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Conserved domains on  [gi|384475517|ref|NP_001244955|]
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triosephosphate isomerase isoform 3 [Homo sapiens]

Protein Classification

beta/alpha barrel domain-containing protein( domain architecture ID 229392)

beta/alpha barrel domain-containing protein belongs to a large superfamily with a wide variety of enzymatic functions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TIM super family cl21457
TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate ...
 1-165 1.33e-97

TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate isomerase (TIM) which, in general, share an eight beta/alpha closed barrel structure.


The actual alignment was detected with superfamily member PTZ00333:

Pssm-ID: 473867  Cd Length: 255  Bit Score: 282.19  E-value: 1.33e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517   1 MIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKD--WSK 78
Cdd:PTZ00333  84 MLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDeaWDN 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517  79 VVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 158
Cdd:PTZ00333 164 IVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASLKPD 243


                 ....*..
gi 384475517 159 FVDIINA 165
Cdd:PTZ00333 244 FVDIIKS 250
 
Name Accession Description Interval E-value
PTZ00333 PTZ00333
triosephosphate isomerase; Provisional
 1-165 1.33e-97

triosephosphate isomerase; Provisional


Pssm-ID: 240365  Cd Length: 255  Bit Score: 282.19  E-value: 1.33e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517   1 MIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKD--WSK 78
Cdd:PTZ00333  84 MLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDeaWDN 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517  79 VVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 158
Cdd:PTZ00333 164 IVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASLKPD 243


                 ....*..
gi 384475517 159 FVDIINA 165
Cdd:PTZ00333 244 FVDIIKS 250
TIM cd00311
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ...
 1-164 2.09e-93

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: 270.95  E-value: 2.09e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517   1 MIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVV 80
Cdd:cd00311   79 MLKDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVV 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517  81 LAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDaVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE-F 159
Cdd:cd00311  159 IAYEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYGE-VAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAEsF 237


                 ....*
gi 384475517 160 VDIIN 164
Cdd:cd00311  238 LDIIK 242
TpiA COG0149
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ...
 1-165 1.38e-88

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: 258.83  E-value: 1.38e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517   1 MIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNV--KDWSK 78
Cdd:COG0149   82 MLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLsaEQAAN 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517  79 VVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 158
Cdd:COG0149  162 VVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDAE 241


                 ....*...
gi 384475517 159 -FVDIINA 165
Cdd:COG0149  242 dFLAIVRA 249
TIM pfam00121
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ...
 1-165 1.94e-85

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: 250.89  E-value: 1.94e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517    1 MIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDW-SKV 79
Cdd:pfam00121  78 MLKDLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEqKNL 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517   80 VLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLkSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE- 158
Cdd:pfam00121 158 VIAYEPVWAIGTGKTATPEQAQEVHAFIRAVL-AELYKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEd 236


                  ....*..
gi 384475517  159 FVDIINA 165
Cdd:pfam00121 237 FLDIINA 243
tim TIGR00419
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ...
 1-158 7.41e-44

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: 143.79  E-value: 7.41e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517    1 MIKDCGATWVVLGHSERRHVfgESDelIGQKVAHALAEGLGVIACIgekldereagiteKVVFEQTKVIAdnvkdWSKVV 80
Cdd:TIGR00419  76 MLKDIGAKGTLINHSERRMK--LAD--IEKKIARLKELGLTSVVCT-------------NNVLTTAAAAA-----LEPDV 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 384475517   81 LAYEPVWAIGTGKTATPQQAQEVHEKLRgwlksnVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 158
Cdd:TIGR00419 134 VAVEPPELIGTGIPVSPAQPEVVHGSVR------AVKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
 
Name Accession Description Interval E-value
PTZ00333 PTZ00333
triosephosphate isomerase; Provisional
 1-165 1.33e-97

triosephosphate isomerase; Provisional


Pssm-ID: 240365  Cd Length: 255  Bit Score: 282.19  E-value: 1.33e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517   1 MIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKD--WSK 78
Cdd:PTZ00333  84 MLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDeaWDN 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517  79 VVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 158
Cdd:PTZ00333 164 IVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASLKPD 243


