|
Name |
Accession |
Description |
Interval |
E-value |
| TpiA |
COG0149 |
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ... |
1-253 |
5.40e-112 |
|
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: 322.39 E-value: 5.40e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 1 MTPIWLGTSWKMNKPLSQAMAWCETLAARMPEgcHPAIQPFVIPPFTAIQPVSHFLQThqLPLLTGAQNMHEADQGAWTG 80
Cdd:COG0149 1 MRKPLIAGNWKMNGTLAEAKALLAALAAALAD--LADVEVVVCPPFTYLAAVAEALAG--SPIALGAQNVHWEDSGAYTG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 81 EISAAMLAETGATLVELGHSERRAAFNESDAAINRKVHSALGHGLRPLICIGDSAEEKRWQVSRESVVRQMKIALYGLSH 160
Cdd:COG0149 77 EISAAMLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLSA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 161 QQALRTLIAYEPVWAIGEhGTPASPQEAGVIHQALRQALCERFGHETGTRIPLLYGGSVTLQNAVELLRQQEINGLFIGR 240
Cdd:COG0149 157 EQAANVVIAYEPVWAIGT-GKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGG 235
|
250
....*....|...
gi 1616137393 241 AAWDAQGYCDIVQ 253
Cdd:COG0149 236 ASLDAEDFLAIVR 248
|
|
| tpiA |
PRK00042 |
triosephosphate isomerase; Provisional |
5-253 |
9.44e-108 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 234589 Cd Length: 250 Bit Score: 311.67 E-value: 9.44e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 5 WLGTSWKMNKPLSQAMAWCETLAARMPEGchPAIQPFVIPPFTAIQPVSHFLQTHqlPLLTGAQNMHEADQGAWTGEISA 84
Cdd:PRK00042 4 IIAGNWKMNKTLAEAKALVEELKAALPDA--DGVEVAVAPPFTALASVKEALKGS--NIKLGAQNVHPEDSGAFTGEISA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 85 AMLAETGATLVELGHSERRAAFNESDAAINRKVHSALGHGLRPLICIGDSAEEKRWQVSRESVVRQMKIALYGLSHQQAL 164
Cdd:PRK00042 80 EMLKDLGVKYVIIGHSERRQYFGETDELVNKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLEAALAGLSAEQFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 165 RTLIAYEPVWAIGeHGTPASPQEAGVIHQALRQALCERFGhETGTRIPLLYGGSVTLQNAVELLRQQEINGLFIGRAAWD 244
Cdd:PRK00042 160 NLVIAYEPVWAIG-TGKTATPEQAQEVHAFIRAVLAELYG-EVAEKVRILYGGSVKPDNAAELMAQPDIDGALVGGASLK 237
|
....*....
gi 1616137393 245 AQGYCDIVQ 253
Cdd:PRK00042 238 AEDFLAIVK 246
|
|
| TIM |
cd00311 |
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ... |
5-253 |
5.18e-100 |
|
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: 291.75 E-value: 5.18e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 5 WLGTSWKMNKPLSQAMAWCETLAARMPEgcHPAIQPFVIPPFTAIQPVSHFLQTHQLPLltGAQNMHEADQGAWTGEISA 84
Cdd:cd00311 2 LVAGNWKMNGTLAEALELAKALNAVLKD--ESGVEVVVAPPFTYLAAVAEALEGSKIKV--GAQNVSPEDSGAFTGEISA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 85 AMLAETGATLVELGHSERRAAFNESDAAINRKVHSALGHGLRPLICIGDSAEEKRWQVSRESVVRQMKIALYGLShqQAL 164
Cdd:cd00311 78 EMLKDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVE--DLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 165 RTLIAYEPVWAIGEhGTPASPQEAGVIHQALRQALCERFGhETGTRIPLLYGGSVTLQNAVELLRQQEINGLFIGRAAWD 244
Cdd:cd00311 156 PVVIAYEPVWAIGT-GKTASPEQAQEVHAFIRKLLAELYG-EVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLK 233
|
....*....
