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Conserved domains on  [gi|306415973|gb|ADM86861|]
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triosephosphate isomerase [Oryza sativa Japonica Group]

Protein Classification

triose-phosphate isomerase( domain architecture ID 10791410)

triose-phosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate and D-glyceraldehyde-3-phosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02561 PLN02561
triosephosphate isomerase
 1-253 0e+00

triosephosphate isomerase


:

Pssm-ID: 178175  Cd Length: 253  Bit Score: 512.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973   1 MGRKFFVGGNWKCNGTTDQVDKIVKILNEGQIASTDVVEVVVSPPYVFLPVVKSQLRPEIQVAAQNCWVKKGGAFTGEVS 80
Cdd:PLN02561   1 MARKFFVGGNWKCNGTVEEVKKIVTTLNEAEVPSEDVVEVVVSPPFVFLPLVKSLLRPDFQVAAQNCWVKKGGAFTGEIS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973  81 AEMLVNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIAERIKDWTN 160
Cdd:PLN02561  81 AEMLVNLGIPWVILGHSERRALLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIADKVSDWAN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 161 VVVAYEPVWAIGTGKVATPDQAQEVHDGLRKWLAANVSAEVAESTRIIYGGSVTGANCKELAAKPDVDGFLVGGASLKPE 240
Cdd:PLN02561 161 VVLAYEPVWAIGTGKVATPAQAQEVHDELRKWLHKNVSPEVAATTRIIYGGSVTGANCKELAAQPDVDGFLVGGASLKPE 240

                        250
                 ....*....|...
gi 306415973 241 FIDIINSATVKSA 253
Cdd:PLN02561 241 FIDIIKSATVKKS 253
 
Name Accession Description Interval E-value
PLN02561 PLN02561
triosephosphate isomerase
 1-253 0e+00

triosephosphate isomerase


Pssm-ID: 178175  Cd Length: 253  Bit Score: 512.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973   1 MGRKFFVGGNWKCNGTTDQVDKIVKILNEGQIASTDVVEVVVSPPYVFLPVVKSQLRPEIQVAAQNCWVKKGGAFTGEVS 80
Cdd:PLN02561   1 MARKFFVGGNWKCNGTVEEVKKIVTTLNEAEVPSEDVVEVVVSPPFVFLPLVKSLLRPDFQVAAQNCWVKKGGAFTGEIS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973  81 AEMLVNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIAERIKDWTN 160
Cdd:PLN02561  81 AEMLVNLGIPWVILGHSERRALLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIADKVSDWAN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 161 VVVAYEPVWAIGTGKVATPDQAQEVHDGLRKWLAANVSAEVAESTRIIYGGSVTGANCKELAAKPDVDGFLVGGASLKPE 240
Cdd:PLN02561 161 VVLAYEPVWAIGTGKVATPAQAQEVHDELRKWLHKNVSPEVAATTRIIYGGSVTGANCKELAAQPDVDGFLVGGASLKPE 240

                        250
                 ....*....|...
gi 306415973 241 FIDIINSATVKSA 253
Cdd:PLN02561 241 FIDIIKSATVKKS 253
TIM cd00311
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ...
 5-246 3.28e-127

Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of dihydroxyacetone phosphate and D-glyceraldehyde-3-phosphate. The reaction is very efficient and requires neither cofactors nor metal ions. TIM, usually homodimeric, but in some organisms tetrameric, is ubiqitous and conserved in function across eukaryotes, bacteria and archaea.


Pssm-ID: 238190  Cd Length: 242  Bit Score: 360.31  E-value: 3.28e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973   5 FFVGGNWKCNGTTDQVDKIVKILNEGQIASTDVvEVVVSPPYVFLPVVKSQLR-PEIQVAAQNCWVKKGGAFTGEVSAEM 83
Cdd:cd00311    1 PLVAGNWKMNGTLAEALELAKALNAVLKDESGV-EVVVAPPFTYLAAVAEALEgSKIKVGAQNVSPEDSGAFTGEISAEM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973  84 LVNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIAERIKDWTNVVV 163
Cdd:cd00311   80 LKDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 164 AYEPVWAIGTGKVATPDQAQEVHDGLRKWLAANVSaEVAESTRIIYGGSVTGANCKELAAKPDVDGFLVGGASLKPE-FI 242
Cdd:cd00311  160 AYEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYG-EVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAEsFL 238


