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Conserved domains on  [gi|260612904|gb|EEX38106|]
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triosephosphate isomerase [Vibrio metschnikovii CIP 69.14]

Protein Classification

triose-phosphate isomerase( domain architecture ID 10791623)

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
SCOP:  4003038

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
tpiA PRK00042
triosephosphate isomerase; Provisional
 2-240 4.63e-130

triosephosphate isomerase; Provisional


:

Pssm-ID: 234589  Cd Length: 250  Bit Score: 367.91  E-value: 4.63e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904   2 RRPVVMGNWKLNGSKTMVTELLNGLNAELEGVNGVDVAVAPPALYLDLAERLIKqgGNKIILGAQNTDLNNSGAFTGDMS 81
Cdd:PRK00042   1 RKPIIAGNWKMNKTLAEAKALVEELKAALPDADGVEVAVAPPFTALASVKEALK--GSNIKLGAQNVHPEDSGAFTGEIS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904  82 PAMLKDFGATHIIIGHSERRQYHHESDEFVAKKFAFLKENGLTPVFCIGESEAQNEAGETEAVCARQIDAVINAYGVEAL 161
Cdd:PRK00042  79 AEMLKDLGVKYVIIGHSERRQYFGETDELVNKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLEAALAGLSAEQF 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260612904 162 NDAIIAYEPIWAIGTGKAATADDAQRIHASIRAHIAAKSPAVAEQVIIQYGGSVKAENAEAYFSQPDIDGALVGGAALD 240
Cdd:PRK00042 159 ANLVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYGEVAEKVRILYGGSVKPDNAAELMAQPDIDGALVGGASLK 237
 
Name Accession Description Interval E-value
tpiA PRK00042
triosephosphate isomerase; Provisional
 2-240 4.63e-130

triosephosphate isomerase; Provisional


Pssm-ID: 234589  Cd Length: 250  Bit Score: 367.91  E-value: 4.63e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904   2 RRPVVMGNWKLNGSKTMVTELLNGLNAELEGVNGVDVAVAPPALYLDLAERLIKqgGNKIILGAQNTDLNNSGAFTGDMS 81
Cdd:PRK00042   1 RKPIIAGNWKMNKTLAEAKALVEELKAALPDADGVEVAVAPPFTALASVKEALK--GSNIKLGAQNVHPEDSGAFTGEIS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904  82 PAMLKDFGATHIIIGHSERRQYHHESDEFVAKKFAFLKENGLTPVFCIGESEAQNEAGETEAVCARQIDAVINAYGVEAL 161
Cdd:PRK00042  79 AEMLKDLGVKYVIIGHSERRQYFGETDELVNKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLEAALAGLSAEQF 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260612904 162 NDAIIAYEPIWAIGTGKAATADDAQRIHASIRAHIAAKSPAVAEQVIIQYGGSVKAENAEAYFSQPDIDGALVGGAALD 240
Cdd:PRK00042 159 ANLVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYGEVAEKVRILYGGSVKPDNAAELMAQPDIDGALVGGASLK 237
TpiA COG0149
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ...
 1-240 8.72e-130

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: 367.07  E-value: 8.72e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904   1 MRRPVVMGNWKLNGSKTMVTELLNGLNAELEGVNGVDVAVAPPALYLDLAERLIKqgGNKIILGAQNTDLNNSGAFTGDM 80
Cdd:COG0149    1 MRKPLIAGNWKMNGTLAEAKALLAALAAALADLADVEVVVCPPFTYLAAVAEALA--GSPIALGAQNVHWEDSGAYTGEI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904  81 SPAMLKDFGATHIIIGHSERRQYHHESDEFVAKKFAFLKENGLTPVFCIGESEAQNEAGETEAVCARQIDAVINAYGVEA 160
Cdd:COG0149   79 SAAMLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLSAEQ 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904 161 LNDAIIAYEPIWAIGTGKAATADDAQRIHASIRAHIAAK-SPAVAEQVIIQYGGSVKAENAEAYFSQPDIDGALVGGAAL 239
Cdd:COG0149  159 AANVVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELyGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASL 238


                 .
gi 260612904 240 D 240
Cdd:COG0149  239 D 239
TIM pfam00121
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ...
 4-240 4.77e-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: 342.18  E-value: 4.77e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904    4 PVVMGNWKLNGSKTMVTELLNGLNAELEGVNGVDVAVAPPALYLDlaeRLIKQGGNKIILGAQNTDLNNSGAFTGDMSPA 83
Cdd:pfam00121   1 PIIAGNWKMNGTLAEAAELLAELAEALADESGVEVVVAPPFTYLS---AVAELLGSNIKVGAQNVDPEESGAFTGEISAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904   84 MLKDFGATHIIIGHSERRQYHHESDEFVAKKFAFLKENGLTPVFCIGESEAQNEAGETEAVCARQIDAVINAYGVEALND 163
Cdd:pfam00121  78 MLKDLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQKNL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260612904  164 aIIAYEPIWAIGTGKAATADDAQRIHASIRAHIAAKSPAVAEQVIIQYGGSVKAENAEAYFSQPDIDGALVGGAALD 240
Cdd:pfam00121 158 -VIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLK 233
TIM cd00311
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ...
 4-240 6.18e-119

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: 339.51  E-value: 6.18e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904   4 PVVMGNWKLNGSKTMVTELLNGLNAELEGVNGVDVAVAPPALYLDLAERLIKqgGNKIILGAQNTDLNNSGAFTGDMSPA 83
Cdd:cd00311    1 PLVAGNWKMNGTLAEALELAKALNAVLKDESGVEVVVAPPFTYLAAVAEALE--GSKIKVGAQNVSPEDSGAFTGEISAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904  84 MLKDFGATHIIIGHSERRQYHHESDEFVAKKFAFLKENGLTPVFCIGESEAQNEAGETEAVCARQIDAVINayGVEALND 163
Cdd:cd00311   79 MLKDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLA--GVEDLAP 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260612904 164 AIIAYEPIWAIGTGKAATADDAQRIHASIRAHIAAKSPAVAEQVIIQYGGSVKAENAEAYFSQPDIDGALVGGAALD 240
Cdd:cd00311  157 VVIAYEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYGEVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLK 233
tim TIGR00419
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ...
 5-239 1.65e-60

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: 190.01  E-value: 1.65e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904    5 VVMGNWK-LNGSKTMVTELLNGLNAELEGVNGVDVAVAPPALYLDLAERLIKqggnkIILGAQNTDLNNSGAFTGDMSPA 83
Cdd:TIGR00419   1 LVIGNWKtYNESRGMRALEVAKIAEEVASEAGVAVAVAPPFVDLPMIKREVE-----IPVYAQHVDAVLSGAHTGEISAE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904   84 MLKDFGATHIIIGHSERRqyHHESDefVAKKFAFLKENGLTPVFCigeseaqneageteavcarqIDAVINAYGVEALND 163
Cdd:TIGR00419  76 MLKDIGAKGTLINHSERR--MKLAD--IEKKIARLKELGLTSVVC--------------------TNNVLTTAAAAALEP 131

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260612904  164 AIIAYEPIWAIGTGKAATADDAQRIHASIRAhiaakSPAVAEQVIIQYGGSVKAENAEAYFSQPDIDGALVGGAAL 239
Cdd:TIGR00419 132 DVVAVEPPELIGTGIPVSPAQPEVVHGSVRA-----VKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSL 202
 
Name Accession Description Interval E-value
tpiA PRK00042
triosephosphate isomerase; Provisional
 2-240 4.63e-130

triosephosphate isomerase; Provisional


Pssm-ID: 234589  Cd Length: 250  Bit Score: 367.91  E-value: 4.63e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904   2 RRPVVMGNWKLNGSKTMVTELLNGLNAELEGVNGVDVAVAPPALYLDLAERLIKqgGNKIILGAQNTDLNNSGAFTGDMS 81
Cdd:PRK00042   1 RKPIIAGNWKMNKTLAEAKALVEELKAALPDADGVEVAVAPPFTALASVKEALK--GSNIKLGAQNVHPEDSGAFTGEIS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904  82 PAMLKDFGATHIIIGHSERRQYHHESDEFVAKKFAFLKENGLTPVFCIGESEAQNEAGETEAVCARQIDAVINAYGVEAL 161
Cdd:PRK00042  79 AEMLKDLGVKYVIIGHSERRQYFGETDELVNKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLEAALAGLSAEQF 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260612904 162 NDAIIAYEPIWAIGTGKAATADDAQRIHASIRAHIAAKSPAVAEQVIIQYGGSVKAENAEAYFSQPDIDGALVGGAALD 240
Cdd:PRK00042 159 ANLVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYGEVAEKVRILYGGSVKPDNAAELMAQPDIDGALVGGASLK 237
TpiA COG0149
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ...
 1-240 8.72e-130

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: 367.07  E-value: 8.72e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904   1 MRRPVVMGNWKLNGSKTMVTELLNGLNAELEGVNGVDVAVAPPALYLDLAERLIKqgGNKIILGAQNTDLNNSGAFTGDM 80
Cdd:COG0149    1 MRKPLIAGNWKMNGTLAEAKALLAALAAALADLADVEVVVCPPFTYLAAVAEALA--GSPIALGAQNVHWEDSGAYTGEI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904  81 SPAMLKDFGATHIIIGHSERRQYHHESDEFVAKKFAFLKENGLTPVFCIGESEAQNEAGETEAVCARQIDAVINAYGVEA 160
Cdd:COG0149   79 SAAMLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLSAEQ 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904 161 LNDAIIAYEPIWAIGTGKAATADDAQRIHASIRAHIAAK-SPAVAEQVIIQYGGSVKAENAEAYFSQPDIDGALVGGAAL 239
Cdd:COG0149  159 AANVVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELyGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASL 238


                 .
gi 260612904 240 D 240
Cdd:COG0149  239 D 239
TIM pfam00121
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ...
 4-240 4.77e-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: 342.18  E-value: 4.77e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904    4 PVVMGNWKLNGSKTMVTELLNGLNAELEGVNGVDVAVAPPALYLDlaeRLIKQGGNKIILGAQNTDLNNSGAFTGDMSPA 83
Cdd:pfam00121   1 PIIAGNWKMNGTLAEAAELLAELAEALADESGVEVVVAPPFTYLS---AVAELLGSNIKVGAQNVDPEESGAFTGEISAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904   84 MLKDFGATHIIIGHSERRQYHHESDEFVAKKFAFLKENGLTPVFCIGESEAQNEAGETEAVCARQIDAVINAYGVEALND 163
Cdd:pfam00121  78 MLKDLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQKNL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260612904  164 aIIAYEPIWAIGTGKAATADDAQRIHASIRAHIAAKSPAVAEQVIIQYGGSVKAENAEAYFSQPDIDGALVGGAALD 240
Cdd:pfam00121 158 -VIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLK 233
TIM cd00311
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ...
 4-240 6.18e-119

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: 339.51  E-value: 6.18e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904   4 PVVMGNWKLNGSKTMVTELLNGLNAELEGVNGVDVAVAPPALYLDLAERLIKqgGNKIILGAQNTDLNNSGAFTGDMSPA 83
Cdd:cd00311    1 PLVAGNWKMNGTLAEALELAKALNAVLKDESGVEVVVAPPFTYLAAVAEALE--GSKIKVGAQNVSPEDSGAFTGEISAE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904  84 MLKDFGATHIIIGHSERRQYHHESDEFVAKKFAFLKENGLTPVFCIGESEAQNEAGETEAVCARQIDAVINayGVEALND 163
Cdd:cd00311   79 MLKDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLA--GVEDLAP 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 260612904 164 AIIAYEPIWAIGTGKAATADDAQRIHASIRAHIAAKSPAVAEQVIIQYGGSVKAENAEAYFSQPDIDGALVGGAALD 240
Cdd:cd00311  157 VVIAYEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYGEVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLK 233
PTZ00333 PTZ00333
triosephosphate isomerase; Provisional
 1-240 1.33e-98

