NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|74271820|ref|NP_001028244|]
View 

triosephosphate isomerase [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
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 2.64e-133

triosephosphate isomerase; Provisional


:

Pssm-ID: 240365  Cd Length: 255  Bit Score: 376.18  E-value: 2.64e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820    2 APSRKFFVGGNWKMNGKKKCLGELICTLNAAKM-PADTEVVCAPPTAYIDFARQKLD-PKIAVAAQNCYKVTNGAFTGEI 79
Cdd:PTZ00333   1 MMKRKPFVGGNWKCNGTKASIKELIDSFNKLKFdPNNVDVVVAPPSLHIPLVQEKLKnKNFKISSQNVSLTGSGAFTGEI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820   80 SPGMIKDLGATWVVLGHSERRHVFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITDKVVFEQTKAIADNVKD-- 157
Cdd:PTZ00333  81 SAEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDea 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820  158 WSKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKCNVSEEVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASL 237
Cdd:PTZ00333 161 WDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASL 240
                        250
                 ....*....|
gi 74271820  238 KPEFVDIINA 247
Cdd:PTZ00333 241 KPDFVDIIKS 250
 
Name Accession Description Interval E-value
PTZ00333 PTZ00333
triosephosphate isomerase; Provisional
2-247 2.64e-133

triosephosphate isomerase; Provisional


Pssm-ID: 240365  Cd Length: 255  Bit Score: 376.18  E-value: 2.64e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820    2 APSRKFFVGGNWKMNGKKKCLGELICTLNAAKM-PADTEVVCAPPTAYIDFARQKLD-PKIAVAAQNCYKVTNGAFTGEI 79
Cdd:PTZ00333   1 MMKRKPFVGGNWKCNGTKASIKELIDSFNKLKFdPNNVDVVVAPPSLHIPLVQEKLKnKNFKISSQNVSLTGSGAFTGEI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820   80 SPGMIKDLGATWVVLGHSERRHVFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITDKVVFEQTKAIADNVKD-- 157
Cdd:PTZ00333  81 SAEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDea 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820  158 WSKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKCNVSEEVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASL 237
Cdd:PTZ00333 161 WDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASL 240
                        250
                 ....*....|
gi 74271820  238 KPEFVDIINA 247
Cdd:PTZ00333 241 KPDFVDIIKS 250
TIM cd00311
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ...
7-246 3.09e-126

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: 357.62  E-value: 3.09e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820   7 FFVGGNWKMNGKKKCLGELICTLNAA-KMPADTEVVCAPPTAYIDFARQKL-DPKIAVAAQNCYKVTNGAFTGEISPGMI 84
Cdd:cd00311   1 PLVAGNWKMNGTLAEALELAKALNAVlKDESGVEVVVAPPFTYLAAVAEALeGSKIKVGAQNVSPEDSGAFTGEISAEML 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820  85 KDLGATWVVLGHSERRHVFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITDKVVFEQTKAIADNVKDWSKVVLA 164
Cdd:cd00311  81 KDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVIA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820 165 YEPVWAIGTGKTATPQQAQEVHEKLRGWLKCNVSeEVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE-FVD 243
Cdd:cd00311 161 YEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYG-EVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAEsFLD 239

                ...
gi 74271820 244 IIN 246
Cdd:cd00311 240 IIK 242
TpiA COG0149
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ...
5-247 4.78e-118

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: 337.03  E-value: 4.78e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820   5 RKFFVGGNWKMNGKKKCLGELICTL-NAAKMPADTEVVCAPPTAYIDFARQKL-DPKIAVAAQNCYKVTNGAFTGEISPG 82
Cdd:COG0149   2 RKPLIAGNWKMNGTLAEAKALLAALaAALADLADVEVVVCPPFTYLAAVAEALaGSPIALGAQNVHWEDSGAYTGEISAA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820  83 MIKDLGATWVVLGHSERRHVFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITDKVVFEQTKAIADNV--KDWSK 160
Cdd:COG0149  82 MLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLsaEQAAN 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820 161 VVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKCNVSEEVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 240
Cdd:COG0149 162 VVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDAE 241

                ....*...
gi 74271820 241 -FVDIINA 247
Cdd:COG0149 242 dFLAIVRA 249
TIM pfam00121
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ...
7-247 1.04e-117

