|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00333 |
PTZ00333 |
triosephosphate isomerase; Provisional |
2-247 |
2.97e-136 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 240365 Cd Length: 255 Bit Score: 383.50 E-value: 2.97e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 2 APSRKFFVGGNWKMNGRKQSLGELIGTLNAAKV-PADTEVVCAPPTAYIDFARQKLD-PKIAVAAQNCYKVTNGAFTGEI 79
Cdd:PTZ00333 1 MMKRKPFVGGNWKCNGTKASIKELIDSFNKLKFdPNNVDVVVAPPSLHIPLVQEKLKnKNFKISSQNVSLTGSGAFTGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 80 SPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKD-- 157
Cdd:PTZ00333 81 SAEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDea 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 158 WSKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASL 237
Cdd:PTZ00333 161 WDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASL 240
|
250
....*....|
gi 4507645 238 KPEFVDIINA 247
Cdd:PTZ00333 241 KPDFVDIIKS 250
|
|
| TIM |
cd00311 |
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ... |
7-246 |
8.35e-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: 366.48 E-value: 8.35e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 7 FFVGGNWKMNGRKQSLGELIGTLNAA-KVPADTEVVCAPPTAYIDFARQKL-DPKIAVAAQNCYKVTNGAFTGEISPGMI 84
Cdd:cd00311 1 PLVAGNWKMNGTLAEALELAKALNAVlKDESGVEVVVAPPFTYLAAVAEALeGSKIKVGAQNVSPEDSGAFTGEISAEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 85 KDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVVLA 164
Cdd:cd00311 81 KDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 165 YEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDaVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE-FVD 243
Cdd:cd00311 161 YEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYGE-VAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAEsFLD 239
|
...
gi 4507645 244 IIN 246
Cdd:cd00311 240 IIK 242
|
|
| TpiA |
COG0149 |
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ... |
5-247 |
8.73e-121 |
|
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: 343.96 E-value: 8.73e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 5 RKFFVGGNWKMNGRKQSLGELIGTL-NAAKVPADTEVVCAPPTAYIDFARQKL-DPKIAVAAQNCYKVTNGAFTGEISPG 82
Cdd:COG0149 2 RKPLIAGNWKMNGTLAEAKALLAALaAALADLADVEVVVCPPFTYLAAVAEALaGSPIALGAQNVHWEDSGAYTGEISAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 83 MIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTK-VIAD-NVKDWSK 160
Cdd:COG0149 82 MLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKaALAGlSAEQAAN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 161 VVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 240
Cdd:COG0149 162 VVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDAE 241
|
....*...
gi 4507645 241 -FVDIINA 247
Cdd:COG0149 242 dFLAIVRA 249
|
|
| TIM |
pfam00121 |
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ... |
7-247 |
1.34e-119 |
|
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: 341.03 E-value: 1.34e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 7 FFVGGNWKMNGRKQSLGELIGTLNAAKVPA-DTEVVCAPPTAYIDFARQKLDPKIAVAAQNCYKVTNGAFTGEISPGMIK 85
Cdd:pfam00121 1 PIIAGNWKMNGTLAEAAELLAELAEALADEsGVEVVVAPPFTYLSAVAELLGSNIKVGAQNVDPEESGAFTGEISAEMLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 86 DCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDW-SKVVLA 164
Cdd:pfam00121 81 DLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEqKNLVIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 165 YEPVWAIGTGKTATPQQAQEVHEKLRGWLkSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE-FVD 243
Cdd:pfam00121 161 YEPVWAIGTGKTATPEQAQEVHAFIRAVL-AELYKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEdFLD 239
|
....
