|
Name |
Accession |
Description |
Interval |
E-value |
| tpiA |
PRK00042 |
triosephosphate isomerase; Provisional |
2-240 |
7.83e-128 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 234589 Cd Length: 250 Bit Score: 362.13 E-value: 7.83e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 2 RHPVVMGNWKLNGSKEMVVDLLNGLNAELEGVTGVDVAVAPPALFVDLAERTLteAGSAIILGAQNSDLNNSGAFTGDMS 81
Cdd:PRK00042 1 RKPIIAGNWKMNKTLAEAKALVEELKAALPDADGVEVAVAPPFTALASVKEAL--KGSNIKLGAQNVHPEDSGAFTGEIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 82 PAMLKEFGASHIIIGHSERREYHNESDEFVAKKFAFLKENGLTPVLCIGESEAQNEAGETVAVCARQLDAVINTQGVEAL 161
Cdd:PRK00042 79 AEMLKDLGVKYVIIGHSERRQYFGETDELVNKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLEAALAGLSAEQF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 857962664 162 EGAIIAYEPIWAIGTGKAATAEDAQRIHAQIRAHIAEKSEEVAKKVVIQYGGSVKPENAAAYFAQPDIDGALVGGAALD 240
Cdd:PRK00042 159 ANLVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYGEVAEKVRILYGGSVKPDNAAELMAQPDIDGALVGGASLK 237
|
|
| TpiA |
COG0149 |
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ... |
1-240 |
1.49e-127 |
|
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: 361.30 E-value: 1.49e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 1 MRHPVVMGNWKLNGSKEMVVDLLNGLNAELEGVTGVDVAVAPPALFVDLAERTLteAGSAIILGAQNSDLNNSGAFTGDM 80
Cdd:COG0149 1 MRKPLIAGNWKMNGTLAEAKALLAALAAALADLADVEVVVCPPFTYLAAVAEAL--AGSPIALGAQNVHWEDSGAYTGEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 81 SPAMLKEFGASHIIIGHSERREYHNESDEFVAKKFAFLKENGLTPVLCIGESEAQNEAGETVAVCARQLDAVINTQGVEA 160
Cdd:COG0149 79 SAAMLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLSAEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 161 LEGAIIAYEPIWAIGTGKAATAEDAQRIHAQIRAHIAEK-SEEVAKKVVIQYGGSVKPENAAAYFAQPDIDGALVGGAAL 239
Cdd:COG0149 159 AANVVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELyGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASL 238
|
.
gi 857962664 240 D 240
Cdd:COG0149 239 D 239
|
|
| TIM |
cd00311 |
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ... |
4-240 |
7.93e-117 |
|
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: 334.12 E-value: 7.93e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 4 PVVMGNWKLNGSKEMVVDLLNGLNAELEGVTGVDVAVAPPALFVDLAERTLteAGSAIILGAQNSDLNNSGAFTGDMSPA 83
Cdd:cd00311 1 PLVAGNWKMNGTLAEALELAKALNAVLKDESGVEVVVAPPFTYLAAVAEAL--EGSKIKVGAQNVSPEDSGAFTGEISAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 84 MLKEFGASHIIIGHSERREYHNESDEFVAKKFAFLKENGLTPVLCIGESEAQNEAGETVAVCARQLDAVIntQGVEALEG 163
Cdd:cd00311 79 MLKDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVL--AGVEDLAP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 857962664 164 AIIAYEPIWAIGTGKAATAEDAQRIHAQIRAHIAEKSEEVAKKVVIQYGGSVKPENAAAYFAQPDIDGALVGGAALD 240
Cdd:cd00311 157 VVIAYEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYGEVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLK 233
|
|
| TIM |
pfam00121 |
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ... |
4-240 |
7.39e-116 |
|
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: 331.78 E-value: 7.39e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 4 PVVMGNWKLNGSKEMVVDLLNGLNAELEGVTGVDVAVAPPALFVDLAERTLteaGSAIILGAQNSDLNNSGAFTGDMSPA 83
