|
Name |
Accession |
Description |
Interval |
E-value |
| TpiA |
COG0149 |
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ... |
1-150 |
9.14e-101 |
|
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: 288.88 E-value: 9.14e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163717556 1 KCEVVVCPTFVCLDAVKKAVEGTNIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKKVK 80
Cdd:COG0149 35 DVEVVVCPPFTYLAAVAEALAGSPIALGAQNVHWEDSGAYTGEISAAMLKDLGCRYVIVGHSERRQYFGETDELVNKKVK 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163717556 81 AAFAHNLTPILCCGETLEQRENGTTNDVIKAQITADLEGLTKEQAEKVVIAYEPIWAIGTGKTATSDQAN 150
Cdd:COG0149 115 AALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLSAEQAANVVIAYEPVWAIGTGKTATPEQAQ 184
|
|
| tpiA |
PRK00042 |
triosephosphate isomerase; Provisional |
1-150 |
6.75e-98 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 234589 Cd Length: 250 Bit Score: 281.62 E-value: 6.75e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163717556 1 KCEVVVCPTFVCLDAVKKAVEGTNIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKKVK 80
Cdd:PRK00042 34 GVEVAVAPPFTALASVKEALKGSNIKLGAQNVHPEDSGAFTGEISAEMLKDLGVKYVIIGHSERRQYFGETDELVNKKVK 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163717556 81 AAFAHNLTPILCCGETLEQRENGTTNDVIKAQITADLEGLTKEQAEKVVIAYEPIWAIGTGKTATSDQAN 150
Cdd:PRK00042 114 AALKAGLTPILCVGETLEEREAGKTEEVVARQLEAALAGLSAEQFANLVIAYEPVWAIGTGKTATPEQAQ 183
|
|
| TIM |
pfam00121 |
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ... |
2-150 |
3.58e-86 |
|
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: 252.05 E-value: 3.58e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163717556 2 CEVVVCPTFVCLDAVKKAVEgTNIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKKVKA 81
Cdd:pfam00121 33 VEVVVAPPFTYLSAVAELLG-SNIKVGAQNVDPEESGAFTGEISAEMLKDLGVSYVIIGHSERRQYFGETDEDVAKKVKA 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2163717556 82 AFAHNLTPILCCGETLEQRENGTTNDVIKAQITADLEGLTKEQAeKVVIAYEPIWAIGTGKTATSDQAN 150
Cdd:pfam00121 112 ALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQK-NLVIAYEPVWAIGTGKTATPEQAQ 179
|
|
| TIM |
cd00311 |
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ... |
1-150 |
1.76e-85 |
|
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: 250.15 E-value: 1.76e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163717556 1 KCEVVVCPTFVCLDAVKKAVEGTNIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKKVK 80
Cdd:cd00311 32 GVEVVVAPPFTYLAAVAEALEGSKIKVGAQNVSPEDSGAFTGEISAEMLKDAGAKYVIIGHSERRQYFGETDEDVAKKVK 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163717556 81 AAFAHNLTPILCCGETLEQRENGTTNDVIKAQITADLEGLtkEQAEKVVIAYEPIWAIGTGKTATSDQAN 150
Cdd:cd00311 112 AALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGV--EDLAPVVIAYEPVWAIGTGKTASPEQAQ 179
|
|
| tim |
TIGR00419 |
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ... |
2-149 |
2.48e-24 |
|
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: 92.94 E-value: 2.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163717556 2 CEVVVCPTFVCLDAVKKAVEgtnIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERReyFNETDetCNKKVKA 81
Cdd:TIGR00419 33 VAVAVAPPFVDLPMIKREVE---IPVYAQHVDAVLSGAHTGEISAEMLKDIGAKGTLINHSERR--MKLAD--IEKKIAR 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2163717556 82 AFAHNLTPILCcgetleqrengtTNDVIKAQITADLEGltkeqaekVVIAYEPIWAIGTGKTATSDQA 149
Cdd:TIGR00419 106 LKELGLTSVVC------------TNNVLTTAAAAALEP--------DVVAVEPPELIGTGIPVSPAQP 153
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| TpiA |
COG0149 |
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ... |
1-150 |
9.14e-101 |
|
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: 288.88 E-value: 9.14e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163717556 1 KCEVVVCPTFVCLDAVKKAVEGTNIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKKVK 80
Cdd:COG0149 35 DVEVVVCPPFTYLAAVAEALAGSPIALGAQNVHWEDSGAYTGEISAAMLKDLGCRYVIVGHSERRQYFGETDELVNKKVK 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163717556 81 AAFAHNLTPILCCGETLEQRENGTTNDVIKAQITADLEGLTKEQAEKVVIAYEPIWAIGTGKTATSDQAN 150
