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Conserved domains on  [gi|425870889|gb|AFY05422|]
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triosephosphate isomerase, partial [Cremifania nearctica]

Protein Classification

triose-phosphate isomerase( domain architecture ID 10085182)

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:  12206759|11257493

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TIM cd00311
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ...
 3-162 4.96e-78

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: 231.66  E-value: 4.96e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889   3 GNWKMNGSKNSIAEICKNL-GSSTCDSNTEVVIGCPALYLEYTRGLLPKS-FELAAQNCYKVASGAFTGEWSPAMLKDVG 80
Cdd:cd00311    5 GNWKMNGTLAEALELAKALnAVLKDESGVEVVVAPPFTYLAAVAEALEGSkIKVGAQNVSPEDSGAFTGEISAEMLKDAG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889  81 ATWVILGHSERRQIFGETDVLIGEKCAHALAEGLKVIACIGETLEERESNKTEEVVARQMCELTKHIKDWSNVVVAYEPV 160
Cdd:cd00311   85 AKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVIAYEPV 164


                 ..
gi 425870889 161 WA 162
Cdd:cd00311  165 WA 166
 
Name Accession Description Interval E-value
TIM cd00311
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ...
 3-162 4.96e-78

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: 231.66  E-value: 4.96e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889   3 GNWKMNGSKNSIAEICKNL-GSSTCDSNTEVVIGCPALYLEYTRGLLPKS-FELAAQNCYKVASGAFTGEWSPAMLKDVG 80
Cdd:cd00311    5 GNWKMNGTLAEALELAKALnAVLKDESGVEVVVAPPFTYLAAVAEALEGSkIKVGAQNVSPEDSGAFTGEISAEMLKDAG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889  81 ATWVILGHSERRQIFGETDVLIGEKCAHALAEGLKVIACIGETLEERESNKTEEVVARQMCELTKHIKDWSNVVVAYEPV 160
Cdd:cd00311   85 AKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVIAYEPV 164


                 ..
gi 425870889 161 WA 162
Cdd:cd00311  165 WA 166
TIM pfam00121
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ...
 3-162 1.00e-72

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: 218.15  E-value: 1.00e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889    3 GNWKMNGSKNSIAEICKNLGSSTCDSN-TEVVIGCPALYLEYTRGLLPKSFELAAQNCYKVASGAFTGEWSPAMLKDVGA 81
Cdd:pfam00121   5 GNWKMNGTLAEAAELLAELAEALADESgVEVVVAPPFTYLSAVAELLGSNIKVGAQNVDPEESGAFTGEISAEMLKDLGV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889   82 TWVILGHSERRQIFGETDVLIGEKCAHALAEGLKVIACIGETLEERESNKTEEVVARQMCELTKHIKDW-SNVVVAYEPV 160
Cdd:pfam00121  85 SYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEqKNLVIAYEPV 164


                  ..
gi 425870889  161 WA 162
Cdd:pfam00121 165 WA 166
TpiA COG0149
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ...
 3-162 2.86e-72

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: 217.23  E-value: 2.86e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889   3 GNWKMNGSKNSIAEICKNLGSSTCD-SNTEVVIGCPALYLEYTRGLLPKS-FELAAQNCYKVASGAFTGEWSPAMLKDVG 80
Cdd:COG0149    8 GNWKMNGTLAEAKALLAALAAALADlADVEVVVCPPFTYLAAVAEALAGSpIALGAQNVHWEDSGAYTGEISAAMLKDLG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889  81 ATWVILGHSERRQIFGETDVLIGEKCAHALAEGLKVIACIGETLEERESNKTEEVVARQMCELTKHI--KDWSNVVVAYE 158
Cdd:COG0149   88 CRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLsaEQAANVVIAYE 167


                 ....
gi 425870889 159 PVWA 162
Cdd:COG0149  168 PVWA 171
PTZ00333 PTZ00333
triosephosphate isomerase; Provisional
 3-162 6.47e-71

triosephosphate isomerase; Provisional


Pssm-ID: 240365  Cd Length: 255  Bit Score: 214.01  E-value: 6.47e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889   3 GNWKMNGSKNSIAEICKNLGSSTCD-SNTEVVIGCPALYLEYTRGLLPKS-FELAAQNCYKVASGAFTGEWSPAMLKDVG 80
Cdd:PTZ00333  10 GNWKCNGTKASIKELIDSFNKLKFDpNNVDVVVAPPSLHIPLVQEKLKNKnFKISSQNVSLTGSGAFTGEISAEMLKDLG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889  81 ATWVILGHSERRQIFGETDVLIGEKCAHALAEGLKVIACIGETLEERESNKTEEVVARQMCELTKHIKD--WSNVVVAYE 158
Cdd:PTZ00333  90 INWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDeaWDNIVIAYE 169


