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Conserved domains on  [gi|1057717771|gb|AOE46351|]
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triosephosphate isomerase, partial [Clostridium perfringens]

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

EC:  5.3.1.-
Gene Ontology:  GO:0004807|GO:0006094|GO:0006096

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TpiA COG0149
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ...
1-150 9.14e-101

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: 288.88  E-value: 9.14e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057717771   1 KCEVVVCPTFVCLDAVKKAVEGTNIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKKVK 80
Cdd:COG0149    35 DVEVVVCPPFTYLAAVAEALAGSPIALGAQNVHWEDSGAYTGEISAAMLKDLGCRYVIVGHSERRQYFGETDELVNKKVK 114
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057717771  81 AAFAHNLTPILCCGETLEQRENGTTNDVIKAQITADLEGLTKEQAEKVVIAYEPIWAIGTGKTATSDQAN 150
Cdd:COG0149   115 AALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLSAEQAANVVIAYEPVWAIGTGKTATPEQAQ 184
 
Name Accession Description Interval E-value
TpiA COG0149
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ...
1-150 9.14e-101

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: 288.88  E-value: 9.14e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057717771   1 KCEVVVCPTFVCLDAVKKAVEGTNIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKKVK 80
Cdd:COG0149    35 DVEVVVCPPFTYLAAVAEALAGSPIALGAQNVHWEDSGAYTGEISAAMLKDLGCRYVIVGHSERRQYFGETDELVNKKVK 114
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057717771  81 AAFAHNLTPILCCGETLEQRENGTTNDVIKAQITADLEGLTKEQAEKVVIAYEPIWAIGTGKTATSDQAN 150
Cdd:COG0149   115 AALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLSAEQAANVVIAYEPVWAIGTGKTATPEQAQ 184
tpiA PRK00042
triosephosphate isomerase; Provisional
1-150 6.75e-98

triosephosphate isomerase; Provisional


Pssm-ID: 234589  Cd Length: 250  Bit Score: 281.62  E-value: 6.75e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057717771   1 KCEVVVCPTFVCLDAVKKAVEGTNIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKKVK 80
Cdd:PRK00042   34 GVEVAVAPPFTALASVKEALKGSNIKLGAQNVHPEDSGAFTGEISAEMLKDLGVKYVIIGHSERRQYFGETDELVNKKVK 113
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057717771  81 AAFAHNLTPILCCGETLEQRENGTTNDVIKAQITADLEGLTKEQAEKVVIAYEPIWAIGTGKTATSDQAN 150
Cdd:PRK00042  114 AALKAGLTPILCVGETLEEREAGKTEEVVARQLEAALAGLSAEQFANLVIAYEPVWAIGTGKTATPEQAQ 183
TIM pfam00121
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ...
2-150 3.58e-86

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: 252.05  E-value: 3.58e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057717771   2 CEVVVCPTFVCLDAVKKAVEgTNIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKKVKA 81
Cdd:pfam00121  33 VEVVVAPPFTYLSAVAELLG-SNIKVGAQNVDPEESGAFTGEISAEMLKDLGVSYVIIGHSERRQYFGETDEDVAKKVKA 111
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1057717771  82 AFAHNLTPILCCGETLEQRENGTTNDVIKAQITADLEGLTKEQAeKVVIAYEPIWAIGTGKTATSDQAN 150
Cdd:pfam00121 112 ALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQK-NLVIAYEPVWAIGTGKTATPEQAQ 179
TIM cd00311
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ...
1-150 1.76e-85

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: 250.15  E-value: 1.76e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057717771   1 KCEVVVCPTFVCLDAVKKAVEGTNIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKKVK 80
Cdd:cd00311    32 GVEVVVAPPFTYLAAVAEALEGSKIKVGAQNVSPEDSGAFTGEISAEMLKDAGAKYVIIGHSERRQYFGETDEDVAKKVK 111
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057717771  81 AAFAHNLTPILCCGETLEQRENGTTNDVIKAQITADLEGLtkEQAEKVVIAYEPIWAIGTGKTATSDQAN 150
Cdd:cd00311   112 AALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGV--EDLAPVVIAYEPVWAIGTGKTASPEQAQ 179
tim TIGR00419
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ...
2-149 2.48e-24

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: 92.94  E-value: 2.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057717771   2 CEVVVCPTFVCLDAVKKAVEgtnIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERReyFNETDetCNKKVKA 81
Cdd:TIGR00419  33 VAVAVAPPFVDLPMIKREVE---IPVYAQHVDAVLSGAHTGEISAEMLKDIGAKGTLINHSERR--MKLAD--IEKKIAR 105
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1057717771  82 AFAHNLTPILCcgetleqrengtTNDVIKAQITADLEGltkeqaekVVIAYEPIWAIGTGKTATSDQA 149
Cdd:TIGR00419 106 LKELGLTSVVC------------TNNVLTTAAAAALEP--------DVVAVEPPELIGTGIPVSPAQP 153
 
Name Accession Description Interval E-value
TpiA COG0149
Triosephosphate isomerase [Carbohydrate transport and metabolism]; Triosephosphate isomerase ...
1-150 9.14e-101

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: 288.88  E-value: 9.14e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057717771   1 KCEVVVCPTFVCLDAVKKAVEGTNIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKKVK 80
Cdd:COG0149    35 DVEVVVCPPFTYLAAVAEALAGSPIALGAQNVHWEDSGAYTGEISAAMLKDLGCRYVIVGHSERRQYFGETDELVNKKVK 114
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057717771  81 AAFAHNLTPILCCGETLEQRENGTTNDVIKAQITADLEGLTKEQAEKVVIAYEPIWAIGTGKTATSDQAN 150
Cdd:COG0149   115 AALAAGLTPILCVGETLEEREAGKTEEVVARQLKAALAGLSAEQAANVVIAYEPVWAIGTGKTATPEQAQ 184
tpiA PRK00042
triosephosphate isomerase; Provisional
1-150 6.75e-98

triosephosphate isomerase; Provisional


Pssm-ID: 234589  Cd Length: 250  Bit Score: 281.62  E-value: 6.75e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057717771   1 KCEVVVCPTFVCLDAVKKAVEGTNIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKKVK 80
Cdd:PRK00042   34 GVEVAVAPPFTALASVKEALKGSNIKLGAQNVHPEDSGAFTGEISAEMLKDLGVKYVIIGHSERRQYFGETDELVNKKVK 113
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057717771  81 AAFAHNLTPILCCGETLEQRENGTTNDVIKAQITADLEGLTKEQAEKVVIAYEPIWAIGTGKTATSDQAN 150
Cdd:PRK00042  114 AALKAGLTPILCVGETLEEREAGKTEEVVARQLEAALAGLSAEQFANLVIAYEPVWAIGTGKTATPEQAQ 183
TIM pfam00121
Triosephosphate isomerase; Triosephosphate isomerase (EC:5.3.1.1) (TIM) is the glycolytic ...
2-150 3.58e-86

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: 252.05  E-value: 3.58e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057717771   2 CEVVVCPTFVCLDAVKKAVEgTNIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKKVKA 81
Cdd:pfam00121  33 VEVVVAPPFTYLSAVAELLG-SNIKVGAQNVDPEESGAFTGEISAEMLKDLGVSYVIIGHSERRQYFGETDEDVAKKVKA 111
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1057717771  82 AFAHNLTPILCCGETLEQRENGTTNDVIKAQITADLEGLTKEQAeKVVIAYEPIWAIGTGKTATSDQAN 150
Cdd:pfam00121 112 ALKAGLTPILCVGETLEEREAGKTEEVVARQLDAALAGLGAEQK-NLVIAYEPVWAIGTGKTATPEQAQ 179
TIM cd00311
Triosephosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion of ...
1-150 1.76e-85

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: 250.15  E-value: 1.76e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057717771   1 KCEVVVCPTFVCLDAVKKAVEGTNIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKKVK 80
Cdd:cd00311    32 GVEVVVAPPFTYLAAVAEALEGSKIKVGAQNVSPEDSGAFTGEISAEMLKDAGAKYVIIGHSERRQYFGETDEDVAKKVK 111
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057717771  81 AAFAHNLTPILCCGETLEQRENGTTNDVIKAQITADLEGLtkEQAEKVVIAYEPIWAIGTGKTATSDQAN 150
Cdd:cd00311   112 AALEAGLTPILCVGETLEEREAGKTEEVVAAQLAAVLAGV--EDLAPVVIAYEPVWAIGTGKTASPEQAQ 179
PRK13962 PRK13962
bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional
1-150 2.58e-83

bifunctional phosphoglycerate kinase/triosephosphate isomerase; Provisional


Pssm-ID: 237572 [Multi-domain]  Cd Length: 645  Bit Score: 256.96  E-value: 2.58e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057717771   1 KCEVVVCPTFVCLDAVKKAVEGTNIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKKVK 80
Cdd:PRK13962  429 QAEVVVCPPFTALPSVKEAVDGSNIKLGAQNVFYEEKGAYTGEISGPMLAEIGVEYVIIGHSERRQYFGETDELVNKKVL 508
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057717771  81 AAFAHNLTPILCCGETLEQRENGTTNDVIKAQITADLEGLTKEQAEKVVIAYEPIWAIGTGKTATSDQAN 150
Cdd:PRK13962  509 AALKAGLTPILCVGETLDERESGITFDVVRLQLKAALNGLSAEQVKKVVIAYEPVWAIGTGKVATPEQAQ 578
PTZ00333 PTZ00333
triosephosphate isomerase; Provisional
3-150 1.69e-63

triosephosphate isomerase; Provisional


Pssm-ID: 240365  Cd Length: 255  Bit Score: 194.75  E-value: 1.69e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057717771   3 EVVVCPTFVCLDAVKKAVEGTNIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKKVKAA 82
Cdd:PTZ00333   39 DVVVAPPSLHIPLVQEKLKNKNFKISSQNVSLTGSGAFTGEISAEMLKDLGINWTILGHSERRQYFGETNEIVAQKVKNA 118
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1057717771  83 FAHNLTPILCCGETLEQRENGTTNDVIKAQITADLEGLTKEQAEKVVIAYEPIWAIGTGKTATSDQAN 150
Cdd:PTZ00333  119 LENGLKVILCIGETLEEREAGQTSDVLSKQLEAIVKKVSDEAWDNIVIAYEPVWAIGTGKVATPEQAQ 186
PLN02561 PLN02561
triosephosphate isomerase
3-149 1.97e-44

triosephosphate isomerase


Pssm-ID: 178175  Cd Length: 253  Bit Score: 146.12  E-value: 1.97e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057717771   3 EVVVCPTFVCLDAVKKAVEgTNIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKKVKAA 82
Cdd:PLN02561   39 EVVVSPPFVFLPLVKSLLR-PDFQVAAQNCWVKKGGAFTGEISAEMLVNLGIPWVILGHSERRALLGESNEFVGDKVAYA 117
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1057717771  83 FAHNLTPILCCGETLEQRENGTTNDVIKAQitadleglTKEQAEK------VVIAYEPIWAIGTGKTATSDQA 149
Cdd:PLN02561  118 LSQGLKVIACVGETLEQRESGSTMDVVAAQ--------TKAIADKvsdwanVVLAYEPVWAIGTGKVATPAQA 182
PRK14905 PRK14905
triosephosphate isomerase/PTS system glucose/sucrose-specific transporter subunit IIB; ...
3-148 2.53e-44

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


Pssm-ID: 184898 [Multi-domain]  Cd Length: 355  Bit Score: 148.64  E-value: 2.53e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057717771   3 EVVVCPTFVCL-DAVKKAVEGT---NIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKK 78
Cdd:PRK14905   41 ELFVIPSYIALkDAVEAAASETghpKIKIGAQNMNAKDKGQFTGEISPLMLKELGIELVMIGHSERRHVLKETDQEENEK 120
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057717771  79 VKAAFAHNLTPILCCGETLEQRENGTTNDVIKAQITADLEGLTKEQAEKVVIAYEPIWAIGTGKTATSDQ 148
Cdd:PRK14905  121 VLAALKHGFITLLCIGETLEQKNYNISDEVLRTQLKIGLHGVSAEQLPHLFIAYEPVWAIGEGGIPASAE 190
PRK15492 PRK15492
triosephosphate isomerase; Provisional
3-150 3.82e-44

triosephosphate isomerase; Provisional


Pssm-ID: 185389  Cd Length: 260  Bit Score: 145.52  E-value: 3.82e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057717771   3 EVVVCPTFVCLDAVKKAVEGTN----IKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKK 78
Cdd:PRK15492   40 ELFVIPSFTAIQDAIAATLAIPhdhpIIIGAQNMNPNDNGQFTGDISPLMLKEIGTQLVMIGHSERRHKFGETDQEENAK 119
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1057717771  79 VKAAFAHNLTPILCCGETLEQRENGTTNDVIKAQITADLEGLTKEQAEKVVIAYEPIWAIGT-GKTATSDQAN 150
Cdd:PRK15492  120 VLAALKHDFTTLLCVGETLEQKNYGISDEILRTQLKIGLHGINPDQLAKLRIAYEPVWAIGEaGIPASADYAD 192
PRK14565 PRK14565
triosephosphate isomerase; Provisional
1-147 1.35e-42

triosephosphate isomerase; Provisional


Pssm-ID: 237758  Cd Length: 237  Bit Score: 141.05  E-value: 1.35e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057717771   1 KCEVVVCPTFVCLDAVkkaVEGT-NIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKKV 79
Cdd:PRK14565   35 TLKLVICPPFTAMSSF---VECNpNIKLGAQNCFYGSSGGYTGEISAKMLKECGCSYVILGHSERRSTFHETDSDIRLKA 111
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057717771  80 KAAFAHNLTPILCCGETLEQRENGTTNDVIKAQITADL--EGltkeqaeKVVIAYEPIWAIGTGKTATSD 147
Cdd:PRK14565  112 ESAIESGLIPIICVGETLEDRENGMTKDVLLEQCSNCLpkHG-------EFIIAYEPVWAIGGSTIPSND 174
PLN02429 PLN02429
triosephosphate isomerase
3-149 2.59e-33

triosephosphate isomerase


Pssm-ID: 166070  Cd Length: 315  Bit Score: 119.13  E-value: 2.59e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057717771   3 EVVVCPTFVCLDAVKKAVEgTNIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDETCNKKVKAA 82
Cdd:PLN02429   98 DVVVSPPFVYIDQVKSSLT-DRIDISGQNSWVGKGGAFTGEISVEQLKDLGCKWVILGHSERRHVIGEKDEFIGKKAAYA 176
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1057717771  83 FAHNLTPILCCGETLEQRENGTTNDVIKAQITADLEGLTkeQAEKVVIAYEPIWAIGTGKTATSDQA 149
Cdd:PLN02429  177 LSEGLGVIACIGEKLEEREAGKTFDVCFAQLKAFADAVP--SWDNIVVAYEPVWAIGTGKVASPQQA 241
tim TIGR00419
triosephosphate isomerase; Triosephosphate isomerase (tim/TPIA) is the glycolytic enzyme that ...
2-149 2.48e-24

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: 92.94  E-value: 2.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057717771   2 CEVVVCPTFVCLDAVKKAVEgtnIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERReyFNETDetCNKKVKA 81
Cdd:TIGR00419  33 VAVAVAPPFVDLPMIKREVE---IPVYAQHVDAVLSGAHTGEISAEMLKDIGAKGTLINHSERR--MKLAD--IEKKIAR 105
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1057717771  82 AFAHNLTPILCcgetleqrengtTNDVIKAQITADLEGltkeqaekVVIAYEPIWAIGTGKTATSDQA 149
Cdd:TIGR00419 106 LKELGLTSVVC------------TNNVLTTAAAAALEP--------DVVAVEPPELIGTGIPVSPAQP 153
PRK04302 PRK04302
triosephosphate isomerase; Provisional
3-92 2.63e-08

triosephosphate isomerase; Provisional


Pssm-ID: 235274  Cd Length: 223  Bit Score: 50.64  E-value: 2.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1057717771   3 EVVVCPTFVCLDAVKKAVEgtnIKVGAQNMHFEEKGAFTGEIAPRMLEAMNIDYVIIGHSERREYFNETDetcnKKVKAA 82
Cdd:PRK04302   38 RIAVAPQALDIRRVAEEVD---IPVYAQHVDPVEPGSHTGHILPEAVKDAGAVGTLINHSERRLTLADIE----AVVERA 110
                          90
                  ....*....|
gi 1057717771  83 FAHNLTPILC 92
Cdd:PRK04302  111 KKLGLESVVC 120
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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