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


Pssm-ID: 459680  Cd Length: 244  Bit Score: 336.02  E-value: 1.04e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820     7 FFVGGNWKMNGKKKCLGELICTLNAAKMPA-DTEVVCAPPTAYIDFARQKLDPKIAVAAQNCYKVTNGAFTGEISPGMIK 85
Cdd:pfam00121   1 PIIAGNWKMNGTLAEAAELLAELAEALADEsGVEVVVAPPFTYLSAVAELLGSNIKVGAQNVDPEESGAFTGEISAEMLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820    86 DLGATWVVLGHSERRHVFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITDKVVFEQTKAIADNVKDW-SKVVLA 164
Cdd:pfam00121  81 DLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEqKNLVIA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820   165 YEPVWAIGTGKTATPQQAQEVHEKLRGWLKcNVSEEVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE-FVD 243
Cdd:pfam00121 161 YEPVWAIGTGKTATPEQAQEVHAFIRAVLA-ELYKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEdFLD 239

                  ....
gi 74271820   244 IINA 247
Cdd:pfam00121 240 IINA 243
tim TIGR00419
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ...
8-240 7.32e-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: 195.41  E-value: 7.32e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820     8 FVGGNWKM-NGKKKCLGELICTLNA-AKMPADTEVVCAPPTAYIDFARQKLdpKIAVAAQNCYKVTNGAFTGEISPGMIK 85
Cdd:TIGR00419   1 LVIGNWKTyNESRGMRALEVAKIAEeVASEAGVAVAVAPPFVDLPMIKREV--EIPVYAQHVDAVLSGAHTGEISAEMLK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820    86 DLGATWVVLGHSERRHVfgESDelIGQKVNHALSEGLGVIACIgekldereagitdKVVFEQTKAIAdnvkdWSKVVLAY 165
Cdd:TIGR00419  79 DIGAKGTLINHSERRMK--LAD--IEKKIARLKELGLTSVVCT-------------NNVLTTAAAAA-----LEPDVVAV 136
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74271820   166 EPVWAIGTGKTATPQQAQEVHEKLRgwlkcnVSEEVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 240
Cdd:TIGR00419 137 EPPELIGTGIPVSPAQPEVVHGSVR------AVKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
 
Name Accession Description Interval E-value
PTZ00333 PTZ00333
triosephosphate isomerase; Provisional
2-247 2.64e-133

triosephosphate isomerase; Provisional


Pssm-ID: 240365  Cd Length: 255  Bit Score: 376.18  E-value: 2.64e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820    2 APSRKFFVGGNWKMNGKKKCLGELICTLNAAKM-PADTEVVCAPPTAYIDFARQKLD-PKIAVAAQNCYKVTNGAFTGEI 79
Cdd:PTZ00333   1 MMKRKPFVGGNWKCNGTKASIKELIDSFNKLKFdPNNVDVVVAPPSLHIPLVQEKLKnKNFKISSQNVSLTGSGAFTGEI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820   80 SPGMIKDLGATWVVLGHSERRHVFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITDKVVFEQTKAIADNVKD-- 157
Cdd:PTZ00333  81 SAEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDea 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820  158 WSKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKCNVSEEVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASL 237
Cdd:PTZ00333 161 WDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASL 240
                        250
                 ....*....|
gi 74271820  238 KPEFVDIINA 247
Cdd:PTZ00333 241 KPDFVDIIKS 250
PLN02561 PLN02561
triosephosphate isomerase
4-247 2.57e-126

triosephosphate isomerase


Pssm-ID: 178175  Cd Length: 253  Bit Score: 358.37  E-value: 2.57e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820    4 SRKFFVGGNWKMNGKKKCLGELICTLNAAKMPA--DTEVVCAPPTAYIDFARQKLDPKIAVAAQNCYKVTNGAFTGEISP 81
Cdd:PLN02561   2 ARKFFVGGNWKCNGTVEEVKKIVTTLNEAEVPSedVVEVVVSPPFVFLPLVKSLLRPDFQVAAQNCWVKKGGAFTGEISA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820   82 GMIKDLGATWVVLGHSERRHVFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITDKVVFEQTKAIADNVKDWSKV 161
Cdd:PLN02561  82 EMLVNLGIPWVILGHSERRALLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIADKVSDWANV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820  162 VLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKCNVSEEVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPEF 241
Cdd:PLN02561 162 VLAYEPVWAIGTGKVATPAQAQEVHDELRKWLHKNVSPEVAATTRIIYGGSVTGANCKELAAQPDVDGFLVGGASLKPEF 241

