|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00333 |
PTZ00333 |
triosephosphate isomerase; Provisional |
1-245 |
8.47e-131 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 240365 Cd Length: 255 Bit Score: 369.63 E-value: 8.47e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 1 MSRKFCVGGNWKMNGDQKSIAEIAKTLSSAALDP-NTEVVIGCPAIYLMYARNLLPCE-LGLAGQNAYKVAKGAFTGEIS 78
Cdd:PTZ00333 2 MKRKPFVGGNWKCNGTKASIKELIDSFNKLKFDPnNVDVVVAPPSLHIPLVQEKLKNKnFKISSQNVSLTGSGAFTGEIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 79 PAMLKDIGADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTNEVVARQMCAYAQKIKD--W 156
Cdd:PTZ00333 82 AEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDeaW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 157 KNVVVAYEPVWAIGTGQTATPDQAQEVHAFLRQWLSDNISKEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLK 236
Cdd:PTZ00333 162 DNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASLK 241
|
....*....
gi 28572008 237 PEFVDIINA 245
Cdd:PTZ00333 242 PDFVDIIKS 250
|
|
| TIM |
cd00311 |
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ... |
5-244 |
6.59e-128 |
|
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: 361.85 E-value: 6.59e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 5 FCVGGNWKMNGDQKSIAEIAKTLSSAALDP-NTEVVIGCPAIYLMYARNLLP-CELGLAGQNAYKVAKGAFTGEISPAML 82
Cdd:cd00311 1 PLVAGNWKMNGTLAEALELAKALNAVLKDEsGVEVVVAPPFTYLAAVAEALEgSKIKVGAQNVSPEDSGAFTGEISAEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 83 KDIGADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTNEVVARQMCAYAQKIKDWKNVVVA 162
Cdd:cd00311 81 KDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 163 YEPVWAIGTGQTATPDQAQEVHAFLRQWLSDNISkEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLKPE-FVD 241
Cdd:cd00311 161 YEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYG-EVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAEsFLD 239
|
...
gi 28572008 242 IIN 244
Cdd:cd00311 240 IIK 242
|
|
| TpiA |
COG0149 |
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ... |
1-245 |
1.50e-125 |
|
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: 355.90 E-value: 1.50e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 1 MSRKFcVGGNWKMNGDQKSIAEIAKTLSSAALD-PNTEVVIGCPAIYLMYARNLL-PCELGLAGQNAYKVAKGAFTGEIS 78
Cdd:COG0149 1 MRKPL-IAGNWKMNGTLAEAKALLAALAAALADlADVEVVVCPPFTYLAAVAEALaGSPIALGAQNVHWEDSGAYTGEIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 79 PAMLKDIGADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTNEVVARQMCA--YAQKIKDW 156
Cdd:COG0149 80 AAMLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAalAGLSAEQA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 157 KNVVVAYEPVWAIGTGQTATPDQAQEVHAFLRQWLSDNISKEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLK 236
Cdd:COG0149 160 ANVVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLD 239
|
250
....*....|
gi 28572008 237 PE-FVDIINA 245
Cdd:COG0149 240 AEdFLAIVRA 249
|
|
| TIM |
pfam00121 |
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ... |
7-245 |
1.55e-124 |
|
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: 353.35 E-value: 1.55e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 7 VGGNWKMNGDQKSIAEIAKTLSSAALD-PNTEVVIGCPAIYLMYARNLLPCELGLAGQNAYKVAKGAFTGEISPAMLKDI 85
Cdd:pfam00121 3 IAGNWKMNGTLAEAAELLAELAEALADeSGVEVVVAPPFTYLSAVAELLGSNIKVGAQNVDPEESGAFTGEISAEMLKDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 86 GADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTNEVVARQMCAYAQKIKDW-KNVVVAYE 164
Cdd:pfam00121 83 GVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEqKNLVIAYE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 165 PVWAIGTGQTATPDQAQEVHAFLRQWLSDnISKEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLKPE-FVDII 243
Cdd:pfam00121 163 PVWAIGTGKTATPEQAQEVHAFIRAVLAE-LYKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEdFLDII 241
|
..
