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Conserved domains on  [gi|1246174916|ref|XP_022433164|]
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triosephosphate isomerase [Delphinapterus leucas]

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

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List of domain hits

 Name Accession Description Interval E-value
PTZ00333 PTZ00333
triosephosphate isomerase; Provisional
 39-284 1.21e-134

triosephosphate isomerase; Provisional


:

Pssm-ID: 240365  Cd Length: 255  Bit Score: 380.80  E-value: 1.21e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916  39 APSRKFFVGGNWKMNGRKNNLGELINTLNAAKV-PADTEVVCAPPTAYIDFARQKLDHK-IAVAAQNCYKVANGAFTGEI 116
Cdd:PTZ00333    1 MMKRKPFVGGNWKCNGTKASIKELIDSFNKLKFdPNNVDVVVAPPSLHIPLVQEKLKNKnFKISSQNVSLTGSGAFTGEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 117 SPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKD-- 194
Cdd:PTZ00333   81 SAEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDea 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 195 WGKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNISDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASL 274
Cdd:PTZ00333  161 WDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASL 240

                         250
                  ....*....|
gi 1246174916 275 KPEFVDIINA 284
Cdd:PTZ00333  241 KPDFVDIIKS 250
 
Name Accession Description Interval E-value
PTZ00333 PTZ00333
triosephosphate isomerase; Provisional
 39-284 1.21e-134

triosephosphate isomerase; Provisional


Pssm-ID: 240365  Cd Length: 255  Bit Score: 380.80  E-value: 1.21e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916  39 APSRKFFVGGNWKMNGRKNNLGELINTLNAAKV-PADTEVVCAPPTAYIDFARQKLDHK-IAVAAQNCYKVANGAFTGEI 116
Cdd:PTZ00333    1 MMKRKPFVGGNWKCNGTKASIKELIDSFNKLKFdPNNVDVVVAPPSLHIPLVQEKLKNKnFKISSQNVSLTGSGAFTGEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 117 SPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKD-- 194
Cdd:PTZ00333   81 SAEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDea 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 195 WGKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNISDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASL 274
Cdd:PTZ00333  161 WDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASL 240

                         250
                  ....*....|
gi 1246174916 275 KPEFVDIINA 284
Cdd:PTZ00333  241 KPDFVDIIKS 250
TIM cd00311
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ...
 44-283 2.00e-128

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: 364.55  E-value: 2.00e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916  44 FFVGGNWKMNGRKNNLGELINTLNAA-KVPADTEVVCAPPTAYIDFARQKLDH-KIAVAAQNCYKVANGAFTGEISPGMI 121
Cdd:cd00311     1 PLVAGNWKMNGTLAEALELAKALNAVlKDESGVEVVVAPPFTYLAAVAEALEGsKIKVGAQNVSPEDSGAFTGEISAEML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 122 KDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWGKVVLA 201
Cdd:cd00311    81 KDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 202 YEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNISDaVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE-FVD 280
Cdd:cd00311   161 YEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYGE-VAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAEsFLD 239


                  ...
gi 1246174916 281 IIN 283
Cdd:cd00311   240 IIK 242
TpiA COG0149
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ...
 42-284 7.08e-119

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: 340.88  E-value: 7.08e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916  42 RKFFVGGNWKMNGRKNNLGELINTL-NAAKVPADTEVVCAPPTAYIDFARQKL-DHKIAVAAQNCYKVANGAFTGEISPG 119
Cdd:COG0149     2 RKPLIAGNWKMNGTLAEAKALLAALaAALADLADVEVVVCPPFTYLAAVAEALaGSPIALGAQNVHWEDSGAYTGEISAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 120 MIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTK-VIAD-NVKDWGK 197
Cdd:COG0149    82 MLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKaALAGlSAEQAAN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 198 VVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNISDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 277
Cdd:COG0149   162 VVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDAE 241


                  ....*...
gi 1246174916 278 -FVDIINA 284
Cdd:COG0149   242 dFLAIVRA 249
TIM pfam00121
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ...
 44-284 2.41e-118

