|
Name |
Accession |
Description |
Interval |
E-value |
| Glycolytic |
pfam00274 |
Fructose-bisphosphate aldolase class-I; |
15-365 |
0e+00 |
|
Fructose-bisphosphate aldolase class-I;
Pssm-ID: 459742 Cd Length: 349 Bit Score: 696.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 15 ELRSIANAIVTPGKGILAADESTGSMDKRLNSIGLENTEENRRKYRQLLFTAGADLNKYISGVIMFHETFYQKTDDGKPF 94
Cdd:pfam00274 1 ELIATAKAIVAPGKGILAADESTGTIGKRLASIGVENTEENRRAYRQLLFTTDGELGEYISGVILFHETLYQKTDDGKPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 95 TALLQEQGIIPGIKVDKGVVPMAGTIGEGTTQGLDDLNARCAQYKKDGAQFAKWRCVHKISSTTPSVTALKEIASNLARY 174
Cdd:pfam00274 81 VDLLKEKGIIPGIKVDKGVVPLAGTNGETTTQGLDGLAERCAQYYKDGARFAKWRCVLKIGENTPSELAIQENANVLARY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 175 ASICQQNGLVPIVEPEILPDGEHCLARGQKITETVLSYVYHALNEHHVFLEGTLLKPNMVTSGQSFTgEKPSNADIGLAT 254
Cdd:pfam00274 161 ASICQQNGLVPIVEPEILPDGDHDLERCQKVTEKVLAAVYKALNDHHVYLEGTLLKPNMVTPGADCP-KKYTPEEIAEAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 255 VTALQRGVPSAVPGVVFLSGGQSEEDATLNLNAINQVSGKKPWALTFSYGRALQASCLAKWAGKDENIAAAQEVLLHRAQ 334
Cdd:pfam00274 240 VTALRRTVPPAVPGVTFLSGGQSEEEATVNLNAINKLPLKKPWALTFSYGRALQASVLKAWGGKKENVKAAQEELLKRAK 319
|
330 340 350
....*....|....*....|....*....|.
gi 25150450 335 VNSLASVGKYTGdASADAAASQSLFVANHSY 365
Cdd:pfam00274 320 ANSLASLGKYVG-GVEGAAASESLFVANYAY 349
|
|
| FBP_aldolase_I_a |
cd00948 |
Fructose-1,6-bisphosphate aldolase; Fructose-1,6-bisphosphate aldolase. The enzyme catalyzes ... |
13-344 |
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: 605.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 13 EDELRSIANAIVTPGKGILAADESTGSMDKRLNSIGLENTEENRRKYRQLLFTAGaDLNKYISGVIMFHETFYQKTDDGK 92
Cdd:cd00948 1 KEELIKTAKAIVAPGKGILAADESTGTIGKRFASIGVENTEENRRAYRELLFTTP-GLGQYISGVILFEETLYQKTDDGK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 93 PFTALLQEQGIIPGIKVDKGVVPMAGTIGEGTTQGLDDLNARCAQYKKDGAQFAKWRCVHKISSTTPSVTALKEIASNLA 172
Cdd:cd00948 80 PFVDILKEKGIVPGIKVDKGLVPLAGTDGETTTQGLDGLAERCAKYYKQGARFAKWRAVLKIGNGTPSELAIKENAHGLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 173 RYASICQQNGLVPIVEPEILPDGEHCLARGQKITETVLSYVYHALNEHHVFLEGTLLKPNMVTSGQSfTGEKPSNADIGL 252
Cdd:cd00948 160 RYAAICQENGLVPIVEPEVLMDGDHDIERCQEVTEKVLAAVYKALNDHHVLLEGTLLKPNMVTPGAD-CKKKASPEEVAE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 253 ATVTALQRGVPSAVPGVVFLSGGQSEEDATLNLNAINQVSGKKPWALTFSYGRALQASCLAKWAGKDENIAAAQEVLLHR 332
Cdd:cd00948 239 YTVRALRRTVPAAVPGIVFLSGGQSEEEATLNLNAMNKLPLPKPWALSFSYGRALQASALKAWGGKKENVEAAQKALLKR 318
|
330
....*....|..