                 ....
gi 306415973 243 DIIN 246
Cdd:cd00311  239 DIIK 242
TIM pfam00121
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ...
 5-248 9.70e-120

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: 341.41  E-value: 9.70e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973    5 FFVGGNWKCNGTTDQVDKIVKILNEgQIASTDVVEVVVSPPYVFLPVVKSQLRPEIQVAAQNCWVKKGGAFTGEVSAEML 84
Cdd:pfam00121   1 PIIAGNWKMNGTLAEAAELLAELAE-ALADESGVEVVVAPPFTYLSAVAELLGSNIKVGAQNVDPEESGAFTGEISAEML 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973   85 VNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIAERIKDWT-NVVV 163
Cdd:pfam00121  80 KDLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQkNLVI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973  164 AYEPVWAIGTGKVATPDQAQEVHDGLRKWLAANvSAEVAESTRIIYGGSVTGANCKELAAKPDVDGFLVGGASLKPE-FI 242
Cdd:pfam00121 160 AYEPVWAIGTGKTATPEQAQEVHAFIRAVLAEL-YKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEdFL 238


                  ....*.
gi 306415973  243 DIINSA 248
Cdd:pfam00121 239 DIINAA 244
TpiA COG0149
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ...
 3-247 2.84e-119

Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 439919 [Multi-domain]  Cd Length: 249  Bit Score: 340.50  E-value: 2.84e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973   3 RKFFVGGNWKCNGTTDQVDKIVKILNEGqIASTDVVEVVVSPPYVFLPVVKSQLR-PEIQVAAQNCWVKKGGAFTGEVSA 81
Cdd:COG0149    2 RKPLIAGNWKMNGTLAEAKALLAALAAA-LADLADVEVVVCPPFTYLAAVAEALAgSPIALGAQNVHWEDSGAYTGEISA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973  82 EMLVNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIAERI--KDWT 159
Cdd:COG0149   81 AMLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLsaEQAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 160 NVVVAYEPVWAIGTGKVATPDQAQEVHDGLRKWLAANVSAEVAESTRIIYGGSVTGANCKELAAKPDVDGFLVGGASLKP 239
Cdd:COG0149  161 NVVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDA 240


                 ....*....
gi 306415973 240 E-FIDIINS 247
Cdd:COG0149  241 EdFLAIVRA 249
tim TIGR00419
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ...
 6-240 6.38e-80

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: 238.93  E-value: 6.38e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973    6 FVGGNWK-CNGTTDQVDKIVKILNEgQIASTDVVEVVVSPPYVFLPVVKSQLrpEIQVAAQNCWVKKGGAFTGEVSAEML 84
Cdd:TIGR00419   1 LVIGNWKtYNESRGMRALEVAKIAE-EVASEAGVAVAVAPPFVDLPMIKREV--EIPVYAQHVDAVLSGAHTGEISAEML 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973   85 VNLSIPWVILGHSERRSLLGEsnefVGDKVAYALSQGLKVIACVgetleqresgstmDVVAAQTKAIAerikdWTNVVVA 164
Cdd:TIGR00419  78 KDIGAKGTLINHSERRMKLAD----IEKKIARLKELGLTSVVCT-------------NNVLTTAAAAA-----LEPDVVA 135

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 306415973  165 YEPVWAIGTGKVATPDQAQEVHDGLRkwlaanVSAEVAESTRIIYGGSVTGANCKELAAKPDVDGFLVGGASLKPE 240
Cdd:TIGR00419 136 VEPPELIGTGIPVSPAQPEVVHGSVR------AVKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
 
Name Accession Description Interval E-value
PLN02561 PLN02561
triosephosphate isomerase
 1-253 0e+00

triosephosphate isomerase


Pssm-ID: 178175  Cd Length: 253  Bit Score: 512.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973   1 MGRKFFVGGNWKCNGTTDQVDKIVKILNEGQIASTDVVEVVVSPPYVFLPVVKSQLRPEIQVAAQNCWVKKGGAFTGEVS 80
Cdd:PLN02561   1 MARKFFVGGNWKCNGTVEEVKKIVTTLNEAEVPSEDVVEVVVSPPFVFLPLVKSLLRPDFQVAAQNCWVKKGGAFTGEIS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973  81 AEMLVNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIAERIKDWTN 160
Cdd:PLN02561  81 AEMLVNLGIPWVILGHSERRALLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIADKVSDWAN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 161 VVVAYEPVWAIGTGKVATPDQAQEVHDGLRKWLAANVSAEVAESTRIIYGGSVTGANCKELAAKPDVDGFLVGGASLKPE 240
Cdd:PLN02561 161 VVLAYEPVWAIGTGKVATPAQAQEVHDELRKWLHKNVSPEVAATTRIIYGGSVTGANCKELAAQPDVDGFLVGGASLKPE 240