gi 28572008 244 NA 245
Cdd:pfam00121 242 NA 243
|
|
| tim |
TIGR00419 |
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ... |
7-238 |
5.85e-54 |
|
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: 172.68 E-value: 5.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 7 VGGNWKM-NGDQKSIAEIAKTLSSAALDPN-TEVVIGCPAIYL-MYARNLlpcELGLAGQNAYKVAKGAFTGEISPAMLK 83
Cdd:TIGR00419 2 VIGNWKTyNESRGMRALEVAKIAEEVASEAgVAVAVAPPFVDLpMIKREV---EIPVYAQHVDAVLSGAHTGEISAEMLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 84 DIGADWVILGHSERRaiFGESDalIAEKAEHALAEGLKVIACIgetleereagktnEVVARQMCAYAqkikdWKNVVVAY 163
Cdd:TIGR00419 79 DIGAKGTLINHSERR--MKLAD--IEKKIARLKELGLTSVVCT-------------NNVLTTAAAAA-----LEPDVVAV 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28572008 164 EPVWAIGTGQTATPDQAQEVHAFLRqwlsdnISKEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLKPE 238
Cdd:TIGR00419 137 EPPELIGTGIPVSPAQPEVVHGSVR------AVKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00333 |
PTZ00333 |
triosephosphate isomerase; Provisional |
1-245 |
8.47e-131 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 240365 Cd Length: 255 Bit Score: 369.63 E-value: 8.47e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 1 MSRKFCVGGNWKMNGDQKSIAEIAKTLSSAALDP-NTEVVIGCPAIYLMYARNLLPCE-LGLAGQNAYKVAKGAFTGEIS 78
Cdd:PTZ00333 2 MKRKPFVGGNWKCNGTKASIKELIDSFNKLKFDPnNVDVVVAPPSLHIPLVQEKLKNKnFKISSQNVSLTGSGAFTGEIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 79 PAMLKDIGADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTNEVVARQMCAYAQKIKD--W 156
Cdd:PTZ00333 82 AEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDeaW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 157 KNVVVAYEPVWAIGTGQTATPDQAQEVHAFLRQWLSDNISKEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLK 236
Cdd:PTZ00333 162 DNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASLK 241
|
....*....
gi 28572008 237 PEFVDIINA 245
Cdd:PTZ00333 242 PDFVDIIKS 250
|
|
| TIM |
cd00311 |
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ... |
5-244 |
6.59e-128 |
|
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: 361.85 E-value: 6.59e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 5 FCVGGNWKMNGDQKSIAEIAKTLSSAALDP-NTEVVIGCPAIYLMYARNLLP-CELGLAGQNAYKVAKGAFTGEISPAML 82
Cdd:cd00311 1 PLVAGNWKMNGTLAEALELAKALNAVLKDEsGVEVVVAPPFTYLAAVAEALEgSKIKVGAQNVSPEDSGAFTGEISAEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 83 KDIGADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTNEVVARQMCAYAQKIKDWKNVVVA 162
Cdd:cd00311 81 KDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 163 YEPVWAIGTGQTATPDQAQEVHAFLRQWLSDNISkEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLKPE-FVD 241
Cdd:cd00311 161 YEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYG-EVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAEsFLD 239
|
...