gi 25150450 333 AQVNSLASVGKY 344
Cdd:cd00948 319 AKANSLAALGKY 330
|
|
| PTZ00019 |
PTZ00019 |
fructose-bisphosphate aldolase; Provisional |
13-365 |
0e+00 |
|
fructose-bisphosphate aldolase; Provisional
Pssm-ID: 240231 Cd Length: 355 Bit Score: 530.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 13 EDELRSIANAIVTPGKGILAADESTGSMDKRLNSIGLENTEENRRKYRQLLFTAgADLNKYISGVIMFHETFYQKTDDGK 92
Cdd:PTZ00019 4 AKELAETAKKIAAPGKGILAADESTGTIKKRFDPIGLENTEENRRAYRELLFTT-EGLEQYISGVILFEETVYQKAPSGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 93 PFTALLQEQGIIPGIKVDKGVVPMAGTIGEGTTQGLDDLNARCAQYKKDGAQFAKWRCVHKISST--TPSVTALKEIASN 170
Cdd:PTZ00019 83 TFVELLKEKGIVPGIKVDKGLVTLPGTDGETSTQGLDGLAERAKKYYKAGARFAKWRAVLKIDPAkgKPSELAIQENAWT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 171 LARYASICQQNGLVPIVEPEILPDGEHCLARGQKITETVLSYVYHALNEHHVFLEGTLLKPNMVTSGqSFTGEKPSNADI 250
Cdd:PTZ00019 163 LARYAAICQENGLVPIVEPEILIDGSHSIEVCQKVTEKVLAEVFKALNDHGVLLEGCLLKPNMVTPG-SDCGVKATPQEV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 251 GLATVTALQRGVPSAVPGVVFLSGGQSEEDATLNLNAINQVSGKKPWALTFSYGRALQASCLAKWAGKDENIAAAQEVLL 330
Cdd:PTZ00019 242 AFYTVRTLSRTVPPALPGVMFLSGGQSEEEASLNLNAMNKLTLPRPWALSFSYGRALQSSALKTWKGKDENVAAAQKALL 321
|
330 340 350
....*....|....*....|....*....|....*
gi 25150450 331 HRAQVNSLASVGKYTGdASADAAASQSLFVANHSY 365
Cdd:PTZ00019 322 HRAKANSLAQLGKYKG-GDGGAAASESLYVKDYKY 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: 505.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 15 ELRSIANAIVTPGKGILAADESTGSMDKRLNSIGLENTEENRRKYRQLLFTAgADLNKYISGVIMFHETFYQKTDDGKPF 94
Cdd:NF033379 1 ELEETAQAMVAPGKGILAADESTGTINKRFEAIGVESTEENRRAYRELLFTT-PGLGDYISGVILFDETIRQKTADGTPF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 95 TALLQEQGIIPGIKVDKGVVPMAGTIGEGTTQGLDDLNARCAQYKKDGAQFAKWRCVHKISSTTPSVTALKEIASNLARY 174
Cdd:NF033379 80 PKVLADAGIIPGIKVDKGAKPLAGFPGEKVTEGLDGLRERLAEYYELGARFAKWRAVITIGDGIPSRACIEANAHALARY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 175 ASICQQNGLVPIVEPEILPDGEHCLARGQKITETVLSYVYHALNEHHVFLEGTLLKPNMVTSGQSfTGEKPSNADIGLAT 254
Cdd:NF033379 160 AALCQEAGLVPIVEPEVLMDGDHSIERCAEVTEEVLKEVFEELYRQGVDLEGMILKPNMVLPGKD-CPDQASPEEVAEAT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 255 VTALQRGVPSAVPGVVFLSGGQSEEDATLNLNAINQVsGKKPWALTFSYGRALQASCLAKWAGKDENIAAAQEVLLHRAQ 334
Cdd:NF033379 239 VRCLRRTVPAAVPGIAFLSGGQSDEEATAHLNAMNKL-GPLPWPLTFSYGRALQQPALKAWGGKAENVAAAQKALLHRAR 317
|
....*.
