|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02561 |
PLN02561 |
triosephosphate isomerase |
1-253 |
0e+00 |
|
triosephosphate isomerase
Pssm-ID: 178175 Cd Length: 253 Bit Score: 512.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 1 MGRKFFVGGNWKCNGTTDQVDKIVKILNEGQIASTDVVEVVVSPPYVFLPVVKSQLRPEIQVAAQNCWVKKGGAFTGEVS 80
Cdd:PLN02561 1 MARKFFVGGNWKCNGTVEEVKKIVTTLNEAEVPSEDVVEVVVSPPFVFLPLVKSLLRPDFQVAAQNCWVKKGGAFTGEIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 81 AEMLVNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIAERIKDWTN 160
Cdd:PLN02561 81 AEMLVNLGIPWVILGHSERRALLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIADKVSDWAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 161 VVVAYEPVWAIGTGKVATPDQAQEVHDGLRKWLAANVSAEVAESTRIIYGGSVTGANCKELAAKPDVDGFLVGGASLKPE 240
Cdd:PLN02561 161 VVLAYEPVWAIGTGKVATPAQAQEVHDELRKWLHKNVSPEVAATTRIIYGGSVTGANCKELAAQPDVDGFLVGGASLKPE 240
|
250
....*....|...
gi 306415973 241 FIDIINSATVKSA 253
Cdd:PLN02561 241 FIDIIKSATVKKS 253
|
|
| TIM |
cd00311 |
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ... |
5-246 |
3.28e-127 |
|
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of dihydroxyacetone phosphate and D-glyceraldehyde-3-phosphate. The reaction is very efficient and requires neither cofactors nor metal ions. TIM, usually homodimeric, but in some organisms tetrameric, is ubiqitous and conserved in function across eukaryotes, bacteria and archaea.
Pssm-ID: 238190 Cd Length: 242 Bit Score: 360.31 E-value: 3.28e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 5 FFVGGNWKCNGTTDQVDKIVKILNEGQIASTDVvEVVVSPPYVFLPVVKSQLR-PEIQVAAQNCWVKKGGAFTGEVSAEM 83
Cdd:cd00311 1 PLVAGNWKMNGTLAEALELAKALNAVLKDESGV-EVVVAPPFTYLAAVAEALEgSKIKVGAQNVSPEDSGAFTGEISAEM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 84 LVNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIAERIKDWTNVVV 163
Cdd:cd00311 80 LKDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 164 AYEPVWAIGTGKVATPDQAQEVHDGLRKWLAANVSaEVAESTRIIYGGSVTGANCKELAAKPDVDGFLVGGASLKPE-FI 242
Cdd:cd00311 160 AYEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYG-EVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAEsFL 238
|
....
gi 306415973 243 DIIN 246
Cdd:cd00311 239 DIIK 242
|
|
| TIM |
pfam00121 |
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ... |
5-248 |
9.70e-120 |
|
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic enzyme that catalyzes the reversible interconversion of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. TIM plays an important role in several metabolic pathways and is essential for efficient energy production, present in eukaryotes and prokaryotes. TIM is a dimer of identical subunits, each of which is made up of about 250 amino-acid residues. A glutamic acid residue is involved in the catalytic mechanism. The tertiary structure of TIM has eight beta/alpha motifs folded into a barrel structure. The sequence around the active site residue is perfectly conserved in all known TIM's. Deficiencies in TIM are associated with haemolytic anaemia coupled with a progressive, severe neurological disorder.
Pssm-ID: 459680 Cd Length: 244 Bit Score: 341.41 E-value: 9.70e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 5 FFVGGNWKCNGTTDQVDKIVKILNEgQIASTDVVEVVVSPPYVFLPVVKSQLRPEIQVAAQNCWVKKGGAFTGEVSAEML 84
Cdd:pfam00121 1 PIIAGNWKMNGTLAEAAELLAELAE-ALADESGVEVVVAPPFTYLSAVAELLGSNIKVGAQNVDPEESGAFTGEISAEML 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 85 VNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIAERIKDWT-NVVV 163
Cdd:pfam00121 80 KDLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQkNLVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 164 AYEPVWAIGTGKVATPDQAQEVHDGLRKWLAANvSAEVAESTRIIYGGSVTGANCKELAAKPDVDGFLVGGASLKPE-FI 242
Cdd:pfam00121 160 AYEPVWAIGTGKTATPEQAQEVHAFIRAVLAEL-YKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEdFL 238
|
....*.
