|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00333 |
PTZ00333 |
triosephosphate isomerase; Provisional |
102-346 |
7.67e-131 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 240365 Cd Length: 255 Bit Score: 373.87 E-value: 7.67e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 102 MSRKFCVGGNWKMNGDQKSIAEIAKTLSSAALDP-NTEVVIGCPAIYLMYARNLLPCE-LGLAGQNAYKVAKGAFTGEIS 179
Cdd:PTZ00333 2 MKRKPFVGGNWKCNGTKASIKELIDSFNKLKFDPnNVDVVVAPPSLHIPLVQEKLKNKnFKISSQNVSLTGSGAFTGEIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 180 PAMLKDIGADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTNEVVARQMCAYAQKIKD--W 257
Cdd:PTZ00333 82 AEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDeaW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 258 KNVVVAYEPVWAIGTGQTATPDQAQEVHAFLRQWLSDNISKEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLK 337
Cdd:PTZ00333 162 DNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASLK 241
|
....*....
gi 28572004 338 PEFVDIINA 346
Cdd:PTZ00333 242 PDFVDIIKS 250
|
|
| TIM |
cd00311 |
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ... |
106-345 |
1.26e-130 |
|
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: 373.02 E-value: 1.26e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 106 FCVGGNWKMNGDQKSIAEIAKTLSSAALDP-NTEVVIGCPAIYLMYARNLLP-CELGLAGQNAYKVAKGAFTGEISPAML 183
Cdd:cd00311 1 PLVAGNWKMNGTLAEALELAKALNAVLKDEsGVEVVVAPPFTYLAAVAEALEgSKIKVGAQNVSPEDSGAFTGEISAEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 184 KDIGADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTNEVVARQMCAYAQKIKDWKNVVVA 263
Cdd:cd00311 81 KDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 264 YEPVWAIGTGQTATPDQAQEVHAFLRQWLSDNISkEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLKPE-FVD 342
Cdd:cd00311 161 YEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYG-EVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAEsFLD 239
|
...
gi 28572004 343 IIN 345
Cdd:cd00311 240 IIK 242
|
|
| TpiA |
COG0149 |
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ... |
102-346 |
1.96e-128 |
|
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: 367.46 E-value: 1.96e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 102 MSRKFcVGGNWKMNGDQKSIAEIAKTLSSAALD-PNTEVVIGCPAIYLMYARNLL-PCELGLAGQNAYKVAKGAFTGEIS 179
Cdd:COG0149 1 MRKPL-IAGNWKMNGTLAEAKALLAALAAALADlADVEVVVCPPFTYLAAVAEALaGSPIALGAQNVHWEDSGAYTGEIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 180 PAMLKDIGADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTNEVVARQMCA--YAQKIKDW 257
Cdd:COG0149 80 AAMLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAalAGLSAEQA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 258 KNVVVAYEPVWAIGTGQTATPDQAQEVHAFLRQWLSDNISKEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLK 337
Cdd:COG0149 160 ANVVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLD 239
|
250
....*....|
gi 28572004 338 PE-FVDIINA 346
Cdd:COG0149 240 AEdFLAIVRA 249
|
|
| TIM |
pfam00121 |
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ... |
108-346 |
1.87e-127 |
|
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: 364.91 E-value: 1.87e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 108 VGGNWKMNGDQKSIAEIAKTLSSAALD-PNTEVVIGCPAIYLMYARNLLPCELGLAGQNAYKVAKGAFTGEISPAMLKDI 186
Cdd:pfam00121 3 IAGNWKMNGTLAEAAELLAELAEALADeSGVEVVVAPPFTYLSAVAELLGSNIKVGAQNVDPEESGAFTGEISAEMLKDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 187 GADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTNEVVARQMCAYAQKIKDW-KNVVVAYE 265
Cdd:pfam00121 83 GVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEqKNLVIAYE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 266 PVWAIGTGQTATPDQAQEVHAFLRQWLSDnISKEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLKPE-FVDII 344
Cdd:pfam00121 163 PVWAIGTGKTATPEQAQEVHAFIRAVLAE-LYKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEdFLDII 241
|
..
