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Conserved domains on  [gi|766466122|gb|AJR90215|]
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Tdh3p, partial [Saccharomyces cerevisiae YJM981]

Protein Classification

GapA superfamily protein( domain architecture ID 1903262)

GapA superfamily protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GapA super family cl43010
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-123 1.56e-75

Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]; Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase is part of the Pathway/BioSystem: Glycolysis


The actual alignment was detected with superfamily member COG0057:

Pssm-ID: 439827 [Multi-domain]  Cd Length: 334  Bit Score: 226.82  E-value: 1.56e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766466122   1 GAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLDKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSH 80
Cdd:COG0057  211 GAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPH 290

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 766466122  81 SSIFDASAGIQLSPKFVKLVSWYDNEYGYSTRVVDLVEHVAKA 123
Cdd:COG0057  291 SSIFDALQTIVIGGNLVKVLAWYDNEWGYSNRMVDLAEYMAKL 333
 
Name Accession Description Interval E-value
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-123 1.56e-75

Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]; Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 439827 [Multi-domain]  Cd Length: 334  Bit Score: 226.82  E-value: 1.56e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766466122   1 GAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLDKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSH 80
Cdd:COG0057  211 GAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPH 290

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 766466122  81 SSIFDASAGIQLSPKFVKLVSWYDNEYGYSTRVVDLVEHVAKA 123
Cdd:COG0057  291 SSIFDALQTIVIGGNLVKVLAWYDNEWGYSNRMVDLAEYMAKL 333
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 1-106 6.26e-70

C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (1.2.1.12), NADP (1.2.1.13) or either (1.2.1.59). The family corresponds to the ubiquitous NAD+ or NADP+ utilizing type I GAPDH and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose.


Pssm-ID: 467676  Cd Length: 165  Bit Score: 206.54  E-value: 6.26e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766466122   1 GAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLDKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSH 80
Cdd:cd18126   60 GAAKAVGLVIPELKGKLTGMAFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPH 139

                         90       100
                 ....*....|....*....|....*.
gi 766466122  81 SSIFDASAGIQLSPKFVKLVSWYDNE 106
Cdd:cd18126  140 SSIFDATATIVLGGNLVKVVAWYDNE 165
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 1-121 6.64e-70

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 215.11  E-value: 6.64e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766466122   1 GAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLDKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSH 80
Cdd:PLN02272 295 GAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSR 374

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 766466122  81 SSIFDASAGIQLSPKFVKLVSWYDNEYGYSTRVVDLVEHVA 121
Cdd:PLN02272 375 SSIFDAKAGIGLSASFMKLVSWYDNEWGYSNRVLDLIEHMA 415
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 1-115 2.67e-58

glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the enzyme responsible for the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. Forms exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (1.2.1.59). In some species, NAD- and NADP- utilizing forms exist, generally being responsible for reactions in the anabolic and catabolic directions respectively. Two Pfam models cover the two functional domains of this protein; pfam00044 represents the N-terminal NAD(P)-binding domain and pfam02800 represents the C-terminal catalytic domain. An additional form of gap gene is found in gamma proteobacteria and is responsible for the conversion of erythrose-4-phosphate (E4P) to 4-phospho-erythronate in the biosynthesis of pyridoxine. This pathway of pyridoxine biosynthesis appears to be limited, however, to a relatively small number of bacterial species although it is prevalent among the gamma-proteobacteria. This enzyme is described by TIGR001532. These sequences generally score between trusted and noise to this GAPDH model due to the close evolutionary relationship. There exists the possiblity that some forms of GAPDH may be bifunctional and act on E4P in species which make pyridoxine and via hydroxythreonine and lack a separate E4PDH enzyme (for instance, the GAPDH from Bacillus stearothermophilus has been shown to posess a limited E4PD activity as well as a robust GAPDH activity). There are a great number of sequences in the databases which score between trusted and noise to this model, nearly all of them due to fragmentary sequences. It seems that study of this gene has been carried out in many species utilizing PCR probes which exclude the extreme ends of the consenses used to define this model. The noise level is set relative not to E4PD, but the next closest outliers, the class II GAPDH's (found in archaea, TIGR01546) and aspartate semialdehyde dehydrogenase (ASADH, TIGR01296) both of which have highest-scoring hits around -225 to the prior model. [Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 273675 [Multi-domain]  Cd Length: 326  Bit Score: 182.48  E-value: 2.67e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766466122    1 GAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLDKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSH 80
Cdd:TIGR01534 210 GAAKAIGKVLPELAGKLTGMAIRVPTPNVSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPY 289

