|
Name |
Accession |
Description |
Interval |
E-value |
| tpiA |
PRK00042 |
triosephosphate isomerase; Provisional |
3-250 |
4.26e-137 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 234589 Cd Length: 250 Bit Score: 385.63 E-value: 4.26e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 3 RKPIIAGNWKMNKTPQEAKAFVEAVESKLPSNDLVDVAVAAPAVDLVTTIEAAKDSVLKVAAQNCYFENAGAFTGETSPK 82
Cdd:PRK00042 1 RKPIIAGNWKMNKTLAEAKALVEELKAALPDADGVEVAVAPPFTALASVKEALKGSNIKLGAQNVHPEDSGAFTGEISAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 83 VLAEMGADYVVIGHSERRDYFHETDEDINKKAKAIFANGLTPILCCGESLETYEAGKAVEFVGAQVSAALAGLSEEQVAS 162
Cdd:PRK00042 81 MLKDLGVKYVIIGHSERRQYFGETDELVNKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLEAALAGLSAEQFAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 163 LVLAYEPIWAIGTGKSATQDDAQKMCKAVRDVVAADFGqEVADKVRVQYGGSVKPENVKDYMACPDVDGALVGGASLEAD 242
Cdd:PRK00042 161 LVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYG-EVAEKVRILYGGSVKPDNAAELMAQPDIDGALVGGASLKAE 239
|
....*...
gi 806828986 243 SFLALLDF 250
Cdd:PRK00042 240 DFLAIVKA 247
|
|
| TpiA |
COG0149 |
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ... |
3-250 |
6.31e-137 |
|
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: 385.18 E-value: 6.31e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 3 RKPIIAGNWKMNKTPQEAKAFVEAVESKLPSNDLVDVAVAAPAVDLVTTIEAAKDSVLKVAAQNCYFENAGAFTGETSPK 82
Cdd:COG0149 2 RKPLIAGNWKMNGTLAEAKALLAALAAALADLADVEVVVCPPFTYLAAVAEALAGSPIALGAQNVHWEDSGAYTGEISAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 83 VLAEMGADYVVIGHSERRDYFHETDEDINKKAKAIFANGLTPILCCGESLETYEAGKAVEFVGAQVSAALAGLSEEQVAS 162
Cdd:COG0149 82 MLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLSAEQAAN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 163 LVLAYEPIWAIGTGKSATQDDAQKMCKAVRDVVAADFGQEVADKVRVQYGGSVKPENVKDYMACPDVDGALVGGASLEAD 242
Cdd:COG0149 162 VVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDAE 241
|
....*...
gi 806828986 243 SFLALLDF 250
Cdd:COG0149 242 DFLAIVRA 249
|
|
| TIM |
pfam00121 |
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ... |
5-251 |
4.82e-119 |
|
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: 339.49 E-value: 4.82e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 5 PIIAGNWKMNKTPQEAKAFVEAVESKLPSNDLVDVAVAAPAVDLVTTIEAAKDSVlKVAAQNCYFENAGAFTGETSPKVL 84
Cdd:pfam00121 1 PIIAGNWKMNGTLAEAAELLAELAEALADESGVEVVVAPPFTYLSAVAELLGSNI-KVGAQNVDPEESGAFTGEISAEML 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 85 AEMGADYVVIGHSERRDYFHETDEDINKKAKAIFANGLTPILCCGESLETYEAGKAVEFVGAQVSAALAGLSEEQvASLV 164
Cdd:pfam00121 80 KDLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQ-KNLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 165 LAYEPIWAIGTGKSATQDDAQKMCKAVRDVVAADFgQEVADKVRVQYGGSVKPENVKDYMACPDVDGALVGGASLEADSF 244
Cdd:pfam00121 159 IAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELY-KEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEDF 237
|
....*..