gi 25150450 335 VNSLAS 340
Cdd:NF033379 318 MNSLAA 323
|
|
| PLN02455 |
PLN02455 |
fructose-bisphosphate aldolase |
13-365 |
1.91e-178 |
|
fructose-bisphosphate aldolase
Pssm-ID: 178074 Cd Length: 358 Bit Score: 499.28 E-value: 1.91e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 13 EDELRSIANAIVTPGKGILAADESTGSMDKRLNSIGLENTEENRRKYRQLLFTAGADLnKYISGVIMFHETFYQKTDDGK 92
Cdd:PLN02455 9 ADELIKNAKYIATPGKGILAADESTGTIGKRLASINVENVESNRQALRELLFTAPGAL-QYLSGVILFEETLYQKTSDGK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 93 PFTALLQEQGIIPGIKVDKGVVPMAGTIGEGTTQGLDDLNARCAQYKKDGAQFAKWRCVHKISSTTPSVTALKEIASNLA 172
Cdd:PLN02455 88 PFVDVLKENGVLPGIKVDKGTVELAGTNGETTTQGLDGLGARCAKYYEAGARFAKWRAVLKIGPTEPSELAIQENAQGLA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 173 RYASICQQNGLVPIVEPEILPDGEHCLARGQKITETVLSYVYHALNEHHVFLEGTLLKPNMVTSGQSftGEKPSNADIGL 252
Cdd:PLN02455 168 RYAIICQENGLVPIVEPEILVDGSHDIKKCAAVTERVLAACYKALNDHHVLLEGTLLKPNMVTPGSD--SPKVSPEVIAE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 253 ATVTALQRGVPSAVPGVVFLSGGQSEEDATLNLNAINQVSGKKPWALTFSYGRALQASCLAKWAGKDENIAAAQEVLLHR 332
Cdd:PLN02455 246 YTVRALQRTVPPAVPGIVFLSGGQSEEEATLNLNAMNKLKTLKPWTLSFSFGRALQQSTLKAWAGKKENVAKAQAAFLVR 325
|
330 340 350
....*....|....*....|....*....|...
gi 25150450 333 AQVNSLASVGKYTGDASADAAASQSLFVANHSY 365
Cdd:PLN02455 326 CKANSEATLGKYKGDAAGGEGASESLHVKDYKY 358
|
|
| PLN02425 |
PLN02425 |
probable fructose-bisphosphate aldolase |
14-365 |
6.20e-140 |
|
probable fructose-bisphosphate aldolase
Pssm-ID: 215234 Cd Length: 390 Bit Score: 402.86 E-value: 6.20e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 14 DELRSIANAIVTPGKGILAADESTGSMDKRLNSIGLENTEENRRKYRQLLFTAgADLNKYISGVIMFHETFYQKTDDGKP 93
Cdd:PLN02425 45 DELVQTAKSVASPGRGILAIDESNATCGKRLASIGLDNTETNRQAYRQLLLTT-PGLGEYISGAILFEETLYQSTTDGKK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 94 FTALLQEQGIIPGIKVDKGVVPMAGTIGEGTTQGLDDLNARCAQYKKDGAQFAKWRCVHKIsSTTPSVTALKEIASNLAR 173
Cdd:PLN02425 124 FVDCLRDQNIVPGIKVDKGLVPLPGSNNESWCQGLDGLASRSAEYYKQGARFAKWRTVVSI-PCGPSALAVKEAAWGLAR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 174 YASICQQNGLVPIVEPEILPDGEHCLARGQKITETVLSYVYHALNEHHVFLEGTLLKPNMVTSGQSFTgEKPSNADIGLA 253
Cdd:PLN02425 203 YAAISQDNGLVPIVEPEILLDGDHPIERTLEVAEKVWSEVFFYLAQNNVLFEGILLKPSMVTPGAEHK-EKASPETIAKY 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 254 TVTALQRGVPSAVPGVVFLSGGQSEEDATLNLNAINQvsGKKPWALTFSYGRALQASCLAKWAGKDENIAAAQEVLLHRA 333
Cdd:PLN02425 282 TLTMLRRRVPPAVPGIMFLSGGQSEVEATLNLNAMNQ--SPNPWHVSFSYARALQNSVLKTWQGRPENVEAAQKALLVRA 359
|
330 340 350
....*....|....*....|....*....|..
