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Conserved domains on  [gi|1958729382|ref|XP_038952175|]
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triosephosphate isomerase-like [Rattus norvegicus]

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
 2-247 1.19e-133

triosephosphate isomerase; Provisional


:

Pssm-ID: 240365  Cd Length: 255  Bit Score: 376.95  E-value: 1.19e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382   2 APSRKFFVGGNWKMNGRKKCLGELICTLNAAKM-PADTEVVCAPPTAYIDFARQKLD-PKIAVAAQNCYKVTNGAFTGEI 79
Cdd:PTZ00333    1 MMKRKPFVGGNWKCNGTKASIKELIDSFNKLKFdPNNVDVVVAPPSLHIPLVQEKLKnKNFKISSQNVSLTGSGAFTGEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382  80 SPGMIKDLGATWVVLGHSERRHIFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITEKVVFEQTKAIADNVKD-- 157
Cdd:PTZ00333   81 SAEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDea 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382 158 WSKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKCNVSEGVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASL 237
Cdd:PTZ00333  161 WDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASL 240

                         250
                  ....*....|
gi 1958729382 238 KPEFLDIINA 247
Cdd:PTZ00333  241 KPDFVDIIKS 250
 
Name Accession Description Interval E-value
PTZ00333 PTZ00333
triosephosphate isomerase; Provisional
 2-247 1.19e-133

triosephosphate isomerase; Provisional


Pssm-ID: 240365  Cd Length: 255  Bit Score: 376.95  E-value: 1.19e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382   2 APSRKFFVGGNWKMNGRKKCLGELICTLNAAKM-PADTEVVCAPPTAYIDFARQKLD-PKIAVAAQNCYKVTNGAFTGEI 79
Cdd:PTZ00333    1 MMKRKPFVGGNWKCNGTKASIKELIDSFNKLKFdPNNVDVVVAPPSLHIPLVQEKLKnKNFKISSQNVSLTGSGAFTGEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382  80 SPGMIKDLGATWVVLGHSERRHIFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITEKVVFEQTKAIADNVKD-- 157
Cdd:PTZ00333   81 SAEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDea 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382 158 WSKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKCNVSEGVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASL 237
Cdd:PTZ00333  161 WDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASL 240

                         250
                  ....*....|
gi 1958729382 238 KPEFLDIINA 247
Cdd:PTZ00333  241 KPDFVDIIKS 250
TIM cd00311
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ...
 7-246 1.38e-127

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: 361.08  E-value: 1.38e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382   7 FFVGGNWKMNGRKKCLGELICTLNAA-KMPADTEVVCAPPTAYIDFARQKL-DPKIAVAAQNCYKVTNGAFTGEISPGMI 84
Cdd:cd00311     1 PLVAGNWKMNGTLAEALELAKALNAVlKDESGVEVVVAPPFTYLAAVAEALeGSKIKVGAQNVSPEDSGAFTGEISAEML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382  85 KDLGATWVVLGHSERRHIFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITEKVVFEQTKAIADNVKDWSKVVLA 164
Cdd:cd00311    81 KDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382 165 YEPVWAIGTGKTATPQQAQEVHEKLRGWLKCNVSEgVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE-FLD 243
Cdd:cd00311   161 YEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYGE-VAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAEsFLD 239


                  ...
gi 1958729382 244 IIN 246
Cdd:cd00311   240 IIK 242
TpiA COG0149
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ...
 5-247 2.51e-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: 340.50  E-value: 2.51e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382   5 RKFFVGGNWKMNGRKKCLGELICTL-NAAKMPADTEVVCAPPTAYIDFARQKL-DPKIAVAAQNCYKVTNGAFTGEISPG 82
Cdd:COG0149     2 RKPLIAGNWKMNGTLAEAKALLAALaAALADLADVEVVVCPPFTYLAAVAEALaGSPIALGAQNVHWEDSGAYTGEISAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382  83 MIKDLGATWVVLGHSERRHIFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITEKVVFEQTKAIADNV--KDWSK 160
Cdd:COG0149    82 MLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLsaEQAAN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382 161 VVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKCNVSEGVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 240
Cdd:COG0149   162 VVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDAE 241