gi 1616137393 245 AQGYCDIVQ 253
Cdd:cd00311 234 AESFLDIIK 242
|
|
| TIM |
pfam00121 |
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ... |
5-253 |
1.80e-92 |
|
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: 272.85 E-value: 1.80e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 5 WLGTSWKMNKPLSQAMAWCETLAARMPEgcHPAIQPFVIPPFTAIQPVSHFLQThqlPLLTGAQNMHEADQGAWTGEISA 84
Cdd:pfam00121 2 IIAGNWKMNGTLAEAAELLAELAEALAD--ESGVEVVVAPPFTYLSAVAELLGS---NIKVGAQNVDPEESGAFTGEISA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 85 AMLAETGATLVELGHSERRAAFNESDAAINRKVHSALGHGLRPLICIGDSAEEKRWQVSRESVVRQMKIALYGLSHQQAl 164
Cdd:pfam00121 77 EMLKDLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQK- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 165 RTLIAYEPVWAIGEhGTPASPQEAGVIHQALRQALCERFGhETGTRIPLLYGGSVTLQNAVELLRQQEINGLFIGRAAWD 244
Cdd:pfam00121 156 NLVIAYEPVWAIGT-GKTATPEQAQEVHAFIRAVLAELYK-EVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLK 233
|
....*....
gi 1616137393 245 AQGYCDIVQ 253
Cdd:pfam00121 234 AEDFLDIIN 242
|
|
| tim |
TIGR00419 |
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ... |
23-241 |
2.26e-25 |
|
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: 99.49 E-value: 2.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 23 CETLAArmPEGCHPAIQPfvipPFTAIQPVSHflqthQLPLLTGAQNMHEADQGAWTGEISAAMLAETGATLVELGHSER 102
Cdd:TIGR00419 24 AEEVAS--EAGVAVAVAP----PFVDLPMIKR-----EVEIPVYAQHVDAVLSGAHTGEISAEMLKDIGAKGTLINHSER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 103 RAAfnESDaaINRKVHSALGHGLRPLICIgdsaeekrwqvsrESVVRQMKIALYGlshqqalRTLIAYEPVWAIGEhGTP 182
Cdd:TIGR00419 93 RMK--LAD--IEKKIARLKELGLTSVVCT-------------NNVLTTAAAAALE-------PDVVAVEPPELIGT-GIP 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1616137393 183 ASPQEAGVIHQALRQAlcerfgHETGTRIPLLYGGSVTLQNAVELLRQQEINGLFIGRA 241
Cdd:TIGR00419 148 VSPAQPEVVHGSVRAV------KEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASG 200
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| TpiA |
COG0149 |
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ... |
1-253 |
5.40e-112 |
|
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: 322.39 E-value: 5.40e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 1 MTPIWLGTSWKMNKPLSQAMAWCETLAARMPEgcHPAIQPFVIPPFTAIQPVSHFLQThqLPLLTGAQNMHEADQGAWTG 80
Cdd:COG0149 1 MRKPLIAGNWKMNGTLAEAKALLAALAAALAD--LADVEVVVCPPFTYLAAVAEALAG--SPIALGAQNVHWEDSGAYTG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 81 EISAAMLAETGATLVELGHSERRAAFNESDAAINRKVHSALGHGLRPLICIGDSAEEKRWQVSRESVVRQMKIALYGLSH 160
Cdd:COG0149 77 EISAAMLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLSA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 161 QQALRTLIAYEPVWAIGEhGTPASPQEAGVIHQALRQALCERFGHETGTRIPLLYGGSVTLQNAVELLRQQEINGLFIGR 240
Cdd:COG0149 157 EQAANVVIAYEPVWAIGT-GKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGG 235
|
250
....*....|...
gi 1616137393 241 AAWDAQGYCDIVQ 253
Cdd:COG0149 236 ASLDAEDFLAIVR 248
|
|
| tpiA |
PRK00042 |
triosephosphate isomerase; Provisional |
5-253 |
9.44e-108 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 234589 Cd Length: 250 Bit Score: 311.67 E-value: 9.44e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 5 WLGTSWKMNKPLSQAMAWCETLAARMPEGchPAIQPFVIPPFTAIQPVSHFLQTHqlPLLTGAQNMHEADQGAWTGEISA 84
Cdd:PRK00042 4 IIAGNWKMNKTLAEAKALVEELKAALPDA--DGVEVAVAPPFTALASVKEALKGS--NIKLGAQNVHPEDSGAFTGEISA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 85 AMLAETGATLVELGHSERRAAFNESDAAINRKVHSALGHGLRPLICIGDSAEEKRWQVSRESVVRQMKIALYGLSHQQAL 164
Cdd:PRK00042 80 EMLKDLGVKYVIIGHSERRQYFGETDELVNKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLEAALAGLSAEQFA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 165 RTLIAYEPVWAIGeHGTPASPQEAGVIHQALRQALCERFGhETGTRIPLLYGGSVTLQNAVELLRQQEINGLFIGRAAWD 244
Cdd:PRK00042 160 NLVIAYEPVWAIG-TGKTATPEQAQEVHAFIRAVLAELYG-EVAEKVRILYGGSVKPDNAAELMAQPDIDGALVGGASLK 237
|
....*....