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 766466122   81 SSIFDASAGIQ--LSPKFVKLVSWYDNEYGYSTRVVD 115
Cdd:TIGR01534 290 SSIVDATATKVtgLGDSLVKVYAWYDNEWGYSNRLVD 326
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 1-103 1.44e-53

Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. C-terminal domain is a mixed alpha/antiparallel beta fold.


Pssm-ID: 460700  Cd Length: 158  Bit Score: 165.07  E-value: 1.44e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766466122    1 GAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLDKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSH 80
Cdd:pfam02800  56 GAAKAVGLVLPELKGKLDGMAVRVPTPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPH 135

                          90       100
                  ....*....|....*....|...
gi 766466122   81 SSIFDASAGIQLSPKFVKLVSWY 103
Cdd:pfam02800 136 SSIFDAKETIVVNGNFVKVVAWY 158
 
Name Accession Description Interval E-value
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-123 1.56e-75

Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]; Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 439827 [Multi-domain]  Cd Length: 334  Bit Score: 226.82  E-value: 1.56e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766466122   1 GAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLDKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSH 80
Cdd:COG0057  211 GAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPH 290

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 766466122  81 SSIFDASAGIQLSPKFVKLVSWYDNEYGYSTRVVDLVEHVAKA 123
Cdd:COG0057  291 SSIFDALQTIVIGGNLVKVLAWYDNEWGYSNRMVDLAEYMAKL 333
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 1-106 6.26e-70

C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (1.2.1.12), NADP (1.2.1.13) or either (1.2.1.59). The family corresponds to the ubiquitous NAD+ or NADP+ utilizing type I GAPDH and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose.


Pssm-ID: 467676  Cd Length: 165  Bit Score: 206.54  E-value: 6.26e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766466122   1 GAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLDKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSH 80
Cdd:cd18126   60 GAAKAVGLVIPELKGKLTGMAFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPH 139

                         90       100
                 ....*....|....*....|....*.
gi 766466122  81 SSIFDASAGIQLSPKFVKLVSWYDNE 106
Cdd:cd18126  140 SSIFDATATIVLGGNLVKVVAWYDNE 165
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 1-121 6.64e-70

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 215.11  E-value: 6.64e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766466122   1 GAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLDKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSH 80
Cdd:PLN02272 295 GAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSR 374

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 766466122  81 SSIFDASAGIQLSPKFVKLVSWYDNEYGYSTRVVDLVEHVA 121
Cdd:PLN02272 375 SSIFDAKAGIGLSASFMKLVSWYDNEWGYSNRVLDLIEHMA 415
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
 1-123 4.18e-60

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 187.62  E-value: 4.18e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766466122   1 GAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLDKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSH 80
Cdd:PLN02358 216 GAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNR 295