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: 339.10  E-value: 2.41e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916  44 FFVGGNWKMNGRKNNLGELINTLNAAKVPA-DTEVVCAPPTAYIDFARQKLDHKIAVAAQNCYKVANGAFTGEISPGMIK 122
Cdd:pfam00121   1 PIIAGNWKMNGTLAEAAELLAELAEALADEsGVEVVVAPPFTYLSAVAELLGSNIKVGAQNVDPEESGAFTGEISAEMLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 123 DCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWG-KVVLA 201
Cdd:pfam00121  81 DLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQkNLVIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 202 YEPVWAIGTGKTATPQQAQEVHEKLRGWLkSNISDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE-FVD 280
Cdd:pfam00121 161 YEPVWAIGTGKTATPEQAQEVHAFIRAVL-AELYKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEdFLD 239


                  ....
gi 1246174916 281 IINA 284
Cdd:pfam00121 240 IINA 243
tim TIGR00419
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ...
 45-277 5.73e-63

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: 197.33  E-value: 5.73e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916  45 FVGGNWKM-NGRKNNLGELINTLNA-AKVPADTEVVCAPPTAYIDFARQKLdhKIAVAAQNCYKVANGAFTGEISPGMIK 122
Cdd:TIGR00419   1 LVIGNWKTyNESRGMRALEVAKIAEeVASEAGVAVAVAPPFVDLPMIKREV--EIPVYAQHVDAVLSGAHTGEISAEMLK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 123 DCGATWVVLGHSERRHVfgESDelIGQKVAHALAEGLGVIACIgekldereagiteKVVFEQTKVIAdnvkdWGKVVLAY 202
Cdd:TIGR00419  79 DIGAKGTLINHSERRMK--LAD--IEKKIARLKELGLTSVVCT-------------NNVLTTAAAAA-----LEPDVVAV 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246174916 203 EPVWAIGTGKTATPQQAQEVHEKLRgwlksnISDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 277
Cdd:TIGR00419 137 EPPELIGTGIPVSPAQPEVVHGSVR------AVKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
 
Name Accession Description Interval E-value
PTZ00333 PTZ00333
triosephosphate isomerase; Provisional
 39-284 1.21e-134

triosephosphate isomerase; Provisional


Pssm-ID: 240365  Cd Length: 255  Bit Score: 380.80  E-value: 1.21e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916  39 APSRKFFVGGNWKMNGRKNNLGELINTLNAAKV-PADTEVVCAPPTAYIDFARQKLDHK-IAVAAQNCYKVANGAFTGEI 116
Cdd:PTZ00333    1 MMKRKPFVGGNWKCNGTKASIKELIDSFNKLKFdPNNVDVVVAPPSLHIPLVQEKLKNKnFKISSQNVSLTGSGAFTGEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 117 SPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKD-- 194
Cdd:PTZ00333   81 SAEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDea 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 195 WGKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNISDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASL 274
Cdd:PTZ00333  161 WDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASL 240

                         250
                  ....*....|
gi 1246174916 275 KPEFVDIINA 284
Cdd:PTZ00333  241 KPDFVDIIKS 250
TIM cd00311
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ...
 44-283 2.00e-128

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: 364.55  E-value: 2.00e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916  44 FFVGGNWKMNGRKNNLGELINTLNAA-KVPADTEVVCAPPTAYIDFARQKLDH-KIAVAAQNCYKVANGAFTGEISPGMI 121
Cdd:cd00311     1 PLVAGNWKMNGTLAEALELAKALNAVlKDESGVEVVVAPPFTYLAAVAEALEGsKIKVGAQNVSPEDSGAFTGEISAEML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 122 KDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWGKVVLA 201
Cdd:cd00311    81 KDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 202 YEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNISDaVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE-FVD 280
Cdd:cd00311   161 YEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYGE-VAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAEsFLD 239