                        250
                 ....*....|...
gi 306415973 241 FIDIINSATVKSA 253
Cdd:PLN02561 241 FIDIIKSATVKKS 253
PTZ00333 PTZ00333
triosephosphate isomerase; Provisional
 1-248 1.08e-137

triosephosphate isomerase; Provisional


Pssm-ID: 240365  Cd Length: 255  Bit Score: 387.35  E-value: 1.08e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973   1 MGRKFFVGGNWKCNGTTDQVDKIVKILNEGQIaSTDVVEVVVSPPYVFLPVVKSQLR-PEIQVAAQNCWVKKGGAFTGEV 79
Cdd:PTZ00333   2 MKRKPFVGGNWKCNGTKASIKELIDSFNKLKF-DPNNVDVVVAPPSLHIPLVQEKLKnKNFKISSQNVSLTGSGAFTGEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973  80 SAEMLVNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIAERIKD-- 157
Cdd:PTZ00333  81 SAEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDea 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 158 WTNVVVAYEPVWAIGTGKVATPDQAQEVHDGLRKWLAANVSAEVAESTRIIYGGSVTGANCKELAAKPDVDGFLVGGASL 237
Cdd:PTZ00333 161 WDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASL 240

                        250
                 ....*....|.
gi 306415973 238 KPEFIDIINSA 248
Cdd:PTZ00333 241 KPDFVDIIKSA 251
TIM cd00311
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ...
 5-246 3.28e-127

Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of dihydroxyacetone phosphate and D-glyceraldehyde-3-phosphate. The reaction is very efficient and requires neither cofactors nor metal ions. TIM, usually homodimeric, but in some organisms tetrameric, is ubiqitous and conserved in function across eukaryotes, bacteria and archaea.


Pssm-ID: 238190  Cd Length: 242  Bit Score: 360.31  E-value: 3.28e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973   5 FFVGGNWKCNGTTDQVDKIVKILNEGQIASTDVvEVVVSPPYVFLPVVKSQLR-PEIQVAAQNCWVKKGGAFTGEVSAEM 83
Cdd:cd00311    1 PLVAGNWKMNGTLAEALELAKALNAVLKDESGV-EVVVAPPFTYLAAVAEALEgSKIKVGAQNVSPEDSGAFTGEISAEM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973  84 LVNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIAERIKDWTNVVV 163
Cdd:cd00311   80 LKDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGVEDLAPVVI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 164 AYEPVWAIGTGKVATPDQAQEVHDGLRKWLAANVSaEVAESTRIIYGGSVTGANCKELAAKPDVDGFLVGGASLKPE-FI 242
Cdd:cd00311  160 AYEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYG-EVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAEsFL 238


                 ....
gi 306415973 243 DIIN 246
Cdd:cd00311  239 DIIK 242
TIM pfam00121
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ...
 5-248 9.70e-120

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: 341.41  E-value: 9.70e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973    5 FFVGGNWKCNGTTDQVDKIVKILNEgQIASTDVVEVVVSPPYVFLPVVKSQLRPEIQVAAQNCWVKKGGAFTGEVSAEML 84
Cdd:pfam00121   1 PIIAGNWKMNGTLAEAAELLAELAE-ALADESGVEVVVAPPFTYLSAVAELLGSNIKVGAQNVDPEESGAFTGEISAEML 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973   85 VNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIAERIKDWT-NVVV 163
Cdd:pfam00121  80 KDLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQkNLVI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973  164 AYEPVWAIGTGKVATPDQAQEVHDGLRKWLAANvSAEVAESTRIIYGGSVTGANCKELAAKPDVDGFLVGGASLKPE-FI 242
Cdd:pfam00121 160 AYEPVWAIGTGKTATPEQAQEVHAFIRAVLAEL-YKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEdFL 238


                  ....*.
gi 306415973  243 DIINSA 248
Cdd:pfam00121 239 DIINAA 244
TpiA COG0149
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ...
 3-247 2.84e-119

Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 439919 [Multi-domain]  Cd Length: 249  Bit Score: 340.50  E-value: 2.84e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973   3 RKFFVGGNWKCNGTTDQVDKIVKILNEGqIASTDVVEVVVSPPYVFLPVVKSQLR-PEIQVAAQNCWVKKGGAFTGEVSA 81
Cdd:COG0149    2 RKPLIAGNWKMNGTLAEAKALLAALAAA-LADLADVEVVVCPPFTYLAAVAEALAgSPIALGAQNVHWEDSGAYTGEISA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973  82 EMLVNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIAERI--KDWT 159
Cdd:COG0149   81 AMLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLsaEQAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 160 NVVVAYEPVWAIGTGKVATPDQAQEVHDGLRKWLAANVSAEVAESTRIIYGGSVTGANCKELAAKPDVDGFLVGGASLKP 239
Cdd:COG0149  161 NVVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELYGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDA 240


                 ....*....
gi 306415973 240 E-FIDIINS 247
Cdd:COG0149  241 EdFLAIVRA 249
tpiA PRK00042
triosephosphate isomerase; Provisional
 3-248 1.89e-113

triosephosphate isomerase; Provisional


Pssm-ID: 234589  Cd Length: 250  Bit Score: 325.54  E-value: 1.89e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973   3 RKFFVGGNWKCNGTTDQVDKIVKILNEgQIASTDVVEVVVSPPYVFLPVVKSQLRPE-IQVAAQNCWVKKGGAFTGEVSA 81
Cdd:PRK00042   1 RKPIIAGNWKMNKTLAEAKALVEELKA-ALPDADGVEVAVAPPFTALASVKEALKGSnIKLGAQNVHPEDSGAFTGEISA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973  82 EMLVNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIAERI--KDWT 159
Cdd:PRK00042  80 EMLKDLGVKYVIIGHSERRQYFGETDELVNKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLEAALAGLsaEQFA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 160 NVVVAYEPVWAIGTGKVATPDQAQEVHDGLRKWLAANVSaEVAESTRIIYGGSVTGANCKELAAKPDVDGFLVGGASLKP 239
Cdd:PRK00042 160 NLVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYG-EVAEKVRILYGGSVKPDNAAELMAQPDIDGALVGGASLKA 238

                        250
                 ....*....|
gi 306415973 240 E-FIDIINSA 248
Cdd:PRK00042 239 EdFLAIVKAA 248
PLN02429 PLN02429
triosephosphate isomerase
 4-251 5.42e-98

triosephosphate isomerase


Pssm-ID: 166070  Cd Length: 315  Bit Score: 289.00  E-value: 5.42e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973   4 KFFVGGNWKCNGTTDQVDKIVKILNEGQIASTdvVEVVVSPPYVFLPVVKSQLRPEIQVAAQNCWVKKGGAFTGEVSAEM 83
Cdd:PLN02429  65 KFFVGGNWKCNGTKDSIAKLISDLNSATLEAD--VDVVVSPPFVYIDQVKSSLTDRIDISGQNSWVGKGGAFTGEISVEQ 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973  84 LVNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIAERIKDWTNVVV 163
Cdd:PLN02429 143 LKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVPSWDNIVV 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 164 AYEPVWAIGTGKVATPDQAQEVHDGLRKWLAANVSAEVAESTRIIYGGSVTGANCKELAAKPDVDGFLVGGASLK-PEFI 242
Cdd:PLN02429 223 AYEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKgPEFA 302


                 ....*....
gi 306415973 243 DIINSATVK 251
Cdd:PLN02429 303 TIVNSVTSK 311
PRK13962 PRK13962
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional
 3-249 2.70e-84

bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional


Pssm-ID: 237572 [Multi-domain]  Cd Length: 645  Bit Score: 263.90  E-value: 2.70e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973   3 RKFFVGGNWKCNGTTDQ----VDKIVKILNEGQiastdvVEVVVSPPYVFLPVVKSQLR-PEIQVAAQNCWVKKGGAFTG 77
Cdd:PRK13962 397 RKPIIAGNWKMNKTPAEakefVNELKKYVKDAQ------AEVVVCPPFTALPSVKEAVDgSNIKLGAQNVFYEEKGAYTG 470

