NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|296317286|ref|NP_001171739|]
View 

triosephosphate isomerase 1 [Saccoglossus kowalevskii]

Protein Classification

triose-phosphate isomerase( domain architecture ID 10794370)

triose-phosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate and D-glyceraldehyde-3-phosphate

CATH:  3.20.20.70
EC:  5.3.1.1
Gene Ontology:  GO:0004807|GO:0006096|GO:0031625|GO:0042803
PubMed:  11257493|12206759

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PTZ00333 PTZ00333
triosephosphate isomerase; Provisional
 2-247 3.53e-136

triosephosphate isomerase; Provisional


:

Pssm-ID: 240365  Cd Length: 255  Bit Score: 383.11  E-value: 3.53e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286   2 ASERKFFVGGNWKMNGNKESIDGIVKFLNEGGLNP-NTEVVVAPSPIYLPYVRGKL-NSQIGVAAQNCYKVEKGAFTGEI 79
Cdd:PTZ00333   1 MMKRKPFVGGNWKCNGTKASIKELIDSFNKLKFDPnNVDVVVAPPSLHIPLVQEKLkNKNFKISSQNVSLTGSGAFTGEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286  80 SPAMLKDNGIDWAILGHSERRHVFGESDELIAAKVSHALSCGIKVIACIGEKLDEREAGKTEEVVFRQTKAIKEAVSD-- 157
Cdd:PTZ00333  81 SAEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDea 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286 158 WSKVVLAYEPVWAIGTGKTATPDQAQEVHASLRKYLTDNVSADVAKSVRILYGGSVTPKNCKELAGKPDVDGFLVGGASL 237
Cdd:PTZ00333 161 WDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASL 240

                        250
                 ....*....|
gi 296317286 238 KPDFCEIINA 247
Cdd:PTZ00333 241 KPDFVDIIKS 250
 
Name Accession Description Interval E-value
PTZ00333 PTZ00333
triosephosphate isomerase; Provisional
 2-247 3.53e-136

triosephosphate isomerase; Provisional


Pssm-ID: 240365  Cd Length: 255  Bit Score: 383.11  E-value: 3.53e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286   2 ASERKFFVGGNWKMNGNKESIDGIVKFLNEGGLNP-NTEVVVAPSPIYLPYVRGKL-NSQIGVAAQNCYKVEKGAFTGEI 79
Cdd:PTZ00333   1 MMKRKPFVGGNWKCNGTKASIKELIDSFNKLKFDPnNVDVVVAPPSLHIPLVQEKLkNKNFKISSQNVSLTGSGAFTGEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286  80 SPAMLKDNGIDWAILGHSERRHVFGESDELIAAKVSHALSCGIKVIACIGEKLDEREAGKTEEVVFRQTKAIKEAVSD-- 157
Cdd:PTZ00333  81 SAEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDea 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286 158 WSKVVLAYEPVWAIGTGKTATPDQAQEVHASLRKYLTDNVSADVAKSVRILYGGSVTPKNCKELAGKPDVDGFLVGGASL 237
Cdd:PTZ00333 161 WDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASL 240

                        250
                 ....*....|
gi 296317286 238 KPDFCEIINA 247
Cdd:PTZ00333 241 KPDFVDIIKS 250
TIM cd00311
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ...
 7-246 7.45e-134

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: 376.88  E-value: 7.45e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286   7 FFVGGNWKMNGNKESIDGIVKFLNEGGLNP-NTEVVVAPSPIYLPYVRGKLN-SQIGVAAQNCYKVEKGAFTGEISPAML 84
Cdd:cd00311    1 PLVAGNWKMNGTLAEALELAKALNAVLKDEsGVEVVVAPPFTYLAAVAEALEgSKIKVGAQNVSPEDSGAFTGEISAEML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286  85 KDNGIDWAILGHSERRHVFGESDELIAAKVSHALSCGIKVIACIGEKLDEREAGKTEEVVFRQTKAIKEAVSDWSKVVLA 164
Cdd:cd00311   81 KDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286 165 YEPVWAIGTGKTATPDQAQEVHASLRKYLTDNVSaDVAKSVRILYGGSVTPKNCKELAGKPDVDGFLVGGASLKPD-FCE 243
Cdd:cd00311  161 YEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYG-EVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAEsFLD 239