                 ....*..
gi 384475517 159 FVDIINA 165
Cdd:PTZ00333 244 FVDIIKS 250
TIM cd00311
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ...
 1-164 2.09e-93

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: 270.95  E-value: 2.09e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517   1 MIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVV 80
Cdd:cd00311   79 MLKDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVV 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517  81 LAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDaVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE-F 159
Cdd:cd00311  159 IAYEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYGE-VAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAEsF 237


                 ....*
gi 384475517 160 VDIIN 164
Cdd:cd00311  238 LDIIK 242
PLN02561 PLN02561
triosephosphate isomerase
 1-165 1.41e-92

triosephosphate isomerase


Pssm-ID: 178175  Cd Length: 253  Bit Score: 269.38  E-value: 1.41e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517   1 MIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVV 80
Cdd:PLN02561  83 MLVNLGIPWVILGHSERRALLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIADKVSDWANVV 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517  81 LAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPEFV 160
Cdd:PLN02561 163 LAYEPVWAIGTGKVATPAQAQEVHDELRKWLHKNVSPEVAATTRIIYGGSVTGANCKELAAQPDVDGFLVGGASLKPEFI 242


                 ....*
gi 384475517 161 DIINA 165
Cdd:PLN02561 243 DIIKS 247
TpiA COG0149
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ...
 1-165 1.38e-88

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: 258.83  E-value: 1.38e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517   1 MIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNV--KDWSK 78
Cdd:COG0149   82 MLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLsaEQAAN 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517  79 VVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 158
Cdd:COG0149  162 VVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDAE 241


                 ....*...
gi 384475517 159 -FVDIINA 165
Cdd:COG0149  242 dFLAIVRA 249
TIM pfam00121
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ...
 1-165 1.94e-85

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: 250.89  E-value: 1.94e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517    1 MIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDW-SKV 79
Cdd:pfam00121  78 MLKDLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEqKNL 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517   80 VLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLkSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE- 158
Cdd:pfam00121 158 VIAYEPVWAIGTGKTATPEQAQEVHAFIRAVL-AELYKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEd 236


                  ....*..
gi 384475517  159 FVDIINA 165
Cdd:pfam00121 237 FLDIINA 243
tpiA PRK00042
triosephosphate isomerase; Provisional
 1-165 3.43e-85

triosephosphate isomerase; Provisional


Pssm-ID: 234589  Cd Length: 250  Bit Score: 250.42  E-value: 3.43e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517   1 MIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNV--KDWSK 78
Cdd:PRK00042  81 MLKDLGVKYVIIGHSERRQYFGETDELVNKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLEAALAGLsaEQFAN 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517  79 VVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDaVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 158
Cdd:PRK00042 161 LVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYGE-VAEKVRILYGGSVKPDNAAELMAQPDIDGALVGGASLKAE 239


                 ....*...
gi 384475517 159 -FVDIINA 165
Cdd:PRK00042 240 dFLAIVKA 247
PLN02429 PLN02429
triosephosphate isomerase
 2-165 3.40e-76

triosephosphate isomerase


Pssm-ID: 166070  Cd Length: 315  Bit Score: 230.06  E-value: 3.40e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517   2 IKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVVL 81
Cdd:PLN02429 143 LKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDNIVV 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517  82 AYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLK-PEFV 160
Cdd:PLN02429 223 AYEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKgPEFA 302


                 ....*
gi 384475517 161 DIINA 165
Cdd:PLN02429 303 TIVNS 307
PRK13962 PRK13962
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional
 1-165 1.23e-60

bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional


Pssm-ID: 237572 [Multi-domain]  Cd Length: 645  Bit Score: 198.03  E-value: 1.23e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517   1 MIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNV--KDWSK 78
Cdd:PRK13962 476 MLAEIGVEYVIIGHSERRQYFGETDELVNKKVLAALKAGLTPILCVGETLDERESGITFDVVRLQLKAALNGLsaEQVKK 555

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517  79 VVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKP- 157
Cdd:PRK13962 556 VVIAYEPVWAIGTGKVATPEQAQEVHAFIRKLVAELYGEEAARKVRILYGGSVKSENAAGLFNQPDIDGGLVGGASLKAq 635