gi 306415973 243 DIINSA 248
Cdd:pfam00121 239 DIINAA 244
|
|
| TpiA |
COG0149 |
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ... |
3-247 |
2.84e-119 |
|
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 439919 [Multi-domain] Cd Length: 249 Bit Score: 340.50 E-value: 2.84e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 3 RKFFVGGNWKCNGTTDQVDKIVKILNEGqIASTDVVEVVVSPPYVFLPVVKSQLR-PEIQVAAQNCWVKKGGAFTGEVSA 81
Cdd:COG0149 2 RKPLIAGNWKMNGTLAEAKALLAALAAA-LADLADVEVVVCPPFTYLAAVAEALAgSPIALGAQNVHWEDSGAYTGEISA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 82 EMLVNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIAERI--KDWT 159
Cdd:COG0149 81 AMLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLsaEQAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 160 NVVVAYEPVWAIGTGKVATPDQAQEVHDGLRKWLAANVSAEVAESTRIIYGGSVTGANCKELAAKPDVDGFLVGGASLKP 239
Cdd:COG0149 161 NVVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDA 240
|
....*....
gi 306415973 240 E-FIDIINS 247
Cdd:COG0149 241 EdFLAIVRA 249
|
|
| tim |
TIGR00419 |
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ... |
6-240 |
6.38e-80 |
|
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that catalyzes the reversible interconversion of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. The active site of the enzyme is located between residues 240-258 of the model ([AV]-Y-E-P-[LIVM]-W-[SA]-I-G-T-[GK]) with E being the active site residue. There is a slight deviation from this sequence within the archeal members of this family. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 129513 [Multi-domain] Cd Length: 205 Bit Score: 238.93 E-value: 6.38e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 6 FVGGNWK-CNGTTDQVDKIVKILNEgQIASTDVVEVVVSPPYVFLPVVKSQLrpEIQVAAQNCWVKKGGAFTGEVSAEML 84
Cdd:TIGR00419 1 LVIGNWKtYNESRGMRALEVAKIAE-EVASEAGVAVAVAPPFVDLPMIKREV--EIPVYAQHVDAVLSGAHTGEISAEML 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 85 VNLSIPWVILGHSERRSLLGEsnefVGDKVAYALSQGLKVIACVgetleqresgstmDVVAAQTKAIAerikdWTNVVVA 164
Cdd:TIGR00419 78 KDIGAKGTLINHSERRMKLAD----IEKKIARLKELGLTSVVCT-------------NNVLTTAAAAA-----LEPDVVA 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 306415973 165 YEPVWAIGTGKVATPDQAQEVHDGLRkwlaanVSAEVAESTRIIYGGSVTGANCKELAAKPDVDGFLVGGASLKPE 240
Cdd:TIGR00419 136 VEPPELIGTGIPVSPAQPEVVHGSVR------AVKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02561 |
PLN02561 |
triosephosphate isomerase |
1-253 |
0e+00 |
|
triosephosphate isomerase
Pssm-ID: 178175 Cd Length: 253 Bit Score: 512.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 1 MGRKFFVGGNWKCNGTTDQVDKIVKILNEGQIASTDVVEVVVSPPYVFLPVVKSQLRPEIQVAAQNCWVKKGGAFTGEVS 80
Cdd:PLN02561 1 MARKFFVGGNWKCNGTVEEVKKIVTTLNEAEVPSEDVVEVVVSPPFVFLPLVKSLLRPDFQVAAQNCWVKKGGAFTGEIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 81 AEMLVNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIAERIKDWTN 160
Cdd:PLN02561 81 AEMLVNLGIPWVILGHSERRALLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIADKVSDWAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 161 VVVAYEPVWAIGTGKVATPDQAQEVHDGLRKWLAANVSAEVAESTRIIYGGSVTGANCKELAAKPDVDGFLVGGASLKPE 240
Cdd:PLN02561 161 VVLAYEPVWAIGTGKVATPAQAQEVHDELRKWLHKNVSPEVAATTRIIYGGSVTGANCKELAAQPDVDGFLVGGASLKPE 240
|
250
....*....|...