                 ...
gi 296317286 244 IIN 246
Cdd:cd00311  240 IIK 242
TpiA COG0149
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ...
 5-247 9.56e-130

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: 366.69  E-value: 9.56e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286   5 RKFFVGGNWKMNGNKESIDGIVKFLNEG-GLNPNTEVVVAPSPIYLPYVRGKL-NSQIGVAAQNCYKVEKGAFTGEISPA 82
Cdd:COG0149    2 RKPLIAGNWKMNGTLAEAKALLAALAAAlADLADVEVVVCPPFTYLAAVAEALaGSPIALGAQNVHWEDSGAYTGEISAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286  83 MLKDNGIDWAILGHSERRHVFGESDELIAAKVSHALSCGIKVIACIGEKLDEREAGKTEEVVFRQTKAIKEAVS--DWSK 160
Cdd:COG0149   82 MLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLSaeQAAN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286 161 VVLAYEPVWAIGTGKTATPDQAQEVHASLRKYLTDNVSADVAKSVRILYGGSVTPKNCKELAGKPDVDGFLVGGASLKP- 239
Cdd:COG0149  162 VVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDAe 241


                 ....*...
gi 296317286 240 DFCEIINA 247
Cdd:COG0149  242 DFLAIVRA 249
TIM pfam00121
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ...
 7-247 1.18e-127

Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic enzyme that catalyzes the reversible interconversion of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. TIM plays an important role in several metabolic pathways and is essential for efficient energy production, present in eukaryotes and prokaryotes. TIM is a dimer of identical subunits, each of which is made up of about 250 amino-acid residues. A glutamic acid residue is involved in the catalytic mechanism. The tertiary structure of TIM has eight beta/alpha motifs folded into a barrel structure. The sequence around the active site residue is perfectly conserved in all known TIM's. Deficiencies in TIM are associated with haemolytic anaemia coupled with a progressive, severe neurological disorder.


Pssm-ID: 459680  Cd Length: 244  Bit Score: 361.06  E-value: 1.18e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286    7 FFVGGNWKMNGNKESIDGIVKFLNEGGLN-PNTEVVVAPSPIYLPYVRGKLNSQIGVAAQNCYKVEKGAFTGEISPAMLK 85
Cdd:pfam00121   1 PIIAGNWKMNGTLAEAAELLAELAEALADeSGVEVVVAPPFTYLSAVAELLGSNIKVGAQNVDPEESGAFTGEISAEMLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286   86 DNGIDWAILGHSERRHVFGESDELIAAKVSHALSCGIKVIACIGEKLDEREAGKTEEVVFRQTKAIKEAVSDW-SKVVLA 164
Cdd:pfam00121  81 DLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEqKNLVIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286  165 YEPVWAIGTGKTATPDQAQEVHASLRKYLTDNvSADVAKSVRILYGGSVTPKNCKELAGKPDVDGFLVGGASLKP-DFCE 243
Cdd:pfam00121 161 YEPVWAIGTGKTATPEQAQEVHAFIRAVLAEL-YKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAeDFLD 239


                  ....
gi 296317286  244 IINA 247
Cdd:pfam00121 240 IINA 243
tim TIGR00419
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ...
 8-240 4.28e-61