Cdd:pfam00121 1 PIIAGNWKMNGTLAEAAELLAELAEALADESGVEVVVAPPFTYLSAVAELL---GSNIKVGAQNVDPEESGAFTGEISAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 84 MLKEFGASHIIIGHSERREYHNESDEFVAKKFAFLKENGLTPVLCIGESEAQNEAGETVAVCARQLDAVINTQGVEAlEG 163
Cdd:pfam00121 78 MLKDLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQ-KN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 857962664 164 AIIAYEPIWAIGTGKAATAEDAQRIHAQIRAHIAEKSEEVAKKVVIQYGGSVKPENAAAYFAQPDIDGALVGGAALD 240
Cdd:pfam00121 157 LVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLK 233
|
|
| tim |
TIGR00419 |
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ... |
5-239 |
3.16e-59 |
|
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: 186.55 E-value: 3.16e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 5 VVMGNWK-LNGSKEMVVDLLNGLNAELEGVTGVDVAVAPPALFVDLAERTLTeagsaIILGAQNSDLNNSGAFTGDMSPA 83
Cdd:TIGR00419 1 LVIGNWKtYNESRGMRALEVAKIAEEVASEAGVAVAVAPPFVDLPMIKREVE-----IPVYAQHVDAVLSGAHTGEISAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 84 MLKEFGASHIIIGHSERReyHNESDefVAKKFAFLKENGLTPVLCIgeseaqneagetvavcarqlDAVINTQGVEALEG 163
Cdd:TIGR00419 76 MLKDIGAKGTLINHSERR--MKLAD--IEKKIARLKELGLTSVVCT--------------------NNVLTTAAAAALEP 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 857962664 164 AIIAYEPIWAIGTGKAATAEDAQRIHAQIRAhiaekSEEVAKKVVIQYGGSVKPENAAAYFAQPDIDGALVGGAAL 239
Cdd:TIGR00419 132 DVVAVEPPELIGTGIPVSPAQPEVVHGSVRA-----VKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSL 202
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| tpiA |
PRK00042 |
triosephosphate isomerase; Provisional |
2-240 |
7.83e-128 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 234589 Cd Length: 250 Bit Score: 362.13 E-value: 7.83e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 2 RHPVVMGNWKLNGSKEMVVDLLNGLNAELEGVTGVDVAVAPPALFVDLAERTLteAGSAIILGAQNSDLNNSGAFTGDMS 81
Cdd:PRK00042 1 RKPIIAGNWKMNKTLAEAKALVEELKAALPDADGVEVAVAPPFTALASVKEAL--KGSNIKLGAQNVHPEDSGAFTGEIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 82 PAMLKEFGASHIIIGHSERREYHNESDEFVAKKFAFLKENGLTPVLCIGESEAQNEAGETVAVCARQLDAVINTQGVEAL 161
Cdd:PRK00042 79 AEMLKDLGVKYVIIGHSERRQYFGETDELVNKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLEAALAGLSAEQF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 857962664 162 EGAIIAYEPIWAIGTGKAATAEDAQRIHAQIRAHIAEKSEEVAKKVVIQYGGSVKPENAAAYFAQPDIDGALVGGAALD 240
Cdd:PRK00042 159 ANLVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYGEVAEKVRILYGGSVKPDNAAELMAQPDIDGALVGGASLK 237
|
|
| TpiA |
COG0149 |
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ... |
1-240 |
1.49e-127 |
|
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: 361.30 E-value: 1.49e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 1 MRHPVVMGNWKLNGSKEMVVDLLNGLNAELEGVTGVDVAVAPPALFVDLAERTLteAGSAIILGAQNSDLNNSGAFTGDM 80
Cdd:COG0149 1 MRKPLIAGNWKMNGTLAEAKALLAALAAALADLADVEVVVCPPFTYLAAVAEAL--AGSPIALGAQNVHWEDSGAYTGEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 81 SPAMLKEFGASHIIIGHSERREYHNESDEFVAKKFAFLKENGLTPVLCIGESEAQNEAGETVAVCARQLDAVINTQGVEA 160
Cdd:COG0149 79 SAAMLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLSAEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 161 LEGAIIAYEPIWAIGTGKAATAEDAQRIHAQIRAHIAEK-SEEVAKKVVIQYGGSVKPENAAAYFAQPDIDGALVGGAAL 239
Cdd:COG0149 159 AANVVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELyGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASL 238
|
.