gi 4507645 244 IINA 247
Cdd:pfam00121 240 IINA 243
|
|
| tim |
TIGR00419 |
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ... |
8-240 |
2.64e-62 |
|
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: 194.25 E-value: 2.64e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 8 FVGGNWKM-NGRKQSLGELIGTLNA-AKVPADTEVVCAPPTAYIDFARQKLdpKIAVAAQNCYKVTNGAFTGEISPGMIK 85
Cdd:TIGR00419 1 LVIGNWKTyNESRGMRALEVAKIAEeVASEAGVAVAVAPPFVDLPMIKREV--EIPVYAQHVDAVLSGAHTGEISAEMLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 86 DCGATWVVLGHSERRHVfgESDelIGQKVAHALAEGLGVIACIgekldereagiteKVVFEQTKVIAdnvkdWSKVVLAY 165
Cdd:TIGR00419 79 DIGAKGTLINHSERRMK--LAD--IEKKIARLKELGLTSVVCT-------------NNVLTTAAAAA-----LEPDVVAV 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4507645 166 EPVWAIGTGKTATPQQAQEVHEKLRgwlksnVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 240
Cdd:TIGR00419 137 EPPELIGTGIPVSPAQPEVVHGSVR------AVKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00333 |
PTZ00333 |
triosephosphate isomerase; Provisional |
2-247 |
2.97e-136 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 240365 Cd Length: 255 Bit Score: 383.50 E-value: 2.97e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 2 APSRKFFVGGNWKMNGRKQSLGELIGTLNAAKV-PADTEVVCAPPTAYIDFARQKLD-PKIAVAAQNCYKVTNGAFTGEI 79
Cdd:PTZ00333 1 MMKRKPFVGGNWKCNGTKASIKELIDSFNKLKFdPNNVDVVVAPPSLHIPLVQEKLKnKNFKISSQNVSLTGSGAFTGEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 80 SPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKD-- 157
Cdd:PTZ00333 81 SAEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDea 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 158 WSKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASL 237
Cdd:PTZ00333 161 WDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASL 240
|
250
....*....|
gi 4507645 238 KPEFVDIINA 247
Cdd:PTZ00333 241 KPDFVDIIKS 250
|
|
| TIM |
cd00311 |
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ... |
7-246 |
8.35e-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: 366.48 E-value: 8.35e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 7 FFVGGNWKMNGRKQSLGELIGTLNAA-KVPADTEVVCAPPTAYIDFARQKL-DPKIAVAAQNCYKVTNGAFTGEISPGMI 84
Cdd:cd00311 1 PLVAGNWKMNGTLAEALELAKALNAVlKDESGVEVVVAPPFTYLAAVAEALeGSKIKVGAQNVSPEDSGAFTGEISAEML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 85 KDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVVLA 164
Cdd:cd00311 81 KDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 165 YEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDaVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE-FVD 243
Cdd:cd00311 161 YEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYGE-VAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAEsFLD 239
|
...
gi 4507645 244 IIN 246
Cdd:cd00311 240 IIK 242
|
|
| PLN02561 |
PLN02561 |
triosephosphate isomerase |
4-247 |
5.32e-124 |
|
triosephosphate isomerase
Pssm-ID: 178175 Cd Length: 253 Bit Score: 352.59 E-value: 5.32e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 4 SRKFFVGGNWKMNGRKQSLGELIGTLNAAKVPA--DTEVVCAPPTAYIDFARQKLDPKIAVAAQNCYKVTNGAFTGEISP 81
Cdd:PLN02561 2 ARKFFVGGNWKCNGTVEEVKKIVTTLNEAEVPSedVVEVVVSPPFVFLPLVKSLLRPDFQVAAQNCWVKKGGAFTGEISA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 82 GMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKV 161
Cdd:PLN02561 82 EMLVNLGIPWVILGHSERRALLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIADKVSDWANV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 162 VLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPEF 241
Cdd:PLN02561 162 VLAYEPVWAIGTGKVATPAQAQEVHDELRKWLHKNVSPEVAATTRIIYGGSVTGANCKELAAQPDVDGFLVGGASLKPEF 241
|
....*.
gi 4507645 242 VDIINA 247
Cdd:PLN02561 242 IDIIKS 247
|
|
| TpiA |
COG0149 |
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ... |
5-247 |
8.73e-121 |
|
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: 343.96 E-value: 8.73e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 5 RKFFVGGNWKMNGRKQSLGELIGTL-NAAKVPADTEVVCAPPTAYIDFARQKL-DPKIAVAAQNCYKVTNGAFTGEISPG 82
Cdd:COG0149 2 RKPLIAGNWKMNGTLAEAKALLAALaAALADLADVEVVVCPPFTYLAAVAEALaGSPIALGAQNVHWEDSGAYTGEISAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 83 MIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTK-VIAD-NVKDWSK 160
Cdd:COG0149 82 MLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKaALAGlSAEQAAN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 161 VVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 240
Cdd:COG0149 162 VVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDAE 241
|
....*...
gi 4507645 241 -FVDIINA 247
Cdd:COG0149 242 dFLAIVRA 249
|
|
| TIM |
pfam00121 |
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ... |
7-247 |
1.34e-119 |
|
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: 341.03 E-value: 1.34e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 7 FFVGGNWKMNGRKQSLGELIGTLNAAKVPA-DTEVVCAPPTAYIDFARQKLDPKIAVAAQNCYKVTNGAFTGEISPGMIK 85
Cdd:pfam00121 1 PIIAGNWKMNGTLAEAAELLAELAEALADEsGVEVVVAPPFTYLSAVAELLGSNIKVGAQNVDPEESGAFTGEISAEMLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 86 DCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDW-SKVVLA 164
Cdd:pfam00121 81 DLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEqKNLVIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 165 YEPVWAIGTGKTATPQQAQEVHEKLRGWLkSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE-FVD 243
Cdd:pfam00121 161 YEPVWAIGTGKTATPEQAQEVHAFIRAVL-AELYKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEdFLD 239
|
....