gi 306415973 241 FIDIINSATVKSA 253
Cdd:PLN02561 241 FIDIIKSATVKKS 253
|
|
| PTZ00333 |
PTZ00333 |
triosephosphate isomerase; Provisional |
1-248 |
1.08e-137 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 240365 Cd Length: 255 Bit Score: 387.35 E-value: 1.08e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 1 MGRKFFVGGNWKCNGTTDQVDKIVKILNEGQIaSTDVVEVVVSPPYVFLPVVKSQLR-PEIQVAAQNCWVKKGGAFTGEV 79
Cdd:PTZ00333 2 MKRKPFVGGNWKCNGTKASIKELIDSFNKLKF-DPNNVDVVVAPPSLHIPLVQEKLKnKNFKISSQNVSLTGSGAFTGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 80 SAEMLVNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIAERIKD-- 157
Cdd:PTZ00333 81 SAEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDea 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 158 WTNVVVAYEPVWAIGTGKVATPDQAQEVHDGLRKWLAANVSAEVAESTRIIYGGSVTGANCKELAAKPDVDGFLVGGASL 237
Cdd:PTZ00333 161 WDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASL 240
|
250
....*....|.
gi 306415973 238 KPEFIDIINSA 248
Cdd:PTZ00333 241 KPDFVDIIKSA 251
|
|
| TIM |
cd00311 |
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ... |
5-246 |
3.28e-127 |
|
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of dihydroxyacetone phosphate and D-glyceraldehyde-3-phosphate. The reaction is very efficient and requires neither cofactors nor metal ions. TIM, usually homodimeric, but in some organisms tetrameric, is ubiqitous and conserved in function across eukaryotes, bacteria and archaea.
Pssm-ID: 238190 Cd Length: 242 Bit Score: 360.31 E-value: 3.28e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 5 FFVGGNWKCNGTTDQVDKIVKILNEGQIASTDVvEVVVSPPYVFLPVVKSQLR-PEIQVAAQNCWVKKGGAFTGEVSAEM 83
Cdd:cd00311 1 PLVAGNWKMNGTLAEALELAKALNAVLKDESGV-EVVVAPPFTYLAAVAEALEgSKIKVGAQNVSPEDSGAFTGEISAEM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 84 LVNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIAERIKDWTNVVV 163
Cdd:cd00311 80 LKDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 164 AYEPVWAIGTGKVATPDQAQEVHDGLRKWLAANVSaEVAESTRIIYGGSVTGANCKELAAKPDVDGFLVGGASLKPE-FI 242
Cdd:cd00311 160 AYEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYG-EVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAEsFL 238
|
....
gi 306415973 243 DIIN 246
Cdd:cd00311 239 DIIK 242
|
|
| TIM |
pfam00121 |
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ... |
5-248 |
9.70e-120 |
|
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic enzyme that catalyzes the reversible interconversion of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. TIM plays an important role in several metabolic pathways and is essential for efficient energy production, present in eukaryotes and prokaryotes. TIM is a dimer of identical subunits, each of which is made up of about 250 amino-acid residues. A glutamic acid residue is involved in the catalytic mechanism. The tertiary structure of TIM has eight beta/alpha motifs folded into a barrel structure. The sequence around the active site residue is perfectly conserved in all known TIM's. Deficiencies in TIM are associated with haemolytic anaemia coupled with a progressive, severe neurological disorder.
Pssm-ID: 459680 Cd Length: 244 Bit Score: 341.41 E-value: 9.70e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 5 FFVGGNWKCNGTTDQVDKIVKILNEgQIASTDVVEVVVSPPYVFLPVVKSQLRPEIQVAAQNCWVKKGGAFTGEVSAEML 84
Cdd:pfam00121 1 PIIAGNWKMNGTLAEAAELLAELAE-ALADESGVEVVVAPPFTYLSAVAELLGSNIKVGAQNVDPEESGAFTGEISAEML 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 85 VNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIAERIKDWT-NVVV 163
Cdd:pfam00121 80 KDLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQkNLVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 164 AYEPVWAIGTGKVATPDQAQEVHDGLRKWLAANvSAEVAESTRIIYGGSVTGANCKELAAKPDVDGFLVGGASLKPE-FI 242
Cdd:pfam00121 160 AYEPVWAIGTGKTATPEQAQEVHAFIRAVLAEL-YKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEdFL 238
|
....*.