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: 191.17  E-value: 4.28e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286    8 FVGGNWKM-NGNKESIDGIVKFLNEGGLNPN-TEVVVAPSPIYLPYVRGKLNsqIGVAAQNCYKVEKGAFTGEISPAMLK 85
Cdd:TIGR00419   1 LVIGNWKTyNESRGMRALEVAKIAEEVASEAgVAVAVAPPFVDLPMIKREVE--IPVYAQHVDAVLSGAHTGEISAEMLK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286   86 DNGIDWAILGHSERRHVfgESDelIAAKVSHALSCGIKVIACIgekldereagkteEVVFRQTKAIKeavsdWSKVVLAY 165
Cdd:TIGR00419  79 DIGAKGTLINHSERRMK--LAD--IEKKIARLKELGLTSVVCT-------------NNVLTTAAAAA-----LEPDVVAV 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296317286  166 EPVWAIGTGKTATPDQAQEVHASLRkyltdnVSADVAKSVRILYGGSVTPKNCKELAGKPDVDGFLVGGASLKPD 240
Cdd:TIGR00419 137 EPPELIGTGIPVSPAQPEVVHGSVR------AVKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
 
Name Accession Description Interval E-value
PTZ00333 PTZ00333
triosephosphate isomerase; Provisional
 2-247 3.53e-136

triosephosphate isomerase; Provisional


Pssm-ID: 240365  Cd Length: 255  Bit Score: 383.11  E-value: 3.53e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286   2 ASERKFFVGGNWKMNGNKESIDGIVKFLNEGGLNP-NTEVVVAPSPIYLPYVRGKL-NSQIGVAAQNCYKVEKGAFTGEI 79
Cdd:PTZ00333   1 MMKRKPFVGGNWKCNGTKASIKELIDSFNKLKFDPnNVDVVVAPPSLHIPLVQEKLkNKNFKISSQNVSLTGSGAFTGEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286  80 SPAMLKDNGIDWAILGHSERRHVFGESDELIAAKVSHALSCGIKVIACIGEKLDEREAGKTEEVVFRQTKAIKEAVSD-- 157
Cdd:PTZ00333  81 SAEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDea 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286 158 WSKVVLAYEPVWAIGTGKTATPDQAQEVHASLRKYLTDNVSADVAKSVRILYGGSVTPKNCKELAGKPDVDGFLVGGASL 237
Cdd:PTZ00333 161 WDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASL 240

                        250
                 ....*....|
gi 296317286 238 KPDFCEIINA 247
Cdd:PTZ00333 241 KPDFVDIIKS 250
TIM cd00311
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ...
 7-246 7.45e-134

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: 376.88  E-value: 7.45e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286   7 FFVGGNWKMNGNKESIDGIVKFLNEGGLNP-NTEVVVAPSPIYLPYVRGKLN-SQIGVAAQNCYKVEKGAFTGEISPAML 84
Cdd:cd00311    1 PLVAGNWKMNGTLAEALELAKALNAVLKDEsGVEVVVAPPFTYLAAVAEALEgSKIKVGAQNVSPEDSGAFTGEISAEML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286  85 KDNGIDWAILGHSERRHVFGESDELIAAKVSHALSCGIKVIACIGEKLDEREAGKTEEVVFRQTKAIKEAVSDWSKVVLA 164
Cdd:cd00311   81 KDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286 165 YEPVWAIGTGKTATPDQAQEVHASLRKYLTDNVSaDVAKSVRILYGGSVTPKNCKELAGKPDVDGFLVGGASLKPD-FCE 243
Cdd:cd00311  161 YEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYG-EVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAEsFLD 239


                 ...
gi 296317286 244 IIN 246
Cdd:cd00311  240 IIK 242
TpiA COG0149
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ...
 5-247 9.56e-130

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: 366.69  E-value: 9.56e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286   5 RKFFVGGNWKMNGNKESIDGIVKFLNEG-GLNPNTEVVVAPSPIYLPYVRGKL-NSQIGVAAQNCYKVEKGAFTGEISPA 82
Cdd:COG0149    2 RKPLIAGNWKMNGTLAEAKALLAALAAAlADLADVEVVVCPPFTYLAAVAEALaGSPIALGAQNVHWEDSGAYTGEISAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286  83 MLKDNGIDWAILGHSERRHVFGESDELIAAKVSHALSCGIKVIACIGEKLDEREAGKTEEVVFRQTKAIKEAVS--DWSK 160
Cdd:COG0149   82 MLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLSaeQAAN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286 161 VVLAYEPVWAIGTGKTATPDQAQEVHASLRKYLTDNVSADVAKSVRILYGGSVTPKNCKELAGKPDVDGFLVGGASLKP- 239
Cdd:COG0149  162 VVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDAe 241