gi 25150450 334 QVNSLASVGKYTGdASADAAASQSLFVANHSY 365
Cdd:PLN02425 360 KANSLAQLGRYSA-EGESEEAKKGMFVKGYTY 390
|
|
| FBP_aldolase_I |
cd00344 |
Fructose-bisphosphate aldolase class I; Fructose-bisphosphate aldolase class I. Fructose-1, ... |
13-339 |
9.19e-139 |
|
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: 397.64 E-value: 9.19e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 13 EDELRSIANAIVTPGKGILAADESTGSMDKRLNSIGLENTEENRRKYRQLLFTAGADLNKYISGVIMFHETFYQKTDDGK 92
Cdd:cd00344 1 KKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPRIGGVILFHETLYQKADDGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 93 PFTALLQEQGIIPGIKVDKGVVPMAGTIGEGTTQGLDDLNARCAQYKKDGAQFAKWRCVHKISSTTPSVTALKEIASNLA 172
Cdd:cd00344 81 PFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 173 RYASICQQNGLVPIVEPEILPDGEHCLARGQKITETVLSYVYHALNEHHVFLEGTLLKPNMVTSGQSFTgEKPSNADIGL 252
Cdd:cd00344 161 RYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACT-QKFSHEEIAM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 253 ATVTALQRGVPSAVPGVVFLSGGQSEEDATLNLNAINQVSGKKPWALTFSYGRALQASCLAKWAGKDENIAAAQEVLLHR 332
Cdd:cd00344 240 ATVTALRRTVPPAVTGVTFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKR 319
|
....*..
gi 25150450 333 AQVNSLA 339
Cdd:cd00344 320 ALANSLA 326
|
|
| PLN02227 |
PLN02227 |
fructose-bisphosphate aldolase I |
11-365 |
1.02e-116 |
|
fructose-bisphosphate aldolase I
Pssm-ID: 177872 Cd Length: 399 Bit Score: 344.09 E-value: 1.02e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 11 AQEDELRSIANAIVTPGKGILAADESTGSMDKRLNSIGLENTEENRRKYRQLLFTAGAdLNKYISGVIMFHETFYQKTDD 90
Cdd:PLN02227 51 AYADELVKTAKTIASPGHGIMAMDESNATCGKRLASIGLENTEANRQAYRTLLVSAPG-LGQYISGAILFEETLYQSTTD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 91 GKPFTALLQEQGIIPGIKVDKGVVPMAGTIGEGTTQGLDDLNARCAQYKKDGAQFAKWRCVHKISStTPSVTALKEIASN 170
Cdd:PLN02227 130 GKKMVDVLVEQNIVPGIKVDKGLVPLVGSYDESWCQGLDGLASRTAAYYQQGARFAKWRTVVSIPN-GPSALAVKEAAWG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 171 LARYASICQQNGLVPIVEPEILPDGEHCLARGQKITETVLSYVYHALNEHHVFLEGTLLKPNMVTSGQSFTgEKPSNADI 250
Cdd:PLN02227 209 LARYAAISQDSGLVPIVEPEIMLDGEHGIDRTYDVAEKVWAEVFFYLAQNNVMFEGILLKPSMVTPGAEAT-DRATPEQV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 251 GLATVTALQRGVPSAVPGVVFLSGGQSEEDATLNLNAINQvsGKKPWALTFSYGRALQASCLAKWAGKDENIAAAQEVLL 330
Cdd:PLN02227 288 ASYTLKLLRNRIPPAVPGIMFLSGGQSELEATLNLNAMNQ--APNPWHVSFSYARALQNTCLKTWGGKEENVKAAQDILL 365
|
330 340 350
....*....|....*....|....*....|....*
gi 25150450 331 HRAQVNSLASVGKYTGdASADAAASQSLFVANHSY 365
Cdd:PLN02227 366 ARAKANSLAQLGKYTG-EGESEEAKEGMFVKGYTY 399
|
|
| Fba1 |
COG3588 |
Fructose-bisphosphate aldolase class 1 [Carbohydrate transport and metabolism]; ... |
14-329 |
3.78e-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: 331.31 E-value: 3.78e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 14 DELRSIANAIVTPGKGILAA-DESTGSMDKRLNSIGLENTEENRR--------KYRQLLFTAGADLNKYISGVIMFHETF 84