                 ....*.
gi 74271820  242 VDIINA 247
Cdd:PLN02561 242 IDIIKS 247
TIM cd00311
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ...
7-246 3.09e-126

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: 357.62  E-value: 3.09e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820   7 FFVGGNWKMNGKKKCLGELICTLNAA-KMPADTEVVCAPPTAYIDFARQKL-DPKIAVAAQNCYKVTNGAFTGEISPGMI 84
Cdd:cd00311   1 PLVAGNWKMNGTLAEALELAKALNAVlKDESGVEVVVAPPFTYLAAVAEALeGSKIKVGAQNVSPEDSGAFTGEISAEML 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820  85 KDLGATWVVLGHSERRHVFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITDKVVFEQTKAIADNVKDWSKVVLA 164
Cdd:cd00311  81 KDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVIA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820 165 YEPVWAIGTGKTATPQQAQEVHEKLRGWLKCNVSeEVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE-FVD 243
Cdd:cd00311 161 YEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYG-EVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAEsFLD 239

                ...
gi 74271820 244 IIN 246
Cdd:cd00311 240 IIK 242
TpiA COG0149
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ...
5-247 4.78e-118

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: 337.03  E-value: 4.78e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820   5 RKFFVGGNWKMNGKKKCLGELICTL-NAAKMPADTEVVCAPPTAYIDFARQKL-DPKIAVAAQNCYKVTNGAFTGEISPG 82
Cdd:COG0149   2 RKPLIAGNWKMNGTLAEAKALLAALaAALADLADVEVVVCPPFTYLAAVAEALaGSPIALGAQNVHWEDSGAYTGEISAA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820  83 MIKDLGATWVVLGHSERRHVFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITDKVVFEQTKAIADNV--KDWSK 160
Cdd:COG0149  82 MLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLsaEQAAN 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820 161 VVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKCNVSEEVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 240
Cdd:COG0149 162 VVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDAE 241

                ....*...
gi 74271820 241 -FVDIINA 247
Cdd:COG0149 242 dFLAIVRA 249
TIM pfam00121
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ...
7-247 1.04e-117

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


Pssm-ID: 459680  Cd Length: 244  Bit Score: 336.02  E-value: 1.04e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820     7 FFVGGNWKMNGKKKCLGELICTLNAAKMPA-DTEVVCAPPTAYIDFARQKLDPKIAVAAQNCYKVTNGAFTGEISPGMIK 85
Cdd:pfam00121   1 PIIAGNWKMNGTLAEAAELLAELAEALADEsGVEVVVAPPFTYLSAVAELLGSNIKVGAQNVDPEESGAFTGEISAEMLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820    86 DLGATWVVLGHSERRHVFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITDKVVFEQTKAIADNVKDW-SKVVLA 164
Cdd:pfam00121  81 DLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEqKNLVIA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820   165 YEPVWAIGTGKTATPQQAQEVHEKLRGWLKcNVSEEVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE-FVD 243
Cdd:pfam00121 161 YEPVWAIGTGKTATPEQAQEVHAFIRAVLA-ELYKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEdFLD 239

                  ....
gi 74271820   244 IINA 247
Cdd:pfam00121 240 IINA 243
tpiA PRK00042
triosephosphate isomerase; Provisional
5-247 8.90e-112

triosephosphate isomerase; Provisional


Pssm-ID: 234589  Cd Length: 250  Bit Score: 321.30  E-value: 8.90e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820    5 RKFFVGGNWKMNGKKKCLGELICTLNAA-KMPADTEVVCAPPTAYIDFARQKLDP-KIAVAAQNCYKVTNGAFTGEISPG 82
Cdd:PRK00042   1 RKPIIAGNWKMNKTLAEAKALVEELKAAlPDADGVEVAVAPPFTALASVKEALKGsNIKLGAQNVHPEDSGAFTGEISAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820   83 MIKDLGATWVVLGHSERRHVFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITDKVVFEQTKAIADNV--KDWSK 160
Cdd:PRK00042  81 MLKDLGVKYVIIGHSERRQYFGETDELVNKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLEAALAGLsaEQFAN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820  161 VVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKCNVSeEVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 240
Cdd:PRK00042 161 LVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYG-EVAEKVRILYGGSVKPDNAAELMAQPDIDGALVGGASLKAE 239

                 ....*...
gi 74271820  241 -FVDIINA 247
Cdd:PRK00042 240 dFLAIVKA 247
PLN02429 PLN02429
triosephosphate isomerase
1-247 2.45e-102

triosephosphate isomerase


Pssm-ID: 166070  Cd Length: 315  Bit Score: 299.78  E-value: 2.45e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820    1 MAPSRKFFVGGNWKMNGKKKCLGELICTLNAAKMPADTEVVCAPPTAYIDFARQKLDPKIAVAAQNCYKVTNGAFTGEIS 80
Cdd:PLN02429  60 MAGSGKFFVGGNWKCNGTKDSIAKLISDLNSATLEADVDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEIS 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820   81 PGMIKDLGATWVVLGHSERRHVFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITDKVVFEQTKAIADNVKDWSK 160
Cdd:PLN02429 140 VEQLKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDN 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820  161 VVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKCNVSEEVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASLK-P 239
Cdd:PLN02429 220 IVVAYEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKgP 299

                 ....*...
gi 74271820  240 EFVDIINA 247
Cdd:PLN02429 300 EFATIVNS 307
PRK13962 PRK13962
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional
2-247 1.25e-84

bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional


Pssm-ID: 237572 [Multi-domain]  Cd Length: 645  Bit Score: 264.67  E-value: 1.25e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820    2 APSRKFFVGGNWKMNGKKKCLGELICTLNAAKMPADTEVVCAPPTAYIDFARQKLD-PKIAVAAQNCYKVTNGAFTGEIS 80
Cdd:PRK13962 394 KNPRKPIIAGNWKMNKTPAEAKEFVNELKKYVKDAQAEVVVCPPFTALPSVKEAVDgSNIKLGAQNVFYEEKGAYTGEIS 473
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820   81 PGMIKDLGATWVVLGHSERRHVFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITDKVVFEQTKAIADNV--KDW 158
Cdd:PRK13962 474 GPMLAEIGVEYVIIGHSERRQYFGETDELVNKKVLAALKAGLTPILCVGETLDERESGITFDVVRLQLKAALNGLsaEQV 553
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820  159 SKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKCNVSEEVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASLK 238
Cdd:PRK13962 554 KKVVIAYEPVWAIGTGKVATPEQAQEVHAFIRKLVAELYGEEAARKVRILYGGSVKSENAAGLFNQPDIDGGLVGGASLK 633
                        250
                 ....*....|
gi 74271820  239 P-EFVDIINA 247
Cdd:PRK13962 634 AqEFAAIANY 643
tim TIGR00419
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ...
8-240 7.32e-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: 195.41  E-value: 7.32e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820     8 FVGGNWKM-NGKKKCLGELICTLNA-AKMPADTEVVCAPPTAYIDFARQKLdpKIAVAAQNCYKVTNGAFTGEISPGMIK 85
Cdd:TIGR00419   1 LVIGNWKTyNESRGMRALEVAKIAEeVASEAGVAVAVAPPFVDLPMIKREV--EIPVYAQHVDAVLSGAHTGEISAEMLK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820    86 DLGATWVVLGHSERRHVfgESDelIGQKVNHALSEGLGVIACIgekldereagitdKVVFEQTKAIAdnvkdWSKVVLAY 165
Cdd:TIGR00419  79 DIGAKGTLINHSERRMK--LAD--IEKKIARLKELGLTSVVCT-------------NNVLTTAAAAA-----LEPDVVAV 136
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74271820   166 EPVWAIGTGKTATPQQAQEVHEKLRgwlkcnVSEEVAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 240
Cdd:TIGR00419 137 EPPELIGTGIPVSPAQPEVVHGSVR------AVKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
PRK14565 PRK14565
triosephosphate isomerase; Provisional
7-245 6.66e-53

triosephosphate isomerase; Provisional


Pssm-ID: 237758  Cd Length: 237  Bit Score: 171.09  E-value: 6.66e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820    7 FFVGGNWKMNGKKKCLGELICTLNA--AKMPADTEVVCAPP----TAYIDfarqkLDPKIAVAAQNCYKVTNGAFTGEIS 80
Cdd:PRK14565   3 FLIVANWKMNGDFSLFSSFLKELSNklANNEITLKLVICPPftamSSFVE-----CNPNIKLGAQNCFYGSSGGYTGEIS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820   81 PGMIKDLGATWVVLGHSERRHVFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITDKVVFEQTKaiaDNVKDWSK 160
Cdd:PRK14565  78 AKMLKECGCSYVILGHSERRSTFHETDSDIRLKAESAIESGLIPIICVGETLEDRENGMTKDVLLEQCS---NCLPKHGE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820  161 VVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWlkcnvseevAQCTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 240
Cdd:PRK14565 155 FIIAYEPVWAIGGSTIPSNDAIAEAFEIIRSY---------DSKSHIIYGGSVNQENIRDLKSINQLSGVLVGSASLDVD 225

