|
Name |
Accession |
Description |
Interval |
E-value |
| TIM |
cd00311 |
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ... |
5-245 |
2.65e-124 |
|
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: 352.61 E-value: 2.65e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 5 FFVGGNFKLNGSKQSIKEIVERLNTASI-PENVEVVICPPATYLDYSVSLVKKPQVTVGAQNAYLKASGAFTGENSVDQI 83
Cdd:cd00311 1 PLVAGNWKMNGTLAEALELAKALNAVLKdESGVEVVVAPPFTYLAAVAEALEGSKIKVGAQNVSPEDSGAFTGEISAEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 84 KDVGAKWVILGHSERRSYFHEDDKFIADKTKFALGQGVGVILCIGETLEEKKAGKTLDVVERQLNAVLEEVKDWTNVVVA 163
Cdd:cd00311 81 KDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 164 YEPVWAIGTGLAATPEDAQDIHASIRKFLAsKLGDKAASELRILYGGSANGSNAVTFKDKADVDGFLVGGASLKPE-FVD 242
Cdd:cd00311 161 YEPVWAIGTGKTASPEQAQEVHAFIRKLLA-ELYGEVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAEsFLD 239
|
...
gi 6320255 243 IIN 245
Cdd:cd00311 240 IIK 242
|
|
| TpiA |
COG0149 |
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ... |
3-246 |
2.73e-122 |
|
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: 347.81 E-value: 2.73e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 3 RTFFVGGNFKLNGSKQSIKEIVERL-NTASIPENVEVVICPPATYLDYSVSLVKKPQVTVGAQNAYLKASGAFTGENSVD 81
Cdd:COG0149 2 RKPLIAGNWKMNGTLAEAKALLAALaAALADLADVEVVVCPPFTYLAAVAEALAGSPIALGAQNVHWEDSGAYTGEISAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 82 QIKDVGAKWVILGHSERRSYFHEDDKFIADKTKFALGQGVGVILCIGETLEEKKAGKTLDVVERQLNAVLEEV--KDWTN 159
Cdd:COG0149 82 MLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLsaEQAAN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 160 VVVAYEPVWAIGTGLAATPEDAQDIHASIRKFLASKLGDKAASELRILYGGSANGSNAVTFKDKADVDGFLVGGASLKPE 239
Cdd:COG0149 162 VVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDAE 241
|
....*...
gi 6320255 240 -FVDIINS 246
Cdd:COG0149 242 dFLAIVRA 249
|
|
| PTZ00333 |
PTZ00333 |
triosephosphate isomerase; Provisional |
1-246 |
7.59e-121 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 240365 Cd Length: 255 Bit Score: 344.59 E-value: 7.59e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 1 MARTFFVGGNFKLNGSKQSIKEIVERLNTASI-PENVEVVICPPATYLDYSVSLVKKPQVTVGAQNAYLKASGAFTGENS 79
Cdd:PTZ00333 2 MKRKPFVGGNWKCNGTKASIKELIDSFNKLKFdPNNVDVVVAPPSLHIPLVQEKLKNKNFKISSQNVSLTGSGAFTGEIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 80 VDQIKDVGAKWVILGHSERRSYFHEDDKFIADKTKFALGQGVGVILCIGETLEEKKAGKTLDVVERQLNAVLEEVKD--W 157
Cdd:PTZ00333 82 AEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDeaW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 158 TNVVVAYEPVWAIGTGLAATPEDAQDIHASIRKFLASKLGDKAASELRILYGGSANGSNAVTFKDKADVDGFLVGGASLK 237
Cdd:PTZ00333 162 DNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASLK 241
|
....*....