gi 28572008 242 IIN 244
Cdd:cd00311 240 IIK 242
|
|
| TpiA |
COG0149 |
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ... |
1-245 |
1.50e-125 |
|
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: 355.90 E-value: 1.50e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 1 MSRKFcVGGNWKMNGDQKSIAEIAKTLSSAALD-PNTEVVIGCPAIYLMYARNLL-PCELGLAGQNAYKVAKGAFTGEIS 78
Cdd:COG0149 1 MRKPL-IAGNWKMNGTLAEAKALLAALAAALADlADVEVVVCPPFTYLAAVAEALaGSPIALGAQNVHWEDSGAYTGEIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 79 PAMLKDIGADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTNEVVARQMCA--YAQKIKDW 156
Cdd:COG0149 80 AAMLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAalAGLSAEQA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 157 KNVVVAYEPVWAIGTGQTATPDQAQEVHAFLRQWLSDNISKEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLK 236
Cdd:COG0149 160 ANVVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLD 239
|
250
....*....|
gi 28572008 237 PE-FVDIINA 245
Cdd:COG0149 240 AEdFLAIVRA 249
|
|
| TIM |
pfam00121 |
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ... |
7-245 |
1.55e-124 |
|
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: 353.35 E-value: 1.55e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 7 VGGNWKMNGDQKSIAEIAKTLSSAALD-PNTEVVIGCPAIYLMYARNLLPCELGLAGQNAYKVAKGAFTGEISPAMLKDI 85
Cdd:pfam00121 3 IAGNWKMNGTLAEAAELLAELAEALADeSGVEVVVAPPFTYLSAVAELLGSNIKVGAQNVDPEESGAFTGEISAEMLKDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 86 GADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTNEVVARQMCAYAQKIKDW-KNVVVAYE 164
Cdd:pfam00121 83 GVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEqKNLVIAYE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 165 PVWAIGTGQTATPDQAQEVHAFLRQWLSDnISKEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLKPE-FVDII 243
Cdd:pfam00121 163 PVWAIGTGKTATPEQAQEVHAFIRAVLAE-LYKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEdFLDII 241
|
..
gi 28572008 244 NA 245
Cdd:pfam00121 242 NA 243
|
|
| tpiA |
PRK00042 |
triosephosphate isomerase; Provisional |
3-245 |
8.71e-120 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 234589 Cd Length: 250 Bit Score: 341.33 E-value: 8.71e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 3 RKFCVGGNWKMNGDQKSIAEIAKTLSSAALD-PNTEVVIGCPAIYL-MYARNLLPCELGLAGQNAYKVAKGAFTGEISPA 80
Cdd:PRK00042 1 RKPIIAGNWKMNKTLAEAKALVEELKAALPDaDGVEVAVAPPFTALaSVKEALKGSNIKLGAQNVHPEDSGAFTGEISAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 81 MLKDIGADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTNEVVARQMCA--YAQKIKDWKN 158
Cdd:PRK00042 81 MLKDLGVKYVIIGHSERRQYFGETDELVNKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLEAalAGLSAEQFAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 159 VVVAYEPVWAIGTGQTATPDQAQEVHAFLRQWLSDnISKEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLKPE 238
Cdd:PRK00042 161 LVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAE-LYGEVAEKVRILYGGSVKPDNAAELMAQPDIDGALVGGASLKAE 239
|
....*...
gi 28572008 239 -FVDIINA 245
Cdd:PRK00042 240 dFLAIVKA 247
|
|
| PLN02561 |
PLN02561 |
triosephosphate isomerase |
1-245 |
6.43e-119 |
|
triosephosphate isomerase
Pssm-ID: 178175 Cd Length: 253 Bit Score: 339.49 E-value: 6.43e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 1 MSRKFCVGGNWKMNGDQKSIAEIAKTLSSAALDPN--TEVVIGCPAIYLMYARNLLPCELGLAGQNAYKVAKGAFTGEIS 78
Cdd:PLN02561 1 MARKFFVGGNWKCNGTVEEVKKIVTTLNEAEVPSEdvVEVVVSPPFVFLPLVKSLLRPDFQVAAQNCWVKKGGAFTGEIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 79 PAMLKDIGADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTNEVVARQMCAYAQKIKDWKN 158
Cdd:PLN02561 81 AEMLVNLGIPWVILGHSERRALLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIADKVSDWAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 159 VVVAYEPVWAIGTGQTATPDQAQEVHAFLRQWLSDNISKEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLKPE 238
Cdd:PLN02561 161 VVLAYEPVWAIGTGKVATPAQAQEVHDELRKWLHKNVSPEVAATTRIIYGGSVTGANCKELAAQPDVDGFLVGGASLKPE 240
|
....*..