                 ....*...
gi 296317286 240 DFCEIINA 247
Cdd:COG0149  242 DFLAIVRA 249
TIM pfam00121
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ...
 7-247 1.18e-127

Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic enzyme that catalyzes the reversible interconversion of glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. TIM plays an important role in several metabolic pathways and is essential for efficient energy production, present in eukaryotes and prokaryotes. TIM is a dimer of identical subunits, each of which is made up of about 250 amino-acid residues. A glutamic acid residue is involved in the catalytic mechanism. The tertiary structure of TIM has eight beta/alpha motifs folded into a barrel structure. The sequence around the active site residue is perfectly conserved in all known TIM's. Deficiencies in TIM are associated with haemolytic anaemia coupled with a progressive, severe neurological disorder.


Pssm-ID: 459680  Cd Length: 244  Bit Score: 361.06  E-value: 1.18e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286    7 FFVGGNWKMNGNKESIDGIVKFLNEGGLN-PNTEVVVAPSPIYLPYVRGKLNSQIGVAAQNCYKVEKGAFTGEISPAMLK 85
Cdd:pfam00121   1 PIIAGNWKMNGTLAEAAELLAELAEALADeSGVEVVVAPPFTYLSAVAELLGSNIKVGAQNVDPEESGAFTGEISAEMLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286   86 DNGIDWAILGHSERRHVFGESDELIAAKVSHALSCGIKVIACIGEKLDEREAGKTEEVVFRQTKAIKEAVSDW-SKVVLA 164
Cdd:pfam00121  81 DLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEqKNLVIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286  165 YEPVWAIGTGKTATPDQAQEVHASLRKYLTDNvSADVAKSVRILYGGSVTPKNCKELAGKPDVDGFLVGGASLKP-DFCE 243
Cdd:pfam00121 161 YEPVWAIGTGKTATPEQAQEVHAFIRAVLAEL-YKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAeDFLD 239


                  ....
gi 296317286  244 IINA 247
Cdd:pfam00121 240 IINA 243
tpiA PRK00042
triosephosphate isomerase; Provisional
 5-247 1.06e-124

triosephosphate isomerase; Provisional


Pssm-ID: 234589  Cd Length: 250  Bit Score: 354.04  E-value: 1.06e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286   5 RKFFVGGNWKMNGNK-ESIDGIVKFLNEGGLNPNTEVVVAPSPIYLPYVRGKL-NSQIGVAAQNCYKVEKGAFTGEISPA 82
Cdd:PRK00042   1 RKPIIAGNWKMNKTLaEAKALVEELKAALPDADGVEVAVAPPFTALASVKEALkGSNIKLGAQNVHPEDSGAFTGEISAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286  83 MLKDNGIDWAILGHSERRHVFGESDELIAAKVSHALSCGIKVIACIGEKLDEREAGKTEEVVFRQTKAIKEAVS--DWSK 160
Cdd:PRK00042  81 MLKDLGVKYVIIGHSERRQYFGETDELVNKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLEAALAGLSaeQFAN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286 161 VVLAYEPVWAIGTGKTATPDQAQEVHASLRKYLTDNVSaDVAKSVRILYGGSVTPKNCKELAGKPDVDGFLVGGASLKP- 239
Cdd:PRK00042 161 LVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYG-EVAEKVRILYGGSVKPDNAAELMAQPDIDGALVGGASLKAe 239