gi 1616137393 245 AQGYCDIVQ 253
Cdd:PRK00042 238 AEDFLAIVK 246
|
|
| TIM |
cd00311 |
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ... |
5-253 |
5.18e-100 |
|
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: 291.75 E-value: 5.18e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 5 WLGTSWKMNKPLSQAMAWCETLAARMPEgcHPAIQPFVIPPFTAIQPVSHFLQTHQLPLltGAQNMHEADQGAWTGEISA 84
Cdd:cd00311 2 LVAGNWKMNGTLAEALELAKALNAVLKD--ESGVEVVVAPPFTYLAAVAEALEGSKIKV--GAQNVSPEDSGAFTGEISA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 85 AMLAETGATLVELGHSERRAAFNESDAAINRKVHSALGHGLRPLICIGDSAEEKRWQVSRESVVRQMKIALYGLShqQAL 164
Cdd:cd00311 78 EMLKDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVE--DLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 165 RTLIAYEPVWAIGEhGTPASPQEAGVIHQALRQALCERFGhETGTRIPLLYGGSVTLQNAVELLRQQEINGLFIGRAAWD 244
Cdd:cd00311 156 PVVIAYEPVWAIGT-GKTASPEQAQEVHAFIRKLLAELYG-EVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLK 233
|
....*....
gi 1616137393 245 AQGYCDIVQ 253
Cdd:cd00311 234 AESFLDIIK 242
|
|
| TIM |
pfam00121 |
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ... |
5-253 |
1.80e-92 |
|
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: 272.85 E-value: 1.80e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 5 WLGTSWKMNKPLSQAMAWCETLAARMPEgcHPAIQPFVIPPFTAIQPVSHFLQThqlPLLTGAQNMHEADQGAWTGEISA 84
Cdd:pfam00121 2 IIAGNWKMNGTLAEAAELLAELAEALAD--ESGVEVVVAPPFTYLSAVAELLGS---NIKVGAQNVDPEESGAFTGEISA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 85 AMLAETGATLVELGHSERRAAFNESDAAINRKVHSALGHGLRPLICIGDSAEEKRWQVSRESVVRQMKIALYGLSHQQAl 164
Cdd:pfam00121 77 EMLKDLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQK- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 165 RTLIAYEPVWAIGEhGTPASPQEAGVIHQALRQALCERFGhETGTRIPLLYGGSVTLQNAVELLRQQEINGLFIGRAAWD 244
Cdd:pfam00121 156 NLVIAYEPVWAIGT-GKTATPEQAQEVHAFIRAVLAELYK-EVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLK 233
|
....*....
gi 1616137393 245 AQGYCDIVQ 253
Cdd:pfam00121 234 AEDFLDIIN 242
|
|
| PRK14905 |
PRK14905 |
triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; ... |
4-248 |
6.40e-73 |
|
triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; Provisional
Pssm-ID: 184898 [Multi-domain] Cd Length: 355 Bit Score: 226.84 E-value: 6.40e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 4 IWLGTSWKMNKP-------LSQAMAWCETLAARMPegchpaIQPFVIPPFTAIQPVSHFL--QTHQLPLLTGAQNMHEAD 74
Cdd:PRK14905 5 IYFGTNLKMYKGnaetvdyLSELLAFAEKFKSDYD------IELFVIPSYIALKDAVEAAasETGHPKIKIGAQNMNAKD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 75 QGAWTGEISAAMLAETGATLVELGHSERRAAFNESDAAINRKVHSALGHGLRPLICIGDSAEEKRWQVSRESVVRQMKIA 154
Cdd:PRK14905 79 KGQFTGEISPLMLKELGIELVMIGHSERRHVLKETDQEENEKVLAALKHGFITLLCIGETLEQKNYNISDEVLRTQLKIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 155 LYGLSHQQALRTLIAYEPVWAIGEHGTPASPQEAGVIHQALRQALCERFGHETgTRIPLLYGGSVTLQNAVELLRQQEIN 234
Cdd:PRK14905 159 LHGVSAEQLPHLFIAYEPVWAIGEGGIPASAEYADEKHAIIKQCLFELFAEES-KKIPVLYGGSVNLENANELIMKPHID 237
|
250
....*....|....