gi 6320255 238 PEFVDIINS 246
Cdd:PTZ00333 242 PDFVDIIKS 250
|
|
| TIM |
pfam00121 |
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ... |
5-246 |
3.12e-117 |
|
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: 334.86 E-value: 3.12e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 5 FFVGGNFKLNGSKQSIKEIVERLNTASIPEN-VEVVICPPATYLDYSVSLVKKPqVTVGAQNAYLKASGAFTGENSVDQI 83
Cdd:pfam00121 1 PIIAGNWKMNGTLAEAAELLAELAEALADESgVEVVVAPPFTYLSAVAELLGSN-IKVGAQNVDPEESGAFTGEISAEML 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 84 KDVGAKWVILGHSERRSYFHEDDKFIADKTKFALGQGVGVILCIGETLEEKKAGKTLDVVERQLNAVLEEVKDWT-NVVV 162
Cdd:pfam00121 80 KDLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQkNLVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 163 AYEPVWAIGTGLAATPEDAQDIHASIRKFLASKLGDkAASELRILYGGSANGSNAVTFKDKADVDGFLVGGASLKPE-FV 241
Cdd:pfam00121 160 AYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYKE-VAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEdFL 238
|
....*
gi 6320255 242 DIINS 246
Cdd:pfam00121 239 DIINA 243
|
|
| tim |
TIGR00419 |
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ... |
6-239 |
1.10e-48 |
|
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: 159.20 E-value: 1.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 6 FVGGNFK-LNGSKQSIKEIVERLN-TASIPENVEVVICPPATYLDysvSLVKKPQVTVGAQNAYLKASGAFTGENSVDQI 83
Cdd:TIGR00419 1 LVIGNWKtYNESRGMRALEVAKIAeEVASEAGVAVAVAPPFVDLP---MIKREVEIPVYAQHVDAVLSGAHTGEISAEML 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 84 KDVGAKWVILGHSERRsyFHEDDkfIADKTKFALGQGVGVILCIGETLEEKKAGKtldvverqlnavleevkdWTNVVVA 163
Cdd:TIGR00419 78 KDIGAKGTLINHSERR--MKLAD--IEKKIARLKELGLTSVVCTNNVLTTAAAAA------------------LEPDVVA 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6320255 164 YEPVWAIGTGLAATPEDAQDIHASIRkflASKlgdKAASELRILYGGSANGSNAVTFKDKADVDGFLVGGASLKPE 239
Cdd:TIGR00419 136 VEPPELIGTGIPVSPAQPEVVHGSVR---AVK---EVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| TIM |
cd00311 |
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ... |
5-245 |
2.65e-124 |
|
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: 352.61 E-value: 2.65e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 5 FFVGGNFKLNGSKQSIKEIVERLNTASI-PENVEVVICPPATYLDYSVSLVKKPQVTVGAQNAYLKASGAFTGENSVDQI 83
Cdd:cd00311 1 PLVAGNWKMNGTLAEALELAKALNAVLKdESGVEVVVAPPFTYLAAVAEALEGSKIKVGAQNVSPEDSGAFTGEISAEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 84 KDVGAKWVILGHSERRSYFHEDDKFIADKTKFALGQGVGVILCIGETLEEKKAGKTLDVVERQLNAVLEEVKDWTNVVVA 163
Cdd:cd00311 81 KDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 164 YEPVWAIGTGLAATPEDAQDIHASIRKFLAsKLGDKAASELRILYGGSANGSNAVTFKDKADVDGFLVGGASLKPE-FVD 242
Cdd:cd00311 161 YEPVWAIGTGKTASPEQAQEVHAFIRKLLA-ELYGEVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAEsFLD 239
|
...
gi 6320255 243 IIN 245
Cdd:cd00311 240 IIK 242
|
|
| TpiA |
COG0149 |
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ... |
3-246 |
2.73e-122 |
|
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: 347.81 E-value: 2.73e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 3 RTFFVGGNFKLNGSKQSIKEIVERL-NTASIPENVEVVICPPATYLDYSVSLVKKPQVTVGAQNAYLKASGAFTGENSVD 81
Cdd:COG0149 2 RKPLIAGNWKMNGTLAEAKALLAALaAALADLADVEVVVCPPFTYLAAVAEALAGSPIALGAQNVHWEDSGAYTGEISAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 82 QIKDVGAKWVILGHSERRSYFHEDDKFIADKTKFALGQGVGVILCIGETLEEKKAGKTLDVVERQLNAVLEEV--KDWTN 159
Cdd:COG0149 82 MLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLsaEQAAN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 160 VVVAYEPVWAIGTGLAATPEDAQDIHASIRKFLASKLGDKAASELRILYGGSANGSNAVTFKDKADVDGFLVGGASLKPE 239
Cdd:COG0149 162 VVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDAE 241
|
....*...