gi 806828986 245 LALLDFL 251
Cdd:pfam00121 238 LDIINAA 244
|
|
| TIM |
cd00311 |
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ... |
5-249 |
2.37e-116 |
|
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: 332.58 E-value: 2.37e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 5 PIIAGNWKMNKTPQEAKAFVEAVESKLPSNDLVDVAVAAPAVDLVTTIEAAKDSVLKVAAQNCYFENAGAFTGETSPKVL 84
Cdd:cd00311 1 PLVAGNWKMNGTLAEALELAKALNAVLKDESGVEVVVAPPFTYLAAVAEALEGSKIKVGAQNVSPEDSGAFTGEISAEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 85 AEMGADYVVIGHSERRDYFHETDEDINKKAKAIFANGLTPILCCGESLETYEAGKAVEFVGAQVSAALAGLseEQVASLV 164
Cdd:cd00311 81 KDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGV--EDLAPVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 165 LAYEPIWAIGTGKSATQDDAQKMCKAVRDVVAADFGqEVADKVRVQYGGSVKPENVKDYMACPDVDGALVGGASLEADSF 244
Cdd:cd00311 159 IAYEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYG-EVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAESF 237
|
....*
gi 806828986 245 LALLD 249
Cdd:cd00311 238 LDIIK 242
|
|
| tim |
TIGR00419 |
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ... |
6-242 |
6.82e-34 |
|
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: 121.45 E-value: 6.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 6 IIAGNWKmnkTPQEAKAFVEAVESKLPSNDLVDVAVAAPAVDLVTTIEAAKDSV-LKVAAQNCYFENAGAFTGETSPKVL 84
Cdd:TIGR00419 1 LVIGNWK---TYNESRGMRALEVAKIAEEVASEAGVAVAVAPPFVDLPMIKREVeIPVYAQHVDAVLSGAHTGEISAEML 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 85 AEMGADYVVIGHSERRdyfhETDEDINKKAKAIFANGLTPILCCGESLETyeagkavefvgaQVSAALAGlseeqvasLV 164
Cdd:TIGR00419 78 KDIGAKGTLINHSERR----MKLADIEKKIARLKELGLTSVVCTNNVLTT------------AAAAALEP--------DV 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 806828986 165 LAYEPIWAIGTGKSATQDDAQKMCKAVRDVvaadfgQEVADKVRVQYGGSVKPENVKDYMACPDVDGALVGGASLEAD 242
Cdd:TIGR00419 134 VAVEPPELIGTGIPVSPAQPEVVHGSVRAV------KEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| tpiA |
PRK00042 |
triosephosphate isomerase; Provisional |
3-250 |
4.26e-137 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 234589 Cd Length: 250 Bit Score: 385.63 E-value: 4.26e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 3 RKPIIAGNWKMNKTPQEAKAFVEAVESKLPSNDLVDVAVAAPAVDLVTTIEAAKDSVLKVAAQNCYFENAGAFTGETSPK 82
Cdd:PRK00042 1 RKPIIAGNWKMNKTLAEAKALVEELKAALPDADGVEVAVAPPFTALASVKEALKGSNIKLGAQNVHPEDSGAFTGEISAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 83 VLAEMGADYVVIGHSERRDYFHETDEDINKKAKAIFANGLTPILCCGESLETYEAGKAVEFVGAQVSAALAGLSEEQVAS 162
Cdd:PRK00042 81 MLKDLGVKYVIIGHSERRQYFGETDELVNKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLEAALAGLSAEQFAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 163 LVLAYEPIWAIGTGKSATQDDAQKMCKAVRDVVAADFGqEVADKVRVQYGGSVKPENVKDYMACPDVDGALVGGASLEAD 242
Cdd:PRK00042 161 LVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYG-EVAEKVRILYGGSVKPDNAAELMAQPDIDGALVGGASLKAE 239
|
....*...