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 766466122  81 SSIFDASAGIQLSPKFVKLVSWYDNEYGYSTRVVDLVEHVAKA 123
Cdd:PLN02358 296 SSIFDAKAGIALSDKFVKLVSWYDNEWGYSSRVVDLIVHMSKA 338
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 1-115 2.67e-58

glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the enzyme responsible for the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. Forms exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (1.2.1.59). In some species, NAD- and NADP- utilizing forms exist, generally being responsible for reactions in the anabolic and catabolic directions respectively. Two Pfam models cover the two functional domains of this protein; pfam00044 represents the N-terminal NAD(P)-binding domain and pfam02800 represents the C-terminal catalytic domain. An additional form of gap gene is found in gamma proteobacteria and is responsible for the conversion of erythrose-4-phosphate (E4P) to 4-phospho-erythronate in the biosynthesis of pyridoxine. This pathway of pyridoxine biosynthesis appears to be limited, however, to a relatively small number of bacterial species although it is prevalent among the gamma-proteobacteria. This enzyme is described by TIGR001532. These sequences generally score between trusted and noise to this GAPDH model due to the close evolutionary relationship. There exists the possiblity that some forms of GAPDH may be bifunctional and act on E4P in species which make pyridoxine and via hydroxythreonine and lack a separate E4PDH enzyme (for instance, the GAPDH from Bacillus stearothermophilus has been shown to posess a limited E4PD activity as well as a robust GAPDH activity). There are a great number of sequences in the databases which score between trusted and noise to this model, nearly all of them due to fragmentary sequences. It seems that study of this gene has been carried out in many species utilizing PCR probes which exclude the extreme ends of the consenses used to define this model. The noise level is set relative not to E4PD, but the next closest outliers, the class II GAPDH's (found in archaea, TIGR01546) and aspartate semialdehyde dehydrogenase (ASADH, TIGR01296) both of which have highest-scoring hits around -225 to the prior model. [Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 273675 [Multi-domain]  Cd Length: 326  Bit Score: 182.48  E-value: 2.67e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766466122    1 GAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLDKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSH 80
Cdd:TIGR01534 210 GAAKAIGKVLPELAGKLTGMAIRVPTPNVSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPY 289

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 766466122   81 SSIFDASAGIQ--LSPKFVKLVSWYDNEYGYSTRVVD 115
Cdd:TIGR01534 290 SSIVDATATKVtgLGDSLVKVYAWYDNEWGYSNRLVD 326
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
 1-122 6.77e-58

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 181.96  E-value: 6.77e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766466122   1 GAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLDKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSH 80
Cdd:PTZ00023 214 GAAKAVGKVIPELNGKLTGMAFRVPVPDVSVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKR 293

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 766466122  81 SSIFDASAGIQLSPKFVKLVSWYDNEYGYSTRVVDLVEHVAK 122
Cdd:PTZ00023 294 SSIFDVKAGIALNDTFVKLVSWYDNEWGYSNRLLDLAHYITQ 335
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
1-122 1.76e-54

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 173.00  E-value: 1.76e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766466122   1 GAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLDKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSH 80
Cdd:PRK15425 210 GAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVC 289

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 766466122  81 SSIFDASAGIQLSPKFVKLVSWYDNEYGYSTRVVDLVEHVAK 122
Cdd:PRK15425 290 TSVFDAKAGIALNDNFVKLVSWYDNETGYSNKVLDLIAHISK 331
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 1-103 1.44e-53

Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. C-terminal domain is a mixed alpha/antiparallel beta fold.


Pssm-ID: 460700  Cd Length: 158  Bit Score: 165.07  E-value: 1.44e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766466122    1 GAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLDKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSH 80
Cdd:pfam02800  56 GAAKAVGLVLPELKGKLDGMAVRVPTPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPH 135

                          90       100
                  ....*....|....*....|...
gi 766466122   81 SSIFDASAGIQLSPKFVKLVSWY 103
Cdd:pfam02800 136 SSIFDAKETIVVNGNFVKVVAWY 158
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 1-121 2.47e-49

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 160.61  E-value: 2.47e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766466122   1 GAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLDKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSH 80
Cdd:PTZ00434 228 GAAKAVGMVIPSTKGKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNR 307

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 766466122  81 SSIFDASAGIQLS----PKFVKLVSWYDNEYGYSTRVVDLVEHVA 121
Cdd:PTZ00434 308 SSIYDSKATLQNNlpgeRRFFKIVSWYDNEWGYSHRVVDLVRYMA 352
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-122 5.56e-49