                 ....*...
gi 384475517 158 EFVDIINA 165
Cdd:PRK13962 636 EFAAIANY 643
tim TIGR00419
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ...
 1-158 7.41e-44

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: 143.79  E-value: 7.41e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517    1 MIKDCGATWVVLGHSERRHVfgESDelIGQKVAHALAEGLGVIACIgekldereagiteKVVFEQTKVIAdnvkdWSKVV 80
Cdd:TIGR00419  76 MLKDIGAKGTLINHSERRMK--LAD--IEKKIARLKELGLTSVVCT-------------NNVLTTAAAAA-----LEPDV 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 384475517   81 LAYEPVWAIGTGKTATPQQAQEVHEKLRgwlksnVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE 158
Cdd:TIGR00419 134 VAVEPPELIGTGIPVSPAQPEVVHGSVR------AVKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
PRK14565 PRK14565
triosephosphate isomerase; Provisional
 1-163 9.36e-37

triosephosphate isomerase; Provisional


Pssm-ID: 237758  Cd Length: 237  Bit Score: 126.80  E-value: 9.36e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517   1 MIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKviaDNVKDWSKVV 80
Cdd:PRK14565  80 MLKECGCSYVILGHSERRSTFHETDSDIRLKAESAIESGLIPIICVGETLEDRENGMTKDVLLEQCS---NCLPKHGEFI 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517  81 LAYEPVWAIGTGKTATPQQAQEVHEKLRGWlkSNVSDavaqstrIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE-F 159
Cdd:PRK14565 157 IAYEPVWAIGGSTIPSNDAIAEAFEIIRSY--DSKSH-------IIYGGSVNQENIRDLKSINQLSGVLVGSASLDVDsF 227


                 ....
gi 384475517 160 VDII 163
Cdd:PRK14565 228 CKII 231
PRK15492 PRK15492
triosephosphate isomerase; Provisional
 1-151 2.44e-30

triosephosphate isomerase; Provisional


Pssm-ID: 185389  Cd Length: 260  Bit Score: 110.85  E-value: 2.44e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517   1 MIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKV--IADNVKDWSK 78
Cdd:PRK15492  89 MLKEIGTQLVMIGHSERRHKFGETDQEENAKVLAALKHDFTTLLCVGETLEQKNYGISDEILRTQLKIglHGINPDQLAK 168

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 384475517  79 VVLAYEPVWAIGT-GKTATPQQAQEVHEKLRGWLKSNVSDAvAQSTRIIYGGSVTGATCKELASQPDVDGFLVG 151
Cdd:PRK15492 169 LRIAYEPVWAIGEaGIPASADYADEKHAVIKQCLIELFGDA-GDDIPVFYGGSVNAENANELFGQPHIDGLFIG 241
PRK14905 PRK14905
triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; ...
 1-151 9.66e-30

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


Pssm-ID: 184898 [Multi-domain]  Cd Length: 355  Bit Score: 111.28  E-value: 9.66e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384475517   1 MIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKVIADNV--KDWSK 78
Cdd:PRK14905  90 MLKELGIELVMIGHSERRHVLKETDQEENEKVLAALKHGFITLLCIGETLEQKNYNISDEVLRTQLKIGLHGVsaEQLPH 169

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 384475517  79 VVLAYEPVWAIGTGKT-ATPQQAQEVHEKLRGWLKSNVSDAvAQSTRIIYGGSVTGATCKELASQPDVDGFLVG 151
Cdd:PRK14905 170 LFIAYEPVWAIGEGGIpASAEYADEKHAIIKQCLFELFAEE-SKKIPVLYGGSVNLENANELIMKPHIDGLFIG 242
PRK04302 PRK04302
triosephosphate isomerase; Provisional
 1-45 7.53e-03

triosephosphate isomerase; Provisional


Pssm-ID: 235274  Cd Length: 223  Bit Score: 35.61  E-value: 7.53e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 384475517   1 MIKDCGATWVVLGHSERRHVFGEsdelIGQKVAHALAEGLGVIAC 45
Cdd:PRK04302  80 AVKDAGAVGTLINHSERRLTLAD----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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