gi 857962664 240 D 240
Cdd:COG0149 239 D 239
|
|
| TIM |
cd00311 |
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ... |
4-240 |
7.93e-117 |
|
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: 334.12 E-value: 7.93e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 4 PVVMGNWKLNGSKEMVVDLLNGLNAELEGVTGVDVAVAPPALFVDLAERTLteAGSAIILGAQNSDLNNSGAFTGDMSPA 83
Cdd:cd00311 1 PLVAGNWKMNGTLAEALELAKALNAVLKDESGVEVVVAPPFTYLAAVAEAL--EGSKIKVGAQNVSPEDSGAFTGEISAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 84 MLKEFGASHIIIGHSERREYHNESDEFVAKKFAFLKENGLTPVLCIGESEAQNEAGETVAVCARQLDAVIntQGVEALEG 163
Cdd:cd00311 79 MLKDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVL--AGVEDLAP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 857962664 164 AIIAYEPIWAIGTGKAATAEDAQRIHAQIRAHIAEKSEEVAKKVVIQYGGSVKPENAAAYFAQPDIDGALVGGAALD 240
Cdd:cd00311 157 VVIAYEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYGEVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLK 233
|
|
| TIM |
pfam00121 |
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ... |
4-240 |
7.39e-116 |
|
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: 331.78 E-value: 7.39e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 4 PVVMGNWKLNGSKEMVVDLLNGLNAELEGVTGVDVAVAPPALFVDLAERTLteaGSAIILGAQNSDLNNSGAFTGDMSPA 83
Cdd:pfam00121 1 PIIAGNWKMNGTLAEAAELLAELAEALADESGVEVVVAPPFTYLSAVAELL---GSNIKVGAQNVDPEESGAFTGEISAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 84 MLKEFGASHIIIGHSERREYHNESDEFVAKKFAFLKENGLTPVLCIGESEAQNEAGETVAVCARQLDAVINTQGVEAlEG 163
Cdd:pfam00121 78 MLKDLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQ-KN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 857962664 164 AIIAYEPIWAIGTGKAATAEDAQRIHAQIRAHIAEKSEEVAKKVVIQYGGSVKPENAAAYFAQPDIDGALVGGAALD 240
Cdd:pfam00121 157 LVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLK 233
|
|
| PTZ00333 |
PTZ00333 |
triosephosphate isomerase; Provisional |
1-240 |
8.41e-95 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 240365 Cd Length: 255 Bit Score: 278.72 E-value: 8.41e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 1 MRHPVVMGNWKLNGSKEMVVDLLNGLNAELEGVTGVDVAVAPPALFVDLAERTLTEAGSAIilGAQNSDLNNSGAFTGDM 80
Cdd:PTZ00333 3 KRKPFVGGNWKCNGTKASIKELIDSFNKLKFDPNNVDVVVAPPSLHIPLVQEKLKNKNFKI--SSQNVSLTGSGAFTGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 81 SPAMLKEFGASHIIIGHSERREYHNESDEFVAKKFAFLKENGLTPVLCIGESEAQNEAGETVAVCARQLDAVINTQGVEA 160
Cdd:PTZ00333 81 SAEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 161 LEGAIIAYEPIWAIGTGKAATAEDAQRIHAQIRAHIAEK-SEEVAKKVVIQYGGSVKPENAAAYFAQPDIDGALVGGAAL 239
Cdd:PTZ00333 161 WDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKvGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASL 240
|
.
gi 857962664 240 D 240
Cdd:PTZ00333 241 K 241
|
|
| PRK13962 |
PRK13962 |
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional |
1-240 |
2.30e-83 |
|
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional
Pssm-ID: 237572 [Multi-domain] Cd Length: 645 Bit Score: 261.59 E-value: 2.30e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 1 MRHPVVMGNWKLNGSKEMVVDLLNGLNAELEGVTGvDVAVAPPalFVDLAERTLTEAGSAIILGAQNSDLNNSGAFTGDM 80
Cdd:PRK13962 396 PRKPIIAGNWKMNKTPAEAKEFVNELKKYVKDAQA-EVVVCPP--FTALPSVKEAVDGSNIKLGAQNVFYEEKGAYTGEI 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 81 SPAMLKEFGASHIIIGHSERREYHNESDEFVAKKFAFLKENGLTPVLCIGESEAQNEAGETVAVCARQLDAVINTQGVEA 160
Cdd:PRK13962 473 SGPMLAEIGVEYVIIGHSERRQYFGETDELVNKKVLAALKAGLTPILCVGETLDERESGITFDVVRLQLKAALNGLSAEQ 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 161 LEGAIIAYEPIWAIGTGKAATAEDAQRIHAQIRAHIAEK-SEEVAKKVVIQYGGSVKPENAAAYFAQPDIDGALVGGAAL 239
Cdd:PRK13962 553 VKKVVIAYEPVWAIGTGKVATPEQAQEVHAFIRKLVAELyGEEAARKVRILYGGSVKSENAAGLFNQPDIDGGLVGGASL 632
|
.