gi 806828986 243 SFLALLDF 250
Cdd:PRK00042 240 DFLAIVKA 247
|
|
| TpiA |
COG0149 |
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ... |
3-250 |
6.31e-137 |
|
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: 385.18 E-value: 6.31e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 3 RKPIIAGNWKMNKTPQEAKAFVEAVESKLPSNDLVDVAVAAPAVDLVTTIEAAKDSVLKVAAQNCYFENAGAFTGETSPK 82
Cdd:COG0149 2 RKPLIAGNWKMNGTLAEAKALLAALAAALADLADVEVVVCPPFTYLAAVAEALAGSPIALGAQNVHWEDSGAYTGEISAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 83 VLAEMGADYVVIGHSERRDYFHETDEDINKKAKAIFANGLTPILCCGESLETYEAGKAVEFVGAQVSAALAGLSEEQVAS 162
Cdd:COG0149 82 MLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLSAEQAAN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 163 LVLAYEPIWAIGTGKSATQDDAQKMCKAVRDVVAADFGQEVADKVRVQYGGSVKPENVKDYMACPDVDGALVGGASLEAD 242
Cdd:COG0149 162 VVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDAE 241
|
....*...
gi 806828986 243 SFLALLDF 250
Cdd:COG0149 242 DFLAIVRA 249
|
|
| TIM |
pfam00121 |
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ... |
5-251 |
4.82e-119 |
|
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: 339.49 E-value: 4.82e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 5 PIIAGNWKMNKTPQEAKAFVEAVESKLPSNDLVDVAVAAPAVDLVTTIEAAKDSVlKVAAQNCYFENAGAFTGETSPKVL 84
Cdd:pfam00121 1 PIIAGNWKMNGTLAEAAELLAELAEALADESGVEVVVAPPFTYLSAVAELLGSNI-KVGAQNVDPEESGAFTGEISAEML 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 85 AEMGADYVVIGHSERRDYFHETDEDINKKAKAIFANGLTPILCCGESLETYEAGKAVEFVGAQVSAALAGLSEEQvASLV 164
Cdd:pfam00121 80 KDLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQ-KNLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 165 LAYEPIWAIGTGKSATQDDAQKMCKAVRDVVAADFgQEVADKVRVQYGGSVKPENVKDYMACPDVDGALVGGASLEADSF 244
Cdd:pfam00121 159 IAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELY-KEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEDF 237
|
....*..
gi 806828986 245 LALLDFL 251
Cdd:pfam00121 238 LDIINAA 244
|
|
| TIM |
cd00311 |
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ... |
5-249 |
2.37e-116 |
|
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: 332.58 E-value: 2.37e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 5 PIIAGNWKMNKTPQEAKAFVEAVESKLPSNDLVDVAVAAPAVDLVTTIEAAKDSVLKVAAQNCYFENAGAFTGETSPKVL 84
Cdd:cd00311 1 PLVAGNWKMNGTLAEALELAKALNAVLKDESGVEVVVAPPFTYLAAVAEALEGSKIKVGAQNVSPEDSGAFTGEISAEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 85 AEMGADYVVIGHSERRDYFHETDEDINKKAKAIFANGLTPILCCGESLETYEAGKAVEFVGAQVSAALAGLseEQVASLV 164
Cdd:cd00311 81 KDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGV--EDLAPVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 165 LAYEPIWAIGTGKSATQDDAQKMCKAVRDVVAADFGqEVADKVRVQYGGSVKPENVKDYMACPDVDGALVGGASLEADSF 244
Cdd:cd00311 159 IAYEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYG-EVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAESF 237
|
....*
gi 806828986 245 LALLD 249
Cdd:cd00311 238 LDIIK 242
|
|
| PRK13962 |
PRK13962 |
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional |
3-250 |
3.39e-105 |
|
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional
Pssm-ID: 237572 [Multi-domain] Cd Length: 645 Bit Score: 317.82 E-value: 3.39e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 3 RKPIIAGNWKMNKTPQEAKAFVEAVESKLpsndlVDVAVAAPAVDLVTTIEAAKDSV----LKVAAQNCYFENAGAFTGE 78
Cdd:PRK13962 397 RKPIIAGNWKMNKTPAEAKEFVNELKKYV-----KDAQAEVVVCPPFTALPSVKEAVdgsnIKLGAQNVFYEEKGAYTGE 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 79 TSPKVLAEMGADYVVIGHSERRDYFHETDEDINKKAKAIFANGLTPILCCGESLETYEAGKAVEFVGAQVSAALAGLSEE 158
Cdd:PRK13962 472 ISGPMLAEIGVEYVIIGHSERRQYFGETDELVNKKVLAALKAGLTPILCVGETLDERESGITFDVVRLQLKAALNGLSAE 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 159 QVASLVLAYEPIWAIGTGKSATQDDAQKMCKAVRDVVAADFGQEVADKVRVQYGGSVKPENVKDYMACPDVDGALVGGAS 238
Cdd:PRK13962 552 QVKKVVIAYEPVWAIGTGKVATPEQAQEVHAFIRKLVAELYGEEAARKVRILYGGSVKSENAAGLFNQPDIDGGLVGGAS 631
|
250
....*....|..