gi 306415973 243 DIINSA 248
Cdd:pfam00121 239 DIINAA 244
|
|
| TpiA |
COG0149 |
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ... |
3-247 |
2.84e-119 |
|
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 439919 [Multi-domain] Cd Length: 249 Bit Score: 340.50 E-value: 2.84e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 3 RKFFVGGNWKCNGTTDQVDKIVKILNEGqIASTDVVEVVVSPPYVFLPVVKSQLR-PEIQVAAQNCWVKKGGAFTGEVSA 81
Cdd:COG0149 2 RKPLIAGNWKMNGTLAEAKALLAALAAA-LADLADVEVVVCPPFTYLAAVAEALAgSPIALGAQNVHWEDSGAYTGEISA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 82 EMLVNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIAERI--KDWT 159
Cdd:COG0149 81 AMLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLsaEQAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 160 NVVVAYEPVWAIGTGKVATPDQAQEVHDGLRKWLAANVSAEVAESTRIIYGGSVTGANCKELAAKPDVDGFLVGGASLKP 239
Cdd:COG0149 161 NVVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDA 240
|
....*....
gi 306415973 240 E-FIDIINS 247
Cdd:COG0149 241 EdFLAIVRA 249
|
|
| tpiA |
PRK00042 |
triosephosphate isomerase; Provisional |
3-248 |
1.89e-113 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 234589 Cd Length: 250 Bit Score: 325.54 E-value: 1.89e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 3 RKFFVGGNWKCNGTTDQVDKIVKILNEgQIASTDVVEVVVSPPYVFLPVVKSQLRPE-IQVAAQNCWVKKGGAFTGEVSA 81
Cdd:PRK00042 1 RKPIIAGNWKMNKTLAEAKALVEELKA-ALPDADGVEVAVAPPFTALASVKEALKGSnIKLGAQNVHPEDSGAFTGEISA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 82 EMLVNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIAERI--KDWT 159
Cdd:PRK00042 80 EMLKDLGVKYVIIGHSERRQYFGETDELVNKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLEAALAGLsaEQFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 160 NVVVAYEPVWAIGTGKVATPDQAQEVHDGLRKWLAANVSaEVAESTRIIYGGSVTGANCKELAAKPDVDGFLVGGASLKP 239
Cdd:PRK00042 160 NLVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYG-EVAEKVRILYGGSVKPDNAAELMAQPDIDGALVGGASLKA 238
|
250
....*....|
gi 306415973 240 E-FIDIINSA 248
Cdd:PRK00042 239 EdFLAIVKAA 248
|
|
| PLN02429 |
PLN02429 |
triosephosphate isomerase |
4-251 |
5.42e-98 |
|
triosephosphate isomerase
Pssm-ID: 166070 Cd Length: 315 Bit Score: 289.00 E-value: 5.42e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 4 KFFVGGNWKCNGTTDQVDKIVKILNEGQIASTdvVEVVVSPPYVFLPVVKSQLRPEIQVAAQNCWVKKGGAFTGEVSAEM 83
Cdd:PLN02429 65 KFFVGGNWKCNGTKDSIAKLISDLNSATLEAD--VDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEISVEQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 84 LVNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIAERIKDWTNVVV 163
Cdd:PLN02429 143 LKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDNIVV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 164 AYEPVWAIGTGKVATPDQAQEVHDGLRKWLAANVSAEVAESTRIIYGGSVTGANCKELAAKPDVDGFLVGGASLK-PEFI 242
Cdd:PLN02429 223 AYEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKgPEFA 302
|
....*....
gi 306415973 243 DIINSATVK 251
Cdd:PLN02429 303 TIVNSVTSK 311
|
|
| PRK13962 |
PRK13962 |
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional |
3-249 |
2.70e-84 |
|
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional
Pssm-ID: 237572 [Multi-domain] Cd Length: 645 Bit Score: 263.90 E-value: 2.70e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 3 RKFFVGGNWKCNGTTDQ----VDKIVKILNEGQiastdvVEVVVSPPYVFLPVVKSQLR-PEIQVAAQNCWVKKGGAFTG 77
Cdd:PRK13962 397 RKPIIAGNWKMNKTPAEakefVNELKKYVKDAQ------AEVVVCPPFTALPSVKEAVDgSNIKLGAQNVFYEEKGAYTG 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 78 EVSAEMLVNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAI-----A 152
Cdd:PRK13962 471 EISGPMLAEIGVEYVIIGHSERRQYFGETDELVNKKVLAALKAGLTPILCVGETLDERESGITFDVVRLQLKAAlnglsA 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 153 ERIKDwtnVVVAYEPVWAIGTGKVATPDQAQEVHDGLRKWLAANVSAEVAESTRIIYGGSVTGANCKELAAKPDVDGFLV 232
Cdd:PRK13962 551 EQVKK---VVIAYEPVWAIGTGKVATPEQAQEVHAFIRKLVAELYGEEAARKVRILYGGSVKSENAAGLFNQPDIDGGLV 627
|
250
....*....|....*...