gi 857962664 240 D 240
Cdd:PRK13962 633 K 633
|
|
| PLN02561 |
PLN02561 |
triosephosphate isomerase |
6-239 |
1.32e-60 |
|
triosephosphate isomerase
Pssm-ID: 178175 Cd Length: 253 Bit Score: 191.57 E-value: 1.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 6 VMGNWKLNGSKEMVVDLLNGLN-AELEGVTGVDVAVAPPALFVDLAERTLTeagSAIILGAQNSDLNNSGAFTGDMSPAM 84
Cdd:PLN02561 7 VGGNWKCNGTVEEVKKIVTTLNeAEVPSEDVVEVVVSPPFVFLPLVKSLLR---PDFQVAAQNCWVKKGGAFTGEISAEM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 85 LKEFGASHIIIGHSERREYHNESDEFVAKKFAFLKENGLTPVLCIGESEAQNEAGETVAVCARQLDAVinTQGVEALEGA 164
Cdd:PLN02561 84 LVNLGIPWVILGHSERRALLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAI--ADKVSDWANV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 857962664 165 IIAYEPIWAIGTGKAATAEDAQRIHAQIRAHIAEK-SEEVAKKVVIQYGGSVKPENAAAYFAQPDIDGALVGGAAL 239
Cdd:PLN02561 162 VLAYEPVWAIGTGKVATPAQAQEVHDELRKWLHKNvSPEVAATTRIIYGGSVTGANCKELAAQPDVDGFLVGGASL 237
|
|
| tim |
TIGR00419 |
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ... |
5-239 |
3.16e-59 |
|
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: 186.55 E-value: 3.16e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 5 VVMGNWK-LNGSKEMVVDLLNGLNAELEGVTGVDVAVAPPALFVDLAERTLTeagsaIILGAQNSDLNNSGAFTGDMSPA 83
Cdd:TIGR00419 1 LVIGNWKtYNESRGMRALEVAKIAEEVASEAGVAVAVAPPFVDLPMIKREVE-----IPVYAQHVDAVLSGAHTGEISAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 84 MLKEFGASHIIIGHSERReyHNESDefVAKKFAFLKENGLTPVLCIgeseaqneagetvavcarqlDAVINTQGVEALEG 163
Cdd:TIGR00419 76 MLKDIGAKGTLINHSERR--MKLAD--IEKKIARLKELGLTSVVCT--------------------NNVLTTAAAAALEP 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 857962664 164 AIIAYEPIWAIGTGKAATAEDAQRIHAQIRAhiaekSEEVAKKVVIQYGGSVKPENAAAYFAQPDIDGALVGGAAL 239
Cdd:TIGR00419 132 DVVAVEPPELIGTGIPVSPAQPEVVHGSVRA-----VKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSL 202
|
|
| PLN02429 |
PLN02429 |
triosephosphate isomerase |
13-239 |
1.69e-52 |
|
triosephosphate isomerase
Pssm-ID: 166070 Cd Length: 315 Bit Score: 173.05 E-value: 1.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 13 NGSKEMVVDLLNGLN-AELEGvtGVDVAVAPPALFVDLAERTLTEAgsaIILGAQNSDLNNSGAFTGDMSPAMLKEFGAS 91
Cdd:PLN02429 75 NGTKDSIAKLISDLNsATLEA--DVDVVVSPPFVYIDQVKSSLTDR---IDISGQNSWVGKGGAFTGEISVEQLKDLGCK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 92 HIIIGHSERREYHNESDEFVAKKFAFLKENGLTPVLCIGESEAQNEAGETVAVCARQLDAVINtqGVEALEGAIIAYEPI 171
Cdd:PLN02429 150 WVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFAD--AVPSWDNIVVAYEPV 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 857962664 172 WAIGTGKAATAEDAQRIHAQIRAHIAEK-SEEVAKKVVIQYGGSVKPENAAAYFAQPDIDGALVGGAAL 239
Cdd:PLN02429 228 WAIGTGKVASPQQAQEVHVAVRGWLKKNvSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASL 296
|
|
| PRK14565 |
PRK14565 |
triosephosphate isomerase; Provisional |
6-240 |
1.71e-42 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 237758 Cd Length: 237 Bit Score: 144.52 E-value: 1.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 6 VMGNWKLNGSKEMVVDLLNGLNAELEGVTG-VDVAVAPPalFVDLAerTLTEAGSAIILGAQNSDLNNSGAFTGDMSPAM 84
Cdd:PRK14565 5 IVANWKMNGDFSLFSSFLKELSNKLANNEItLKLVICPP--FTAMS--SFVECNPNIKLGAQNCFYGSSGGYTGEISAKM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 85 LKEFGASHIIIGHSERREYHNESDEFVAKKFAFLKENGLTPVLCIGESEAQNEAGETVAVCARQLDAVINTQGvealeGA 164
Cdd:PRK14565 81 LKECGCSYVILGHSERRSTFHETDSDIRLKAESAIESGLIPIICVGETLEDRENGMTKDVLLEQCSNCLPKHG-----EF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 857962664 165 IIAYEPIWAIGTGKAATAEDAQRIHAQIRAHIAEKSeevakkvvIQYGGSVKPENAAAYFAQPDIDGALVGGAALD 240
Cdd:PRK14565 156 IIAYEPVWAIGGSTIPSNDAIAEAFEIIRSYDSKSH--------IIYGGSVNQENIRDLKSINQLSGVLVGSASLD 223
|
|
| PRK15492 |
PRK15492 |
triosephosphate isomerase; Provisional |
61-240 |
4.56e-42 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 185389 Cd Length: 260 Bit Score: 144.36 E-value: 4.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 61 IILGAQNSDLNNSGAFTGDMSPAMLKEFGASHIIIGHSERREYHNESD-EFVAKKFAFLKENgLTPVLCIGESEAQNEAG 139
Cdd:PRK15492 66 IIIGAQNMNPNDNGQFTGDISPLMLKEIGTQLVMIGHSERRHKFGETDqEENAKVLAALKHD-FTTLLCVGETLEQKNYG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 140 ETVAVCARQLDAVINTQGVEALEGAIIAYEPIWAIGT-GKAATAEDAQRIHAQIRAHIAEKSEEVAKKVVIQYGGSVKPE 218
Cdd:PRK15492 145 ISDEILRTQLKIGLHGINPDQLAKLRIAYEPVWAIGEaGIPASADYADEKHAVIKQCLIELFGDAGDDIPVFYGGSVNAE 224
|
170 180
....*....|....*....|..
gi 857962664 219 NAAAYFAQPDIDGALVGGAALD 240
Cdd:PRK15492 225 NANELFGQPHIDGLFIGRSAWD 246
|
|
| PRK14905 |
PRK14905 |
triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; ... |
9-240 |
2.46e-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: 2.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 9 NWKLNGSKEMVVDLLNGLNA---ELEGVTGVDVAVAPPALFV-DLAERTLTEAG-SAIILGAQNSDLNNSGAFTGDMSPA 83
Cdd:PRK14905 10 NLKMYKGNAETVDYLSELLAfaeKFKSDYDIELFVIPSYIALkDAVEAAASETGhPKIKIGAQNMNAKDKGQFTGEISPL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 84 MLKEFGASHIIIGHSERREYHNESD-EFVAKKFAFLKENGLTpVLCIGESEAQNEAGETVAVCARQLDAVINTQGVEALE 162
Cdd:PRK14905 90 MLKELGIELVMIGHSERRHVLKETDqEENEKVLAALKHGFIT-LLCIGETLEQKNYNISDEVLRTQLKIGLHGVSAEQLP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 857962664 163 GAIIAYEPIWAIGTGK-AATAEDAQRIHAQIRAHIAEKSEEVAKKVVIQYGGSVKPENAAAYFAQPDIDGALVGGAALD 240
Cdd:PRK14905 169 HLFIAYEPVWAIGEGGiPASAEYADEKHAIIKQCLFELFAEESKKIPVLYGGSVNLENANELIMKPHIDGLFIGRSAWD 247
|
|
| PRK04302 |
PRK04302 |
triosephosphate isomerase; Provisional |
34-188 |
5.56e-09 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 235274 Cd Length: 223 Bit Score: 54.87 E-value: 5.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 857962664 34 TGVDVAVAPPALfvDLaeRTLTEAGSAIILgAQNSDLNNSGAFTGDMSPAMLKEFGASHIIIGHSERREYHNESDEFVAK 113
Cdd:PRK04302 35 TGVRIAVAPQAL--DI--RRVAEEVDIPVY-AQHVDPVEPGSHTGHILPEAVKDAGAVGTLINHSERRLTLADIEAVVER 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 857962664 114 kfafLKENGLTPVLCIgeseaqNEAGETVAVCARQLDAVintqgvealegaiiAYEPIWAIGTGKAATAEDAQRI 188
Cdd:PRK04302 110 ----AKKLGLESVVCV------NNPETSAAAAALGPDYV--------------AVEPPELIGTGIPVSKAKPEVV 160
|
|
| |