gi 28572004 345 NA 346
Cdd:pfam00121 242 NA 243
|
|
| tim |
TIGR00419 |
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ... |
108-339 |
1.02e-55 |
|
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: 180.77 E-value: 1.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 108 VGGNWKM-NGDQKSIAEIAKTLSSAALDPN-TEVVIGCPAIYL-MYARNLlpcELGLAGQNAYKVAKGAFTGEISPAMLK 184
Cdd:TIGR00419 2 VIGNWKTyNESRGMRALEVAKIAEEVASEAgVAVAVAPPFVDLpMIKREV---EIPVYAQHVDAVLSGAHTGEISAEMLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 185 DIGADWVILGHSERRaiFGESDalIAEKAEHALAEGLKVIACIgetleereagktnEVVARQMCAYAqkikdWKNVVVAY 264
Cdd:TIGR00419 79 DIGAKGTLINHSERR--MKLAD--IEKKIARLKELGLTSVVCT-------------NNVLTTAAAAA-----LEPDVVAV 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28572004 265 EPVWAIGTGQTATPDQAQEVHAFLRqwlsdnISKEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLKPE 339
Cdd:TIGR00419 137 EPPELIGTGIPVSPAQPEVVHGSVR------AVKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00333 |
PTZ00333 |
triosephosphate isomerase; Provisional |
102-346 |
7.67e-131 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 240365 Cd Length: 255 Bit Score: 373.87 E-value: 7.67e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 102 MSRKFCVGGNWKMNGDQKSIAEIAKTLSSAALDP-NTEVVIGCPAIYLMYARNLLPCE-LGLAGQNAYKVAKGAFTGEIS 179
Cdd:PTZ00333 2 MKRKPFVGGNWKCNGTKASIKELIDSFNKLKFDPnNVDVVVAPPSLHIPLVQEKLKNKnFKISSQNVSLTGSGAFTGEIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 180 PAMLKDIGADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTNEVVARQMCAYAQKIKD--W 257
Cdd:PTZ00333 82 AEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDeaW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 258 KNVVVAYEPVWAIGTGQTATPDQAQEVHAFLRQWLSDNISKEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLK 337
Cdd:PTZ00333 162 DNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASLK 241
|
....*....
gi 28572004 338 PEFVDIINA 346
Cdd:PTZ00333 242 PDFVDIIKS 250
|
|
| TIM |
cd00311 |
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ... |
106-345 |
1.26e-130 |
|
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: 373.02 E-value: 1.26e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 106 FCVGGNWKMNGDQKSIAEIAKTLSSAALDP-NTEVVIGCPAIYLMYARNLLP-CELGLAGQNAYKVAKGAFTGEISPAML 183
Cdd:cd00311 1 PLVAGNWKMNGTLAEALELAKALNAVLKDEsGVEVVVAPPFTYLAAVAEALEgSKIKVGAQNVSPEDSGAFTGEISAEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 184 KDIGADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTNEVVARQMCAYAQKIKDWKNVVVA 263
Cdd:cd00311 81 KDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 264 YEPVWAIGTGQTATPDQAQEVHAFLRQWLSDNISkEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLKPE-FVD 342
Cdd:cd00311 161 YEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYG-EVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAEsFLD 239
|
...