gi 306415973 233 GGASLKP-EFIDIINSAT 249
Cdd:PRK13962 628 GGASLKAqEFAAIANYFI 645
|
|
| tim |
TIGR00419 |
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ... |
6-240 |
6.38e-80 |
|
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that catalyzes the reversible interconversion of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. The active site of the enzyme is located between residues 240-258 of the model ([AV]-Y-E-P-[LIVM]-W-[SA]-I-G-T-[GK]) with E being the active site residue. There is a slight deviation from this sequence within the archeal members of this family. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 129513 [Multi-domain] Cd Length: 205 Bit Score: 238.93 E-value: 6.38e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 6 FVGGNWK-CNGTTDQVDKIVKILNEgQIASTDVVEVVVSPPYVFLPVVKSQLrpEIQVAAQNCWVKKGGAFTGEVSAEML 84
Cdd:TIGR00419 1 LVIGNWKtYNESRGMRALEVAKIAE-EVASEAGVAVAVAPPFVDLPMIKREV--EIPVYAQHVDAVLSGAHTGEISAEML 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 85 VNLSIPWVILGHSERRSLLGEsnefVGDKVAYALSQGLKVIACVgetleqresgstmDVVAAQTKAIAerikdWTNVVVA 164
Cdd:TIGR00419 78 KDIGAKGTLINHSERRMKLAD----IEKKIARLKELGLTSVVCT-------------NNVLTTAAAAA-----LEPDVVA 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 306415973 165 YEPVWAIGTGKVATPDQAQEVHDGLRkwlaanVSAEVAESTRIIYGGSVTGANCKELAAKPDVDGFLVGGASLKPE 240
Cdd:TIGR00419 136 VEPPELIGTGIPVSPAQPEVVHGSVR------AVKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
|
|
| PRK14565 |
PRK14565 |
triosephosphate isomerase; Provisional |
5-248 |
1.13e-59 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 237758 Cd Length: 237 Bit Score: 188.81 E-value: 1.13e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 5 FFVGGNWKCNGTTDQVDKIVKILNEGQIASTDVVEVVVSPPYVFLPVVKSqLRPEIQVAAQNCWVKKGGAFTGEVSAEML 84
Cdd:PRK14565 3 FLIVANWKMNGDFSLFSSFLKELSNKLANNEITLKLVICPPFTAMSSFVE-CNPNIKLGAQNCFYGSSGGYTGEISAKML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 85 VNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKaiaERIKDWTNVVVA 164
Cdd:PRK14565 82 KECGCSYVILGHSERRSTFHETDSDIRLKAESAIESGLIPIICVGETLEDRENGMTKDVLLEQCS---NCLPKHGEFIIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 165 YEPVWAIGTGKVATPDQAQEVHDGLRKWLAAnvsaevaesTRIIYGGSVTGANCKELAAKPDVDGFLVGGASLKPE-FID 243
Cdd:PRK14565 159 YEPVWAIGGSTIPSNDAIAEAFEIIRSYDSK---------SHIIYGGSVNQENIRDLKSINQLSGVLVGSASLDVDsFCK 229
|
....*
gi 306415973 244 IINSA 248
Cdd:PRK14565 230 IIQQV 234
|
|
| PRK14905 |
PRK14905 |
triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; ... |
1-233 |
2.27e-41 |
|
triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; Provisional
Pssm-ID: 184898 [Multi-domain] Cd Length: 355 Bit Score: 144.79 E-value: 2.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 1 MGRKFFVGGNWKC-NGTTDQVDKIVKILNEGQIASTDV-VEVVVSPPYVFLP----VVKSQL-RPEIQVAAQNCWVKKGG 73
Cdd:PRK14905 1 MAKKIYFGTNLKMyKGNAETVDYLSELLAFAEKFKSDYdIELFVIPSYIALKdaveAAASETgHPKIKIGAQNMNAKDKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 74 AFTGEVSAEMLVNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIAE 153
Cdd:PRK14905 81 QFTGEISPLMLKELGIELVMIGHSERRHVLKETDQEENEKVLAALKHGFITLLCIGETLEQKNYNISDEVLRTQLKIGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 154 --RIKDWTNVVVAYEPVWAIGTGKV-ATPDQAQEVHDGLRKWLaANVSAEVAESTRIIYGGSVTGANCKELAAKPDVDGF 230
Cdd:PRK14905 161 gvSAEQLPHLFIAYEPVWAIGEGGIpASAEYADEKHAIIKQCL-FELFAEESKKIPVLYGGSVNLENANELIMKPHIDGL 239
|
...