                 ....
gi 425870889 159 PVWA 162
Cdd:PTZ00333 170 PVWA 173
tim TIGR00419
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ...
 3-162 5.23e-25

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: 95.26  E-value: 5.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889    3 GNWKM-NGSKNSIAEICKNLGSSTCD-SNTEVVIGCPALYLEYTRGLLpkSFELAAQNCYKVASGAFTGEWSPAMLKDVG 80
Cdd:TIGR00419   4 GNWKTyNESRGMRALEVAKIAEEVASeAGVAVAVAPPFVDLPMIKREV--EIPVYAQHVDAVLSGAHTGEISAEMLKDIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889   81 ATWVILGHSERRqiFGETDvlIGEKCAHALAEGLKVIACIGETleeresNKTEEVVArqmceltkhikdWSNVVVAYEPV 160
Cdd:TIGR00419  82 AKGTLINHSERR--MKLAD--IEKKIARLKELGLTSVVCTNNV------LTTAAAAA------------LEPDVVAVEPP 139


                  ..
gi 425870889  161 WA 162
Cdd:TIGR00419 140 EL 141
 
Name Accession Description Interval E-value
TIM cd00311
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ...
 3-162 4.96e-78

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: 231.66  E-value: 4.96e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889   3 GNWKMNGSKNSIAEICKNL-GSSTCDSNTEVVIGCPALYLEYTRGLLPKS-FELAAQNCYKVASGAFTGEWSPAMLKDVG 80
Cdd:cd00311    5 GNWKMNGTLAEALELAKALnAVLKDESGVEVVVAPPFTYLAAVAEALEGSkIKVGAQNVSPEDSGAFTGEISAEMLKDAG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889  81 ATWVILGHSERRQIFGETDVLIGEKCAHALAEGLKVIACIGETLEERESNKTEEVVARQMCELTKHIKDWSNVVVAYEPV 160
Cdd:cd00311   85 AKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVIAYEPV 164


                 ..
gi 425870889 161 WA 162
Cdd:cd00311  165 WA 166
TIM pfam00121
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ...
 3-162 1.00e-72

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: 218.15  E-value: 1.00e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889    3 GNWKMNGSKNSIAEICKNLGSSTCDSN-TEVVIGCPALYLEYTRGLLPKSFELAAQNCYKVASGAFTGEWSPAMLKDVGA 81
Cdd:pfam00121   5 GNWKMNGTLAEAAELLAELAEALADESgVEVVVAPPFTYLSAVAELLGSNIKVGAQNVDPEESGAFTGEISAEMLKDLGV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889   82 TWVILGHSERRQIFGETDVLIGEKCAHALAEGLKVIACIGETLEERESNKTEEVVARQMCELTKHIKDW-SNVVVAYEPV 160
Cdd:pfam00121  85 SYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEqKNLVIAYEPV 164


                  ..
gi 425870889  161 WA 162
Cdd:pfam00121 165 WA 166
TpiA COG0149
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ...
 3-162 2.86e-72

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: 217.23  E-value: 2.86e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889   3 GNWKMNGSKNSIAEICKNLGSSTCD-SNTEVVIGCPALYLEYTRGLLPKS-FELAAQNCYKVASGAFTGEWSPAMLKDVG 80
Cdd:COG0149    8 GNWKMNGTLAEAKALLAALAAALADlADVEVVVCPPFTYLAAVAEALAGSpIALGAQNVHWEDSGAYTGEISAAMLKDLG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889  81 ATWVILGHSERRQIFGETDVLIGEKCAHALAEGLKVIACIGETLEERESNKTEEVVARQMCELTKHI--KDWSNVVVAYE 158
Cdd:COG0149   88 CRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLsaEQAANVVIAYE 167


                 ....
gi 425870889 159 PVWA 162
Cdd:COG0149  168 PVWA 171
PTZ00333 PTZ00333
triosephosphate isomerase; Provisional
 3-162 6.47e-71

triosephosphate isomerase; Provisional


Pssm-ID: 240365  Cd Length: 255  Bit Score: 214.01  E-value: 6.47e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889   3 GNWKMNGSKNSIAEICKNLGSSTCD-SNTEVVIGCPALYLEYTRGLLPKS-FELAAQNCYKVASGAFTGEWSPAMLKDVG 80
Cdd:PTZ00333  10 GNWKCNGTKASIKELIDSFNKLKFDpNNVDVVVAPPSLHIPLVQEKLKNKnFKISSQNVSLTGSGAFTGEISAEMLKDLG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889  81 ATWVILGHSERRQIFGETDVLIGEKCAHALAEGLKVIACIGETLEERESNKTEEVVARQMCELTKHIKD--WSNVVVAYE 158
Cdd:PTZ00333  90 INWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDeaWDNIVIAYE 169