gi 28572004 343 IIN 345
Cdd:cd00311 240 IIK 242
|
|
| TpiA |
COG0149 |
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ... |
102-346 |
1.96e-128 |
|
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: 367.46 E-value: 1.96e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 102 MSRKFcVGGNWKMNGDQKSIAEIAKTLSSAALD-PNTEVVIGCPAIYLMYARNLL-PCELGLAGQNAYKVAKGAFTGEIS 179
Cdd:COG0149 1 MRKPL-IAGNWKMNGTLAEAKALLAALAAALADlADVEVVVCPPFTYLAAVAEALaGSPIALGAQNVHWEDSGAYTGEIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 180 PAMLKDIGADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTNEVVARQMCA--YAQKIKDW 257
Cdd:COG0149 80 AAMLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAalAGLSAEQA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 258 KNVVVAYEPVWAIGTGQTATPDQAQEVHAFLRQWLSDNISKEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLK 337
Cdd:COG0149 160 ANVVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLD 239
|
250
....*....|
gi 28572004 338 PE-FVDIINA 346
Cdd:COG0149 240 AEdFLAIVRA 249
|
|
| TIM |
pfam00121 |
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ... |
108-346 |
1.87e-127 |
|
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: 364.91 E-value: 1.87e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 108 VGGNWKMNGDQKSIAEIAKTLSSAALD-PNTEVVIGCPAIYLMYARNLLPCELGLAGQNAYKVAKGAFTGEISPAMLKDI 186
Cdd:pfam00121 3 IAGNWKMNGTLAEAAELLAELAEALADeSGVEVVVAPPFTYLSAVAELLGSNIKVGAQNVDPEESGAFTGEISAEMLKDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 187 GADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTNEVVARQMCAYAQKIKDW-KNVVVAYE 265
Cdd:pfam00121 83 GVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEqKNLVIAYE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 266 PVWAIGTGQTATPDQAQEVHAFLRQWLSDnISKEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLKPE-FVDII 344
Cdd:pfam00121 163 PVWAIGTGKTATPEQAQEVHAFIRAVLAE-LYKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEdFLDII 241
|
..
gi 28572004 345 NA 346
Cdd:pfam00121 242 NA 243
|
|
| tpiA |
PRK00042 |
triosephosphate isomerase; Provisional |
104-346 |
1.61e-122 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 234589 Cd Length: 250 Bit Score: 352.50 E-value: 1.61e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 104 RKFCVGGNWKMNGDQKSIAEIAKTLSSAALD-PNTEVVIGCPAIYL-MYARNLLPCELGLAGQNAYKVAKGAFTGEISPA 181
Cdd:PRK00042 1 RKPIIAGNWKMNKTLAEAKALVEELKAALPDaDGVEVAVAPPFTALaSVKEALKGSNIKLGAQNVHPEDSGAFTGEISAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 182 MLKDIGADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTNEVVARQMCA--YAQKIKDWKN 259
Cdd:PRK00042 81 MLKDLGVKYVIIGHSERRQYFGETDELVNKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLEAalAGLSAEQFAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 260 VVVAYEPVWAIGTGQTATPDQAQEVHAFLRQWLSDnISKEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLKPE 339
Cdd:PRK00042 161 LVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAE-LYGEVAEKVRILYGGSVKPDNAAELMAQPDIDGALVGGASLKAE 239
|
....*...
gi 28572004 340 -FVDIINA 346
Cdd:PRK00042 240 dFLAIVKA 247
|
|
| PLN02561 |
PLN02561 |
triosephosphate isomerase |
102-346 |
7.96e-120 |
|
triosephosphate isomerase
Pssm-ID: 178175 Cd Length: 253 Bit Score: 346.04 E-value: 7.96e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 102 MSRKFCVGGNWKMNGDQKSIAEIAKTLSSAALDPN--TEVVIGCPAIYLMYARNLLPCELGLAGQNAYKVAKGAFTGEIS 179
Cdd:PLN02561 1 MARKFFVGGNWKCNGTVEEVKKIVTTLNEAEVPSEdvVEVVVSPPFVFLPLVKSLLRPDFQVAAQNCWVKKGGAFTGEIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 180 PAMLKDIGADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTNEVVARQMCAYAQKIKDWKN 259
Cdd:PLN02561 81 AEMLVNLGIPWVILGHSERRALLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIADKVSDWAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 260 VVVAYEPVWAIGTGQTATPDQAQEVHAFLRQWLSDNISKEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLKPE 339
Cdd:PLN02561 161 VVLAYEPVWAIGTGKVATPAQAQEVHDELRKWLHKNVSPEVAATTRIIYGGSVTGANCKELAAQPDVDGFLVGGASLKPE 240
|
....*..