                  ...
gi 1246174916 281 IIN 283
Cdd:cd00311   240 IIK 242
PLN02561 PLN02561
triosephosphate isomerase
 41-284 1.73e-122

triosephosphate isomerase


Pssm-ID: 178175  Cd Length: 253  Bit Score: 350.28  E-value: 1.73e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916  41 SRKFFVGGNWKMNGRKNNLGELINTLNAAKVPA--DTEVVCAPPTAYIDFARQKLDHKIAVAAQNCYKVANGAFTGEISP 118
Cdd:PLN02561    2 ARKFFVGGNWKCNGTVEEVKKIVTTLNEAEVPSedVVEVVVSPPFVFLPLVKSLLRPDFQVAAQNCWVKKGGAFTGEISA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 119 GMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWGKV 198
Cdd:PLN02561   82 EMLVNLGIPWVILGHSERRALLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIADKVSDWANV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 199 VLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNISDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPEF 278
Cdd:PLN02561  162 VLAYEPVWAIGTGKVATPAQAQEVHDELRKWLHKNVSPEVAATTRIIYGGSVTGANCKELAAQPDVDGFLVGGASLKPEF 241


                  ....*.
gi 1246174916 279 VDIINA 284
Cdd:PLN02561  242 IDIIKS 247
TpiA COG0149
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ...
 42-284 7.08e-119

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: 340.88  E-value: 7.08e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916  42 RKFFVGGNWKMNGRKNNLGELINTL-NAAKVPADTEVVCAPPTAYIDFARQKL-DHKIAVAAQNCYKVANGAFTGEISPG 119
Cdd:COG0149     2 RKPLIAGNWKMNGTLAEAKALLAALaAALADLADVEVVVCPPFTYLAAVAEALaGSPIALGAQNVHWEDSGAYTGEISAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 120 MIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTK-VIAD-NVKDWGK 197
Cdd:COG0149    82 MLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKaALAGlSAEQAAN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 198 VVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNISDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 277
Cdd:COG0149   162 VVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDAE 241


                  ....*...
gi 1246174916 278 -FVDIINA 284
Cdd:COG0149   242 dFLAIVRA 249
TIM pfam00121
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ...
 44-284 2.41e-118

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: 339.10  E-value: 2.41e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916  44 FFVGGNWKMNGRKNNLGELINTLNAAKVPA-DTEVVCAPPTAYIDFARQKLDHKIAVAAQNCYKVANGAFTGEISPGMIK 122
Cdd:pfam00121   1 PIIAGNWKMNGTLAEAAELLAELAEALADEsGVEVVVAPPFTYLSAVAELLGSNIKVGAQNVDPEESGAFTGEISAEMLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 123 DCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWG-KVVLA 201
Cdd:pfam00121  81 DLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQkNLVIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 202 YEPVWAIGTGKTATPQQAQEVHEKLRGWLkSNISDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE-FVD 280
Cdd:pfam00121 161 YEPVWAIGTGKTATPEQAQEVHAFIRAVL-AELYKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEdFLD 239


                  ....
gi 1246174916 281 IINA 284
Cdd:pfam00121 240 IINA 243
tpiA PRK00042
triosephosphate isomerase; Provisional
 42-284 6.67e-114

triosephosphate isomerase; Provisional


Pssm-ID: 234589  Cd Length: 250  Bit Score: 328.23  E-value: 6.67e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916  42 RKFFVGGNWKMNGRKNNLGELINTLNAA-KVPADTEVVCAPPTAYIDFARQKLD-HKIAVAAQNCYKVANGAFTGEISPG 119
Cdd:PRK00042    1 RKPIIAGNWKMNKTLAEAKALVEELKAAlPDADGVEVAVAPPFTALASVKEALKgSNIKLGAQNVHPEDSGAFTGEISAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 120 MIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNV--KDWGK 197
Cdd:PRK00042   81 MLKDLGVKYVIIGHSERRQYFGETDELVNKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLEAALAGLsaEQFAN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 198 VVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNISDaVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 277
Cdd:PRK00042  161 LVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYGE-VAEKVRILYGGSVKPDNAAELMAQPDIDGALVGGASLKAE 239