gi 1616137393 235 GLFIGRAAWDAQGY 248
Cdd:PRK14905 238 GLFIGRSAWDAQCF 251
|
|
| PRK15492 |
PRK15492 |
triosephosphate isomerase; Provisional |
1-255 |
1.12e-72 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 185389 Cd Length: 260 Bit Score: 222.95 E-value: 1.12e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 1 MTPIWLGTSWKMNKPLSQAMAWCetlaARMPEGCH--PA---IQPFVIPPFTAIQ-PVSHFLQT-HQLPLLTGAQNMHEA 73
Cdd:PRK15492 1 MKKIYFGTNLKMYKGIADATDFL----AKLSELADdiPAdkdIELFVIPSFTAIQdAIAATLAIpHDHPIIIGAQNMNPN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 74 DQGAWTGEISAAMLAETGATLVELGHSERRAAFNESDAAINRKVHSALGHGLRPLICIGDSAEEKRWQVSRESVVRQMKI 153
Cdd:PRK15492 77 DNGQFTGDISPLMLKEIGTQLVMIGHSERRHKFGETDQEENAKVLAALKHDFTTLLCVGETLEQKNYGISDEILRTQLKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 154 ALYGLSHQQALRTLIAYEPVWAIGEHGTPASPQEAGVIHQALRQALCERFGhETGTRIPLLYGGSVTLQNAVELLRQQEI 233
Cdd:PRK15492 157 GLHGINPDQLAKLRIAYEPVWAIGEAGIPASADYADEKHAVIKQCLIELFG-DAGDDIPVFYGGSVNAENANELFGQPHI 235
|
250 260
....*....|....*....|..
gi 1616137393 234 NGLFIGRAAWDAQGYCDIVQRV 255
Cdd:PRK15492 236 DGLFIGRSAWDADKFFAIIEGI 257
|
|
| PRK13962 |
PRK13962 |
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional |
2-256 |
1.50e-69 |
|
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional
Pssm-ID: 237572 [Multi-domain] Cd Length: 645 Bit Score: 225.76 E-value: 1.50e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 2 TPIWLGtSWKMNKPLSQAMAWCETLAARMPEGCHPAIqpfVIPPFTAIQPVSHFLQTHQLPLltGAQNMHEADQGAWTGE 81
Cdd:PRK13962 398 KPIIAG-NWKMNKTPAEAKEFVNELKKYVKDAQAEVV---VCPPFTALPSVKEAVDGSNIKL--GAQNVFYEEKGAYTGE 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 82 ISAAMLAETGATLVELGHSERRAAFNESDAAINRKVHSALGHGLRPLICIGDSAEEKRWQVSRESVVRQMKIALYGLSHQ 161
Cdd:PRK13962 472 ISGPMLAEIGVEYVIIGHSERRQYFGETDELVNKKVLAALKAGLTPILCVGETLDERESGITFDVVRLQLKAALNGLSAE 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 162 QALRTLIAYEPVWAIGEhGTPASPQEAGVIHQALRQALCERFGHETGTRIPLLYGGSVTLQNAVELLRQQEINGLFIGRA 241
Cdd:PRK13962 552 QVKKVVIAYEPVWAIGT-GKVATPEQAQEVHAFIRKLVAELYGEEAARKVRILYGGSVKSENAAGLFNQPDIDGGLVGGA 630
|
250
....*....|....*
gi 1616137393 242 AWDAQGYCDIVQRVT 256
Cdd:PRK13962 631 SLKAQEFAAIANYFI 645
|
|
| PTZ00333 |
PTZ00333 |
triosephosphate isomerase; Provisional |
5-257 |
9.82e-50 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 240365 Cd Length: 255 Bit Score: 163.93 E-value: 9.82e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 5 WLGTSWKMNkpLSQAMAwcETLAARMPEGCHP--AIQPFVIPPFTAIQPVSHFLQTHQLPLltGAQNMHEADQGAWTGEI 82
Cdd:PTZ00333 7 FVGGNWKCN--GTKASI--KELIDSFNKLKFDpnNVDVVVAPPSLHIPLVQEKLKNKNFKI--SSQNVSLTGSGAFTGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 83 SAAMLAETGATLVELGHSERRAAFNESDAAINRKVHSALGHGLRPLICIGDSAEEkRWQVSRESVVR-QMKIALYGLSHQ 161
Cdd:PTZ00333 81 SAEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEE-REAGQTSDVLSkQLEAIVKKVSDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 162 QALRTLIAYEPVWAIGEhGTPASPQEAGVIHQALRQALCERFGHETGTRIPLLYGGSVTLQNAVELLRQQEINGLFIGRA 241
Cdd:PTZ00333 160 AWDNIVIAYEPVWAIGT-GKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGA 238
|
250
....*....|....*.