gi 6320255 240 -FVDIINS 246
Cdd:COG0149 242 dFLAIVRA 249
|
|
| PTZ00333 |
PTZ00333 |
triosephosphate isomerase; Provisional |
1-246 |
7.59e-121 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 240365 Cd Length: 255 Bit Score: 344.59 E-value: 7.59e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 1 MARTFFVGGNFKLNGSKQSIKEIVERLNTASI-PENVEVVICPPATYLDYSVSLVKKPQVTVGAQNAYLKASGAFTGENS 79
Cdd:PTZ00333 2 MKRKPFVGGNWKCNGTKASIKELIDSFNKLKFdPNNVDVVVAPPSLHIPLVQEKLKNKNFKISSQNVSLTGSGAFTGEIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 80 VDQIKDVGAKWVILGHSERRSYFHEDDKFIADKTKFALGQGVGVILCIGETLEEKKAGKTLDVVERQLNAVLEEVKD--W 157
Cdd:PTZ00333 82 AEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDeaW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 158 TNVVVAYEPVWAIGTGLAATPEDAQDIHASIRKFLASKLGDKAASELRILYGGSANGSNAVTFKDKADVDGFLVGGASLK 237
Cdd:PTZ00333 162 DNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASLK 241
|
....*....
gi 6320255 238 PEFVDIINS 246
Cdd:PTZ00333 242 PDFVDIIKS 250
|
|
| TIM |
pfam00121 |
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ... |
5-246 |
3.12e-117 |
|
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: 334.86 E-value: 3.12e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 5 FFVGGNFKLNGSKQSIKEIVERLNTASIPEN-VEVVICPPATYLDYSVSLVKKPqVTVGAQNAYLKASGAFTGENSVDQI 83
Cdd:pfam00121 1 PIIAGNWKMNGTLAEAAELLAELAEALADESgVEVVVAPPFTYLSAVAELLGSN-IKVGAQNVDPEESGAFTGEISAEML 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 84 KDVGAKWVILGHSERRSYFHEDDKFIADKTKFALGQGVGVILCIGETLEEKKAGKTLDVVERQLNAVLEEVKDWT-NVVV 162
Cdd:pfam00121 80 KDLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQkNLVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 163 AYEPVWAIGTGLAATPEDAQDIHASIRKFLASKLGDkAASELRILYGGSANGSNAVTFKDKADVDGFLVGGASLKPE-FV 241
Cdd:pfam00121 160 AYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYKE-VAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEdFL 238
|
....*
gi 6320255 242 DIINS 246
Cdd:pfam00121 239 DIINA 243
|
|
| tpiA |
PRK00042 |
triosephosphate isomerase; Provisional |
3-245 |
1.09e-116 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 234589 Cd Length: 250 Bit Score: 333.63 E-value: 1.09e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 3 RTFFVGGNFKLNGSKQSIKEIVERLNTA-SIPENVEVVICPPATYLDYSVSLVKKPQVTVGAQNAYLKASGAFTGENSVD 81
Cdd:PRK00042 1 RKPIIAGNWKMNKTLAEAKALVEELKAAlPDADGVEVAVAPPFTALASVKEALKGSNIKLGAQNVHPEDSGAFTGEISAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 82 QIKDVGAKWVILGHSERRSYFHEDDKFIADKTKFALGQGVGVILCIGETLEEKKAGKTLDVVERQLNAVLEEV--KDWTN 159
Cdd:PRK00042 81 MLKDLGVKYVIIGHSERRQYFGETDELVNKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLEAALAGLsaEQFAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 160 VVVAYEPVWAIGTGLAATPEDAQDIHASIRKFLASKLGDkAASELRILYGGSANGSNAVTFKDKADVDGFLVGGASLKPE 239
Cdd:PRK00042 161 LVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYGE-VAEKVRILYGGSVKPDNAAELMAQPDIDGALVGGASLKAE 239
|
....*..