                  ....*...
gi 1246174916 278 -FVDIINA 284
Cdd:PRK00042  240 dFLAIVKA 247
PLN02429 PLN02429
triosephosphate isomerase
 34-284 3.25e-100

triosephosphate isomerase


Pssm-ID: 166070  Cd Length: 315  Bit Score: 295.93  E-value: 3.25e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916  34 GFSAMAPSRKFFVGGNWKMNGRKNNLGELINTLNAAKVPADTEVVCAPPTAYIDFARQKLDHKIAVAAQNCYKVANGAFT 113
Cdd:PLN02429   56 GVVAMAGSGKFFVGGNWKCNGTKDSIAKLISDLNSATLEADVDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFT 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 114 GEISPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVK 193
Cdd:PLN02429  136 GEISVEQLKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVP 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 194 DWGKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNISDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGAS 273
Cdd:PLN02429  216 SWDNIVVAYEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGAS 295

                         250
                  ....*....|..
gi 1246174916 274 LK-PEFVDIINA 284
Cdd:PLN02429  296 LKgPEFATIVNS 307
PRK13962 PRK13962
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional
 30-284 3.12e-84

bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional


Pssm-ID: 237572 [Multi-domain]  Cd Length: 645  Bit Score: 265.05  E-value: 3.12e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916  30 LQCAGFSAMapsRKFFVGGNWKMNGRKNNLGELINTLNAAKVPADTEVVCAPPTAYIDFARQKLDH-KIAVAAQNCYKVA 108
Cdd:PRK13962  388 IACLLDKNP---RKPIIAGNWKMNKTPAEAKEFVNELKKYVKDAQAEVVVCPPFTALPSVKEAVDGsNIKLGAQNVFYEE 464

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 109 NGAFTGEISPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTK-- 186
Cdd:PRK13962  465 KGAYTGEISGPMLAEIGVEYVIIGHSERRQYFGETDELVNKKVLAALKAGLTPILCVGETLDERESGITFDVVRLQLKaa 544

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 187 ---VIADNVKdwgKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNISDAVAQSTRIIYGGSVTGATCKELASQPD 263
Cdd:PRK13962  545 lngLSAEQVK---KVVIAYEPVWAIGTGKVATPEQAQEVHAFIRKLVAELYGEEAARKVRILYGGSVKSENAAGLFNQPD 621

                         250       260
                  ....*....|....*....|..
gi 1246174916 264 VDGFLVGGASLKP-EFVDIINA 284
Cdd:PRK13962  622 IDGGLVGGASLKAqEFAAIANY 643
tim TIGR00419
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ...
 45-277 5.73e-63

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: 197.33  E-value: 5.73e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916  45 FVGGNWKM-NGRKNNLGELINTLNA-AKVPADTEVVCAPPTAYIDFARQKLdhKIAVAAQNCYKVANGAFTGEISPGMIK 122
Cdd:TIGR00419   1 LVIGNWKTyNESRGMRALEVAKIAEeVASEAGVAVAVAPPFVDLPMIKREV--EIPVYAQHVDAVLSGAHTGEISAEMLK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 123 DCGATWVVLGHSERRHVfgESDelIGQKVAHALAEGLGVIACIgekldereagiteKVVFEQTKVIAdnvkdWGKVVLAY 202
Cdd:TIGR00419  79 DIGAKGTLINHSERRMK--LAD--IEKKIARLKELGLTSVVCT-------------NNVLTTAAAAA-----LEPDVVAV 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1246174916 203 EPVWAIGTGKTATPQQAQEVHEKLRgwlksnISDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 277
Cdd:TIGR00419 137 EPPELIGTGIPVSPAQPEVVHGSVR------AVKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
PRK14565 PRK14565
triosephosphate isomerase; Provisional
 44-282 1.10e-55

triosephosphate isomerase; Provisional


Pssm-ID: 237758  Cd Length: 237  Bit Score: 179.57  E-value: 1.10e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916  44 FFVGGNWKMNGRKNNLGELINTLNA--AKVPADTEVVCAPP----TAYIDfarqkLDHKIAVAAQNCYKVANGAFTGEIS 117
Cdd:PRK14565    3 FLIVANWKMNGDFSLFSSFLKELSNklANNEITLKLVICPPftamSSFVE-----CNPNIKLGAQNCFYGSSGGYTGEIS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 118 PGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKviaDNVKDWGK 197
Cdd:PRK14565   78 AKMLKECGCSYVILGHSERRSTFHETDSDIRLKAESAIESGLIPIICVGETLEDRENGMTKDVLLEQCS---NCLPKHGE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 198 VVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWlksnisdavAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 277
Cdd:PRK14565  155 FIIAYEPVWAIGGSTIPSNDAIAEAFEIIRSY---------DSKSHIIYGGSVNQENIRDLKSINQLSGVLVGSASLDVD 225