gi 1616137393 242 AWDAQgYCDIVQRVTQ 257
Cdd:PTZ00333 239 SLKPD-FVDIIKSAEQ 253
|
|
| PRK14565 |
PRK14565 |
triosephosphate isomerase; Provisional |
10-255 |
4.74e-43 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 237758 Cd Length: 237 Bit Score: 146.44 E-value: 4.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 10 WKMNKPLSQAMAWCETLAARMPEGCHpAIQPFVIPPFTAIQPVSHFLQTHQLplltGAQNMHEADQGAWTGEISAAMLAE 89
Cdd:PRK14565 9 WKMNGDFSLFSSFLKELSNKLANNEI-TLKLVICPPFTAMSSFVECNPNIKL----GAQNCFYGSSGGYTGEISAKMLKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 90 TGATLVELGHSERRAAFNESDAAINRKVHSALGHGLRPLICIGDSAEEKRWQVSRESVVRQMKIAL--YGlshqqalRTL 167
Cdd:PRK14565 84 CGCSYVILGHSERRSTFHETDSDIRLKAESAIESGLIPIICVGETLEDRENGMTKDVLLEQCSNCLpkHG-------EFI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 168 IAYEPVWAIGEHGTPASpqeagvihQALRQALCERFGHETGTRIplLYGGSVTLQNAVELLRQQEINGLFIGRAAWDAQG 247
Cdd:PRK14565 157 IAYEPVWAIGGSTIPSN--------DAIAEAFEIIRSYDSKSHI--IYGGSVNQENIRDLKSINQLSGVLVGSASLDVDS 226
|
....*...
gi 1616137393 248 YCDIVQRV 255
Cdd:PRK14565 227 FCKIIQQV 234
|
|
| PLN02561 |
PLN02561 |
triosephosphate isomerase |
5-256 |
4.11e-39 |
|
triosephosphate isomerase
Pssm-ID: 178175 Cd Length: 253 Bit Score: 136.49 E-value: 4.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 5 WLGTSWKMNKPLSQAMAWCETL-AARMPegCHPAIQPFVIPPFTAIQPVSHFLQTHqlpLLTGAQNMHEADQGAWTGEIS 83
Cdd:PLN02561 6 FVGGNWKCNGTVEEVKKIVTTLnEAEVP--SEDVVEVVVSPPFVFLPLVKSLLRPD---FQVAAQNCWVKKGGAFTGEIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 84 AAMLAETGATLVELGHSERRAAFNESDAAINRKVHSALGHGLRPLICIGDSAEEKRWQVSRESVVRQMKIALYGLSHQQa 163
Cdd:PLN02561 81 AEMLVNLGIPWVILGHSERRALLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIADKVSDWA- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 164 lRTLIAYEPVWAIGEhGTPASPQEAGVIHQALRQALCERFGHETGTRIPLLYGGSVTLQNAVELLRQQEINGLFIGRAAW 243
Cdd:PLN02561 160 -NVVLAYEPVWAIGT-GKVATPAQAQEVHDELRKWLHKNVSPEVAATTRIIYGGSVTGANCKELAAQPDVDGFLVGGASL 237
|
250
....*....|...