                 ....
gi 425870889 159 PVWA 162
Cdd:PTZ00333 170 PVWA 173
tpiA PRK00042
triosephosphate isomerase; Provisional
 3-162 1.71e-68

triosephosphate isomerase; Provisional


Pssm-ID: 234589  Cd Length: 250  Bit Score: 207.66  E-value: 1.71e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889   3 GNWKMNGSKNS----IAEICKNLGSSTcdsNTEVVIGCPALYL-EYTRGLLPKSFELAAQNCYKVASGAFTGEWSPAMLK 77
Cdd:PRK00042   7 GNWKMNKTLAEakalVEELKAALPDAD---GVEVAVAPPFTALaSVKEALKGSNIKLGAQNVHPEDSGAFTGEISAEMLK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889  78 DVGATWVILGHSERRQIFGETDVLIGEKCAHALAEGLKVIACIGETLEERESNKTEEVVARQMCELTKHI--KDWSNVVV 155
Cdd:PRK00042  84 DLGVKYVIIGHSERRQYFGETDELVNKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLEAALAGLsaEQFANLVI 163


                 ....*..
gi 425870889 156 AYEPVWA 162
Cdd:PRK00042 164 AYEPVWA 170
PLN02561 PLN02561
triosephosphate isomerase
 3-162 2.21e-61

triosephosphate isomerase


Pssm-ID: 178175  Cd Length: 253  Bit Score: 190.03  E-value: 2.21e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889   3 GNWKMNGSKNSIAEICK--NLGSSTCDSNTEVVIGCPALYLEYTRGLLPKSFELAAQNCYKVASGAFTGEWSPAMLKDVG 80
Cdd:PLN02561   9 GNWKCNGTVEEVKKIVTtlNEAEVPSEDVVEVVVSPPFVFLPLVKSLLRPDFQVAAQNCWVKKGGAFTGEISAEMLVNLG 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889  81 ATWVILGHSERRQIFGETDVLIGEKCAHALAEGLKVIACIGETLEERESNKTEEVVARQMCELTKHIKDWSNVVVAYEPV 160
Cdd:PLN02561  89 IPWVILGHSERRALLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIADKVSDWANVVLAYEPV 168


                 ..
gi 425870889 161 WA 162
Cdd:PLN02561 169 WA 170
PLN02429 PLN02429
triosephosphate isomerase
 1-162 9.43e-49

triosephosphate isomerase


Pssm-ID: 166070  Cd Length: 315  Bit Score: 159.57  E-value: 9.43e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889   1 ASGNWKMNGSKNSIAEICKNLGSSTCDSNTEVVIGCPALYLEYTRGLLPKSFELAAQNCYKVASGAFTGEWSPAMLKDVG 80
Cdd:PLN02429  68 VGGNWKCNGTKDSIAKLISDLNSATLEADVDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEISVEQLKDLG 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889  81 ATWVILGHSERRQIFGETDVLIGEKCAHALAEGLKVIACIGETLEERESNKTEEVVARQMCELTKHIKDWSNVVVAYEPV 160
Cdd:PLN02429 148 CKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDNIVVAYEPV 227


                 ..
gi 425870889 161 WA 162
Cdd:PLN02429 228 WA 229
PRK13962 PRK13962
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional
 1-162 3.25e-48

bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional


Pssm-ID: 237572 [Multi-domain]  Cd Length: 645  Bit Score: 164.51  E-value: 3.25e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889   1 ASGNWKMNGSKNSIAEICKNLGSSTCDSNTEVVIGCPALYLEYTRGLLPKS-FELAAQNCYKVASGAFTGEWSPAMLKDV 79
Cdd:PRK13962 401 IAGNWKMNKTPAEAKEFVNELKKYVKDAQAEVVVCPPFTALPSVKEAVDGSnIKLGAQNVFYEEKGAYTGEISGPMLAEI 480

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889  80 GATWVILGHSERRQIFGETDVLIGEKCAHALAEGLKVIACIGETLEERESNKTEEVVARQMCE----LTKhiKDWSNVVV 155
Cdd:PRK13962 481 GVEYVIIGHSERRQYFGETDELVNKKVLAALKAGLTPILCVGETLDERESGITFDVVRLQLKAalngLSA--EQVKKVVI 558


                 ....*..
gi 425870889 156 AYEPVWA 162
Cdd:PRK13962 559 AYEPVWA 565
PRK14565 PRK14565
triosephosphate isomerase; Provisional
 4-162 1.81e-40

triosephosphate isomerase; Provisional


Pssm-ID: 237758  Cd Length: 237  Bit Score: 136.04  E-value: 1.81e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889   4 NWKMNGSKNSIAEICKNLGSSTC--DSNTEVVIgCPALYLEYTRGLLPKSFELAAQNCYKVASGAFTGEWSPAMLKDVGA 81
Cdd:PRK14565   8 NWKMNGDFSLFSSFLKELSNKLAnnEITLKLVI-CPPFTAMSSFVECNPNIKLGAQNCFYGSSGGYTGEISAKMLKECGC 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889  82 TWVILGHSERRQIFGETDVLIGEKCAHALAEGLKVIACIGETLEERESNKTEEVVARQmCE--LTKHIKdwsnVVVAYEP 159
Cdd:PRK14565  87 SYVILGHSERRSTFHETDSDIRLKAESAIESGLIPIICVGETLEDRENGMTKDVLLEQ-CSncLPKHGE----FIIAYEP 161


                 ...
gi 425870889 160 VWA 162
Cdd:PRK14565 162 VWA 164
tim TIGR00419
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ...
 3-162 5.23e-25

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: 95.26  E-value: 5.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889    3 GNWKM-NGSKNSIAEICKNLGSSTCD-SNTEVVIGCPALYLEYTRGLLpkSFELAAQNCYKVASGAFTGEWSPAMLKDVG 80
Cdd:TIGR00419   4 GNWKTyNESRGMRALEVAKIAEEVASeAGVAVAVAPPFVDLPMIKREV--EIPVYAQHVDAVLSGAHTGEISAEMLKDIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889   81 ATWVILGHSERRqiFGETDvlIGEKCAHALAEGLKVIACIGETleeresNKTEEVVArqmceltkhikdWSNVVVAYEPV 160
Cdd:TIGR00419  82 AKGTLINHSERR--MKLAD--IEKKIARLKELGLTSVVCTNNV------LTTAAAAA------------LEPDVVAVEPP 139


                  ..
gi 425870889  161 WA 162
Cdd:TIGR00419 140 EL 141
PRK14905 PRK14905
triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; ...
 54-162 5.48e-25

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


Pssm-ID: 184898 [Multi-domain]  Cd Length: 355  Bit Score: 98.18  E-value: 5.48e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889  54 LAAQNCYKVASGAFTGEWSPAMLKDVGATWVILGHSERRQIFGETDVLIGEKCAHALAEGLKVIACIGETLEERESNKTE 133
Cdd:PRK14905  69 IGAQNMNAKDKGQFTGEISPLMLKELGIELVMIGHSERRHVLKETDQEENEKVLAALKHGFITLLCIGETLEQKNYNISD 148

                         90       100       110
                 ....*....|....*....|....*....|..
gi 425870889 134 EVVARQMcELTKH---IKDWSNVVVAYEPVWA 162
Cdd:PRK14905 149 EVLRTQL-KIGLHgvsAEQLPHLFIAYEPVWA 179
PRK15492 PRK15492
triosephosphate isomerase; Provisional
 54-162 4.34e-24

triosephosphate isomerase; Provisional


Pssm-ID: 185389  Cd Length: 260  Bit Score: 94.29  E-value: 4.34e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889  54 LAAQNCYKVASGAFTGEWSPAMLKDVGATWVILGHSERRQIFGETDVLIGEKCAHALAEGLKVIACIGETLEERESNKTE 133
Cdd:PRK15492  68 IGAQNMNPNDNGQFTGDISPLMLKEIGTQLVMIGHSERRHKFGETDQEENAKVLAALKHDFTTLLCVGETLEQKNYGISD 147

                         90       100       110
                 ....*....|....*....|....*....|..
gi 425870889 134 EVVARQMcELTKH---IKDWSNVVVAYEPVWA 162
Cdd:PRK15492 148 EILRTQL-KIGLHginPDQLAKLRIAYEPVWA 178
PRK04302 PRK04302
triosephosphate isomerase; Provisional
 14-119 1.11e-07

triosephosphate isomerase; Provisional


Pssm-ID: 235274  Cd Length: 223  Bit Score: 49.48  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 425870889  14 IAEICKNLGSstcDSNTEVVIGCPALYLEytrgLLPKSFELA--AQNCYKVASGAFTGEWSPAMLKDVGATWVILGHSER 91
Cdd:PRK04302  24 IAKAAEKVSK---ETGVRIAVAPQALDIR----RVAEEVDIPvyAQHVDPVEPGSHTGHILPEAVKDAGAVGTLINHSER 96

                         90       100
                 ....*....|....*....|....*...
gi 425870889  92 RQIFGEtdvlIGEKCAHALAEGLKVIAC 119
Cdd:PRK04302  97 RLTLAD----IEAVVERAKKLGLESVVC 120
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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