gi 28572004 340 FVDIINA 346
Cdd:PLN02561 241 FIDIIKS 247
|
|
| PLN02429 |
PLN02429 |
triosephosphate isomerase |
103-346 |
1.27e-88 |
|
triosephosphate isomerase
Pssm-ID: 166070 Cd Length: 315 Bit Score: 268.97 E-value: 1.27e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 103 SRKFCVGGNWKMNGDQKSIAEIAKTLSSAALDPNTEVVIGCPAIYLMYARNLLPCELGLAGQNAYKVAKGAFTGEISPAM 182
Cdd:PLN02429 63 SGKFFVGGNWKCNGTKDSIAKLISDLNSATLEADVDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEISVEQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 183 LKDIGADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTNEVVARQMCAYAQKIKDWKNVVV 262
Cdd:PLN02429 143 LKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDNIVV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 263 AYEPVWAIGTGQTATPDQAQEVHAFLRQWLSDNISKEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLK-PEFV 341
Cdd:PLN02429 223 AYEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKgPEFA 302
|
....*
gi 28572004 342 DIINA 346
Cdd:PLN02429 303 TIVNS 307
|
|
| PRK13962 |
PRK13962 |
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional |
97-346 |
1.66e-85 |
|
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional
Pssm-ID: 237572 [Multi-domain] Cd Length: 645 Bit Score: 270.83 E-value: 1.66e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 97 SNSNNmsRKFCVGGNWKMNGDQKSIAEIAKTLSSAALDPNTEVVIGCPAIYLMYARNLLPCE-LGLAGQNAYKVAKGAFT 175
Cdd:PRK13962 392 LDKNP--RKPIIAGNWKMNKTPAEAKEFVNELKKYVKDAQAEVVVCPPFTALPSVKEAVDGSnIKLGAQNVFYEEKGAYT 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 176 GEISPAMLKDIGADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTNEVVARQMCA--YAQK 253
Cdd:PRK13962 470 GEISGPMLAEIGVEYVIIGHSERRQYFGETDELVNKKVLAALKAGLTPILCVGETLDERESGITFDVVRLQLKAalNGLS 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 254 IKDWKNVVVAYEPVWAIGTGQTATPDQAQEVHAFLRQWLSDNISKEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGG 333
Cdd:PRK13962 550 AEQVKKVVIAYEPVWAIGTGKVATPEQAQEVHAFIRKLVAELYGEEAARKVRILYGGSVKSENAAGLFNQPDIDGGLVGG 629
|
250
....*....|....
gi 28572004 334 ASLKP-EFVDIINA 346
Cdd:PRK13962 630 ASLKAqEFAAIANY 643
|
|
| PRK14565 |
PRK14565 |
triosephosphate isomerase; Provisional |
102-344 |
1.73e-58 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 237758 Cd Length: 237 Bit Score: 188.81 E-value: 1.73e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 102 MSrkFCVGGNWKMNGDQKSIAEIAKTLS--SAALDPNTEVVIgCPAIYLMYARNLLPCELGLAGQNAYKVAKGAFTGEIS 179
Cdd:PRK14565 1 MS--FLIVANWKMNGDFSLFSSFLKELSnkLANNEITLKLVI-CPPFTAMSSFVECNPNIKLGAQNCFYGSSGGYTGEIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 180 PAMLKDIGADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTNEVVARQmCayAQKIKDWKN 259
Cdd:PRK14565 78 AKMLKECGCSYVILGHSERRSTFHETDSDIRLKAESAIESGLIPIICVGETLEDRENGMTKDVLLEQ-C--SNCLPKHGE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 260 VVVAYEPVWAIGTGQtaTPDQAQEVHAFlrqwlsdNISKEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLKPE 339
Cdd:PRK14565 155 FIIAYEPVWAIGGST--IPSNDAIAEAF-------EIIRSYDSKSHIIYGGSVNQENIRDLKSINQLSGVLVGSASLDVD 225
|
....*.