Cdd:COG3588 3 EELNATALAMVANGKGFLAAlDQSGGSTPKALAAYGVEETEYSRReemfdlvhAMRERIITSPAFTGDKISGAILFEETM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 85 YQKTDdGKP-FTALLQEQGIIPGIKVDKGVVPMAGtiGEGTTQGLDDLNARCAQYKKDGAQFAKWRCVHKISsttpSVTA 163
Cdd:COG3588 83 DQKID-GTPtFDYLWEKKGIVPGIKVDKGLKDLAP--GVQLMKGLDGLDERLARAKELGAFGTKWRSVIKIA----NAAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 164 LKEIASNLARYASICQQNGLVPIVEPEILPDGEHCLARGQKITETVLSYVYHALNEHhvflEGTLLKpnMVTSGQSfTGE 243
Cdd:COG3588 156 IKANVHQQARYAALCQEAGLVPIVEPEVLIDGDHKIEREAELTEEILKALFDALPED----EGVMLK--MVIPGKD-NLY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 244 KPSNADiglatvtalqrgvpSAVPGVVFLSGGQSEEDATLNLNAINqvsgkkpwALTFSYGRALQASCLAKWAGKDENIA 323
Cdd:COG3588 229 QALVEH--------------PAVPRVVFLSGGQSREEATAHLNANN--------GLIASFSRALQEGLLAAWSGEEFNAA 286
|
....*.
gi 25150450 324 AAQEVL 329
Cdd:COG3588 287 LAQAID 292
|
|
| FBP_aldolase_I_bact |
cd00949 |
Fructose-1.6-bisphosphate aldolase found in gram +/- bacteria; Fructose-1.6-bisphosphate ... |
13-198 |
6.30e-12 |
|
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: 65.51 E-value: 6.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 13 EDELRSIANaivtpGKGILAA-DESTGSMDKRLNSIGLENTEENRRK--------YRQLLFTAGADLNKYISGVIMFHET 83
Cdd:cd00949 1 QEQLERMKS-----GKGFIAAlDQSGGSTPKALAAYGIEEDAYSNEEemfdlvheMRTRIITSPAFDGDKILGAILFEQT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 84 FYQKTDdGKPFTALL-QEQGIIPGIKVDKGVVPMAGtiGEGTTQGLDDLNARCAQYKKDGAQFAKWRCVHKisstTPSVT 162
Cdd:cd00949 76 MDREIE-GKPTADYLwEKKQIVPFLKVDKGLAEEKN--GVQLMKPIPNLDELLMRAKEKGVFGTKMRSVIK----EANPK 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 25150450 163 ALKEIASNLARYASICQQNGLVPIVEPEI---LPDGEHC 198
Cdd:cd00949 149 GIAAVVDQQFELAKQILSHGLVPIIEPEVdihSADKAKC 187
|
|
| PRK05377 |
PRK05377 |
fructose-1,6-bisphosphate aldolase; Reviewed |
11-191 |
8.32e-09 |
|
fructose-1,6-bisphosphate aldolase; Reviewed
Pssm-ID: 180045 Cd Length: 296 Bit Score: 56.04 E-value: 8.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 11 AQEDELRSIANaivtpGKGILAA-DESTGSMDKRLNSIGLENTEENR--------RKYRQLLFTAGADLNKYISGVIMFH 81
Cdd:PRK05377 2 MNQEQLEKMKN-----GKGFIAAlDQSGGSTPKALKLYGVEEDAYSNeeemfdlvHEMRTRIITSPAFTGDKILGAILFE 76
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150450 82 ETFYQKTDdGKPFTALL-QEQGIIPGIKVDKGVV----------PMAGtigegttqgLDDLNARCAQYKKDGAqfaKWRC 150
Cdd:PRK05377 77 QTMDREIE-GKPTADYLwEKKGVVPFLKVDKGLAeeangvqlmkPIPN---------LDDLLDRAVEKGIFGT---KMRS 143
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170 180 190 200
....*....|....*....|....*....|....*....|.
gi 25150450 151 VHKisstTPSVTALKEIASNLARYASICQQNGLVPIVEPEI 191
Cdd:PRK05377 144 VIK----EANEQGIAAVVAQQFEVAKQILAAGLVPIIEPEV 180
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