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973  78 EVSAEMLVNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAI-----A 152
Cdd:PRK13962 471 EISGPMLAEIGVEYVIIGHSERRQYFGETDELVNKKVLAALKAGLTPILCVGETLDERESGITFDVVRLQLKAAlnglsA 550

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 153 ERIKDwtnVVVAYEPVWAIGTGKVATPDQAQEVHDGLRKWLAANVSAEVAESTRIIYGGSVTGANCKELAAKPDVDGFLV 232
Cdd:PRK13962 551 EQVKK---VVIAYEPVWAIGTGKVATPEQAQEVHAFIRKLVAELYGEEAARKVRILYGGSVKSENAAGLFNQPDIDGGLV 627

                        250
                 ....*....|....*...
gi 306415973 233 GGASLKP-EFIDIINSAT 249
Cdd:PRK13962 628 GGASLKAqEFAAIANYFI 645
tim TIGR00419
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ...
 6-240 6.38e-80

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: 238.93  E-value: 6.38e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973    6 FVGGNWK-CNGTTDQVDKIVKILNEgQIASTDVVEVVVSPPYVFLPVVKSQLrpEIQVAAQNCWVKKGGAFTGEVSAEML 84
Cdd:TIGR00419   1 LVIGNWKtYNESRGMRALEVAKIAE-EVASEAGVAVAVAPPFVDLPMIKREV--EIPVYAQHVDAVLSGAHTGEISAEML 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973   85 VNLSIPWVILGHSERRSLLGEsnefVGDKVAYALSQGLKVIACVgetleqresgstmDVVAAQTKAIAerikdWTNVVVA 164
Cdd:TIGR00419  78 KDIGAKGTLINHSERRMKLAD----IEKKIARLKELGLTSVVCT-------------NNVLTTAAAAA-----LEPDVVA 135

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 306415973  165 YEPVWAIGTGKVATPDQAQEVHDGLRkwlaanVSAEVAESTRIIYGGSVTGANCKELAAKPDVDGFLVGGASLKPE 240
Cdd:TIGR00419 136 VEPPELIGTGIPVSPAQPEVVHGSVR------AVKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
PRK14565 PRK14565
triosephosphate isomerase; Provisional
 5-248 1.13e-59

triosephosphate isomerase; Provisional


Pssm-ID: 237758  Cd Length: 237  Bit Score: 188.81  E-value: 1.13e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973   5 FFVGGNWKCNGTTDQVDKIVKILNEGQIASTDVVEVVVSPPYVFLPVVKSqLRPEIQVAAQNCWVKKGGAFTGEVSAEML 84
Cdd:PRK14565   3 FLIVANWKMNGDFSLFSSFLKELSNKLANNEITLKLVICPPFTAMSSFVE-CNPNIKLGAQNCFYGSSGGYTGEISAKML 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973  85 VNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKaiaERIKDWTNVVVA 164
Cdd:PRK14565  82 KECGCSYVILGHSERRSTFHETDSDIRLKAESAIESGLIPIICVGETLEDRENGMTKDVLLEQCS---NCLPKHGEFIIA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 165 YEPVWAIGTGKVATPDQAQEVHDGLRKWLAAnvsaevaesTRIIYGGSVTGANCKELAAKPDVDGFLVGGASLKPE-FID 243
Cdd:PRK14565 159 YEPVWAIGGSTIPSNDAIAEAFEIIRSYDSK---------SHIIYGGSVNQENIRDLKSINQLSGVLVGSASLDVDsFCK 229


                 ....*
gi 306415973 244 IINSA 248
Cdd:PRK14565 230 IIQQV 234
PRK14905 PRK14905
triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; ...
 1-233 2.27e-41