gi 306415973 231 LVG 233
Cdd:PRK14905 240 FIG 242
|
|
| PRK15492 |
PRK15492 |
triosephosphate isomerase; Provisional |
3-233 |
2.48e-33 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 185389 Cd Length: 260 Bit Score: 121.64 E-value: 2.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 3 RKFFVGGNWKC-NGTTDQVDKIVKiLNE--GQIASTDVVEVVVSPPYVFLPVVKSQLRP-----EIQVAAQNCWVKKGGA 74
Cdd:PRK15492 2 KKIYFGTNLKMyKGIADATDFLAK-LSElaDDIPADKDIELFVIPSFTAIQDAIAATLAiphdhPIIIGAQNMNPNDNGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 75 FTGEVSAEMLVNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIAER 154
Cdd:PRK15492 81 FTGDISPLMLKEIGTQLVMIGHSERRHKFGETDQEENAKVLAALKHDFTTLLCVGETLEQKNYGISDEILRTQLKIGLHG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 155 I--KDWTNVVVAYEPVWAIGTGKV-ATPDQAQEVHDGLRKWLaANVSAEVAESTRIIYGGSVTGANCKELAAKPDVDGFL 231
Cdd:PRK15492 161 InpDQLAKLRIAYEPVWAIGEAGIpASADYADEKHAVIKQCL-IELFGDAGDDIPVFYGGSVNAENANELFGQPHIDGLF 239
|
..
gi 306415973 232 VG 233
Cdd:PRK15492 240 IG 241
|
|
| PRK04302 |
PRK04302 |
triosephosphate isomerase; Provisional |
38-238 |
2.28e-09 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 235274 Cd Length: 223 Bit Score: 56.03 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 38 VEVVVSPPYVFLPVVKSQLrpEIQVAAQNCWVKKGGAFTGEVSAEMLVNLSIPWVILGHSERRSLLGEsnefVGDKVAYA 117
Cdd:PRK04302 37 VRIAVAPQALDIRRVAEEV--DIPVYAQHVDPVEPGSHTGHILPEAVKDAGAVGTLINHSERRLTLAD----IEAVVERA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 118 LSQGLKVIACVGEtleqresgstmdvvAAQTKAIAERIKDWtnvvVAYEPVWAIGTGK-VATPDQaqevhDGLRKwlAAN 196
Cdd:PRK04302 111 KKLGLESVVCVNN--------------PETSAAAAALGPDY----VAVEPPELIGTGIpVSKAKP-----EVVED--AVE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 306415973 197 VSAEVAESTRIIYGGSVTGANCKELAAKPDVDGFLVGGASLK 238
Cdd:PRK04302 166 AVKKVNPDVKVLCGAGISTGEDVKAALELGADGVLLASGVVK 207
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
75-164 |
9.57e-03 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 37.16 E-value: 9.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 75 FTGEVS-AEMLVNLSI-PWVILGHSerrslLGEsneFVGDKVAYALS--QGLKVIACVGETLEQRESGSTMDVVAAQTKA 150
Cdd:COG3321 597 FAVEYAlARLWRSWGVrPDAVIGHS-----VGE---YAAACVAGVLSleDALRLVAARGRLMQALPGGGAMLAVGLSEEE 668
|
90
....*....|....
gi 306415973 151 IAERIKDWTNVVVA 164
Cdd:COG3321 669 VEALLAGYDGVSIA 682
|
|
|