gi 6320255 240 -FVDIIN 245
Cdd:PRK00042 240 dFLAIVK 246
|
|
| PLN02561 |
PLN02561 |
triosephosphate isomerase |
1-246 |
1.69e-103 |
|
triosephosphate isomerase
Pssm-ID: 178175 Cd Length: 253 Bit Score: 300.59 E-value: 1.69e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 1 MARTFFVGGNFKLNGSKQSIKEIVERLNTASIP--ENVEVVICPPATYLDYSVSLVKkPQVTVGAQNAYLKASGAFTGEN 78
Cdd:PLN02561 1 MARKFFVGGNWKCNGTVEEVKKIVTTLNEAEVPseDVVEVVVSPPFVFLPLVKSLLR-PDFQVAAQNCWVKKGGAFTGEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 79 SVDQIKDVGAKWVILGHSERRSYFHEDDKFIADKTKFALGQGVGVILCIGETLEEKKAGKTLDVVERQLNAVLEEVKDWT 158
Cdd:PLN02561 80 SAEMLVNLGIPWVILGHSERRALLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIADKVSDWA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 159 NVVVAYEPVWAIGTGLAATPEDAQDIHASIRKFLASKLGDKAASELRILYGGSANGSNAVTFKDKADVDGFLVGGASLKP 238
Cdd:PLN02561 160 NVVLAYEPVWAIGTGKVATPAQAQEVHDELRKWLHKNVSPEVAATTRIIYGGSVTGANCKELAAQPDVDGFLVGGASLKP 239
|
....*...
gi 6320255 239 EFVDIINS 246
Cdd:PLN02561 240 EFIDIIKS 247
|
|
| PLN02429 |
PLN02429 |
triosephosphate isomerase |
14-246 |
9.73e-82 |
|
triosephosphate isomerase
Pssm-ID: 166070 Cd Length: 315 Bit Score: 247.40 E-value: 9.73e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 14 NGSKQSIKEIVERLNTASIPENVEVVICPPATYLDYSVSLVKKpQVTVGAQNAYLKASGAFTGENSVDQIKDVGAKWVIL 93
Cdd:PLN02429 75 NGTKDSIAKLISDLNSATLEADVDVVVSPPFVYIDQVKSSLTD-RIDISGQNSWVGKGGAFTGEISVEQLKDLGCKWVIL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 94 GHSERRSYFHEDDKFIADKTKFALGQGVGVILCIGETLEEKKAGKTLDVVERQLNAVLEEVKDWTNVVVAYEPVWAIGTG 173
Cdd:PLN02429 154 GHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDNIVVAYEPVWAIGTG 233
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6320255 174 LAATPEDAQDIHASIRKFLASKLGDKAASELRILYGGSANGSNAVTFKDKADVDGFLVGGASLK-PEFVDIINS 246
Cdd:PLN02429 234 KVASPQQAQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKgPEFATIVNS 307
|
|
| PRK13962 |
PRK13962 |
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional |
2-246 |
2.97e-80 |
|
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional
Pssm-ID: 237572 [Multi-domain] Cd Length: 645 Bit Score: 253.11 E-value: 2.97e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 2 ARTFFVGGNFKLNGSKQSIKEIVERLNTASIPENVEVVICPPATYLDYSVSLVKKPQVTVGAQNAYLKASGAFTGENSVD 81
Cdd:PRK13962 396 PRKPIIAGNWKMNKTPAEAKEFVNELKKYVKDAQAEVVVCPPFTALPSVKEAVDGSNIKLGAQNVFYEEKGAYTGEISGP 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 82 QIKDVGAKWVILGHSERRSYFHEDDKFIADKTKFALGQGVGVILCIGETLEEKKAGKTLDVVERQLNAVL-----EEVKD 156
Cdd:PRK13962 476 MLAEIGVEYVIIGHSERRQYFGETDELVNKKVLAALKAGLTPILCVGETLDERESGITFDVVRLQLKAALnglsaEQVKK 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 157 wtnVVVAYEPVWAIGTGLAATPEDAQDIHASIRKFLASKLGDKAASELRILYGGSANGSNAVTFKDKADVDGFLVGGASL 236
Cdd:PRK13962 556 ---VVIAYEPVWAIGTGKVATPEQAQEVHAFIRKLVAELYGEEAARKVRILYGGSVKSENAAGLFNQPDIDGGLVGGASL 632
|
250
....*....|.