gi 28572004 340 -FVDII 344
Cdd:PRK14565 226 sFCKII 231
|
|
| tim |
TIGR00419 |
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ... |
108-339 |
1.02e-55 |
|
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: 180.77 E-value: 1.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 108 VGGNWKM-NGDQKSIAEIAKTLSSAALDPN-TEVVIGCPAIYL-MYARNLlpcELGLAGQNAYKVAKGAFTGEISPAMLK 184
Cdd:TIGR00419 2 VIGNWKTyNESRGMRALEVAKIAEEVASEAgVAVAVAPPFVDLpMIKREV---EIPVYAQHVDAVLSGAHTGEISAEMLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 185 DIGADWVILGHSERRaiFGESDalIAEKAEHALAEGLKVIACIgetleereagktnEVVARQMCAYAqkikdWKNVVVAY 264
Cdd:TIGR00419 79 DIGAKGTLINHSERR--MKLAD--IEKKIARLKELGLTSVVCT-------------NNVLTTAAAAA-----LEPDVVAV 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28572004 265 EPVWAIGTGQTATPDQAQEVHAFLRqwlsdnISKEVSASLRIQYGGSVTAANAKELAKKPDIDGFLVGGASLKPE 339
Cdd:TIGR00419 137 EPPELIGTGIPVSPAQPEVVHGSVR------AVKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
|
|
| PRK14905 |
PRK14905 |
triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; ... |
102-332 |
2.28e-39 |
|
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: 2.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 102 MSRKFCVGGNWKM-NGDQKSI------AEIAKTLSSaalDPNTEVVIGCPAIYLMYARNLLPCELG-----LAGQNAYKV 169
Cdd:PRK14905 1 MAKKIYFGTNLKMyKGNAETVdylselLAFAEKFKS---DYDIELFVIPSYIALKDAVEAAASETGhpkikIGAQNMNAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 170 AKGAFTGEISPAMLKDIGADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTNEVVARQMCA 249
Cdd:PRK14905 78 DKGQFTGEISPLMLKELGIELVMIGHSERRHVLKETDQEENEKVLAALKHGFITLLCIGETLEQKNYNISDEVLRTQLKI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 250 YAQKI--KDWKNVVVAYEPVWAIGTGQT-ATPDQAQEVHAFLRQWLSDNISKEvSASLRIQYGGSVTAANAKELAKKPDI 326
Cdd:PRK14905 158 GLHGVsaEQLPHLFIAYEPVWAIGEGGIpASAEYADEKHAIIKQCLFELFAEE-SKKIPVLYGGSVNLENANELIMKPHI 236
|
....*.
gi 28572004 327 DGFLVG 332
Cdd:PRK14905 237 DGLFIG 242
|
|
| PRK15492 |
PRK15492 |
triosephosphate isomerase; Provisional |
161-332 |
1.33e-36 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 185389 Cd Length: 260 Bit Score: 132.81 E-value: 1.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 161 LAGQNAYKVAKGAFTGEISPAMLKDIGADWVILGHSERRAIFGESDALIAEKAEHALAEGLKVIACIGETLEEREAGKTN 240
Cdd:PRK15492 68 IGAQNMNPNDNGQFTGDISPLMLKEIGTQLVMIGHSERRHKFGETDQEENAKVLAALKHDFTTLLCVGETLEQKNYGISD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 241 EVVARQMCAYAQKI--KDWKNVVVAYEPVWAIGT-GQTATPDQAQEVHAFLRQWLSDnISKEVSASLRIQYGGSVTAANA 317
Cdd:PRK15492 148 EILRTQLKIGLHGInpDQLAKLRIAYEPVWAIGEaGIPASADYADEKHAVIKQCLIE-LFGDAGDDIPVFYGGSVNAENA 226
|
170
....*....|....*
gi 28572004 318 KELAKKPDIDGFLVG 332
Cdd:PRK15492 227 NELFGQPHIDGLFIG 241
|
|
| PRK04302 |
PRK04302 |
triosephosphate isomerase; Provisional |
123-226 |
1.07e-08 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 235274 Cd Length: 223 Bit Score: 54.87 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28572004 123 EIAKTLSSAALDPNTEVVIGCPAIYLmyARNLLPCELGLAGQNAYKVAKGAFTGEISPAMLKDIGADWVILGHSERRAIF 202
Cdd:PRK04302 23 EIAKAAEKVSKETGVRIAVAPQALDI--RRVAEEVDIPVYAQHVDPVEPGSHTGHILPEAVKDAGAVGTLINHSERRLTL 100
|
90 100
....*....|....*....|....
gi 28572004 203 GESDALIaEKAEhalAEGLKVIAC 226
Cdd:PRK04302 101 ADIEAVV-ERAK---KLGLESVVC 120
|
|
| |