gi 28572008 239 FVDIINA 245
Cdd:PLN02561 241 FIDIIKS 247
|
|
| PLN02429 |
PLN02429 |
triosephosphate isomerase |
2-245 |
1.16e-87 |
|
triosephosphate isomerase
Pssm-ID: 166070 Cd Length: 315 Bit Score: 262.42 E-value: 1.16e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 2 SRKFCVGGNWKMNGDQKSIAEIAKTLSSAALDPNTEVVIGCPAIYLMYARNLLPCELGLAGQNAYKVAKGAFTGEISPAM 81
Cdd:PLN02429 63 SGKFFVGGNWKCNGTKDSIAKLISDLNSATLEADVDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEISVEQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 82 LKDIGADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTNEVVARQMCAYAQKIKDWKNVVV 161
Cdd:PLN02429 143 LKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDNIVV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 162 AYEPVWAIGTGQTATPDQAQEVHAFLRQWLSDNISKEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLK-PEFV 240
Cdd:PLN02429 223 AYEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKgPEFA 302
|
....*
gi 28572008 241 DIINA 245
Cdd:PLN02429 303 TIVNS 307
|
|
| PRK13962 |
PRK13962 |
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional |
3-245 |
8.17e-84 |
|
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional
Pssm-ID: 237572 [Multi-domain] Cd Length: 645 Bit Score: 262.36 E-value: 8.17e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 3 RKFCVGGNWKMNGDQKSIAEIAKTLSSAALDPNTEVVIGCPAIYLMYARNLLPCE-LGLAGQNAYKVAKGAFTGEISPAM 81
Cdd:PRK13962 397 RKPIIAGNWKMNKTPAEAKEFVNELKKYVKDAQAEVVVCPPFTALPSVKEAVDGSnIKLGAQNVFYEEKGAYTGEISGPM 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 82 LKDIGADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTNEVVARQMCA--YAQKIKDWKNV 159
Cdd:PRK13962 477 LAEIGVEYVIIGHSERRQYFGETDELVNKKVLAALKAGLTPILCVGETLDERESGITFDVVRLQLKAalNGLSAEQVKKV 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 160 VVAYEPVWAIGTGQTATPDQAQEVHAFLRQWLSDNISKEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLKP-E 238
Cdd:PRK13962 557 VIAYEPVWAIGTGKVATPEQAQEVHAFIRKLVAELYGEEAARKVRILYGGSVKSENAAGLFNQPDIDGGLVGGASLKAqE 636
|
....*..
gi 28572008 239 FVDIINA 245
Cdd:PRK13962 637 FAAIANY 643
|
|
| PRK14565 |
PRK14565 |
triosephosphate isomerase; Provisional |
1-243 |
1.62e-59 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 237758 Cd Length: 237 Bit Score: 188.04 E-value: 1.62e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 1 MSrkFCVGGNWKMNGDQKSIAEIAKTLS--SAALDPNTEVVIgCPAIYLMYARNLLPCELGLAGQNAYKVAKGAFTGEIS 78
Cdd:PRK14565 1 MS--FLIVANWKMNGDFSLFSSFLKELSnkLANNEITLKLVI-CPPFTAMSSFVECNPNIKLGAQNCFYGSSGGYTGEIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 79 PAMLKDIGADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTNEVVARQmCayAQKIKDWKN 158
Cdd:PRK14565 78 AKMLKECGCSYVILGHSERRSTFHETDSDIRLKAESAIESGLIPIICVGETLEDRENGMTKDVLLEQ-C--SNCLPKHGE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 159 VVVAYEPVWAIGTGQtaTPDQAQEVHAFlrqwlsdNISKEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLKPE 238
Cdd:PRK14565 155 FIIAYEPVWAIGGST--IPSNDAIAEAF-------EIIRSYDSKSHIIYGGSVNQENIRDLKSINQLSGVLVGSASLDVD 225
|
....*.