gi 6320255 237 KP-EFVDIINS 246
Cdd:PRK13962 633 KAqEFAAIANY 643
|
|
| PRK14565 |
PRK14565 |
triosephosphate isomerase; Provisional |
4-246 |
3.22e-53 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 237758 Cd Length: 237 Bit Score: 171.87 E-value: 3.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 4 TFFVGGNFKLNGSKQSIKEIVERLNT--ASIPENVEVVICPPATYLDYSVSLVkkPQVTVGAQNAYLKASGAFTGENSVD 81
Cdd:PRK14565 2 SFLIVANWKMNGDFSLFSSFLKELSNklANNEITLKLVICPPFTAMSSFVECN--PNIKLGAQNCFYGSSGGYTGEISAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 82 QIKDVGAKWVILGHSERRSYFHEDDKFIADKTKFALGQGVGVILCIGETLEEKKAGKTLDVVERQLNAVLEEVKDWTnvv 161
Cdd:PRK14565 80 MLKECGCSYVILGHSERRSTFHETDSDIRLKAESAIESGLIPIICVGETLEDRENGMTKDVLLEQCSNCLPKHGEFI--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 162 VAYEPVWAIGTGlaATPedaqDIHASIRKFLASKLGDkaaSELRILYGGSANGSNAVTFKDKADVDGFLVGGASLKPE-F 240
Cdd:PRK14565 157 IAYEPVWAIGGS--TIP----SNDAIAEAFEIIRSYD---SKSHIIYGGSVNQENIRDLKSINQLSGVLVGSASLDVDsF 227
|
....*.
gi 6320255 241 VDIINS 246
Cdd:PRK14565 228 CKIIQQ 233
|
|
| tim |
TIGR00419 |
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ... |
6-239 |
1.10e-48 |
|
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: 159.20 E-value: 1.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 6 FVGGNFK-LNGSKQSIKEIVERLN-TASIPENVEVVICPPATYLDysvSLVKKPQVTVGAQNAYLKASGAFTGENSVDQI 83
Cdd:TIGR00419 1 LVIGNWKtYNESRGMRALEVAKIAeEVASEAGVAVAVAPPFVDLP---MIKREVEIPVYAQHVDAVLSGAHTGEISAEML 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 84 KDVGAKWVILGHSERRsyFHEDDkfIADKTKFALGQGVGVILCIGETLEEKKAGKtldvverqlnavleevkdWTNVVVA 163
Cdd:TIGR00419 78 KDIGAKGTLINHSERR--MKLAD--IEKKIARLKELGLTSVVCTNNVLTTAAAAA------------------LEPDVVA 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6320255 164 YEPVWAIGTGLAATPEDAQDIHASIRkflASKlgdKAASELRILYGGSANGSNAVTFKDKADVDGFLVGGASLKPE 239
Cdd:TIGR00419 136 VEPPELIGTGIPVSPAQPEVVHGSVR---AVK---EVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
|
|
| PRK14905 |
PRK14905 |
triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; ... |
1-232 |
4.26e-39 |
|
triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; Provisional
Pssm-ID: 184898 [Multi-domain] Cd Length: 355 Bit Score: 138.63 E-value: 4.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 1 MARTFFVGGNFKL-NGSKQSIKEIVERLNTASIPE---NVEVVICPPATYLDYSVSLVK----KPQVTVGAQNAYLKASG 72