Cdd:COG0149 115 AALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLSAEQAANVVIAYEPVWAIGTGKTATPEQAQ 184
|
|
| tpiA |
PRK00042 |
triosephosphate isomerase; Provisional |
1-150 |
6.75e-98 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 234589 Cd Length: 250 Bit Score: 281.62 E-value: 6.75e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163717556 1 KCEVVVCPTFVCLDAVKKAVEGTNIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKKVK 80
Cdd:PRK00042 34 GVEVAVAPPFTALASVKEALKGSNIKLGAQNVHPEDSGAFTGEISAEMLKDLGVKYVIIGHSERRQYFGETDELVNKKVK 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163717556 81 AAFAHNLTPILCCGETLEQRENGTTNDVIKAQITADLEGLTKEQAEKVVIAYEPIWAIGTGKTATSDQAN 150
Cdd:PRK00042 114 AALKAGLTPILCVGETLEEREAGKTEEVVARQLEAALAGLSAEQFANLVIAYEPVWAIGTGKTATPEQAQ 183
|
|
| TIM |
pfam00121 |
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ... |
2-150 |
3.58e-86 |
|
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: 252.05 E-value: 3.58e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163717556 2 CEVVVCPTFVCLDAVKKAVEgTNIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKKVKA 81
Cdd:pfam00121 33 VEVVVAPPFTYLSAVAELLG-SNIKVGAQNVDPEESGAFTGEISAEMLKDLGVSYVIIGHSERRQYFGETDEDVAKKVKA 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2163717556 82 AFAHNLTPILCCGETLEQRENGTTNDVIKAQITADLEGLTKEQAeKVVIAYEPIWAIGTGKTATSDQAN 150
Cdd:pfam00121 112 ALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQK-NLVIAYEPVWAIGTGKTATPEQAQ 179
|
|
| TIM |
cd00311 |
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ... |
1-150 |
1.76e-85 |
|
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: 250.15 E-value: 1.76e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163717556 1 KCEVVVCPTFVCLDAVKKAVEGTNIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKKVK 80
Cdd:cd00311 32 GVEVVVAPPFTYLAAVAEALEGSKIKVGAQNVSPEDSGAFTGEISAEMLKDAGAKYVIIGHSERRQYFGETDEDVAKKVK 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163717556 81 AAFAHNLTPILCCGETLEQRENGTTNDVIKAQITADLEGLtkEQAEKVVIAYEPIWAIGTGKTATSDQAN 150
Cdd:cd00311 112 AALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGV--EDLAPVVIAYEPVWAIGTGKTASPEQAQ 179
|
|
| PRK13962 |
PRK13962 |
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional |
1-150 |
2.58e-83 |
|
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional
Pssm-ID: 237572 [Multi-domain] Cd Length: 645 Bit Score: 256.96 E-value: 2.58e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163717556 1 KCEVVVCPTFVCLDAVKKAVEGTNIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKKVK 80
Cdd:PRK13962 429 QAEVVVCPPFTALPSVKEAVDGSNIKLGAQNVFYEEKGAYTGEISGPMLAEIGVEYVIIGHSERRQYFGETDELVNKKVL 508
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163717556 81 AAFAHNLTPILCCGETLEQRENGTTNDVIKAQITADLEGLTKEQAEKVVIAYEPIWAIGTGKTATSDQAN 150
Cdd:PRK13962 509 AALKAGLTPILCVGETLDERESGITFDVVRLQLKAALNGLSAEQVKKVVIAYEPVWAIGTGKVATPEQAQ 578
|
|
| PTZ00333 |
PTZ00333 |
triosephosphate isomerase; Provisional |
3-150 |
1.69e-63 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 240365 Cd Length: 255 Bit Score: 194.75 E-value: 1.69e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163717556 3 EVVVCPTFVCLDAVKKAVEGTNIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKKVKAA 82
Cdd:PTZ00333 39 DVVVAPPSLHIPLVQEKLKNKNFKISSQNVSLTGSGAFTGEISAEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNA 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2163717556 83 FAHNLTPILCCGETLEQRENGTTNDVIKAQITADLEGLTKEQAEKVVIAYEPIWAIGTGKTATSDQAN 150
Cdd:PTZ00333 119 LENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDEAWDNIVIAYEPVWAIGTGKVATPEQAQ 186
|
|
| PLN02561 |
PLN02561 |
triosephosphate isomerase |
3-149 |
1.97e-44 |
|
triosephosphate isomerase
Pssm-ID: 178175 Cd Length: 253 Bit Score: 146.12 E-value: 1.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163717556 3 EVVVCPTFVCLDAVKKAVEgTNIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKKVKAA 82
Cdd:PLN02561 39 EVVVSPPFVFLPLVKSLLR-PDFQVAAQNCWVKKGGAFTGEISAEMLVNLGIPWVILGHSERRALLGESNEFVGDKVAYA 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2163717556 83 FAHNLTPILCCGETLEQRENGTTNDVIKAQitadleglTKEQAEK------VVIAYEPIWAIGTGKTATSDQA 149