gi 28572008 239 -FVDII 243
Cdd:PRK14565 226 sFCKII 231
|
|
| tim |
TIGR00419 |
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ... |
7-238 |
5.85e-54 |
|
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: 172.68 E-value: 5.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 7 VGGNWKM-NGDQKSIAEIAKTLSSAALDPN-TEVVIGCPAIYL-MYARNLlpcELGLAGQNAYKVAKGAFTGEISPAMLK 83
Cdd:TIGR00419 2 VIGNWKTyNESRGMRALEVAKIAEEVASEAgVAVAVAPPFVDLpMIKREV---EIPVYAQHVDAVLSGAHTGEISAEMLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 84 DIGADWVILGHSERRaiFGESDalIAEKAEHALAEGLKVIACIgetleereagktnEVVARQMCAYAqkikdWKNVVVAY 163
Cdd:TIGR00419 79 DIGAKGTLINHSERR--MKLAD--IEKKIARLKELGLTSVVCT-------------NNVLTTAAAAA-----LEPDVVAV 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28572008 164 EPVWAIGTGQTATPDQAQEVHAFLRqwlsdnISKEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLKPE 238
Cdd:TIGR00419 137 EPPELIGTGIPVSPAQPEVVHGSVR------AVKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
|
|
| PRK14905 |
PRK14905 |
triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; ... |
1-231 |
1.42e-40 |
|
triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; Provisional
Pssm-ID: 184898 [Multi-domain] Cd Length: 355 Bit Score: 142.48 E-value: 1.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 1 MSRKFCVGGNWKM-NGDQKSI------AEIAKTLSSaalDPNTEVVIGCPAIYLMYARNLLPCELG-----LAGQNAYKV 68
Cdd:PRK14905 1 MAKKIYFGTNLKMyKGNAETVdylselLAFAEKFKS---DYDIELFVIPSYIALKDAVEAAASETGhpkikIGAQNMNAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 69 AKGAFTGEISPAMLKDIGADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTNEVVARQMCA 148
Cdd:PRK14905 78 DKGQFTGEISPLMLKELGIELVMIGHSERRHVLKETDQEENEKVLAALKHGFITLLCIGETLEQKNYNISDEVLRTQLKI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 149 YAQKI--KDWKNVVVAYEPVWAIGTGQT-ATPDQAQEVHAFLRQWLSDNISKEvSASLRIQYGGSVTAANAKELAKKPDI 225
Cdd:PRK14905 158 GLHGVsaEQLPHLFIAYEPVWAIGEGGIpASAEYADEKHAIIKQCLFELFAEE-SKKIPVLYGGSVNLENANELIMKPHI 236
|
....*.
gi 28572008 226 DGFLVG 231
Cdd:PRK14905 237 DGLFIG 242
|
|
| PRK15492 |
PRK15492 |
triosephosphate isomerase; Provisional |
60-231 |
9.48e-38 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 185389 Cd Length: 260 Bit Score: 132.81 E-value: 9.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 60 LAGQNAYKVAKGAFTGEISPAMLKDIGADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTN 139
Cdd:PRK15492 68 IGAQNMNPNDNGQFTGDISPLMLKEIGTQLVMIGHSERRHKFGETDQEENAKVLAALKHDFTTLLCVGETLEQKNYGISD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 140 EVVARQMCAYAQKI--KDWKNVVVAYEPVWAIGT-GQTATPDQAQEVHAFLRQWLSDnISKEVSASLRIQYGGSVTAANA 216
Cdd:PRK15492 148 EILRTQLKIGLHGInpDQLAKLRIAYEPVWAIGEaGIPASADYADEKHAVIKQCLIE-LFGDAGDDIPVFYGGSVNAENA 226
|
170
....*....|....*
gi 28572008 217 KELAKKPDIDGFLVG 231
Cdd:PRK15492 227 NELFGQPHIDGLFIG 241
|
|
| PRK04302 |
PRK04302 |
triosephosphate isomerase; Provisional |
22-125 |
2.93e-08 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 235274 Cd Length: 223 Bit Score: 52.56 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572008 22 EIAKTLSSAALDPNTEVVIGCPAIYLmyARNLLPCELGLAGQNAYKVAKGAFTGEISPAMLKDIGADWVILGHSERRAIF 101
Cdd:PRK04302 23 EIAKAAEKVSKETGVRIAVAPQALDI--RRVAEEVDIPVYAQHVDPVEPGSHTGHILPEAVKDAGAVGTLINHSERRLTL 100
|
90 100
....*....|....*....|....
gi 28572008 102 GESDALIaEKAEhalAEGLKVIAC 125
Cdd:PRK04302 101 ADIEAVV-ERAK---KLGLESVVC 120
|
|
| |