Cdd:PRK14905 1 MAKKIYFGTNLKMyKGNAETVDYLSELLAFAEKFKsdyDIELFVIPSYIALKDAVEAAAsetgHPKIKIGAQNMNAKDKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 73 AFTGENSVDQIKDVGAKWVILGHSERRSYFHEDDKFIADKTKFALGQGVGVILCIGETLEEKKAGKTLDVVERQLNAVLE 152
Cdd:PRK14905 81 QFTGEISPLMLKELGIELVMIGHSERRHVLKETDQEENEKVLAALKHGFITLLCIGETLEQKNYNISDEVLRTQLKIGLH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 153 --EVKDWTNVVVAYEPVWAIGT-GLAATPEDAQDIHASIRKFLASKLGDKaASELRILYGGSANGSNAVTFKDKADVDGF 229
Cdd:PRK14905 161 gvSAEQLPHLFIAYEPVWAIGEgGIPASAEYADEKHAIIKQCLFELFAEE-SKKIPVLYGGSVNLENANELIMKPHIDGL 239
|
...
gi 6320255 230 LVG 232
Cdd:PRK14905 240 FIG 242
|
|
| PRK15492 |
PRK15492 |
triosephosphate isomerase; Provisional |
3-232 |
2.24e-35 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 185389 Cd Length: 260 Bit Score: 126.65 E-value: 2.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 3 RTFFVGGNFKL-NGSKQSIK---EIVERLNTASIPENVEVVICPPATYLDYSVSLVK----KPQVTVGAQNAYLKASGAF 74
Cdd:PRK15492 2 KKIYFGTNLKMyKGIADATDflaKLSELADDIPADKDIELFVIPSFTAIQDAIAATLaiphDHPIIIGAQNMNPNDNGQF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 75 TGENSVDQIKDVGAKWVILGHSERRSYFHEDDKFIADKTKFALGQGVGVILCIGETLEEKKAGKTLDVVERQLNAVLEEV 154
Cdd:PRK15492 82 TGDISPLMLKEIGTQLVMIGHSERRHKFGETDQEENAKVLAALKHDFTTLLCVGETLEQKNYGISDEILRTQLKIGLHGI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 155 --KDWTNVVVAYEPVWAIGT-GLAATPEDAQDIHASIRKFLASKLGDkAASELRILYGGSANGSNAVTFKDKADVDGFLV 231
Cdd:PRK15492 162 npDQLAKLRIAYEPVWAIGEaGIPASADYADEKHAVIKQCLIELFGD-AGDDIPVFYGGSVNAENANELFGQPHIDGLFI 240
|
.
gi 6320255 232 G 232
Cdd:PRK15492 241 G 241
|
|
| PRK04302 |
PRK04302 |
triosephosphate isomerase; Provisional |
35-179 |
7.04e-05 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 235274 Cd Length: 223 Bit Score: 42.55 E-value: 7.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6320255 35 NVEVVICPPATYLdYSVSlvKKPQVTVGAQNAYLKASGAFTGENSVDQIKDVGAKWVILGHSERRSYFHEddkfIADKTK 114
Cdd:PRK04302 36 GVRIAVAPQALDI-RRVA--EEVDIPVYAQHVDPVEPGSHTGHILPEAVKDAGAVGTLINHSERRLTLAD----IEAVVE 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6320255 115 FALGQGVGVILCIgETLEEKKAGKTLDvverqlnavleevKDWtnvvVAYEPVWAIGTGLA---ATPE 179
Cdd:PRK04302 109 RAKKLGLESVVCV-NNPETSAAAAALG-------------PDY----VAVEPPELIGTGIPvskAKPE 158
|
|
|