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 159.13  E-value: 5.56e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766466122   1 GAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLDKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSH 80
Cdd:PRK07729 211 GAAKALAKVLPHLNGKLHGMALRVPTPNVSLVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTH 290

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 766466122  81 SSIFDASAGIQLSPKFVKLVSWYDNEYGYSTRVVDLVEHVAK 122
Cdd:PRK07729 291 SAIIDGLSTMVMGDRKVKVLAWYDNEWGYSCRVVDLVTLVAD 332
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
1-122 3.26e-44

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 146.59  E-value: 3.26e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766466122   1 GAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLDKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSH 80
Cdd:PRK07403 213 GAAKAVALVIPELKGKLNGIALRVPTPNVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDA 292

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 766466122  81 SSIFDASAGIQLSPKFVKLVSWYDNEYGYSTRVVDLVEHVAK 122
Cdd:PRK07403 293 SSIVDASLTMVMGGDMVKVIAWYDNEWGYSQRVVDLAELVAR 334
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 1-106 2.19e-43

C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (1.2.1.12), NADP (1.2.1.13) or either (1.2.1.59). GADPH family members include the ubiquitous NAD+ or NADP+ utilizing type I, type II NADP+ utilizing mainly from archaea, and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose.


Pssm-ID: 467673  Cd Length: 164  Bit Score: 139.67  E-value: 2.19e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766466122   1 GAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLDKETTYDEIKKVVKAAAEGklKGVLGYTEDAVVSSDFLGDSH 80
Cdd:cd18123   61 GAAKAVGKVLPELNGKLTGMAVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIF 138

                         90       100
                 ....*....|....*....|....*.
gi 766466122  81 SSIFDASAGIQLSPKFVKLVSWYDNE 106
Cdd:cd18123  139 ESVFDAESIIAVNDNEVKLMQWYDNE 164
PRK08289 PRK08289
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
 1-123 1.34e-37

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 236219 [Multi-domain]  Cd Length: 477  Bit Score: 131.97  E-value: 1.34e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766466122   1 GAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLDKETTYDEIKKVVKAAA-EGKLKGVLGYTEDA-VVSSDFLGD 78
Cdd:PRK08289 348 GAAKAVAKALPELAGKLTGNAIRVPTPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQIDYTDSTeVVSSDFVGS 427

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 766466122  79 SHSSIFDASAGIqLSPKFVKLVSWYDNEYGYSTRVVDLVEHVAKA 123
Cdd:PRK08289 428 RHAGVVDSQATI-VNGNRAVLYVWYDNEFGYSCQVVRVMEQMAGV 471
PRK08955 PRK08955
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-123 1.17e-36

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 169599 [Multi-domain]  Cd Length: 334  Bit Score: 127.15  E-value: 1.17e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766466122   1 GAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLDKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSH 80
Cdd:PRK08955 211 GSATAITEIFPELKGKLNGHAVRVPLANASLTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPR 290

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 766466122  81 SSIFDASAGIQLSPKFVKLVSWYDNEYGYSTRVVDLVEHVAKA 123
Cdd:PRK08955 291 SSIVDALSTMVVNGTQVKLYAWYDNEWGYANRTAELARKVGLA 333
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
 1-122 8.27e-35

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 123.50  E-value: 8.27e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766466122   1 GAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLDKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSH 80
Cdd:PLN03096 271 GAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDV 350

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 766466122  81 SSIFDASAGIQLSPKFVKLVSWYDNEYGYSTRVVDLVEHVAK 122
Cdd:PLN03096 351 SSTIDSSLTMVMGDDMVKVVAWYDNEWGYSQRVVDLADIVAN 392
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
 1-122 2.67e-33

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 120.01  E-value: 2.67e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766466122   1 GAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLDKE-TTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDS 79
Cdd:PLN02237 288 GAAKAVSLVLPQLKGKLNGIALRVPTPNVSVVDLVVNVEKKgITAEDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSD 367

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 766466122  80 HSSIFDASAGIQLSPKFVKLVSWYDNEYGYSTRVVDLVEHVAK 122
Cdd:PLN02237 368 VSSTIDASLTMVMGDDMVKVVAWYDNEWGYSQRVVDLAHLVAA 410
GAPDH_C_E4PDH cd23937
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 1-106 4.63e-33

C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar proteins; D-erythrose-4-phosphate dehydrogenase (E4PDH; EC 1.2.1.72), also called E4P dehydrogenase, catalyzes the NAD-dependent conversion of D-erythrose 4-phosphate (E4P) to 4-phosphoerythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose. This enzyme activity appears to have evolved from glyceraldehyde-3-phosphate dehydrogenase (GADPH), whose substrate differs only in the lack of one carbon relative to E4P. E4PDH proteins contain an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal GADPH-like catalytic domain and are members of the GAPDH superfamily of proteins.


Pssm-ID: 467686  Cd Length: 165  Bit Score: 113.28  E-value: 4.63e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766466122   1 GAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLDKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSH 80
Cdd:cd23937   60 KLARGIERILPHLAGRFEAIAVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPH 139

                         90       100
                 ....*....|....*....|....*.
gi 766466122  81 SSIFDASAGIQLSPKFVKLVSWYDNE 106
Cdd:cd23937  140 SCIVDGTQTRVSGKRLVKLLVWCDNE 165
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
 3-123 2.46e-25

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 97.43  E-value: 2.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766466122   3 AKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLDKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSHSS 82
Cdd:PRK13535 215 AAGITRIFPQFNDRFEAISVRVPTINVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSA 294

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 766466122  83 IFDAS----AGIQLspkfVKLVSWYDNEYGYSTRVVDLVEHVAKA 123
Cdd:PRK13535 295 IVDGTqtrvSGAHL----IKTLVWCDNEWGFANRMLDTTLAMAAA 335
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 1-106 4.47e-24

C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) superfamily of proteins; GAPDH-like C-terminal catalytic domains are typically associated with a classic N-terminal Rossmann fold NAD(P)-binding domain. This superfamily includes the C-terminal domains of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), aspartate beta-semialdehyde dehydrogenase (ASADH), acetaldehyde dehydrogenase (ALDH) and USG-1 homolog proteins.


Pssm-ID: 467672 [Multi-domain]  Cd Length: 166  Bit Score: 90.27  E-value: 4.47e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766466122   1 GAAKAVGKVLPELQ--GKLTGMAFRVPTVDVSVVDLTVKLDKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGD 78
Cdd:cd18122   59 KHAPETGKVLGEIGkpIKVDGIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGG 138

                         90       100
                 ....*....|....*....|....*...
gi 766466122  79 SHSSIFDASAGIQLSPKFVKLVSWYDNE 106
Cdd:cd18122  139 VYGVPVGRQREFAFDDNKLKVFSAVDNE 166
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
 3-120 6.18e-15

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 69.13  E-value: 6.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766466122   3 AKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLDKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDShSS 82
Cdd:PTZ00353 216 AETVCKLLPHLVGRISGSAFQVPVKKGCAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCIPNG-KL 294

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 766466122  83 IFDASAGIQLSP-KFVKLVSWYDNEYGYSTRVVDLVEHV 120
Cdd:PTZ00353 295 CYDATSSSSSREgEVHKMVLWFDVECYYAARLLSLVKQL 333
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 105-120 5.80e-04

N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; GAPDH plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (EC 1.2.1.59). The family corresponds to the ubiquitous NAD+ or NADP+ utilizing type I GAPDH and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose.


Pssm-ID: 467614 [Multi-domain]  Cd Length: 164  Bit Score: 37.37  E-value: 5.80e-04
                         10
                 ....*....|....*.
gi 766466122 105 NEYGYSTRVVDLVEHV 120
Cdd:cd05214  149 NEWGYSNRVVDLAEYV 164
 
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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