                 ....*...
gi 296317286 240 DFCEIINA 247
Cdd:PRK00042 240 DFLAIVKA 247
PLN02561 PLN02561
triosephosphate isomerase
 5-247 1.28e-124

triosephosphate isomerase


Pssm-ID: 178175  Cd Length: 253  Bit Score: 354.13  E-value: 1.28e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286   5 RKFFVGGNWKMNGNKESIDGIVKFLNEGGLNPN--TEVVVAPSPIYLPYVRGKLNSQIGVAAQNCYKVEKGAFTGEISPA 82
Cdd:PLN02561   3 RKFFVGGNWKCNGTVEEVKKIVTTLNEAEVPSEdvVEVVVSPPFVFLPLVKSLLRPDFQVAAQNCWVKKGGAFTGEISAE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286  83 MLKDNGIDWAILGHSERRHVFGESDELIAAKVSHALSCGIKVIACIGEKLDEREAGKTEEVVFRQTKAIKEAVSDWSKVV 162
Cdd:PLN02561  83 MLVNLGIPWVILGHSERRALLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIADKVSDWANVV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286 163 LAYEPVWAIGTGKTATPDQAQEVHASLRKYLTDNVSADVAKSVRILYGGSVTPKNCKELAGKPDVDGFLVGGASLKPDFC 242
Cdd:PLN02561 163 LAYEPVWAIGTGKVATPAQAQEVHDELRKWLHKNVSPEVAATTRIIYGGSVTGANCKELAAQPDVDGFLVGGASLKPEFI 242


                 ....*
gi 296317286 243 EIINA 247
Cdd:PLN02561 243 DIIKS 247
PRK13962 PRK13962
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional
 2-247 1.37e-91

bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional


Pssm-ID: 237572 [Multi-domain]  Cd Length: 645  Bit Score: 282.77  E-value: 1.37e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286   2 ASERKFFVGGNWKMNGN----KESIDGIVKFLNEGglnpNTEVVVAPSPIYLPYVRGKLN-SQIGVAAQNCYKVEKGAFT 76
Cdd:PRK13962 394 KNPRKPIIAGNWKMNKTpaeaKEFVNELKKYVKDA----QAEVVVCPPFTALPSVKEAVDgSNIKLGAQNVFYEEKGAYT 469

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286  77 GEISPAMLKDNGIDWAILGHSERRHVFGESDELIAAKVSHALSCGIKVIACIGEKLDEREAGKTEEVVFRQTKAIKEAVS 156
Cdd:PRK13962 470 GEISGPMLAEIGVEYVIIGHSERRQYFGETDELVNKKVLAALKAGLTPILCVGETLDERESGITFDVVRLQLKAALNGLS 549

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286 157 --DWSKVVLAYEPVWAIGTGKTATPDQAQEVHASLRKYLTDNVSADVAKSVRILYGGSVTPKNCKELAGKPDVDGFLVGG 234
Cdd:PRK13962 550 aeQVKKVVIAYEPVWAIGTGKVATPEQAQEVHAFIRKLVAELYGEEAARKVRILYGGSVKSENAAGLFNQPDIDGGLVGG 629

                        250
                 ....*....|....
gi 296317286 235 ASLKP-DFCEIINA 247
Cdd:PRK13962 630 ASLKAqEFAAIANY 643
PLN02429 PLN02429
triosephosphate isomerase
 1-247 5.03e-87

triosephosphate isomerase


Pssm-ID: 166070  Cd Length: 315  Bit Score: 260.88  E-value: 5.03e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286   1 MASERKFFVGGNWKMNGNKESIDGIVKFLNEGGLNPNTEVVVAPSPIYLPYVRGKLNSQIGVAAQNCYKVEKGAFTGEIS 80
Cdd:PLN02429  60 MAGSGKFFVGGNWKCNGTKDSIAKLISDLNSATLEADVDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEIS 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286  81 PAMLKDNGIDWAILGHSERRHVFGESDELIAAKVSHALSCGIKVIACIGEKLDEREAGKTEEVVFRQTKAIKEAVSDWSK 160
Cdd:PLN02429 140 VEQLKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDN 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286 161 VVLAYEPVWAIGTGKTATPDQAQEVHASLRKYLTDNVSADVAKSVRILYGGSVTPKNCKELAGKPDVDGFLVGGASLK-P 239
Cdd:PLN02429 220 IVVAYEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKgP 299