gi 1616137393 244 DAQgYCDIVQRVT 256
Cdd:PLN02561 238 KPE-FIDIIKSAT 249
|
|
| PLN02429 |
PLN02429 |
triosephosphate isomerase |
42-258 |
1.31e-33 |
|
triosephosphate isomerase
Pssm-ID: 166070 Cd Length: 315 Bit Score: 124.13 E-value: 1.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 42 VIPPFTAIQPVSHFLqTHQLPLltGAQNMHEADQGAWTGEISAAMLAETGATLVELGHSERRAAFNESDAAINRKVHSAL 121
Cdd:PLN02429 101 VSPPFVYIDQVKSSL-TDRIDI--SGQNSWVGKGGAFTGEISVEQLKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYAL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 122 GHGLRPLICIGDSAEEKRWQVSRESVVRQMKIALYGLSHQQALrtLIAYEPVWAIGEhGTPASPQEAGVIHQALRQALCE 201
Cdd:PLN02429 178 SEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDNI--VVAYEPVWAIGT-GKVASPQQAQEVHVAVRGWLKK 254
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1616137393 202 RFGHETGTRIPLLYGGSVTLQNAVELLRQQEINGLFIGRAAWDAQGYCDIVQRVTQE 258
Cdd:PLN02429 255 NVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKGPEFATIVNSVTSK 311
|
|
| tim |
TIGR00419 |
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ... |
23-241 |
2.26e-25 |
|
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: 99.49 E-value: 2.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 23 CETLAArmPEGCHPAIQPfvipPFTAIQPVSHflqthQLPLLTGAQNMHEADQGAWTGEISAAMLAETGATLVELGHSER 102
Cdd:TIGR00419 24 AEEVAS--EAGVAVAVAP----PFVDLPMIKR-----EVEIPVYAQHVDAVLSGAHTGEISAEMLKDIGAKGTLINHSER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 103 RAAfnESDaaINRKVHSALGHGLRPLICIgdsaeekrwqvsrESVVRQMKIALYGlshqqalRTLIAYEPVWAIGEhGTP 182
Cdd:TIGR00419 93 RMK--LAD--IEKKIARLKELGLTSVVCT-------------NNVLTTAAAAALE-------PDVVAVEPPELIGT-GIP 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1616137393 183 ASPQEAGVIHQALRQAlcerfgHETGTRIPLLYGGSVTLQNAVELLRQQEINGLFIGRA 241
Cdd:TIGR00419 148 VSPAQPEVVHGSVRAV------KEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASG 200
|
|
| PRK04302 |
PRK04302 |
triosephosphate isomerase; Provisional |
42-130 |
2.71e-08 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 235274 Cd Length: 223 Bit Score: 52.95 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 42 VIPPFTAIQPVShflQTHQLPLLtgAQNMHEADQGAWTGEISAAMLAETGATLVELGHSERRAAFNESDAAINRkvhsAL 121
Cdd:PRK04302 41 VAPQALDIRRVA---EEVDIPVY--AQHVDPVEPGSHTGHILPEAVKDAGAVGTLINHSERRLTLADIEAVVER----AK 111
|
....*....
gi 1616137393 122 GHGLRPLIC 130
Cdd:PRK04302 112 KLGLESVVC 120
|
|
| TIM_phosphate_binding |
cd04722 |
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ... |
48-240 |
8.44e-03 |
|
TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.
Pssm-ID: 240073 [Multi-domain] Cd Length: 200 Bit Score: 36.41 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 48 AIQPVSHFLQTHQLPLLTGAQNMHEADQGAWtgEISAAMLAETGATLVELGHSERRAAfnESDAAINRKVHSALGHGLrP 127
Cdd:cd04722 43 TDDKEVLKEVAAETDLPLGVQLAINDAAAAV--DIAAAAARAAGADGVEIHGAVGYLA--REDLELIRELREAVPDVK-V 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1616137393 128 LICIGDSAEEKRwqvsresvvrqMKIALYGLshqqalrTLIAYEPVWaigehGTPASPQEAGVIHQALRQALCerfghet 207
Cdd:cd04722 118 VVKLSPTGELAA-----------AAAEEAGV-------DEVGLGNGG-----GGGGGRDAVPIADLLLILAKR------- 167
|
170 180 190
....*....|....*....|....*....|...
gi 1616137393 208 GTRIPLLYGGSVTLQNAVELLRQQEINGLFIGR 240
Cdd:cd04722 168 GSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
|
|
|