gi 4507645 244 IINA 247
Cdd:pfam00121 240 IINA 243
|
|
| tpiA |
PRK00042 |
triosephosphate isomerase; Provisional |
5-247 |
1.91e-115 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 234589 Cd Length: 250 Bit Score: 330.54 E-value: 1.91e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 5 RKFFVGGNWKMNGRKQSLGELIGTLNAA-KVPADTEVVCAPPTAYIDFARQKLDP-KIAVAAQNCYKVTNGAFTGEISPG 82
Cdd:PRK00042 1 RKPIIAGNWKMNKTLAEAKALVEELKAAlPDADGVEVAVAPPFTALASVKEALKGsNIKLGAQNVHPEDSGAFTGEISAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 83 MIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNV--KDWSK 160
Cdd:PRK00042 81 MLKDLGVKYVIIGHSERRQYFGETDELVNKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLEAALAGLsaEQFAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 161 VVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDaVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 240
Cdd:PRK00042 161 LVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYGE-VAEKVRILYGGSVKPDNAAELMAQPDIDGALVGGASLKAE 239
|
....*...
gi 4507645 241 -FVDIINA 247
Cdd:PRK00042 240 dFLAIVKA 247
|
|
| PLN02429 |
PLN02429 |
triosephosphate isomerase |
1-247 |
3.88e-99 |
|
triosephosphate isomerase
Pssm-ID: 166070 Cd Length: 315 Bit Score: 291.69 E-value: 3.88e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 1 MAPSRKFFVGGNWKMNGRKQSLGELIGTLNAAKVPADTEVVCAPPTAYIDFARQKLDPKIAVAAQNCYKVTNGAFTGEIS 80
Cdd:PLN02429 60 MAGSGKFFVGGNWKCNGTKDSIAKLISDLNSATLEADVDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEIS 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 81 PGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSK 160
Cdd:PLN02429 140 VEQLKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDN 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 161 VVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLK-P 239
Cdd:PLN02429 220 IVVAYEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKgP 299
|
....*...
gi 4507645 240 EFVDIINA 247
Cdd:PLN02429 300 EFATIVNS 307
|
|
| PRK13962 |
PRK13962 |
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional |
2-247 |
3.30e-83 |
|
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional
Pssm-ID: 237572 [Multi-domain] Cd Length: 645 Bit Score: 260.81 E-value: 3.30e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 2 APSRKFFVGGNWKMNGRKQSLGELIGTLNAAKVPADTEVVCAPPTAYIDFARQKLD-PKIAVAAQNCYKVTNGAFTGEIS 80
Cdd:PRK13962 394 KNPRKPIIAGNWKMNKTPAEAKEFVNELKKYVKDAQAEVVVCPPFTALPSVKEAVDgSNIKLGAQNVFYEEKGAYTGEIS 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 81 PGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTK-----VIADNV 155
Cdd:PRK13962 474 GPMLAEIGVEYVIIGHSERRQYFGETDELVNKKVLAALKAGLTPILCVGETLDERESGITFDVVRLQLKaalngLSAEQV 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 156 KdwsKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGA 235
Cdd:PRK13962 554 K---KVVIAYEPVWAIGTGKVATPEQAQEVHAFIRKLVAELYGEEAARKVRILYGGSVKSENAAGLFNQPDIDGGLVGGA 630
|
250
....*....|...
gi 4507645 236 SLKP-EFVDIINA 247
Cdd:PRK13962 631 SLKAqEFAAIANY 643
|
|
| tim |
TIGR00419 |
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ... |
8-240 |
2.64e-62 |
|
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: 194.25 E-value: 2.64e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 8 FVGGNWKM-NGRKQSLGELIGTLNA-AKVPADTEVVCAPPTAYIDFARQKLdpKIAVAAQNCYKVTNGAFTGEISPGMIK 85
Cdd:TIGR00419 1 LVIGNWKTyNESRGMRALEVAKIAEeVASEAGVAVAVAPPFVDLPMIKREV--EIPVYAQHVDAVLSGAHTGEISAEMLK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 86 DCGATWVVLGHSERRHVfgESDelIGQKVAHALAEGLGVIACIgekldereagiteKVVFEQTKVIAdnvkdWSKVVLAY 165
Cdd:TIGR00419 79 DIGAKGTLINHSERRMK--LAD--IEKKIARLKELGLTSVVCT-------------NNVLTTAAAAA-----LEPDVVAV 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4507645 166 EPVWAIGTGKTATPQQAQEVHEKLRgwlksnVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 240
Cdd:TIGR00419 137 EPPELIGTGIPVSPAQPEVVHGSVR------AVKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
|
|
| PRK14565 |
PRK14565 |
triosephosphate isomerase; Provisional |
7-245 |
1.09e-56 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 237758 Cd Length: 237 Bit Score: 180.72 E-value: 1.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 7 FFVGGNWKMNGRKQSLGELIGTLNA--AKVPADTEVVCAPP----TAYIDfarqkLDPKIAVAAQNCYKVTNGAFTGEIS 80
Cdd:PRK14565 3 FLIVANWKMNGDFSLFSSFLKELSNklANNEITLKLVICPPftamSSFVE-----CNPNIKLGAQNCFYGSSGGYTGEIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 81 PGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKviaDNVKDWSK 160
Cdd:PRK14565 78 AKMLKECGCSYVILGHSERRSTFHETDSDIRLKAESAIESGLIPIICVGETLEDRENGMTKDVLLEQCS---NCLPKHGE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 161 VVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWlkSNVSDavaqstrIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 240
Cdd:PRK14565 155 FIIAYEPVWAIGGSTIPSNDAIAEAFEIIRSY--DSKSH-------IIYGGSVNQENIRDLKSINQLSGVLVGSASLDVD 225
|
....*.