                 ....*...
gi 296317286 240 DFCEIINA 247
Cdd:PLN02429 300 EFATIVNS 307
tim TIGR00419
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ...
 8-240 4.28e-61

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: 191.17  E-value: 4.28e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286    8 FVGGNWKM-NGNKESIDGIVKFLNEGGLNPN-TEVVVAPSPIYLPYVRGKLNsqIGVAAQNCYKVEKGAFTGEISPAMLK 85
Cdd:TIGR00419   1 LVIGNWKTyNESRGMRALEVAKIAEEVASEAgVAVAVAPPFVDLPMIKREVE--IPVYAQHVDAVLSGAHTGEISAEMLK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286   86 DNGIDWAILGHSERRHVfgESDelIAAKVSHALSCGIKVIACIgekldereagkteEVVFRQTKAIKeavsdWSKVVLAY 165
Cdd:TIGR00419  79 DIGAKGTLINHSERRMK--LAD--IEKKIARLKELGLTSVVCT-------------NNVLTTAAAAA-----LEPDVVAV 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296317286  166 EPVWAIGTGKTATPDQAQEVHASLRkyltdnVSADVAKSVRILYGGSVTPKNCKELAGKPDVDGFLVGGASLKPD 240
Cdd:TIGR00419 137 EPPELIGTGIPVSPAQPEVVHGSVR------AVKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
PRK14565 PRK14565
triosephosphate isomerase; Provisional
 7-245 3.10e-55

triosephosphate isomerase; Provisional


Pssm-ID: 237758  Cd Length: 237  Bit Score: 177.26  E-value: 3.10e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286   7 FFVGGNWKMNGNKESIDGIVKFLNEGGLN--PNTEVVVAPSPIYLPYVRGkLNSQIGVAAQNCYKVEKGAFTGEISPAML 84
Cdd:PRK14565   3 FLIVANWKMNGDFSLFSSFLKELSNKLANneITLKLVICPPFTAMSSFVE-CNPNIKLGAQNCFYGSSGGYTGEISAKML 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286  85 KDNGIDWAILGHSERRHVFGESDELIAAKVSHALSCGIKVIACIGEKLDEREAGKTEEVVFRQTkaiKEAVSDWSKVVLA 164
Cdd:PRK14565  82 KECGCSYVILGHSERRSTFHETDSDIRLKAESAIESGLIPIICVGETLEDRENGMTKDVLLEQC---SNCLPKHGEFIIA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286 165 YEPVWAIGTGKTATPDQAQEVHASLRKYltDNVSadvaksvRILYGGSVTPKNCKELAGKPDVDGFLVGGASLKPD-FCE 243
Cdd:PRK14565 159 YEPVWAIGGSTIPSNDAIAEAFEIIRSY--DSKS-------HIIYGGSVNQENIRDLKSINQLSGVLVGSASLDVDsFCK 229


                 ..
gi 296317286 244 II 245
Cdd:PRK14565 230 II 231
PRK14905 PRK14905
triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; ...
 3-233 6.35e-46

triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; Provisional


Pssm-ID: 184898 [Multi-domain]  Cd Length: 355  Bit Score: 156.73  E-value: 6.35e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286   3 SERKFFVGGNWKM-NGNKESIDGIVKFLN---EGGLNPNTEVVVAPSPIYLPYVRGKLNSQIG-----VAAQNCYKVEKG 73
Cdd:PRK14905   1 MAKKIYFGTNLKMyKGNAETVDYLSELLAfaeKFKSDYDIELFVIPSYIALKDAVEAAASETGhpkikIGAQNMNAKDKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286  74 AFTGEISPAMLKDNGIDWAILGHSERRHVFGESDELIAAKVSHALSCGIKVIACIGEKLDEREAGKTEEVVFRQTKAIKE 153
Cdd:PRK14905  81 QFTGEISPLMLKELGIELVMIGHSERRHVLKETDQEENEKVLAALKHGFITLLCIGETLEQKNYNISDEVLRTQLKIGLH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286 154 AVS--DWSKVVLAYEPVWAIGTGKT-ATPDQAQEVHASLRKYLTDnVSADVAKSVRILYGGSVTPKNCKELAGKPDVDGF 230
Cdd:PRK14905 161 GVSaeQLPHLFIAYEPVWAIGEGGIpASAEYADEKHAIIKQCLFE-LFAEESKKIPVLYGGSVNLENANELIMKPHIDGL 239


                 ...
gi 296317286 231 LVG 233
Cdd:PRK14905 240 FIG 242
PRK15492 PRK15492
triosephosphate isomerase; Provisional
 5-240 6.54e-45

triosephosphate isomerase; Provisional


Pssm-ID: 185389  Cd Length: 260  Bit Score: 151.30  E-value: 6.54e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286   5 RKFFVGGNWKM-NGNKESIDGIVKfLNEGG----LNPNTEVVVAPSPIYLPYVRGKLNS-----QIGVAAQNCYKVEKGA 74
Cdd:PRK15492   2 KKIYFGTNLKMyKGIADATDFLAK-LSELAddipADKDIELFVIPSFTAIQDAIAATLAiphdhPIIIGAQNMNPNDNGQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286  75 FTGEISPAMLKDNGIDWAILGHSERRHVFGESDELIAAKVSHALSCGIKVIACIGEKLDEREAGKTEEVVFRQTKAIKEA 154
Cdd:PRK15492  81 FTGDISPLMLKEIGTQLVMIGHSERRHKFGETDQEENAKVLAALKHDFTTLLCVGETLEQKNYGISDEILRTQLKIGLHG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286 155 VS--DWSKVVLAYEPVWAIGT-GKTATPDQAQEVHASLRKYLTDnVSADVAKSVRILYGGSVTPKNCKELAGKPDVDGFL 231
Cdd:PRK15492 161 INpdQLAKLRIAYEPVWAIGEaGIPASADYADEKHAVIKQCLIE-LFGDAGDDIPVFYGGSVNAENANELFGQPHIDGLF 239


                 ....*....
gi 296317286 232 VGGASLKPD 240
Cdd:PRK15492 240 IGRSAWDAD 248
PRK04302 PRK04302
triosephosphate isomerase; Provisional
 37-240 1.01e-09

triosephosphate isomerase; Provisional


Pssm-ID: 235274  Cd Length: 223  Bit Score: 56.80  E-value: 1.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286  37 NTEVVVAPSPIYLPYVRGKLNsqIGVAAQNCYKVEKGAFTGEISPAMLKDNGIDWAILGHSERRHVFGEsdelIAAKVSH 116
Cdd:PRK04302  36 GVRIAVAPQALDIRRVAEEVD--IPVYAQHVDPVEPGSHTGHILPEAVKDAGAVGTLINHSERRLTLAD----IEAVVER 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296317286 117 ALSCGIKVIACigekldereagkTEEVvfRQTKAIKEAVSDWskvvLAYEPVWAIGTGK---TATPDqaqevhaslrkYL 193
Cdd:PRK04302 110 AKKLGLESVVC------------VNNP--ETSAAAAALGPDY----VAVEPPELIGTGIpvsKAKPE-----------VV 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 296317286 194 TDNVSA--DVAKSVRILYGGSVTPKNCKELAGKPDVDGFLVGGASLKPD 240
Cdd:PRK04302 161 EDAVEAvkKVNPDVKVLCGAGISTGEDVKAALELGADGVLLASGVVKAK 209
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH