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Conserved domains on  [gi|1351275|sp|P48499|]
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RecName: Full=Triosephosphate isomerase; Short=TIM; AltName: Full=Triose-phosphate isomerase

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

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List of domain hits

Name Accession Description Interval E-value
PTZ00333 PTZ00333
triosephosphate isomerase; Provisional
2-250 4.62e-145

triosephosphate isomerase; Provisional


:

Pssm-ID: 240365  Cd Length: 255  Bit Score: 405.84  E-value: 4.62e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275     2 SAKPQPIAAANWKCNGTTASIEKLVQVFNEHTIS-HDVQCVVAPTFVHIPLVQAKLRNPKYVISAENAI-AKSGAFTGEV 79
Cdd:PTZ00333   1 MMKRKPFVGGNWKCNGTKASIKELIDSFNKLKFDpNNVDVVVAPPSLHIPLVQEKLKNKNFKISSQNVSlTGSGAFTGEI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275    80 SMPILKDIGVHWVILGHSERRTYYGETDEIVAQKVSEACKQGFMVIACIGETLQQREANQTAKVVLSQTSAIAAKLTKDA 159
Cdd:PTZ00333  81 SAEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDEA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275   160 WNQVVLAYEPVWAIGTGKVATPEQAQEVHLLLRKWVSENIGTDVAAKLRILYGGSVNAANAATLYAKPDINGFLVGGASL 239
Cdd:PTZ00333 161 WDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASL 240
                        250
                 ....*....|.
gi 1351275   240 KPEFRDIIDAT 250
Cdd:PTZ00333 241 KPDFVDIIKSA 251
 
Name Accession Description Interval E-value
PTZ00333 PTZ00333
triosephosphate isomerase; Provisional
2-250 4.62e-145

triosephosphate isomerase; Provisional


Pssm-ID: 240365  Cd Length: 255  Bit Score: 405.84  E-value: 4.62e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275     2 SAKPQPIAAANWKCNGTTASIEKLVQVFNEHTIS-HDVQCVVAPTFVHIPLVQAKLRNPKYVISAENAI-AKSGAFTGEV 79
Cdd:PTZ00333   1 MMKRKPFVGGNWKCNGTKASIKELIDSFNKLKFDpNNVDVVVAPPSLHIPLVQEKLKNKNFKISSQNVSlTGSGAFTGEI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275    80 SMPILKDIGVHWVILGHSERRTYYGETDEIVAQKVSEACKQGFMVIACIGETLQQREANQTAKVVLSQTSAIAAKLTKDA 159
Cdd:PTZ00333  81 SAEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDEA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275   160 WNQVVLAYEPVWAIGTGKVATPEQAQEVHLLLRKWVSENIGTDVAAKLRILYGGSVNAANAATLYAKPDINGFLVGGASL 239
Cdd:PTZ00333 161 WDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASL 240
                        250
                 ....*....|.
gi 1351275   240 KPEFRDIIDAT 250
Cdd:PTZ00333 241 KPDFVDIIKSA 251
TpiA COG0149
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ...
6-249 4.53e-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: 337.41  E-value: 4.53e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275    6 QPIAAANWKCNGTTASIEKLVQVFNEHTISH-DVQCVVAPTFVHIPLVQAKLRNPKYVISAEN-AIAKSGAFTGEVSMPI 83
Cdd:COG0149   3 KPLIAGNWKMNGTLAEAKALLAALAAALADLaDVEVVVCPPFTYLAAVAEALAGSPIALGAQNvHWEDSGAYTGEISAAM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275   84 LKDIGVHWVILGHSERRTYYGETDEIVAQKVSEACKQGFMVIACIGETLQQREANQTAKVVLSQTSAIAAKLTKDAWNQV 163
Cdd:COG0149  83 LKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLSAEQAANV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275  164 VLAYEPVWAIGTGKVATPEQAQEVHLLLRKWVSENIGTDVAAKLRILYGGSVNAANAATLYAKPDINGFLVGGASLKPE- 242
Cdd:COG0149 163 VIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDAEd 242

                ....*..
gi 1351275  243 FRDIIDA 249
Cdd:COG0149 243 FLAIVRA 249
TIM cd00311
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ...
7-248 1.01e-115

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: 331.04  E-value: 1.01e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275    7 PIAAANWKCNGTTASIEKLVQVFNEHTISH-DVQCVVAPTFVHIPLVQAKLRNPKYVISAENA-IAKSGAFTGEVSMPIL 84
Cdd:cd00311   1 PLVAGNWKMNGTLAEALELAKALNAVLKDEsGVEVVVAPPFTYLAAVAEALEGSKIKVGAQNVsPEDSGAFTGEISAEML 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275   85 KDIGVHWVILGHSERRTYYGETDEIVAQKVSEACKQGFMVIACIGETLQQREANQTAKVVLSQTSAIAAKLtkDAWNQVV 164
Cdd:cd00311  81 KDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGV--EDLAPVV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275  165 LAYEPVWAIGTGKVATPEQAQEVHLLLRKWVSENIGtDVAAKLRILYGGSVNAANAATLYAKPDINGFLVGGASLKPE-F 243
Cdd:cd00311 159 IAYEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYG-EVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAEsF 237

                ....*
gi 1351275  244 RDIID 248
Cdd:cd00311 238 LDIIK 242
TIM pfam00121
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ...
7-249 1.42e-106

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: 307.90  E-value: 1.42e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275      7 PIAAANWKCNGTTASIEKLVQVFNEHTISH-DVQCVVAPTFVHIPLVQAKLrNPKYVISAENA-IAKSGAFTGEVSMPIL 84
Cdd:pfam00121   1 PIIAGNWKMNGTLAEAAELLAELAEALADEsGVEVVVAPPFTYLSAVAELL-GSNIKVGAQNVdPEESGAFTGEISAEML 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275     85 KDIGVHWVILGHSERRTYYGETDEIVAQKVSEACKQGFMVIACIGETLQQREANQTAKVVLSQTSAIAAKLTKDAWNqVV 164
Cdd:pfam00121  80 KDLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQKN-LV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275    165 LAYEPVWAIGTGKVATPEQAQEVHLLLRKWVSENIGtDVAAKLRILYGGSVNAANAATLYAKPDINGFLVGGASLKPE-F 243
Cdd:pfam00121 159 IAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYK-EVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEdF 237

                  ....*.
gi 1351275    244 RDIIDA 249
Cdd:pfam00121 238 LDIINA 243
tim TIGR00419
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ...
12-242 5.28e-49

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: 160.35  E-value: 5.28e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275     12 NWK-CNGTTASIEKLVQVFNEHTISHD-VQCVVAPTFVHIPLVQAKLRNPKYvisAENAIA-KSGAFTGEVSMPILKDIG 88
Cdd:TIGR00419   5 NWKtYNESRGMRALEVAKIAEEVASEAgVAVAVAPPFVDLPMIKREVEIPVY---AQHVDAvLSGAHTGEISAEMLKDIG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275     89 VHWVILGHSERRtyYGETDeiVAQKVSEACKQGFMVIACIgetlqqreanqtaKVVLSQTSAIAakltkdaWNQVVLAYE 168
Cdd:TIGR00419  82 AKGTLINHSERR--MKLAD--IEKKIARLKELGLTSVVCT-------------NNVLTTAAAAA-------LEPDVVAVE 137
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1351275    169 PVWAIGTGKVATPEQAQEVHLLLRkwVSENIGTDVaaklRILYGGSVNAANAATLYAKPDINGFLVGGASLKPE 242
Cdd:TIGR00419 138 PPELIGTGIPVSPAQPEVVHGSVR--AVKEVNESV----RVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
 
Name Accession Description Interval E-value
PTZ00333 PTZ00333
triosephosphate isomerase; Provisional
2-250 4.62e-145

triosephosphate isomerase; Provisional


Pssm-ID: 240365  Cd Length: 255  Bit Score: 405.84  E-value: 4.62e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275     2 SAKPQPIAAANWKCNGTTASIEKLVQVFNEHTIS-HDVQCVVAPTFVHIPLVQAKLRNPKYVISAENAI-AKSGAFTGEV 79
Cdd:PTZ00333   1 MMKRKPFVGGNWKCNGTKASIKELIDSFNKLKFDpNNVDVVVAPPSLHIPLVQEKLKNKNFKISSQNVSlTGSGAFTGEI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275    80 SMPILKDIGVHWVILGHSERRTYYGETDEIVAQKVSEACKQGFMVIACIGETLQQREANQTAKVVLSQTSAIAAKLTKDA 159
Cdd:PTZ00333  81 SAEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDEA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275   160 WNQVVLAYEPVWAIGTGKVATPEQAQEVHLLLRKWVSENIGTDVAAKLRILYGGSVNAANAATLYAKPDINGFLVGGASL 239
Cdd:PTZ00333 161 WDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASL 240
                        250
                 ....*....|.
gi 1351275   240 KPEFRDIIDAT 250
Cdd:PTZ00333 241 KPDFVDIIKSA 251
TpiA COG0149
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ...
6-249 4.53e-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: 337.41  E-value: 4.53e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275    6 QPIAAANWKCNGTTASIEKLVQVFNEHTISH-DVQCVVAPTFVHIPLVQAKLRNPKYVISAEN-AIAKSGAFTGEVSMPI 83
Cdd:COG0149   3 KPLIAGNWKMNGTLAEAKALLAALAAALADLaDVEVVVCPPFTYLAAVAEALAGSPIALGAQNvHWEDSGAYTGEISAAM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275   84 LKDIGVHWVILGHSERRTYYGETDEIVAQKVSEACKQGFMVIACIGETLQQREANQTAKVVLSQTSAIAAKLTKDAWNQV 163
Cdd:COG0149  83 LKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLSAEQAANV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275  164 VLAYEPVWAIGTGKVATPEQAQEVHLLLRKWVSENIGTDVAAKLRILYGGSVNAANAATLYAKPDINGFLVGGASLKPE- 242
Cdd:COG0149 163 VIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDAEd 242

                ....*..
gi 1351275  243 FRDIIDA 249
Cdd:COG0149 243 FLAIVRA 249
TIM cd00311
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ...
7-248 1.01e-115

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: 331.04  E-value: 1.01e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275    7 PIAAANWKCNGTTASIEKLVQVFNEHTISH-DVQCVVAPTFVHIPLVQAKLRNPKYVISAENA-IAKSGAFTGEVSMPIL 84
Cdd:cd00311   1 PLVAGNWKMNGTLAEALELAKALNAVLKDEsGVEVVVAPPFTYLAAVAEALEGSKIKVGAQNVsPEDSGAFTGEISAEML 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275   85 KDIGVHWVILGHSERRTYYGETDEIVAQKVSEACKQGFMVIACIGETLQQREANQTAKVVLSQTSAIAAKLtkDAWNQVV 164
Cdd:cd00311  81 KDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGV--EDLAPVV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275  165 LAYEPVWAIGTGKVATPEQAQEVHLLLRKWVSENIGtDVAAKLRILYGGSVNAANAATLYAKPDINGFLVGGASLKPE-F 243
Cdd:cd00311 159 IAYEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYG-EVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAEsF 237

                ....*
gi 1351275  244 RDIID 248
Cdd:cd00311 238 LDIIK 242
tpiA PRK00042
triosephosphate isomerase; Provisional
6-249 4.50e-111

triosephosphate isomerase; Provisional


Pssm-ID: 234589  Cd Length: 250  Bit Score: 319.37  E-value: 4.50e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275     6 QPIAAANWKCNGTTASIEKLVQVFNEHTIS-HDVQCVVAPTFVHIPLVQAKLRNPKYVISAENA-IAKSGAFTGEVSMPI 83
Cdd:PRK00042   2 KPIIAGNWKMNKTLAEAKALVEELKAALPDaDGVEVAVAPPFTALASVKEALKGSNIKLGAQNVhPEDSGAFTGEISAEM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275    84 LKDIGVHWVILGHSERRTYYGETDEIVAQKVSEACKQGFMVIACIGETLQQREANQTAKVVLSQTSAIAAKLTKDAWNQV 163
Cdd:PRK00042  82 LKDLGVKYVIIGHSERRQYFGETDELVNKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLEAALAGLSAEQFANL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275   164 VLAYEPVWAIGTGKVATPEQAQEVHLLLRKWVSENIGtDVAAKLRILYGGSVNAANAATLYAKPDINGFLVGGASLKPE- 242
Cdd:PRK00042 162 VIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYG-EVAEKVRILYGGSVKPDNAAELMAQPDIDGALVGGASLKAEd 240

                 ....*..
gi 1351275   243 FRDIIDA 249
Cdd:PRK00042 241 FLAIVKA 247
PLN02561 PLN02561
triosephosphate isomerase
12-251 1.02e-108

triosephosphate isomerase


Pssm-ID: 178175  Cd Length: 253  Bit Score: 313.68  E-value: 1.02e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275    12 NWKCNGTTASIEKLVQVFNEHTI--SHDVQCVVAPTFVHIPLVQAKLRnPKYVISAENA-IAKSGAFTGEVSMPILKDIG 88
Cdd:PLN02561  10 NWKCNGTVEEVKKIVTTLNEAEVpsEDVVEVVVSPPFVFLPLVKSLLR-PDFQVAAQNCwVKKGGAFTGEISAEMLVNLG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275    89 VHWVILGHSERRTYYGETDEIVAQKVSEACKQGFMVIACIGETLQQREANQTAKVVLSQTSAIAAKLTKdaWNQVVLAYE 168
Cdd:PLN02561  89 IPWVILGHSERRALLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIADKVSD--WANVVLAYE 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275   169 PVWAIGTGKVATPEQAQEVHLLLRKWVSENIGTDVAAKLRILYGGSVNAANAATLYAKPDINGFLVGGASLKPEFRDIID 248
Cdd:PLN02561 167 PVWAIGTGKVATPAQAQEVHDELRKWLHKNVSPEVAATTRIIYGGSVTGANCKELAAQPDVDGFLVGGASLKPEFIDIIK 246

                 ...
gi 1351275   249 ATR 251
Cdd:PLN02561 247 SAT 249
TIM pfam00121
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ...
7-249 1.42e-106

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: 307.90  E-value: 1.42e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275      7 PIAAANWKCNGTTASIEKLVQVFNEHTISH-DVQCVVAPTFVHIPLVQAKLrNPKYVISAENA-IAKSGAFTGEVSMPIL 84
Cdd:pfam00121   1 PIIAGNWKMNGTLAEAAELLAELAEALADEsGVEVVVAPPFTYLSAVAELL-GSNIKVGAQNVdPEESGAFTGEISAEML 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275     85 KDIGVHWVILGHSERRTYYGETDEIVAQKVSEACKQGFMVIACIGETLQQREANQTAKVVLSQTSAIAAKLTKDAWNqVV 164
Cdd:pfam00121  80 KDLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQKN-LV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275    165 LAYEPVWAIGTGKVATPEQAQEVHLLLRKWVSENIGtDVAAKLRILYGGSVNAANAATLYAKPDINGFLVGGASLKPE-F 243
Cdd:pfam00121 159 IAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYK-EVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEdF 237

                  ....*.
gi 1351275    244 RDIIDA 249
Cdd:pfam00121 238 LDIINA 243
PRK13962 PRK13962
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional
7-242 2.61e-85

bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional


Pssm-ID: 237572 [Multi-domain]  Cd Length: 645  Bit Score: 266.59  E-value: 2.61e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275     7 PIAAANWKCNGTTASIEKLVQVFNEHTISHDVQCVVAPTFVHIPLVQAKLRNPKYVISAENAI-AKSGAFTGEVSMPILK 85
Cdd:PRK13962 399 PIIAGNWKMNKTPAEAKEFVNELKKYVKDAQAEVVVCPPFTALPSVKEAVDGSNIKLGAQNVFyEEKGAYTGEISGPMLA 478
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275    86 DIGVHWVILGHSERRTYYGETDEIVAQKVSEACKQGFMVIACIGETLQQREANQTAKVVLSQTSAIAAKLTKDAWNQVVL 165
Cdd:PRK13962 479 EIGVEYVIIGHSERRQYFGETDELVNKKVLAALKAGLTPILCVGETLDERESGITFDVVRLQLKAALNGLSAEQVKKVVI 558
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1351275   166 AYEPVWAIGTGKVATPEQAQEVHLLLRKWVSENIGTDVAAKLRILYGGSVNAANAATLYAKPDINGFLVGGASLKPE 242
Cdd:PRK13962 559 AYEPVWAIGTGKVATPEQAQEVHAFIRKLVAELYGEEAARKVRILYGGSVKSENAAGLFNQPDIDGGLVGGASLKAQ 635
PLN02429 PLN02429
triosephosphate isomerase
1-249 2.69e-79

triosephosphate isomerase


Pssm-ID: 166070  Cd Length: 315  Bit Score: 241.23  E-value: 2.69e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275     1 MSAKPQPIAAANWKCNGTTASIEKLVQVFNEHTISHDVQCVVAPTFVHIPLVQAKLRNpKYVISAENA-IAKSGAFTGEV 79
Cdd:PLN02429  60 MAGSGKFFVGGNWKCNGTKDSIAKLISDLNSATLEADVDVVVSPPFVYIDQVKSSLTD-RIDISGQNSwVGKGGAFTGEI 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275    80 SMPILKDIGVHWVILGHSERRTYYGETDEIVAQKVSEACKQGFMVIACIGETLQQREANQTAKVVLSQTSAIAAKLTkdA 159
Cdd:PLN02429 139 SVEQLKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVP--S 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275   160 WNQVVLAYEPVWAIGTGKVATPEQAQEVHLLLRKWVSENIGTDVAAKLRILYGGSVNAANAATLYAKPDINGFLVGGASL 239
Cdd:PLN02429 217 WDNIVVAYEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASL 296
                        250
                 ....*....|.
gi 1351275   240 K-PEFRDIIDA 249
Cdd:PLN02429 297 KgPEFATIVNS 307
PRK14565 PRK14565
triosephosphate isomerase; Provisional
11-248 1.25e-49

triosephosphate isomerase; Provisional


Pssm-ID: 237758  Cd Length: 237  Bit Score: 163.01  E-value: 1.25e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275    11 ANWKCNGTTASIEKLVQVFNEHTIS--HDVQCVVAPTFVHIPLVQAklRNPKYVISAENAIAK-SGAFTGEVSMPILKDI 87
Cdd:PRK14565   7 ANWKMNGDFSLFSSFLKELSNKLANneITLKLVICPPFTAMSSFVE--CNPNIKLGAQNCFYGsSGGYTGEISAKMLKEC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275    88 GVHWVILGHSERRTYYGETDEIVAQKVSEACKQGFMVIACIGETLQQREANQTAKVVLSQTSAIAAKltkdaWNQVVLAY 167
Cdd:PRK14565  85 GCSYVILGHSERRSTFHETDSDIRLKAESAIESGLIPIICVGETLEDRENGMTKDVLLEQCSNCLPK-----HGEFIIAY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275   168 EPVWAIGTGKVATPEQAQEVHLLLRKWVSenigtdvaaKLRILYGGSVNAANAATLYAKPDINGFLVGGASLKPE-FRDI 246
Cdd:PRK14565 160 EPVWAIGGSTIPSNDAIAEAFEIIRSYDS---------KSHIIYGGSVNQENIRDLKSINQLSGVLVGSASLDVDsFCKI 230

                 ..
gi 1351275   247 ID 248
Cdd:PRK14565 231 IQ 232
tim TIGR00419
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ...
12-242 5.28e-49

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: 160.35  E-value: 5.28e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275     12 NWK-CNGTTASIEKLVQVFNEHTISHD-VQCVVAPTFVHIPLVQAKLRNPKYvisAENAIA-KSGAFTGEVSMPILKDIG 88
Cdd:TIGR00419   5 NWKtYNESRGMRALEVAKIAEEVASEAgVAVAVAPPFVDLPMIKREVEIPVY---AQHVDAvLSGAHTGEISAEMLKDIG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275     89 VHWVILGHSERRtyYGETDeiVAQKVSEACKQGFMVIACIgetlqqreanqtaKVVLSQTSAIAakltkdaWNQVVLAYE 168
Cdd:TIGR00419  82 AKGTLINHSERR--MKLAD--IEKKIARLKELGLTSVVCT-------------NNVLTTAAAAA-------LEPDVVAVE 137
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1351275    169 PVWAIGTGKVATPEQAQEVHLLLRkwVSENIGTDVaaklRILYGGSVNAANAATLYAKPDINGFLVGGASLKPE 242
Cdd:TIGR00419 138 PPELIGTGIPVSPAQPEVVHGSVR--AVKEVNESV----RVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
PRK14905 PRK14905
triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; ...
36-235 2.65e-44

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


Pssm-ID: 184898 [Multi-domain]  Cd Length: 355  Bit Score: 152.49  E-value: 2.65e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275    36 HDVQCVVAPTFV----HIPLVQAKLRNPKYVISAENAIAK-SGAFTGEVSMPILKDIGVHWVILGHSERRTYYGETDEIV 110
Cdd:PRK14905  38 YDIELFVIPSYIalkdAVEAAASETGHPKIKIGAQNMNAKdKGQFTGEISPLMLKELGIELVMIGHSERRHVLKETDQEE 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275   111 AQKVSEACKQGFMVIACIGETLQQREANQTAKVVLSQTSAIAAKLTKDAWNQVVLAYEPVWAIGTGKV-ATPEQAQEVHL 189
Cdd:PRK14905 118 NEKVLAALKHGFITLLCIGETLEQKNYNISDEVLRTQLKIGLHGVSAEQLPHLFIAYEPVWAIGEGGIpASAEYADEKHA 197
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 1351275   190 LLRKWVSENIGTDvAAKLRILYGGSVNAANAATLYAKPDINGFLVG 235
Cdd:PRK14905 198 IIKQCLFELFAEE-SKKIPVLYGGSVNLENANELIMKPHIDGLFIG 242
PRK15492 PRK15492
triosephosphate isomerase; Provisional
18-235 5.75e-40

triosephosphate isomerase; Provisional


Pssm-ID: 185389  Cd Length: 260  Bit Score: 138.59  E-value: 5.75e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275    18 TTASIEKLVQVFNEHTISHDVQCVVAPTFVHIP-LVQAKLRNPK---YVISAENAIAK-SGAFTGEVSMPILKDIGVHWV 92
Cdd:PRK15492  19 ATDFLAKLSELADDIPADKDIELFVIPSFTAIQdAIAATLAIPHdhpIIIGAQNMNPNdNGQFTGDISPLMLKEIGTQLV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275    93 ILGHSERRTYYGETDEIVAQKVSEACKQGFMVIACIGETLQQREANQTAKVVLSQTSAIAAKLTKDAWNQVVLAYEPVWA 172
Cdd:PRK15492  99 MIGHSERRHKFGETDQEENAKVLAALKHDFTTLLCVGETLEQKNYGISDEILRTQLKIGLHGINPDQLAKLRIAYEPVWA 178
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1351275   173 IGTGKV-ATPEQAQEVHLLLRKWVSENIGtDVAAKLRILYGGSVNAANAATLYAKPDINGFLVG 235
Cdd:PRK15492 179 IGEAGIpASADYADEKHAVIKQCLIELFG-DAGDDIPVFYGGSVNAENANELFGQPHIDGLFIG 241
PRK04302 PRK04302
triosephosphate isomerase; Provisional
37-176 2.46e-06

triosephosphate isomerase; Provisional


Pssm-ID: 235274  Cd Length: 223  Bit Score: 47.17  E-value: 2.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351275    37 DVQCVVAPTFVHIPLVQAKLRNPKYV--ISAENAiaksGAFTGEVSMPILKDIGVHWVILGHSERRTYYGETDEIVaqkv 114
Cdd:PRK04302  36 GVRIAVAPQALDIRRVAEEVDIPVYAqhVDPVEP----GSHTGHILPEAVKDAGAVGTLINHSERRLTLADIEAVV---- 107
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1351275   115 sEACKQ-GFMVIACigetlqqreANQTAkvvlsqTSAIAAKLTKDAwnqvvLAYEPVWAIGTG 176
Cdd:PRK04302 108 -ERAKKlGLESVVC---------VNNPE------TSAAAAALGPDY-----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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