                 ....*.
gi 74271820  241 -FVDII 245
Cdd:PRK14565 226 sFCKII 231
PRK14905 PRK14905
triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; ...
4-233 3.53e-42

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


Pssm-ID: 184898 [Multi-domain]  Cd Length: 355  Bit Score: 147.10  E-value: 3.53e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820    4 SRKFFVGGNWKMNgKKKC-----LGELICTLNAAKMPADTEVVCAPptAYIDF-------ARQKLDPKIAVAAQNCYKVT 71
Cdd:PRK14905   2 AKKIYFGTNLKMY-KGNAetvdyLSELLAFAEKFKSDYDIELFVIP--SYIALkdaveaaASETGHPKIKIGAQNMNAKD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820   72 NGAFTGEISPGMIKDLGATWVVLGHSERRHVFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITDKVVFEQTKAI 151
Cdd:PRK14905  79 KGQFTGEISPLMLKELGIELVMIGHSERRHVLKETDQEENEKVLAALKHGFITLLCIGETLEQKNYNISDEVLRTQLKIG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820  152 ADNV--KDWSKVVLAYEPVWAIGTGKT-ATPQQAQEVHEKLRGWLKCNVSEEVAQCTrIIYGGSVTGATCKELASQPDVD 228
Cdd:PRK14905 159 LHGVsaEQLPHLFIAYEPVWAIGEGGIpASAEYADEKHAIIKQCLFELFAEESKKIP-VLYGGSVNLENANELIMKPHID 237

                 ....*
gi 74271820  229 GFLVG 233
Cdd:PRK14905 238 GLFIG 242
PRK15492 PRK15492
triosephosphate isomerase; Provisional
4-233 2.17e-39

triosephosphate isomerase; Provisional


Pssm-ID: 185389  Cd Length: 260  Bit Score: 137.05  E-value: 2.17e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820    4 SRKFFVGGNWKM-NGKKKC------LGELICTLNAAKmpaDTEVVCAPPTAYIDFARQKL-----DPKIAVAAQNCYKVT 71
Cdd:PRK15492   1 MKKIYFGTNLKMyKGIADAtdflakLSELADDIPADK---DIELFVIPSFTAIQDAIAATlaiphDHPIIIGAQNMNPND 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820   72 NGAFTGEISPGMIKDLGATWVVLGHSERRHVFGESDELIGQKVNHALSEGLGVIACIGEKLDEREAGITDKVVFEQTKA- 150
Cdd:PRK15492  78 NGQFTGDISPLMLKEIGTQLVMIGHSERRHKFGETDQEENAKVLAALKHDFTTLLCVGETLEQKNYGISDEILRTQLKIg 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820  151 -IADNVKDWSKVVLAYEPVWAIGT-GKTATPQQAQEVHEKLRGWLkCNVSEEVAQCTRIIYGGSVTGATCKELASQPDVD 228
Cdd:PRK15492 158 lHGINPDQLAKLRIAYEPVWAIGEaGIPASADYADEKHAVIKQCL-IELFGDAGDDIPVFYGGSVNAENANELFGQPHID 236

                 ....*
gi 74271820  229 GFLVG 233
Cdd:PRK15492 237 GLFIG 241
PRK04302 PRK04302
triosephosphate isomerase; Provisional
37-174 1.72e-09

triosephosphate isomerase; Provisional


Pssm-ID: 235274  Cd Length: 223  Bit Score: 56.03  E-value: 1.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271820   37 DTEVVCAPPTAYIDFARQKLDpkIAVAAQNCYKVTNGAFTGEISPGMIKDLGATWVVLGHSERRHVFGEsdelIGQKVNH 116
Cdd:PRK04302  36 GVRIAVAPQALDIRRVAEEVD--IPVYAQHVDPVEPGSHTGHILPEAVKDAGAVGTLINHSERRLTLAD----IEAVVER 109
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 74271820  117 ALSEGLGVIACigekldereagiTDKVvfEQTKAIADNVKDWskvvLAYEPVWAIGTG 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH