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Conserved domains on  [gi|489958712|ref|WP_003862019|]
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MULTISPECIES: triose-phosphate isomerase [Enterobacter]

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
 2-251 2.22e-142

triosephosphate isomerase; Provisional


:

Pssm-ID: 234589  Cd Length: 250  Bit Score: 399.11  E-value: 2.22e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712   2 RHPLVMGNWKLNGSRHMVNELVANLRKELAGVTGCAVAIAPPDMYLDLAKRAADGSHIILGAQNVDVNLSGAFTGETSAE 81
Cdd:PRK00042   1 RKPIIAGNWKMNKTLAEAKALVEELKAALPDADGVEVAVAPPFTALASVKEALKGSNIKLGAQNVHPEDSGAFTGEISAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712  82 MLKDIGAKYIIIGHSERRTYHKESDEFIAKKFAVLKEQGLIPVLCIGETEAENEAGKTEEVCARQIDAVLKTQGAAAFEG 161
Cdd:PRK00042  81 MLKDLGVKYVIIGHSERRQYFGETDELVNKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLEAALAGLSAEQFAN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712 162 AVIAYEPVWAIGTGKSATPAQAQAVHKFIRDHIAKADAKVAEQVIIQYGGSVNASNAAELFTQPDIDGALVGGASLKADA 241
Cdd:PRK00042 161 LVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYGEVAEKVRILYGGSVKPDNAAELMAQPDIDGALVGGASLKAED 240

                        250
                 ....*....|
gi 489958712 242 FAVIVKAAEA 251
Cdd:PRK00042 241 FLAIVKAAAA 250
 
Name Accession Description Interval E-value
tpiA PRK00042
triosephosphate isomerase; Provisional
 2-251 2.22e-142

triosephosphate isomerase; Provisional


Pssm-ID: 234589  Cd Length: 250  Bit Score: 399.11  E-value: 2.22e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712   2 RHPLVMGNWKLNGSRHMVNELVANLRKELAGVTGCAVAIAPPDMYLDLAKRAADGSHIILGAQNVDVNLSGAFTGETSAE 81
Cdd:PRK00042   1 RKPIIAGNWKMNKTLAEAKALVEELKAALPDADGVEVAVAPPFTALASVKEALKGSNIKLGAQNVHPEDSGAFTGEISAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712  82 MLKDIGAKYIIIGHSERRTYHKESDEFIAKKFAVLKEQGLIPVLCIGETEAENEAGKTEEVCARQIDAVLKTQGAAAFEG 161
Cdd:PRK00042  81 MLKDLGVKYVIIGHSERRQYFGETDELVNKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLEAALAGLSAEQFAN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712 162 AVIAYEPVWAIGTGKSATPAQAQAVHKFIRDHIAKADAKVAEQVIIQYGGSVNASNAAELFTQPDIDGALVGGASLKADA 241
Cdd:PRK00042 161 LVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYGEVAEKVRILYGGSVKPDNAAELMAQPDIDGALVGGASLKAED 240

                        250
                 ....*....|
gi 489958712 242 FAVIVKAAEA 251
Cdd:PRK00042 241 FLAIVKAAAA 250
TpiA COG0149
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ...
 1-248 2.09e-140

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: 394.04  E-value: 2.09e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712   1 MRHPLVMGNWKLNGSRHMVNELVANLRKELAGVTGCAVAIAPPDMYLDLAKRAADGSHIILGAQNVDVNLSGAFTGETSA 80
Cdd:COG0149    1 MRKPLIAGNWKMNGTLAEAKALLAALAAALADLADVEVVVCPPFTYLAAVAEALAGSPIALGAQNVHWEDSGAYTGEISA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712  81 EMLKDIGAKYIIIGHSERRTYHKESDEFIAKKFAVLKEQGLIPVLCIGETEAENEAGKTEEVCARQIDAVLKTQGAAAFE 160
Cdd:COG0149   81 AMLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLSAEQAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712 161 GAVIAYEPVWAIGTGKSATPAQAQAVHKFIRDHIAKA-DAKVAEQVIIQYGGSVNASNAAELFTQPDIDGALVGGASLKA 239
Cdd:COG0149  161 NVVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELyGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDA 240


                 ....*....
gi 489958712 240 DAFAVIVKA 248
Cdd:COG0149  241 EDFLAIVRA 249
TIM cd00311
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ...
 4-247 3.88e-128

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: 362.62  E-value: 3.88e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712   4 PLVMGNWKLNGSRHMVNELVANLRKELAGVTGCAVAIAPPDMYLDLAKRAADGSHIILGAQNVDVNLSGAFTGETSAEML 83
Cdd:cd00311    1 PLVAGNWKMNGTLAEALELAKALNAVLKDESGVEVVVAPPFTYLAAVAEALEGSKIKVGAQNVSPEDSGAFTGEISAEML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712  84 KDIGAKYIIIGHSERRTYHKESDEFIAKKFAVLKEQGLIPVLCIGETEAENEAGKTEEVCARQIDAVLKtqGAAAFEGAV 163
Cdd:cd00311   81 KDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLA--GVEDLAPVV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712 164 IAYEPVWAIGTGKSATPAQAQAVHKFIRDHIAKADAKVAEQVIIQYGGSVNASNAAELFTQPDIDGALVGGASLKADAFA 243
Cdd:cd00311  159 IAYEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYGEVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAESFL 238


                 ....
gi 489958712 244 VIVK 247
Cdd:cd00311  239 DIIK 242
TIM pfam00121
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ...
 4-249 1.79e-126

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: 358.36  E-value: 1.79e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712    4 PLVMGNWKLNGSRHMVNELVANLRKELAGVTGCAVAIAPPDMYLDLAKRAADgSHIILGAQNVDVNLSGAFTGETSAEML 83
Cdd:pfam00121   1 PIIAGNWKMNGTLAEAAELLAELAEALADESGVEVVVAPPFTYLSAVAELLG-SNIKVGAQNVDPEESGAFTGEISAEML 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712   84 KDIGAKYIIIGHSERRTYHKESDEFIAKKFAVLKEQGLIPVLCIGETEAENEAGKTEEVCARQIDAVLKTQGAAAfEGAV 163
Cdd:pfam00121  80 KDLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQ-KNLV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712  164 IAYEPVWAIGTGKSATPAQAQAVHKFIRDHIAKADAKVAEQVIIQYGGSVNASNAAELFTQPDIDGALVGGASLKADAFA 243
Cdd:pfam00121 159 IAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEDFL 238


                  ....*.
gi 489958712  244 VIVKAA 249
Cdd:pfam00121 239 DIINAA 244
tim TIGR00419
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ...
 5-240 7.89e-88

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: 259.35  E-value: 7.89e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712    5 LVMGNWK-LNGSRHMVNELVANLRKELAGVTGCAVAIAPPDMYLDLAKRAADgshIILGAQNVDVNLSGAFTGETSAEML 83
Cdd:TIGR00419   1 LVIGNWKtYNESRGMRALEVAKIAEEVASEAGVAVAVAPPFVDLPMIKREVE---IPVYAQHVDAVLSGAHTGEISAEML 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712   84 KDIGAKYIIIGHSERRtyHKESDefIAKKFAVLKEQGLIPVLCIgeteaeneagkteevcarqiDAVLKTQGAAAFEGAV 163
Cdd:TIGR00419  78 KDIGAKGTLINHSERR--MKLAD--IEKKIARLKELGLTSVVCT--------------------NNVLTTAAAAALEPDV 133

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489958712  164 IAYEPVWAIGTGKSATPAQAQAVHKFIRdhiakADAKVAEQVIIQYGGSVNASNAAELFTQPDIDGALVGGASLKAD 240
Cdd:TIGR00419 134 VAVEPPELIGTGIPVSPAQPEVVHGSVR-----AVKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
 
Name Accession Description Interval E-value
tpiA PRK00042
triosephosphate isomerase; Provisional
 2-251 2.22e-142

triosephosphate isomerase; Provisional


Pssm-ID: 234589  Cd Length: 250  Bit Score: 399.11  E-value: 2.22e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712   2 RHPLVMGNWKLNGSRHMVNELVANLRKELAGVTGCAVAIAPPDMYLDLAKRAADGSHIILGAQNVDVNLSGAFTGETSAE 81
Cdd:PRK00042   1 RKPIIAGNWKMNKTLAEAKALVEELKAALPDADGVEVAVAPPFTALASVKEALKGSNIKLGAQNVHPEDSGAFTGEISAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712  82 MLKDIGAKYIIIGHSERRTYHKESDEFIAKKFAVLKEQGLIPVLCIGETEAENEAGKTEEVCARQIDAVLKTQGAAAFEG 161
Cdd:PRK00042  81 MLKDLGVKYVIIGHSERRQYFGETDELVNKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLEAALAGLSAEQFAN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712 162 AVIAYEPVWAIGTGKSATPAQAQAVHKFIRDHIAKADAKVAEQVIIQYGGSVNASNAAELFTQPDIDGALVGGASLKADA 241
Cdd:PRK00042 161 LVIAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYGEVAEKVRILYGGSVKPDNAAELMAQPDIDGALVGGASLKAED 240

                        250
                 ....*....|
gi 489958712 242 FAVIVKAAEA 251
Cdd:PRK00042 241 FLAIVKAAAA 250
TpiA COG0149
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ...
 1-248 2.09e-140

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: 394.04  E-value: 2.09e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712   1 MRHPLVMGNWKLNGSRHMVNELVANLRKELAGVTGCAVAIAPPDMYLDLAKRAADGSHIILGAQNVDVNLSGAFTGETSA 80
Cdd:COG0149    1 MRKPLIAGNWKMNGTLAEAKALLAALAAALADLADVEVVVCPPFTYLAAVAEALAGSPIALGAQNVHWEDSGAYTGEISA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712  81 EMLKDIGAKYIIIGHSERRTYHKESDEFIAKKFAVLKEQGLIPVLCIGETEAENEAGKTEEVCARQIDAVLKTQGAAAFE 160
Cdd:COG0149   81 AMLKDLGCRYVIVGHSERRQYFGETDELVNKKVKAALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLSAEQAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712 161 GAVIAYEPVWAIGTGKSATPAQAQAVHKFIRDHIAKA-DAKVAEQVIIQYGGSVNASNAAELFTQPDIDGALVGGASLKA 239
Cdd:COG0149  161 NVVIAYEPVWAIGTGKTATPEQAQEVHAFIRALLAELyGAEVAEAVRILYGGSVKPGNAAELFAQPDIDGALVGGASLDA 240


                 ....*....
gi 489958712 240 DAFAVIVKA 248
Cdd:COG0149  241 EDFLAIVRA 249
TIM cd00311
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ...
 4-247 3.88e-128

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: 362.62  E-value: 3.88e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712   4 PLVMGNWKLNGSRHMVNELVANLRKELAGVTGCAVAIAPPDMYLDLAKRAADGSHIILGAQNVDVNLSGAFTGETSAEML 83
Cdd:cd00311    1 PLVAGNWKMNGTLAEALELAKALNAVLKDESGVEVVVAPPFTYLAAVAEALEGSKIKVGAQNVSPEDSGAFTGEISAEML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712  84 KDIGAKYIIIGHSERRTYHKESDEFIAKKFAVLKEQGLIPVLCIGETEAENEAGKTEEVCARQIDAVLKtqGAAAFEGAV 163
Cdd:cd00311   81 KDAGAKYVIIGHSERRQYFGETDEDVAKKVKAALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLA--GVEDLAPVV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712 164 IAYEPVWAIGTGKSATPAQAQAVHKFIRDHIAKADAKVAEQVIIQYGGSVNASNAAELFTQPDIDGALVGGASLKADAFA 243
Cdd:cd00311  159 IAYEPVWAIGTGKTASPEQAQEVHAFIRKLLAELYGEVAEKVRILYGGSVNPENAAELLAQPDIDGVLVGGASLKAESFL 238


                 ....
gi 489958712 244 VIVK 247
Cdd:cd00311  239 DIIK 242
TIM pfam00121
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ...
 4-249 1.79e-126

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: 358.36  E-value: 1.79e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712    4 PLVMGNWKLNGSRHMVNELVANLRKELAGVTGCAVAIAPPDMYLDLAKRAADgSHIILGAQNVDVNLSGAFTGETSAEML 83
Cdd:pfam00121   1 PIIAGNWKMNGTLAEAAELLAELAEALADESGVEVVVAPPFTYLSAVAELLG-SNIKVGAQNVDPEESGAFTGEISAEML 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712   84 KDIGAKYIIIGHSERRTYHKESDEFIAKKFAVLKEQGLIPVLCIGETEAENEAGKTEEVCARQIDAVLKTQGAAAfEGAV 163
Cdd:pfam00121  80 KDLGVSYVIIGHSERRQYFGETDEDVAKKVKAALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQ-KNLV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712  164 IAYEPVWAIGTGKSATPAQAQAVHKFIRDHIAKADAKVAEQVIIQYGGSVNASNAAELFTQPDIDGALVGGASLKADAFA 243
Cdd:pfam00121 159 IAYEPVWAIGTGKTATPEQAQEVHAFIRAVLAELYKEVAEGVRILYGGSVKPGNAAELAAQPDIDGALVGGASLKAEDFL 238


                  ....*.
gi 489958712  244 VIVKAA 249
Cdd:pfam00121 239 DIINAA 244
PTZ00333 PTZ00333
triosephosphate isomerase; Provisional
 1-253 1.44e-100

triosephosphate isomerase; Provisional


Pssm-ID: 240365  Cd Length: 255  Bit Score: 293.36  E-value: 1.44e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712   1 MRHPLVMGNWKLNGSRHMVNELVANLRKELAGVTGCAVAIAPPDMYLDLAKRAADGSHIILGAQNVDVNLSGAFTGETSA 80
Cdd:PTZ00333   3 KRKPFVGGNWKCNGTKASIKELIDSFNKLKFDPNNVDVVVAPPSLHIPLVQEKLKNKNFKISSQNVSLTGSGAFTGEISA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712  81 EMLKDIGAKYIIIGHSERRTYHKESDEFIAKKFAVLKEQGLIPVLCIGETEAENEAGKTEEVCARQIDAVLKTQGAAAFE 160
Cdd:PTZ00333  83 EMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNALENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDEAWD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712 161 GAVIAYEPVWAIGTGKSATPAQAQAVHKFIRDHIA-KADAKVAEQVIIQYGGSVNASNAAELFTQPDIDGALVGGASLKA 239
Cdd:PTZ00333 163 NIVIAYEPVWAIGTGKVATPEQAQEVHAFIRKWLAeKVGADVAEATRIIYGGSVNEKNCKELIKQPDIDGFLVGGASLKP 242

                        250
                 ....*....|....
gi 489958712 240 DaFAVIVKAAEAAK 253
Cdd:PTZ00333 243 D-FVDIIKSAEQSK 255
PRK13962 PRK13962
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional
 1-248 6.68e-89

bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional


Pssm-ID: 237572 [Multi-domain]  Cd Length: 645  Bit Score: 275.84  E-value: 6.68e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712   1 MRHPLVMGNWKLNGSRHMVNELVANLRKELAGVTGcAVAIAPPDMYLDLAKRAADGSHIILGAQNVDVNLSGAFTGETSA 80
Cdd:PRK13962 396 PRKPIIAGNWKMNKTPAEAKEFVNELKKYVKDAQA-EVVVCPPFTALPSVKEAVDGSNIKLGAQNVFYEEKGAYTGEISG 474

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712  81 EMLKDIGAKYIIIGHSERRTYHKESDEFIAKKFAVLKEQGLIPVLCIGETEAENEAGKTEEVCARQIDAVLKTQGAAAFE 160
Cdd:PRK13962 475 PMLAEIGVEYVIIGHSERRQYFGETDELVNKKVLAALKAGLTPILCVGETLDERESGITFDVVRLQLKAALNGLSAEQVK 554

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712 161 GAVIAYEPVWAIGTGKSATPAQAQAVHKFIRDHIA-KADAKVAEQVIIQYGGSVNASNAAELFTQPDIDGALVGGASLKA 239
Cdd:PRK13962 555 KVVIAYEPVWAIGTGKVATPEQAQEVHAFIRKLVAeLYGEEAARKVRILYGGSVKSENAAGLFNQPDIDGGLVGGASLKA 634


                 ....*....
gi 489958712 240 DAFAVIVKA 248
Cdd:PRK13962 635 QEFAAIANY 643
tim TIGR00419
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ...
 5-240 7.89e-88

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: 259.35  E-value: 7.89e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712    5 LVMGNWK-LNGSRHMVNELVANLRKELAGVTGCAVAIAPPDMYLDLAKRAADgshIILGAQNVDVNLSGAFTGETSAEML 83
Cdd:TIGR00419   1 LVIGNWKtYNESRGMRALEVAKIAEEVASEAGVAVAVAPPFVDLPMIKREVE---IPVYAQHVDAVLSGAHTGEISAEML 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712   84 KDIGAKYIIIGHSERRtyHKESDefIAKKFAVLKEQGLIPVLCIgeteaeneagkteevcarqiDAVLKTQGAAAFEGAV 163
Cdd:TIGR00419  78 KDIGAKGTLINHSERR--MKLAD--IEKKIARLKELGLTSVVCT--------------------NNVLTTAAAAALEPDV 133

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489958712  164 IAYEPVWAIGTGKSATPAQAQAVHKFIRdhiakADAKVAEQVIIQYGGSVNASNAAELFTQPDIDGALVGGASLKAD 240
Cdd:TIGR00419 134 VAVEPPELIGTGIPVSPAQPEVVHGSVR-----AVKEVNESVRVLCGAGISTGEDAELAAQLGAEGVLLASGSLKAD 205
PLN02561 PLN02561
triosephosphate isomerase
 2-254 3.10e-69

triosephosphate isomerase


Pssm-ID: 178175  Cd Length: 253  Bit Score: 213.53  E-value: 3.10e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712   2 RHPLVMGNWKLNGSRHMVNELVANLRK-ELAGVTGCAVAIAPPDMYLDLAKRAADgSHIILGAQNVDVNLSGAFTGETSA 80
Cdd:PLN02561   3 RKFFVGGNWKCNGTVEEVKKIVTTLNEaEVPSEDVVEVVVSPPFVFLPLVKSLLR-PDFQVAAQNCWVKKGGAFTGEISA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712  81 EMLKDIGAKYIIIGHSERRTYHKESDEFIAKKFAVLKEQGLIPVLCIGETEAENEAGKTEEVCARQIDAVlkTQGAAAFE 160
Cdd:PLN02561  82 EMLVNLGIPWVILGHSERRALLGESNEFVGDKVAYALSQGLKVIACVGETLEQRESGSTMDVVAAQTKAI--ADKVSDWA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712 161 GAVIAYEPVWAIGTGKSATPAQAQAVHKFIRDHIAK-ADAKVAEQVIIQYGGSVNASNAAELFTQPDIDGALVGGASLKA 239
Cdd:PLN02561 160 NVVLAYEPVWAIGTGKVATPAQAQEVHDELRKWLHKnVSPEVAATTRIIYGGSVTGANCKELAAQPDVDGFLVGGASLKP 239

                        250
                 ....*....|....*
gi 489958712 240 DaFAVIVKAAEAAKQ 254
Cdd:PLN02561 240 E-FIDIIKSATVKKS 253
PLN02429 PLN02429
triosephosphate isomerase
 13-255 8.74e-57

triosephosphate isomerase


Pssm-ID: 166070  Cd Length: 315  Bit Score: 183.84  E-value: 8.74e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712  13 NGSRHMVNELVANLRKELAGVTgCAVAIAPPDMYLDLAKRAADgSHIILGAQNVDVNLSGAFTGETSAEMLKDIGAKYII 92
Cdd:PLN02429  75 NGTKDSIAKLISDLNSATLEAD-VDVVVSPPFVYIDQVKSSLT-DRIDISGQNSWVGKGGAFTGEISVEQLKDLGCKWVI 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712  93 IGHSERRTYHKESDEFIAKKFAVLKEQGLIPVLCIGETEAENEAGKTEEVCARQIDAVlkTQGAAAFEGAVIAYEPVWAI 172
Cdd:PLN02429 153 LGHSERRHVIGEKDEFIGKKAAYALSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAF--ADAVPSWDNIVVAYEPVWAI 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712 173 GTGKSATPAQAQAVHKFIRDHIAK-ADAKVAEQVIIQYGGSVNASNAAELFTQPDIDGALVGGASLKADAFAVIVKAAEA 251
Cdd:PLN02429 231 GTGKVASPQQAQEVHVAVRGWLKKnVSEEVASKTRIIYGGSVNGGNSAELAKEEDIDGFLVGGASLKGPEFATIVNSVTS 310


                 ....
gi 489958712 252 AKQA 255
Cdd:PLN02429 311 KKVA 314
PRK14565 PRK14565
triosephosphate isomerase; Provisional
 5-250 2.64e-56

triosephosphate isomerase; Provisional


Pssm-ID: 237758  Cd Length: 237  Bit Score: 179.95  E-value: 2.64e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712   5 LVMGNWKLNGSRHMVNELVANLRKELAGVTG-CAVAIAPPdmYLDLAKRAADGSHIILGAQNVDVNLSGAFTGETSAEML 83
Cdd:PRK14565   4 LIVANWKMNGDFSLFSSFLKELSNKLANNEItLKLVICPP--FTAMSSFVECNPNIKLGAQNCFYGSSGGYTGEISAKML 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712  84 KDIGAKYIIIGHSERRTYHKESDEFIAKKFAVLKEQGLIPVLCIGETEAENEAGKTEEVCARQIDAVLKTQGAaafegAV 163
Cdd:PRK14565  82 KECGCSYVILGHSERRSTFHETDSDIRLKAESAIESGLIPIICVGETLEDRENGMTKDVLLEQCSNCLPKHGE-----FI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712 164 IAYEPVWAIGTGKSATPAQAQAVHKFIRDHIAKADakvaeqviIQYGGSVNASNAAELFTQPDIDGALVGGASLKADAFA 243
Cdd:PRK14565 157 IAYEPVWAIGGSTIPSNDAIAEAFEIIRSYDSKSH--------IIYGGSVNQENIRDLKSINQLSGVLVGSASLDVDSFC 228


                 ....*..
gi 489958712 244 VIVKAAE 250
Cdd:PRK14565 229 KIIQQVE 235
PRK15492 PRK15492
triosephosphate isomerase; Provisional
 50-247 1.51e-40

triosephosphate isomerase; Provisional


Pssm-ID: 185389  Cd Length: 260  Bit Score: 140.51  E-value: 1.51e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712  50 AKRAADGSH-IILGAQNVDVNLSGAFTGETSAEMLKDIGAKYIIIGHSERRTYHKESD-EFIAKKFAVLKEQgLIPVLCI 127
Cdd:PRK15492  56 ATLAIPHDHpIIIGAQNMNPNDNGQFTGDISPLMLKEIGTQLVMIGHSERRHKFGETDqEENAKVLAALKHD-FTTLLCV 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712 128 GETEAENEAGKTEEVCARQIDAVLKTQGAAAFEGAVIAYEPVWAIGT-GKSATPAQAQAVHKFIRDHIAKADAKVAEQVI 206
Cdd:PRK15492 135 GETLEQKNYGISDEILRTQLKIGLHGINPDQLAKLRIAYEPVWAIGEaGIPASADYADEKHAVIKQCLIELFGDAGDDIP 214

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 489958712 207 IQYGGSVNASNAAELFTQPDIDGALVGGASLKADAFAVIVK 247
Cdd:PRK15492 215 VFYGGSVNAENANELFGQPHIDGLFIGRSAWDADKFFAIIE 255
PRK14905 PRK14905
triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; ...
 47-249 4.69e-40

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


Pssm-ID: 184898 [Multi-domain]  Cd Length: 355  Bit Score: 141.71  E-value: 4.69e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712  47 LDLAKRAADGSHIILGAQNVDVNLSGAFTGETSAEMLKDIGAKYIIIGHSERRTYHKESDEFIAKKFAVLKEQGLIPVLC 126
Cdd:PRK14905  55 VEAAASETGHPKIKIGAQNMNAKDKGQFTGEISPLMLKELGIELVMIGHSERRHVLKETDQEENEKVLAALKHGFITLLC 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712 127 IGETEAENEAGKTEEVCARQIDAVLKTQGAAAFEGAVIAYEPVWAIGTGksATPAQAQAV---HKFIRDHIAKADAKVAE 203
Cdd:PRK14905 135 IGETLEQKNYNISDEVLRTQLKIGLHGVSAEQLPHLFIAYEPVWAIGEG--GIPASAEYAdekHAIIKQCLFELFAEESK 212

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 489958712 204 QVIIQYGGSVNASNAAELFTQPDIDGALVGGASLKADAFAVIVKAA 249
Cdd:PRK14905 213 KIPVLYGGSVNLENANELIMKPHIDGLFIGRSAWDAQCFHALIADA 258
PRK04302 PRK04302
triosephosphate isomerase; Provisional
 23-240 5.80e-12

triosephosphate isomerase; Provisional


Pssm-ID: 235274  Cd Length: 223  Bit Score: 63.35  E-value: 5.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712  23 VANLRKELAGVTGCAVAIAPPdmYLDLAkRAADGSHIILGAQNVDVNLSGAFTGETSAEMLKDIGAKYIIIGHSERRTyh 102
Cdd:PRK04302  24 IAKAAEKVSKETGVRIAVAPQ--ALDIR-RVAEEVDIPVYAQHVDPVEPGSHTGHILPEAVKDAGAVGTLINHSERRL-- 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712 103 KESDefIAKKFAVLKEQGLIPVLCigeteAENeagkteevcarqidaVLKTQGAAAFEGAVIAYEPVWAIGTGKSATPAQ 182
Cdd:PRK04302  99 TLAD--IEAVVERAKKLGLESVVC-----VNN---------------PETSAAAAALGPDYVAVEPPELIGTGIPVSKAK 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489958712 183 AQAVHKFIrDHIAKADAKVAeqVI----IQYGGSVNAsnAAELFTqpdiDGALVGGASLKAD 240
Cdd:PRK04302 157 PEVVEDAV-EAVKKVNPDVK--VLcgagISTGEDVKA--ALELGA----DGVLLASGVVKAK 209
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 6-234 2.71e-04

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 41.03  E-value: 2.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712   6 VMGNWKLNGSRHMVNELVANLRKELAGVTGCAVAIAPPDMYL----DLAKRAADGSHIILGAQNVDVNLSGAFTGEtsAE 81
Cdd:cd04722    1 VILALLAGGPSGDPVELAKAAAEAGADAIIVGTRSSDPEEAEtddkEVLKEVAAETDLPLGVQLAINDAAAAVDIA--AA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489958712  82 MLKDIGAKYIIIGHSERRTyhkesDEFIAKKFAVLKEQ--GLIPVLCIGETEAENEAGkteevcarqidavlktqgAAAF 159
Cdd:cd04722   79 AARAAGADGVEIHGAVGYL-----AREDLELIRELREAvpDVKVVVKLSPTGELAAAA------------------AEEA 135

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489958712 160 EGAVIAYEPVWAIGTGKSATPaqaqavhkfiRDHIAKADAKVAEQVIIQYGGSVNASNAAELFTQPDIDGALVGG 234
Cdd:cd04722  136 GVDEVGLGNGGGGGGGRDAVP----------IADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
 
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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