                  ....*...
gi 1958729382 241 -FLDIINA 247
Cdd:COG0149   242 dFLAIVRA 249
TIM pfam00121
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ...
 7-247 4.43e-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: 339.49  E-value: 4.43e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382   7 FFVGGNWKMNGRKKCLGELICTLNAAKMPA-DTEVVCAPPTAYIDFARQKLDPKIAVAAQNCYKVTNGAFTGEISPGMIK 85
Cdd:pfam00121   1 PIIAGNWKMNGTLAEAAELLAELAEALADEsGVEVVVAPPFTYLSAVAELLGSNIKVGAQNVDPEESGAFTGEISAEMLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382  86 DLGATWVVLGHSERRHIFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITEKVVFEQTKAIADNVKDW-SKVVLA 164
Cdd:pfam00121  81 DLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEqKNLVIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382 165 YEPVWAIGTGKTATPQQAQEVHEKLRGWLKcNVSEGVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE-FLD 243
Cdd:pfam00121 161 YEPVWAIGTGKTATPEQAQEVHAFIRAVLA-ELYKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEdFLD 239


                  ....
gi 1958729382 244 IINA 247
Cdd:pfam00121 240 IINA 243
tim TIGR00419
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ...
 8-240 4.55e-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: 193.48  E-value: 4.55e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382   8 FVGGNWKM-NGRKKCLGELICTLNA-AKMPADTEVVCAPPTAYIDFARQKLdpKIAVAAQNCYKVTNGAFTGEISPGMIK 85
Cdd:TIGR00419   1 LVIGNWKTyNESRGMRALEVAKIAEeVASEAGVAVAVAPPFVDLPMIKREV--EIPVYAQHVDAVLSGAHTGEISAEMLK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382  86 DLGATWVVLGHSERRHIfgESDelIGQKVNHALSEGLGVIACIgekldereagiteKVVFEQTKAIAdnvkdWSKVVLAY 165
Cdd:TIGR00419  79 DIGAKGTLINHSERRMK--LAD--IEKKIARLKELGLTSVVCT-------------NNVLTTAAAAA-----LEPDVVAV 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958729382 166 EPVWAIGTGKTATPQQAQEVHEKLRgwlkcnVSEGVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 240
Cdd:TIGR00419 137 EPPELIGTGIPVSPAQPEVVHGSVR------AVKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
 
Name Accession Description Interval E-value
PTZ00333 PTZ00333
triosephosphate isomerase; Provisional
 2-247 1.19e-133

triosephosphate isomerase; Provisional


Pssm-ID: 240365  Cd Length: 255  Bit Score: 376.95  E-value: 1.19e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382   2 APSRKFFVGGNWKMNGRKKCLGELICTLNAAKM-PADTEVVCAPPTAYIDFARQKLD-PKIAVAAQNCYKVTNGAFTGEI 79
Cdd:PTZ00333    1 MMKRKPFVGGNWKCNGTKASIKELIDSFNKLKFdPNNVDVVVAPPSLHIPLVQEKLKnKNFKISSQNVSLTGSGAFTGEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382  80 SPGMIKDLGATWVVLGHSERRHIFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITEKVVFEQTKAIADNVKD-- 157
Cdd:PTZ00333   81 SAEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDea 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382 158 WSKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKCNVSEGVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASL 237
Cdd:PTZ00333  161 WDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASL 240

                         250
                  ....*....|
gi 1958729382 238 KPEFLDIINA 247
Cdd:PTZ00333  241 KPDFVDIIKS 250
TIM cd00311
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ...
 7-246 1.38e-127

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: 361.08  E-value: 1.38e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382   7 FFVGGNWKMNGRKKCLGELICTLNAA-KMPADTEVVCAPPTAYIDFARQKL-DPKIAVAAQNCYKVTNGAFTGEISPGMI 84
Cdd:cd00311     1 PLVAGNWKMNGTLAEALELAKALNAVlKDESGVEVVVAPPFTYLAAVAEALeGSKIKVGAQNVSPEDSGAFTGEISAEML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382  85 KDLGATWVVLGHSERRHIFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITEKVVFEQTKAIADNVKDWSKVVLA 164
Cdd:cd00311    81 KDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382 165 YEPVWAIGTGKTATPQQAQEVHEKLRGWLKCNVSEgVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE-FLD 243
Cdd:cd00311   161 YEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYGE-VAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAEsFLD 239


                  ...
gi 1958729382 244 IIN 246
Cdd:cd00311   240 IIK 242
PLN02561 PLN02561
triosephosphate isomerase
 4-247 1.19e-125

triosephosphate isomerase


Pssm-ID: 178175  Cd Length: 253  Bit Score: 356.44  E-value: 1.19e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382   4 SRKFFVGGNWKMNGRKKCLGELICTLNAAKMPA--DTEVVCAPPTAYIDFARQKLDPKIAVAAQNCYKVTNGAFTGEISP 81
Cdd:PLN02561    2 ARKFFVGGNWKCNGTVEEVKKIVTTLNEAEVPSedVVEVVVSPPFVFLPLVKSLLRPDFQVAAQNCWVKKGGAFTGEISA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382  82 GMIKDLGATWVVLGHSERRHIFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITEKVVFEQTKAIADNVKDWSKV 161
Cdd:PLN02561   82 EMLVNLGIPWVILGHSERRALLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIADKVSDWANV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382 162 VLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKCNVSEGVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPEF 241
Cdd:PLN02561  162 VLAYEPVWAIGTGKVATPAQAQEVHDELRKWLHKNVSPEVAATTRIIYGGSVTGANCKELAAQPDVDGFLVGGASLKPEF 241


                  ....*.
gi 1958729382 242 LDIINA 247
Cdd:PLN02561  242 IDIIKS 247
TpiA COG0149
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ...
 5-247 2.51e-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: 340.50  E-value: 2.51e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382   5 RKFFVGGNWKMNGRKKCLGELICTL-NAAKMPADTEVVCAPPTAYIDFARQKL-DPKIAVAAQNCYKVTNGAFTGEISPG 82
Cdd:COG0149     2 RKPLIAGNWKMNGTLAEAKALLAALaAALADLADVEVVVCPPFTYLAAVAEALaGSPIALGAQNVHWEDSGAYTGEISAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382  83 MIKDLGATWVVLGHSERRHIFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITEKVVFEQTKAIADNV--KDWSK 160
Cdd:COG0149    82 MLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLsaEQAAN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382 161 VVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKCNVSEGVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 240
Cdd:COG0149   162 VVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDAE 241


                  ....*...
gi 1958729382 241 -FLDIINA 247
Cdd:COG0149   242 dFLAIVRA 249
TIM pfam00121
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ...
 7-247 4.43e-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: 339.49  E-value: 4.43e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382   7 FFVGGNWKMNGRKKCLGELICTLNAAKMPA-DTEVVCAPPTAYIDFARQKLDPKIAVAAQNCYKVTNGAFTGEISPGMIK 85
Cdd:pfam00121   1 PIIAGNWKMNGTLAEAAELLAELAEALADEsGVEVVVAPPFTYLSAVAELLGSNIKVGAQNVDPEESGAFTGEISAEMLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382  86 DLGATWVVLGHSERRHIFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITEKVVFEQTKAIADNVKDW-SKVVLA 164
Cdd:pfam00121  81 DLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEqKNLVIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382 165 YEPVWAIGTGKTATPQQAQEVHEKLRGWLKcNVSEGVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE-FLD 243
Cdd:pfam00121 161 YEPVWAIGTGKTATPEQAQEVHAFIRAVLA-ELYKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEdFLD 239


                  ....
gi 1958729382 244 IINA 247
Cdd:pfam00121 240 IINA 243
tpiA PRK00042
triosephosphate isomerase; Provisional
 5-247 5.99e-114

triosephosphate isomerase; Provisional


Pssm-ID: 234589  Cd Length: 250  Bit Score: 326.69  E-value: 5.99e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382   5 RKFFVGGNWKMNGRKKCLGELICTLNAA-KMPADTEVVCAPPTAYIDFARQKLDP-KIAVAAQNCYKVTNGAFTGEISPG 82
Cdd:PRK00042    1 RKPIIAGNWKMNKTLAEAKALVEELKAAlPDADGVEVAVAPPFTALASVKEALKGsNIKLGAQNVHPEDSGAFTGEISAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382  83 MIKDLGATWVVLGHSERRHIFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITEKVVFEQTKAIADNV--KDWSK 160
Cdd:PRK00042   81 MLKDLGVKYVIIGHSERRQYFGETDELVNKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLEAALAGLsaEQFAN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382 161 VVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKCNVSEgVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 240
Cdd:PRK00042  161 LVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYGE-VAEKVRILYGGSVKPDNAAELMAQPDIDGALVGGASLKAE 239