gi 806828986 239 LEADSFLALLDF 250
Cdd:PRK13962 632 LKAQEFAAIANY 643
|
|
| PTZ00333 |
PTZ00333 |
triosephosphate isomerase; Provisional |
1-242 |
7.05e-85 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 240365 Cd Length: 255 Bit Score: 253.30 E-value: 7.05e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 1 MSRKPIIAGNWKMNKTPQEAKAFVEAVESKLPSNDLVDVAVAAPAVDLVTTIEAAKDSVLKVAAQNCYFENAGAFTGETS 80
Cdd:PTZ00333 2 MKRKPFVGGNWKCNGTKASIKELIDSFNKLKFDPNNVDVVVAPPSLHIPLVQEKLKNKNFKISSQNVSLTGSGAFTGEIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 81 PKVLAEMGADYVVIGHSERRDYFHETDEDINKKAKAIFANGLTPILCCGESLETYEAGKAVEFVGAQVSAALAGLSEEQV 160
Cdd:PTZ00333 82 AEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDEAW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 161 ASLVLAYEPIWAIGTGKSATQDDAQKMCKAVRDVVAADFGQEVADKVRVQYGGSVKPENVKDYMACPDVDGALVGGASLE 240
Cdd:PTZ00333 162 DNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASLK 241
|
..
gi 806828986 241 AD 242
Cdd:PTZ00333 242 PD 243
|
|
| PLN02561 |
PLN02561 |
triosephosphate isomerase |
1-240 |
7.53e-58 |
|
triosephosphate isomerase
Pssm-ID: 178175 Cd Length: 253 Bit Score: 184.64 E-value: 7.53e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 1 MSRKPIIAGNWKMNKTPQEAKAFVEAV-ESKLPSNDLVDVAVAAPAVDLvTTIEAAKDSVLKVAAQNCYFENAGAFTGET 79
Cdd:PLN02561 1 MARKFFVGGNWKCNGTVEEVKKIVTTLnEAEVPSEDVVEVVVSPPFVFL-PLVKSLLRPDFQVAAQNCWVKKGGAFTGEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 80 SPKVLAEMGADYVVIGHSERRDYFHETDEDINKKAKAIFANGLTPILCCGESLETYEAGKAVEFVGAQVSAALAGLSEEq 159
Cdd:PLN02561 80 SAEMLVNLGIPWVILGHSERRALLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIADKVSDW- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 160 vASLVLAYEPIWAIGTGKSATQDDAQKMCKAVRDVVAADFGQEVADKVRVQYGGSVKPENVKDYMACPDVDGALVGGASL 239
Cdd:PLN02561 159 -ANVVLAYEPVWAIGTGKVATPAQAQEVHDELRKWLHKNVSPEVAATTRIIYGGSVTGANCKELAAQPDVDGFLVGGASL 237
|
.
gi 806828986 240 E 240
Cdd:PLN02561 238 K 238
|
|
| PRK14565 |
PRK14565 |
triosephosphate isomerase; Provisional |
6-249 |
2.27e-51 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 237758 Cd Length: 237 Bit Score: 167.24 E-value: 2.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 6 IIAGNWKMNKTPQEAKAFVEAVESKLPSNDLVDVAVAAPAVDLVTTIEAAKDSVlKVAAQNCYFENAGAFTGETSPKVLA 85
Cdd:PRK14565 4 LIVANWKMNGDFSLFSSFLKELSNKLANNEITLKLVICPPFTAMSSFVECNPNI-KLGAQNCFYGSSGGYTGEISAKMLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 86 EMGADYVVIGHSERRDYFHETDEDINKKAKAIFANGLTPILCCGESLETYEAGKAVEFVGAQVSAALAGLSEeqvasLVL 165
Cdd:PRK14565 83 ECGCSYVILGHSERRSTFHETDSDIRLKAESAIESGLIPIICVGETLEDRENGMTKDVLLEQCSNCLPKHGE-----FII 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 166 AYEPIWAIGTGKSATQDdaqkMCKAVRDVVaadfgQEVADKVRVQYGGSVKPENVKDYMACPDVDGALVGGASLEADSFL 245
Cdd:PRK14565 158 AYEPVWAIGGSTIPSND----AIAEAFEII-----RSYDSKSHIIYGGSVNQENIRDLKSINQLSGVLVGSASLDVDSFC 228
|
....
gi 806828986 246 ALLD 249
Cdd:PRK14565 229 KIIQ 232
|
|
| PRK15492 |
PRK15492 |
triosephosphate isomerase; Provisional |
50-249 |
1.20e-44 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 185389 Cd Length: 260 Bit Score: 150.91 E-value: 1.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 50 TTIEAAKDSVLKVAAQNCYFENAGAFTGETSPKVLAEMGADYVVIGHSERRDYFHETDEDINKKAKAIFANGLTPILCCG 129
Cdd:PRK15492 56 ATLAIPHDHPIIIGAQNMNPNDNGQFTGDISPLMLKEIGTQLVMIGHSERRHKFGETDQEENAKVLAALKHDFTTLLCVG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 130 ESLETYEAGKAVEFVGAQVSAALAGLSEEQVASLVLAYEPIWAIGT-GKSATQDDAQKMCKAVRDVVAADFGQEvADKVR 208
Cdd:PRK15492 136 ETLEQKNYGISDEILRTQLKIGLHGINPDQLAKLRIAYEPVWAIGEaGIPASADYADEKHAVIKQCLIELFGDA-GDDIP 214
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 806828986 209 VQYGGSVKPENVKDYMACPDVDGALVGGASLEADSFLALLD 249
Cdd:PRK15492 215 VFYGGSVNAENANELFGQPHIDGLFIGRSAWDADKFFAIIE 255
|
|
| PRK14905 |
PRK14905 |
triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; ... |
1-249 |
4.80e-43 |
|
triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; Provisional
Pssm-ID: 184898 [Multi-domain] Cd Length: 355 Bit Score: 149.41 E-value: 4.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 1 MSRKPIIAGNWKMNKTPQEAKAFVE---AVESKLPSNDLVDVAVAAPAVDLVTTIEAAKDSV----LKVAAQNCYFENAG 73
Cdd:PRK14905 1 MAKKIYFGTNLKMYKGNAETVDYLSellAFAEKFKSDYDIELFVIPSYIALKDAVEAAASETghpkIKIGAQNMNAKDKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 74 AFTGETSPKVLAEMGADYVVIGHSERRDYFHETDEDINKKAKAIFANGLTPILCCGESLETYEAGKAVEFVGAQVSAALA 153
Cdd:PRK14905 81 QFTGEISPLMLKELGIELVMIGHSERRHVLKETDQEENEKVLAALKHGFITLLCIGETLEQKNYNISDEVLRTQLKIGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 154 GLSEEQVASLVLAYEPIWAIGTGK-SATQDDAQKMCKAVRDVVAADFGQEvADKVRVQYGGSVKPENVKDYMACPDVDGA 232
Cdd:PRK14905 161 GVSAEQLPHLFIAYEPVWAIGEGGiPASAEYADEKHAIIKQCLFELFAEE-SKKIPVLYGGSVNLENANELIMKPHIDGL 239
|
250
....*....|....*..
gi 806828986 233 LVGGASLEADSFLALLD 249
Cdd:PRK14905 240 FIGRSAWDAQCFHALIA 256
|
|
| PLN02429 |
PLN02429 |
triosephosphate isomerase |
60-249 |
1.65e-40 |
|
triosephosphate isomerase
Pssm-ID: 166070 Cd Length: 315 Bit Score: 141.85 E-value: 1.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 60 LKVAAQNCYFENAGAFTGETSPKVLAEMGADYVVIGHSERRDYFHETDEDINKKAKAIFANGLTPILCCGESLETYEAGK 139
Cdd:PLN02429 119 IDISGQNSWVGKGGAFTGEISVEQLKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 140 AVEFVGAQVSAALAGLSEEQvaSLVLAYEPIWAIGTGKSATQDDAQKMCKAVRDVVAADFGQEVADKVRVQYGGSVKPEN 219
Cdd:PLN02429 199 TFDVCFAQLKAFADAVPSWD--NIVVAYEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGN 276
|
170 180 190
....*....|....*....|....*....|
gi 806828986 220 VKDYMACPDVDGALVGGASLEADSFLALLD 249
Cdd:PLN02429 277 SAELAKEEDIDGFLVGGASLKGPEFATIVN 306
|
|
| tim |
TIGR00419 |
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ... |
6-242 |
6.82e-34 |
|
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: 121.45 E-value: 6.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 6 IIAGNWKmnkTPQEAKAFVEAVESKLPSNDLVDVAVAAPAVDLVTTIEAAKDSV-LKVAAQNCYFENAGAFTGETSPKVL 84
Cdd:TIGR00419 1 LVIGNWK---TYNESRGMRALEVAKIAEEVASEAGVAVAVAPPFVDLPMIKREVeIPVYAQHVDAVLSGAHTGEISAEML 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 85 AEMGADYVVIGHSERRdyfhETDEDINKKAKAIFANGLTPILCCGESLETyeagkavefvgaQVSAALAGlseeqvasLV 164
Cdd:TIGR00419 78 KDIGAKGTLINHSERR----MKLADIEKKIARLKELGLTSVVCTNNVLTT------------AAAAALEP--------DV 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 806828986 165 LAYEPIWAIGTGKSATQDDAQKMCKAVRDVvaadfgQEVADKVRVQYGGSVKPENVKDYMACPDVDGALVGGASLEAD 242
Cdd:TIGR00419 134 VAVEPPELIGTGIPVSPAQPEVVHGSVRAV------KEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
|
|
| PRK04302 |
PRK04302 |
triosephosphate isomerase; Provisional |
60-250 |
8.45e-09 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 235274 Cd Length: 223 Bit Score: 54.10 E-value: 8.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 60 LKVAAQNCYFENAGAFTGETSPKVLAEMGADYVVIGHSERRDyfheTDEDINKKAKAIFANGLTPILCCgESLETyeagk 139
Cdd:PRK04302 57 IPVYAQHVDPVEPGSHTGHILPEAVKDAGAVGTLINHSERRL----TLADIEAVVERAKKLGLESVVCV-NNPET----- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 806828986 140 avefvgaqvSAALAGLSEEQVaslvlAYEPIWAIGTGKSATQDDAQKMCKAVRDVvaadfgQEVADKVRVQYGGSVKP-E 218
Cdd:PRK04302 127 ---------SAAAAALGPDYV-----AVEPPELIGTGIPVSKAKPEVVEDAVEAV------KKVNPDVKVLCGAGISTgE 186
|
170 180 190
....*....|....*....|....*....|...
gi 806828986 219 NVKDYMACpDVDGALVGGASLEADSF-LALLDF 250
Cdd:PRK04302 187 DVKAALEL-GADGVLLASGVVKAKDPeAALRDL 218
|
|
|