK05377 |
fructose-1,6-bisphosphate aldolase; Reviewed |
13-305 |
8.92e-09 |
|
fructose-1,6-bisphosphate aldolase; Reviewed
Pssm-ID: 180045 Cd Length: 296 Bit Score: 56.42 E-value: 8.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 13 QDELREIAQkivapGKGILAA-DESGPTMGKRLQDIGVENTE--------DNRRAYRQLLFSTDPKLAENISGVILFHET 83
Cdd:PRK05377 4 QEQLEKMKN-----GKGFIAAlDQSGGSTPKALKLYGVEEDAysneeemfDLVHEMRTRIITSPAFTGDKILGAILFEQT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 84 LYQKADdGTPFAEIL-KKKGIILGIKVDKGVVPLfgsEDEVttQ------GLDDLAARCAQYKKDGcdfAKWRCVLKigk 156
Cdd:PRK05377 79 MDREIE-GKPTADYLwEKKGVVPFLKVDKGLAEE---ANGV--QlmkpipNLDDLLDRAVEKGIFG---TKMRSVIK--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111145099 157 nTPSYQSIlenANVLAR---YASICQSQRIVPIVEPEVlpdgD-HDLDRAqKVTETVLAAVYKALS----DHHVYLEGTL 228
Cdd:PRK05377 147 -EANEQGI---AAVVAQqfeVAKQILAAGLVPIIEPEV----DiNSPDKA-EAEAILKAEILKQLDalpeDQQVMLKLTI 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 111145099 229 lkPNmvtagqsaKKNTPEEIAlatvqalrrTVPaAVTGVTFLSGGQSEEEATVNLSAinNVPLIRpwaltfSYGRAL 305
Cdd:PRK05377 218 --PT--------EANLYKELI---------DHP-RVLRVVALSGGYSRDEANELLAR--NHGLIA------SFSRAL 266
|
|
| |