triosephosphate isomerase; Provisional


Pssm-ID: 240365  Cd Length: 255  Bit Score: 288.35  E-value: 1.33e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904   1 MRRPVVMGNWKLNGSKTMVTELLNGLNAELEGVNGVDVAVAPPALYLDLAERLIKQGGNKIilGAQNTDLNNSGAFTGDM 80
Cdd:PTZ00333   3 KRKPFVGGNWKCNGTKASIKELIDSFNKLKFDPNNVDVVVAPPSLHIPLVQEKLKNKNFKI--SSQNVSLTGSGAFTGEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904  81 SPAMLKDFGATHIIIGHSERRQYHHESDEFVAKKFAFLKENGLTPVFCIGESEAQNEAGETEAVCARQIDAVINAYGVEA 160
Cdd:PTZ00333  81 SAEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904 161 LNDAIIAYEPIWAIGTGKAATADDAQRIHASIRAHIAAK-SPAVAEQVIIQYGGSVKAENAEAYFSQPDIDGALVGGAAL 239
Cdd:PTZ00333 161 WDNIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAEKvGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASL 240


                 .
gi 260612904 240 D 240
Cdd:PTZ00333 241 K 241
PRK13962 PRK13962
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional
 1-240 1.84e-80

bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional


Pssm-ID: 237572 [Multi-domain]  Cd Length: 645  Bit Score: 254.27  E-value: 1.84e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904   1 MRRPVVMGNWKLNGSKTMVTELLNGLNAELEGVNGvDVAVAPPALYLDLAERLIKqgGNKIILGAQNTDLNNSGAFTGDM 80
Cdd:PRK13962 396 PRKPIIAGNWKMNKTPAEAKEFVNELKKYVKDAQA-EVVVCPPFTALPSVKEAVD--GSNIKLGAQNVFYEEKGAYTGEI 472

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904  81 SPAMLKDFGATHIIIGHSERRQYHHESDEFVAKKFAFLKENGLTPVFCIGESEAQNEAGETEAVCARQIDAVINAYGVEA 160
Cdd:PRK13962 473 SGPMLAEIGVEYVIIGHSERRQYFGETDELVNKKVLAALKAGLTPILCVGETLDERESGITFDVVRLQLKAALNGLSAEQ 552

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904 161 LNDAIIAYEPIWAIGTGKAATADDAQRIHASIRAHIAAK-SPAVAEQVIIQYGGSVKAENAEAYFSQPDIDGALVGGAAL 239
Cdd:PRK13962 553 VKKVVIAYEPVWAIGTGKVATPEQAQEVHAFIRKLVAELyGEEAARKVRILYGGSVKSENAAGLFNQPDIDGGLVGGASL 632


                 .
gi 260612904 240 D 240
Cdd:PRK13962 633 K 633
PLN02561 PLN02561
triosephosphate isomerase
 2-239 7.12e-64

triosephosphate isomerase


Pssm-ID: 178175  Cd Length: 253  Bit Score: 200.05  E-value: 7.12e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904   2 RRPVVMGNWKLNGSKTMVTELLNGLN-AELEGVNGVDVAVAPPALYLDLAERLIKQggnKIILGAQNTDLNNSGAFTGDM 80
Cdd:PLN02561   3 RKFFVGGNWKCNGTVEEVKKIVTTLNeAEVPSEDVVEVVVSPPFVFLPLVKSLLRP---DFQVAAQNCWVKKGGAFTGEI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904  81 SPAMLKDFGATHIIIGHSERRQYHHESDEFVAKKFAFLKENGLTPVFCIGESEAQNEAGETEAVCARQIDAVinAYGVEA 160
Cdd:PLN02561  80 SAEMLVNLGIPWVILGHSERRALLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAI--ADKVSD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904 161 LNDAIIAYEPIWAIGTGKAATADDAQRIHASIRAHIAAK-SPAVAEQVIIQYGGSVKAENAEAYFSQPDIDGALVGGAAL 239
Cdd:PLN02561 158 WANVVLAYEPVWAIGTGKVATPAQAQEVHDELRKWLHKNvSPEVAATTRIIYGGSVTGANCKELAAQPDVDGFLVGGASL 237
tim TIGR00419
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ...
 5-239 1.65e-60

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: 190.01  E-value: 1.65e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904    5 VVMGNWK-LNGSKTMVTELLNGLNAELEGVNGVDVAVAPPALYLDLAERLIKqggnkIILGAQNTDLNNSGAFTGDMSPA 83
Cdd:TIGR00419   1 LVIGNWKtYNESRGMRALEVAKIAEEVASEAGVAVAVAPPFVDLPMIKREVE-----IPVYAQHVDAVLSGAHTGEISAE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904   84 MLKDFGATHIIIGHSERRqyHHESDefVAKKFAFLKENGLTPVFCigeseaqneageteavcarqIDAVINAYGVEALND 163
Cdd:TIGR00419  76 MLKDIGAKGTLINHSERR--MKLAD--IEKKIARLKELGLTSVVC--------------------TNNVLTTAAAAALEP 131

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260612904  164 AIIAYEPIWAIGTGKAATADDAQRIHASIRAhiaakSPAVAEQVIIQYGGSVKAENAEAYFSQPDIDGALVGGAAL 239
Cdd:TIGR00419 132 DVVAVEPPELIGTGIPVSPAQPEVVHGSVRA-----VKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSL 202
PLN02429 PLN02429
triosephosphate isomerase
 3-239 9.82e-50

triosephosphate isomerase


Pssm-ID: 166070  Cd Length: 315  Bit Score: 165.73  E-value: 9.82e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904   3 RPVVMGNWKLNGSKTMVTELLNGLN-AELEGvnGVDVAVAPPALYLDLAERLIKqggNKIILGAQNTDLNNSGAFTGDMS 81
Cdd:PLN02429  65 KFFVGGNWKCNGTKDSIAKLISDLNsATLEA--DVDVVVSPPFVYIDQVKSSLT---DRIDISGQNSWVGKGGAFTGEIS 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904  82 PAMLKDFGATHIIIGHSERRQYHHESDEFVAKKFAFLKENGLTPVFCIGESEAQNEAGETEAVCARQIDAVINAygVEAL 161
Cdd:PLN02429 140 VEQLKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADA--VPSW 217

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 260612904 162 NDAIIAYEPIWAIGTGKAATADDAQRIHASIRAHIAAK-SPAVAEQVIIQYGGSVKAENAEAYFSQPDIDGALVGGAAL 239
Cdd:PLN02429 218 DNIVVAYEPVWAIGTGKVASPQQAQEVHVAVRGWLKKNvSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASL 296
PRK14565 PRK14565
triosephosphate isomerase; Provisional
 6-240 4.97e-43

triosephosphate isomerase; Provisional


Pssm-ID: 237758  Cd Length: 237  Bit Score: 146.06  E-value: 4.97e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904   6 VMGNWKLNGSKTMVTELLNGLNAELEGVNG-VDVAVAPPALYLDLaerlIKQGGNKIILGAQNTDLNNSGAFTGDMSPAM 84
Cdd:PRK14565   5 IVANWKMNGDFSLFSSFLKELSNKLANNEItLKLVICPPFTAMSS----FVECNPNIKLGAQNCFYGSSGGYTGEISAKM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904  85 LKDFGATHIIIGHSERRQYHHESDEFVAKKFAFLKENGLTPVFCIGESEAQNEAGETEAVCARQIDAVINAYGvealnDA 164
Cdd:PRK14565  81 LKECGCSYVILGHSERRSTFHETDSDIRLKAESAIESGLIPIICVGETLEDRENGMTKDVLLEQCSNCLPKHG-----EF 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260612904 165 IIAYEPIWAIGTGKAATADDAQRIHASIRAHIAAKSpavaeqviIQYGGSVKAENAEAYFSQPDIDGALVGGAALD 240
Cdd:PRK14565 156 IIAYEPVWAIGGSTIPSNDAIAEAFEIIRSYDSKSH--------IIYGGSVNQENIRDLKSINQLSGVLVGSASLD 223
PRK15492 PRK15492
triosephosphate isomerase; Provisional
 17-240 7.40e-40

triosephosphate isomerase; Provisional


Pssm-ID: 185389  Cd Length: 260  Bit Score: 138.59  E-value: 7.40e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904  17 TMVTELLNGLNAElegvNGVDVAVAPP--ALYLDLAERLIKQGGNKIILGAQNTDLNNSGAFTGDMSPAMLKDFGATHII 94
Cdd:PRK15492  24 AKLSELADDIPAD----KDIELFVIPSftAIQDAIAATLAIPHDHPIIIGAQNMNPNDNGQFTGDISPLMLKEIGTQLVM 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904  95 IGHSERRQYHHESD-EFVAKKFAFLKENgLTPVFCIGESEAQNEAGETEAVCARQIDAVINAYGVEALNDAIIAYEPIWA 173
Cdd:PRK15492 100 IGHSERRHKFGETDqEENAKVLAALKHD-FTTLLCVGETLEQKNYGISDEILRTQLKIGLHGINPDQLAKLRIAYEPVWA 178

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 260612904 174 IGT-GKAATADDAQRIHASIRAHIAAKSPAVAEQVIIQYGGSVKAENAEAYFSQPDIDGALVGGAALD 240
Cdd:PRK15492 179 IGEaGIPASADYADEKHAVIKQCLIELFGDAGDDIPVFYGGSVNAENANELFGQPHIDGLFIGRSAWD 246
PRK14905 PRK14905
triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; ...
 19-240 5.54e-38

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


Pssm-ID: 184898 [Multi-domain]  Cd Length: 355  Bit Score: 136.31  E-value: 5.54e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904  19 VTELLNgLNAELEGVNGVDVAVAPPALYLDLAERLIKQ--GGNKIILGAQNTDLNNSGAFTGDMSPAMLKDFGATHIIIG 96
Cdd:PRK14905  24 LSELLA-FAEKFKSDYDIELFVIPSYIALKDAVEAAASetGHPKIKIGAQNMNAKDKGQFTGEISPLMLKELGIELVMIG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904  97 HSERRQYHHESD-EFVAKKFAFLKENGLTpVFCIGESEAQNEAGETEAVCARQIDAVINAYGVEALNDAIIAYEPIWAIG 175
Cdd:PRK14905 103 HSERRHVLKETDqEENEKVLAALKHGFIT-LLCIGETLEQKNYNISDEVLRTQLKIGLHGVSAEQLPHLFIAYEPVWAIG 181

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260612904 176 TGK-AATADDAQRIHASIRAHIAAKSPAVAEQVIIQYGGSVKAENAEAYFSQPDIDGALVGGAALD 240
Cdd:PRK14905 182 EGGiPASAEYADEKHAIIKQCLFELFAEESKKIPVLYGGSVNLENANELIMKPHIDGLFIGRSAWD 247
PRK04302 PRK04302
triosephosphate isomerase; Provisional
 35-217 2.83e-10

triosephosphate isomerase; Provisional


Pssm-ID: 235274  Cd Length: 223  Bit Score: 58.34  E-value: 2.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904  35 GVDVAVAPPALYLdlaeRLIKQGGNkIILGAQNTDLNNSGAFTGDMSPAMLKDFGATHIIIGHSERRQYHHESDEFVAKk 114
Cdd:PRK04302  36 GVRIAVAPQALDI----RRVAEEVD-IPVYAQHVDPVEPGSHTGHILPEAVKDAGAVGTLINHSERRLTLADIEAVVER- 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260612904 115 fafLKENGLTPVfcigeseaqneageteaVCArqiDAVINAYGVEALNDAIIAYEPIWAIGTGKAATADDAQRIHASIRA 194
Cdd:PRK04302 110 ---AKKLGLESV-----------------VCV---NNPETSAAAAALGPDYVAVEPPELIGTGIPVSKAKPEVVEDAVEA 166

                        170       180
                 ....*....|....*....|....*..
gi 260612904 195 hIAAKSPAVAeqVI----IQYGGSVKA 217
Cdd:PRK04302 167 -VKKVNPDVK--VLcgagISTGEDVKA 190
 
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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