gi 4507645 241 -FVDII 245
Cdd:PRK14565 226 sFCKII 231
|
|
| PRK14905 |
PRK14905 |
triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; ... |
4-233 |
9.40e-41 |
|
triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; Provisional
Pssm-ID: 184898 [Multi-domain] Cd Length: 355 Bit Score: 143.25 E-value: 9.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 4 SRKFFVGGNWKM---NGRK-QSLGELIGTLNAAKVPADTEVVCAPptAYIDF-------ARQKLDPKIAVAAQNCYKVTN 72
Cdd:PRK14905 2 AKKIYFGTNLKMykgNAETvDYLSELLAFAEKFKSDYDIELFVIP--SYIALkdaveaaASETGHPKIKIGAQNMNAKDK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 73 GAFTGEISPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIA 152
Cdd:PRK14905 80 GQFTGEISPLMLKELGIELVMIGHSERRHVLKETDQEENEKVLAALKHGFITLLCIGETLEQKNYNISDEVLRTQLKIGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 153 DNV--KDWSKVVLAYEPVWAIGTGKT-ATPQQAQEVHEKLRGWLKSNVSDAvAQSTRIIYGGSVTGATCKELASQPDVDG 229
Cdd:PRK14905 160 HGVsaEQLPHLFIAYEPVWAIGEGGIpASAEYADEKHAIIKQCLFELFAEE-SKKIPVLYGGSVNLENANELIMKPHIDG 238
|
....
gi 4507645 230 FLVG 233
Cdd:PRK14905 239 LFIG 242
|
|
| PRK15492 |
PRK15492 |
triosephosphate isomerase; Provisional |
4-233 |
2.64e-40 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 185389 Cd Length: 260 Bit Score: 139.36 E-value: 2.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 4 SRKFFVGGNWKM-NGRKQS------LGELIGTLNAAKvpaDTEVVCAPPTAYIDFARQKL-----DPKIAVAAQNCYKVT 71
Cdd:PRK15492 1 MKKIYFGTNLKMyKGIADAtdflakLSELADDIPADK---DIELFVIPSFTAIQDAIAATlaiphDHPIIIGAQNMNPND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 72 NGAFTGEISPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKV- 150
Cdd:PRK15492 78 NGQFTGDISPLMLKEIGTQLVMIGHSERRHKFGETDQEENAKVLAALKHDFTTLLCVGETLEQKNYGISDEILRTQLKIg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 151 -IADNVKDWSKVVLAYEPVWAIGT-GKTATPQQAQEVHEKLRGWLKSNVSDAvAQSTRIIYGGSVTGATCKELASQPDVD 228
Cdd:PRK15492 158 lHGINPDQLAKLRIAYEPVWAIGEaGIPASADYADEKHAVIKQCLIELFGDA-GDDIPVFYGGSVNAENANELFGQPHID 236
|
....*
gi 4507645 229 GFLVG 233
Cdd:PRK15492 237 GLFIG 241
|
|
| PRK04302 |
PRK04302 |
triosephosphate isomerase; Provisional |
31-127 |
2.15e-09 |
|
triosephosphate isomerase; Provisional
Pssm-ID: 235274 Cd Length: 223 Bit Score: 56.03 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4507645 31 AAKVPADTEV--VCAPPTAYIDFARQKLDpkIAVAAQNCYKVTNGAFTGEISPGMIKDCGATWVVLGHSERRHVFGEsde 108
Cdd:PRK04302 28 AEKVSKETGVriAVAPQALDIRRVAEEVD--IPVYAQHVDPVEPGSHTGHILPEAVKDAGAVGTLINHSERRLTLAD--- 102
|
90
....*....|....*....
gi 4507645 109 lIGQKVAHALAEGLGVIAC 127
Cdd:PRK04302 103 -IEAVVERAKKLGLESVVC 120
|
|
| |