                  ....*...
gi 1958729382 241 -FLDIINA 247
Cdd:PRK00042  240 dFLAIVKA 247
PLN02429 PLN02429
triosephosphate isomerase
 1-247 5.27e-101

triosephosphate isomerase


Pssm-ID: 166070  Cd Length: 315  Bit Score: 296.70  E-value: 5.27e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382   1 MAPSRKFFVGGNWKMNGRKKCLGELICTLNAAKMPADTEVVCAPPTAYIDFARQKLDPKIAVAAQNCYKVTNGAFTGEIS 80
Cdd:PLN02429   60 MAGSGKFFVGGNWKCNGTKDSIAKLISDLNSATLEADVDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEIS 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382  81 PGMIKDLGATWVVLGHSERRHIFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITEKVVFEQTKAIADNVKDWSK 160
Cdd:PLN02429  140 VEQLKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDN 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382 161 VVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKCNVSEGVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASLK-P 239
Cdd:PLN02429  220 IVVAYEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKgP 299


                  ....*...
gi 1958729382 240 EFLDIINA 247
Cdd:PLN02429  300 EFATIVNS 307
PRK13962 PRK13962
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional
 2-245 3.71e-83

bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional


Pssm-ID: 237572 [Multi-domain]  Cd Length: 645  Bit Score: 260.81  E-value: 3.71e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382   2 APSRKFFVGGNWKMNGRKKCLGELICTLNAAKMPADTEVVCAPPTAYIDFARQKLD-PKIAVAAQNCYKVTNGAFTGEIS 80
Cdd:PRK13962  394 KNPRKPIIAGNWKMNKTPAEAKEFVNELKKYVKDAQAEVVVCPPFTALPSVKEAVDgSNIKLGAQNVFYEEKGAYTGEIS 473

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382  81 PGMIKDLGATWVVLGHSERRHIFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITEKVVFEQTKAIADNV--KDW 158
Cdd:PRK13962  474 GPMLAEIGVEYVIIGHSERRQYFGETDELVNKKVLAALKAGLTPILCVGETLDERESGITFDVVRLQLKAALNGLsaEQV 553

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382 159 SKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKCNVSEGVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASLK 238
Cdd:PRK13962  554 KKVVIAYEPVWAIGTGKVATPEQAQEVHAFIRKLVAELYGEEAARKVRILYGGSVKSENAAGLFNQPDIDGGLVGGASLK 633


                  ....*..
gi 1958729382 239 PEFLDII 245
Cdd:PRK13962  634 AQEFAAI 640
tim TIGR00419
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ...
 8-240 4.55e-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: 193.48  E-value: 4.55e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382   8 FVGGNWKM-NGRKKCLGELICTLNA-AKMPADTEVVCAPPTAYIDFARQKLdpKIAVAAQNCYKVTNGAFTGEISPGMIK 85
Cdd:TIGR00419   1 LVIGNWKTyNESRGMRALEVAKIAEeVASEAGVAVAVAPPFVDLPMIKREV--EIPVYAQHVDAVLSGAHTGEISAEMLK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382  86 DLGATWVVLGHSERRHIfgESDelIGQKVNHALSEGLGVIACIgekldereagiteKVVFEQTKAIAdnvkdWSKVVLAY 165
Cdd:TIGR00419  79 DIGAKGTLINHSERRMK--LAD--IEKKIARLKELGLTSVVCT-------------NNVLTTAAAAA-----LEPDVVAV 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958729382 166 EPVWAIGTGKTATPQQAQEVHEKLRgwlkcnVSEGVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 240
Cdd:TIGR00419 137 EPPELIGTGIPVSPAQPEVVHGSVR------AVKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
PRK14565 PRK14565
triosephosphate isomerase; Provisional
 7-245 2.74e-53

triosephosphate isomerase; Provisional


Pssm-ID: 237758  Cd Length: 237  Bit Score: 172.25  E-value: 2.74e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382   7 FFVGGNWKMNGRKKCLGELICTLNA--AKMPADTEVVCAPP----TAYIDfarqkLDPKIAVAAQNCYKVTNGAFTGEIS 80
Cdd:PRK14565    3 FLIVANWKMNGDFSLFSSFLKELSNklANNEITLKLVICPPftamSSFVE-----CNPNIKLGAQNCFYGSSGGYTGEIS 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382  81 PGMIKDLGATWVVLGHSERRHIFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITEKVVFEQTKaiaDNVKDWSK 160
Cdd:PRK14565   78 AKMLKECGCSYVILGHSERRSTFHETDSDIRLKAESAIESGLIPIICVGETLEDRENGMTKDVLLEQCS---NCLPKHGE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382 161 VVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWlkcnvsegvAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 240
Cdd:PRK14565  155 FIIAYEPVWAIGGSTIPSNDAIAEAFEIIRSY---------DSKSHIIYGGSVNQENIRDLKSINQLSGVLVGSASLDVD 225


                  ....*.
gi 1958729382 241 -FLDII 245
Cdd:PRK14565  226 sFCKII 231
PRK14905 PRK14905
triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; ...
 4-233 1.97e-39

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


Pssm-ID: 184898 [Multi-domain]  Cd Length: 355  Bit Score: 139.78  E-value: 1.97e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382   4 SRKFFVGGNWKMNgRKKC-----LGELICTLNAAKMPADTEVVCAPptAYIDF-------ARQKLDPKIAVAAQNCYKVT 71
Cdd:PRK14905    2 AKKIYFGTNLKMY-KGNAetvdyLSELLAFAEKFKSDYDIELFVIP--SYIALkdaveaaASETGHPKIKIGAQNMNAKD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382  72 NGAFTGEISPGMIKDLGATWVVLGHSERRHIFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITEKVVFEQTKAI 151
Cdd:PRK14905   79 KGQFTGEISPLMLKELGIELVMIGHSERRHVLKETDQEENEKVLAALKHGFITLLCIGETLEQKNYNISDEVLRTQLKIG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382 152 ADNV--KDWSKVVLAYEPVWAIGTGktATPQQAQEVHEKLRGWLKCnVSEGVAQCTR---IIYGGSVTGATCKELASQPD 226
Cdd:PRK14905  159 LHGVsaEQLPHLFIAYEPVWAIGEG--GIPASAEYADEKHAIIKQC-LFELFAEESKkipVLYGGSVNLENANELIMKPH 235


                  ....*..
gi 1958729382 227 VDGFLVG 233
Cdd:PRK14905  236 IDGLFIG 242
PRK15492 PRK15492
triosephosphate isomerase; Provisional
 4-233 2.17e-37

triosephosphate isomerase; Provisional


Pssm-ID: 185389  Cd Length: 260  Bit Score: 132.04  E-value: 2.17e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382   4 SRKFFVGGNWKM-NGRKKC------LGELICTLNAAKmpaDTEVVCAPPTAYIDFARQKL-----DPKIAVAAQNCYKVT 71
Cdd:PRK15492    1 MKKIYFGTNLKMyKGIADAtdflakLSELADDIPADK---DIELFVIPSFTAIQDAIAATlaiphDHPIIIGAQNMNPND 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382  72 NGAFTGEISPGMIKDLGATWVVLGHSERRHIFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITEKVVFEQTKA- 150
Cdd:PRK15492   78 NGQFTGDISPLMLKEIGTQLVMIGHSERRHKFGETDQEENAKVLAALKHDFTTLLCVGETLEQKNYGISDEILRTQLKIg 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382 151 -IADNVKDWSKVVLAYEPVWAIGT-GKTATPQQAQEVHEKLRgwlKCNVS----EGvaQCTRIIYGGSVTGATCKELASQ 224
Cdd:PRK15492  158 lHGINPDQLAKLRIAYEPVWAIGEaGIPASADYADEKHAVIK---QCLIElfgdAG--DDIPVFYGGSVNAENANELFGQ 232


                  ....*....
gi 1958729382 225 PDVDGFLVG 233
Cdd:PRK15492  233 PHIDGLFIG 241
PRK04302 PRK04302
triosephosphate isomerase; Provisional
 37-174 1.92e-09

triosephosphate isomerase; Provisional


Pssm-ID: 235274  Cd Length: 223  Bit Score: 56.03  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958729382  37 DTEVVCAPPTAYIDFARQKLDpkIAVAAQNCYKVTNGAFTGEISPGMIKDLGATWVVLGHSERRHIFGEsdelIGQKVNH 116
Cdd:PRK04302   36 GVRIAVAPQALDIRRVAEEVD--IPVYAQHVDPVEPGSHTGHILPEAVKDAGAVGTLINHSERRLTLAD----IEAVVER 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958729382 117 ALSEGLGVIACigekldereagiTEKVvfEQTKAIADNVKDWskvvLAYEPVWAIGTG 174
Cdd:PRK04302  110 AKKLGLESVVC------------VNNP--ETSAAAAALGPDY----VAVEPPELIGTG 149
 
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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