Cdd:PLN02561 118 LSQGLKVIACVGETLEQRESGSTMDVVAAQ--------TKAIADKvsdwanVVLAYEPVWAIGTGKVATPAQA 182
|
|
| PRK14905 |
PRK14905 |
triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; ... |
3-148 |
2.53e-44 |
|
triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; Provisional
Pssm-ID: 184898 [Multi-domain] Cd Length: 355 Bit Score: 148.64 E-value: 2.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163717556 3 EVVVCPTFVCL-DAVKKAVEGT---NIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKK 78
Cdd:PRK14905 41 ELFVIPSYIALkDAVEAAASETghpKIKIGAQNMNAKDKGQFTGEISPLMLKELGIELVMIGHSERRHVLKETDQEENEK 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163717556 79 VKAAFAHNLTPILCCGETLEQRENGTTNDVIKAQITADLEGLTKEQAEKVVIAYEPIWAIGTGKTATSDQ 148
Cdd:PRK14905 121 VLAALKHGFITLLCIGETLEQKNYNISDEVLRTQLKIGLHGVSAEQLPHLFIAYEPVWAIGEGGIPASAE 190
|
|
| PRK15492 |
PRK15492 |
triosephosphate isomerase; Provisional |
3-150 |
3.82e-44 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 185389 Cd Length: 260 Bit Score: 145.52 E-value: 3.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163717556 3 EVVVCPTFVCLDAVKKAVEGTN----IKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKK 78
Cdd:PRK15492 40 ELFVIPSFTAIQDAIAATLAIPhdhpIIIGAQNMNPNDNGQFTGDISPLMLKEIGTQLVMIGHSERRHKFGETDQEENAK 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2163717556 79 VKAAFAHNLTPILCCGETLEQRENGTTNDVIKAQITADLEGLTKEQAEKVVIAYEPIWAIGT-GKTATSDQAN 150
Cdd:PRK15492 120 VLAALKHDFTTLLCVGETLEQKNYGISDEILRTQLKIGLHGINPDQLAKLRIAYEPVWAIGEaGIPASADYAD 192
|
|
| PRK14565 |
PRK14565 |
triosephosphate isomerase; Provisional |
1-147 |
1.35e-42 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 237758 Cd Length: 237 Bit Score: 141.05 E-value: 1.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163717556 1 KCEVVVCPTFVCLDAVkkaVEGT-NIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKKV 79
Cdd:PRK14565 35 TLKLVICPPFTAMSSF---VECNpNIKLGAQNCFYGSSGGYTGEISAKMLKECGCSYVILGHSERRSTFHETDSDIRLKA 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163717556 80 KAAFAHNLTPILCCGETLEQRENGTTNDVIKAQITADL--EGltkeqaeKVVIAYEPIWAIGTGKTATSD 147
Cdd:PRK14565 112 ESAIESGLIPIICVGETLEDRENGMTKDVLLEQCSNCLpkHG-------EFIIAYEPVWAIGGSTIPSND 174
|
|
| PLN02429 |
PLN02429 |
triosephosphate isomerase |
3-149 |
2.59e-33 |
|
triosephosphate isomerase
Pssm-ID: 166070 Cd Length: 315 Bit Score: 119.13 E-value: 2.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163717556 3 EVVVCPTFVCLDAVKKAVEgTNIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKKVKAA 82
Cdd:PLN02429 98 DVVVSPPFVYIDQVKSSLT-DRIDISGQNSWVGKGGAFTGEISVEQLKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYA 176
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2163717556 83 FAHNLTPILCCGETLEQRENGTTNDVIKAQITADLEGLTkeQAEKVVIAYEPIWAIGTGKTATSDQA 149
Cdd:PLN02429 177 LSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVP--SWDNIVVAYEPVWAIGTGKVASPQQA 241
|
|
| tim |
TIGR00419 |
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ... |
2-149 |
2.48e-24 |
|
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: 92.94 E-value: 2.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163717556 2 CEVVVCPTFVCLDAVKKAVEgtnIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERReyFNETDetCNKKVKA 81
Cdd:TIGR00419 33 VAVAVAPPFVDLPMIKREVE---IPVYAQHVDAVLSGAHTGEISAEMLKDIGAKGTLINHSERR--MKLAD--IEKKIAR 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2163717556 82 AFAHNLTPILCcgetleqrengtTNDVIKAQITADLEGltkeqaekVVIAYEPIWAIGTGKTATSDQA 149
Cdd:TIGR00419 106 LKELGLTSVVC------------TNNVLTTAAAAALEP--------DVVAVEPPELIGTGIPVSPAQP 153
|
|
| PRK04302 |
PRK04302 |
triosephosphate isomerase; Provisional |
3-92 |
2.63e-08 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 235274 Cd Length: 223 Bit Score: 50.64 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2163717556 3 EVVVCPTFVCLDAVKKAVEgtnIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDetcnKKVKAA 82
Cdd:PRK04302 38 RIAVAPQALDIRRVAEEVD---IPVYAQHVDPVEPGSHTGHILPEAVKDAGAVGTLINHSERRLTLADIE----AVVERA 110
|
90
....*....|
gi 2163717556 83 FAHNLTPILC 92
Cdd:PRK04302 111 KKLGLESVVC 120
|
|
|