                  ....*.
gi 1246174916 278 -FVDII 282
Cdd:PRK14565  226 sFCKII 231
PRK15492 PRK15492
triosephosphate isomerase; Provisional
 41-270 7.73e-41

triosephosphate isomerase; Provisional


Pssm-ID: 185389  Cd Length: 260  Bit Score: 142.05  E-value: 7.73e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916  41 SRKFFVGGNWKMngRKNN---------LGELINTLNAAKvpaDTEVVCAPPTAYIDFARQKL-----DHKIAVAAQNCYK 106
Cdd:PRK15492    1 MKKIYFGTNLKM--YKGIadatdflakLSELADDIPADK---DIELFVIPSFTAIQDAIAATlaiphDHPIIIGAQNMNP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 107 VANGAFTGEISPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTK 186
Cdd:PRK15492   76 NDNGQFTGDISPLMLKEIGTQLVMIGHSERRHKFGETDQEENAKVLAALKHDFTTLLCVGETLEQKNYGISDEILRTQLK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 187 V--IADNVKDWGKVVLAYEPVWAIGT-GKTATPQQAQEVHEKLRGWLKSNISDAvAQSTRIIYGGSVTGATCKELASQPD 263
Cdd:PRK15492  156 IglHGINPDQLAKLRIAYEPVWAIGEaGIPASADYADEKHAVIKQCLIELFGDA-GDDIPVFYGGSVNAENANELFGQPH 234


                  ....*..
gi 1246174916 264 VDGFLVG 270
Cdd:PRK15492  235 IDGLFIG 241
PRK14905 PRK14905
triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; ...
 41-270 3.71e-39

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


Pssm-ID: 184898 [Multi-domain]  Cd Length: 355  Bit Score: 140.17  E-value: 3.71e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916  41 SRKFFVGGNWKMngRKNN------LGELINTLNAAKVPADTEVVCAPptAYI------DFARQKLDH-KIAVAAQNCYKV 107
Cdd:PRK14905    2 AKKIYFGTNLKM--YKGNaetvdyLSELLAFAEKFKSDYDIELFVIP--SYIalkdavEAAASETGHpKIKIGAQNMNAK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 108 ANGAFTGEISPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKV 187
Cdd:PRK14905   78 DKGQFTGEISPLMLKELGIELVMIGHSERRHVLKETDQEENEKVLAALKHGFITLLCIGETLEQKNYNISDEVLRTQLKI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916 188 IADNV--KDWGKVVLAYEPVWAIGTGKT-ATPQQAQEVHEKLRGWLKSNISDAvAQSTRIIYGGSVTGATCKELASQPDV 264
Cdd:PRK14905  158 GLHGVsaEQLPHLFIAYEPVWAIGEGGIpASAEYADEKHAIIKQCLFELFAEE-SKKIPVLYGGSVNLENANELIMKPHI 236


                  ....*.
gi 1246174916 265 DGFLVG 270
Cdd:PRK14905  237 DGLFIG 242
PRK04302 PRK04302
triosephosphate isomerase; Provisional
 68-164 4.26e-09

triosephosphate isomerase; Provisional


Pssm-ID: 235274  Cd Length: 223  Bit Score: 55.64  E-value: 4.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246174916  68 AAKVPADTEV--VCAPPTAYIDFARQKLDhkIAVAAQNCYKVANGAFTGEISPGMIKDCGATWVVLGHSERRHVFGEsde 145
Cdd:PRK04302   28 AEKVSKETGVriAVAPQALDIRRVAEEVD--IPVYAQHVDPVEPGSHTGHILPEAVKDAGAVGTLINHSERRLTLAD--- 102

                          90
                  ....*....|....*....
gi 1246174916 146 lIGQKVAHALAEGLGVIAC 164
Cdd:PRK04302  103 -IEAVVERAKKLGLESVVC 120
 
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.
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