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


Pssm-ID: 184898 [Multi-domain]  Cd Length: 355  Bit Score: 144.79  E-value: 2.27e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973   1 MGRKFFVGGNWKC-NGTTDQVDKIVKILNEGQIASTDV-VEVVVSPPYVFLP----VVKSQL-RPEIQVAAQNCWVKKGG 73
Cdd:PRK14905   1 MAKKIYFGTNLKMyKGNAETVDYLSELLAFAEKFKSDYdIELFVIPSYIALKdaveAAASETgHPKIKIGAQNMNAKDKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973  74 AFTGEVSAEMLVNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIAE 153
Cdd:PRK14905  81 QFTGEISPLMLKELGIELVMIGHSERRHVLKETDQEENEKVLAALKHGFITLLCIGETLEQKNYNISDEVLRTQLKIGLH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 154 --RIKDWTNVVVAYEPVWAIGTGKV-ATPDQAQEVHDGLRKWLaANVSAEVAESTRIIYGGSVTGANCKELAAKPDVDGF 230
Cdd:PRK14905 161 gvSAEQLPHLFIAYEPVWAIGEGGIpASAEYADEKHAIIKQCL-FELFAEESKKIPVLYGGSVNLENANELIMKPHIDGL 239


                 ...
gi 306415973 231 LVG 233
Cdd:PRK14905 240 FIG 242
PRK15492 PRK15492
triosephosphate isomerase; Provisional
 3-233 2.48e-33

triosephosphate isomerase; Provisional


Pssm-ID: 185389  Cd Length: 260  Bit Score: 121.64  E-value: 2.48e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973   3 RKFFVGGNWKC-NGTTDQVDKIVKiLNE--GQIASTDVVEVVVSPPYVFLPVVKSQLRP-----EIQVAAQNCWVKKGGA 74
Cdd:PRK15492   2 KKIYFGTNLKMyKGIADATDFLAK-LSElaDDIPADKDIELFVIPSFTAIQDAIAATLAiphdhPIIIGAQNMNPNDNGQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973  75 FTGEVSAEMLVNLSIPWVILGHSERRSLLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAIAER 154
Cdd:PRK15492  81 FTGDISPLMLKEIGTQLVMIGHSERRHKFGETDQEENAKVLAALKHDFTTLLCVGETLEQKNYGISDEILRTQLKIGLHG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 155 I--KDWTNVVVAYEPVWAIGTGKV-ATPDQAQEVHDGLRKWLaANVSAEVAESTRIIYGGSVTGANCKELAAKPDVDGFL 231
Cdd:PRK15492 161 InpDQLAKLRIAYEPVWAIGEAGIpASADYADEKHAVIKQCL-IELFGDAGDDIPVFYGGSVNAENANELFGQPHIDGLF 239


                 ..
gi 306415973 232 VG 233
Cdd:PRK15492 240 IG 241
PRK04302 PRK04302
triosephosphate isomerase; Provisional
 38-238 2.28e-09

triosephosphate isomerase; Provisional


Pssm-ID: 235274  Cd Length: 223  Bit Score: 56.03  E-value: 2.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973  38 VEVVVSPPYVFLPVVKSQLrpEIQVAAQNCWVKKGGAFTGEVSAEMLVNLSIPWVILGHSERRSLLGEsnefVGDKVAYA 117
Cdd:PRK04302  37 VRIAVAPQALDIRRVAEEV--DIPVYAQHVDPVEPGSHTGHILPEAVKDAGAVGTLINHSERRLTLAD----IEAVVERA 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973 118 LSQGLKVIACVGEtleqresgstmdvvAAQTKAIAERIKDWtnvvVAYEPVWAIGTGK-VATPDQaqevhDGLRKwlAAN 196
Cdd:PRK04302 111 KKLGLESVVCVNN--------------PETSAAAAALGPDY----VAVEPPELIGTGIpVSKAKP-----EVVED--AVE 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 306415973 197 VSAEVAESTRIIYGGSVTGANCKELAAKPDVDGFLVGGASLK 238
Cdd:PRK04302 166 AVKKVNPDVKVLCGAGISTGEDVKAALELGADGVLLASGVVK 207
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 75-164 9.57e-03

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 37.16  E-value: 9.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306415973   75 FTGEVS-AEMLVNLSI-PWVILGHSerrslLGEsneFVGDKVAYALS--QGLKVIACVGETLEQRESGSTMDVVAAQTKA 150
Cdd:COG3321   597 FAVEYAlARLWRSWGVrPDAVIGHS-----VGE---YAAACVAGVLSleDALRLVAARGRLMQALPGGGAMLAVGLSEEE 668

                          90
                  ....*....|....
gi 306415973  151 IAERIKDWTNVVVA 164
Cdd:COG3321   669 VEALLAGYDGVSIA 682
 
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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