NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|308193620|gb|ADO16341|]
View 

glyceraldehyde-3-phosphate dehydrogenase, partial [Enterococcus faecium]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GAPDH_like_C super family cl49616
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 1-130 2.20e-70

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.


The actual alignment was detected with superfamily member cd18126:

Pssm-ID: 483956  Cd Length: 165  Bit Score: 208.08  E-value: 2.20e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193620   1 VEGLMTTIHAYTGDQMTLDGPHpkGDFRRARAAAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSLTELVTVL 80
Cdd:cd18126   20 EEGLMTTVHAYTNDQKLVDGPH--KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMAFRVPTPNVSVVDLTVRL 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 308193620  81 EKEVTVDEINAAMKEASNESY----GYNTDEIVSSDIVGMTYGSLFDATQTKVM 130
Cdd:cd18126   98 EKPVTVEEVNAALKKAAEGPLkgilGYTEDPLVSSDFVGDPHSSIFDATATIVL 151
 
Name Accession Description Interval E-value
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 1-130 2.20e-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: 208.08  E-value: 2.20e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193620   1 VEGLMTTIHAYTGDQMTLDGPHpkGDFRRARAAAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSLTELVTVL 80
Cdd:cd18126   20 EEGLMTTVHAYTNDQKLVDGPH--KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMAFRVPTPNVSVVDLTVRL 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 308193620  81 EKEVTVDEINAAMKEASNESY----GYNTDEIVSSDIVGMTYGSLFDATQTKVM 130
Cdd:cd18126   98 EKPVTVEEVNAALKKAAEGPLkgilGYTEDPLVSSDFVGDPHSSIFDATATIVL 151
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-130 3.97e-69

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: 210.64  E-value: 3.97e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193620   1 VEGLMTTIHAYTGDQMTLDGPHpkGDFRRARAAAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSLTELVTVL 80
Cdd:COG0057  171 EKGLMTTIHAYTNDQNLLDAPH--KDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVEL 248

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 308193620  81 EKEVTVDEINAAMKEASNESY----GYNTDEIVSSDIVGMTYGSLFDATQTKVM 130
Cdd:COG0057  249 EKETTVEEVNAALKEAAEGPLkgilGYTEEPLVSSDFNGDPHSSIFDALQTIVI 302
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 1-131 1.16e-63

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: 196.73  E-value: 1.16e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193620    1 VEGLMTTIHAYTGDQMTLDGPHpkGDFRRARAAAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSLTELVTVL 80
Cdd:TIGR01534 170 VSGLMTTVHAYTNDQNLLDGPH--KDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNVSLVDLVVNL 247

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 308193620   81 EKEVTVDEINAAMKEAS----NESYGYNTDEIVSSDIVGMTYGSLFDATQTKVMT 131
Cdd:TIGR01534 248 EKDVTVEEVNAALKEASegelKGVLGYTEDELVSSDFIGSPYSSIVDATATKVTG 302
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 1-130 2.13e-58

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: 177.78  E-value: 2.13e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193620    1 VEGLMTTIHAYTGDQMTLDGPHPKgDFRRARAAAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSLTELVTVL 80
Cdd:pfam02800  15 KKGLMTTVHAYTNDQKLLDGPHHK-DLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSVVDLVVEL 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 308193620   81 EKEVTVDEINAAMKEASNESY----GYNTDEIVSSDIVGMTYGSLFDATQTKVM 130
Cdd:pfam02800  94 EKPVTVEEVNAALKEAAEGALkgilSYTEDPLVSSDFIGDPHSSIFDAKETIVV 147
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 3-130 5.42e-37

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 128.32  E-value: 5.42e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193620   3 GLMTTIHAYTGDQMTLDGPHPkgDFRRARAAAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSLTELVTVLEK 82
Cdd:PRK07729 173 GLMTTVHAYTNDQKNIDNPHK--DLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNVSLVDLVVDVKR 250

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 308193620  83 EVTVDEINAAMKEASNESY----GYNTDEIVSSDIVGMTYGSLFDATQTKVM 130
Cdd:PRK07729 251 DVTVEEINEAFKTAANGALkgilEFSEEPLVSIDFNTNTHSAIIDGLSTMVM 302
 
Name Accession Description Interval E-value
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 1-130 2.20e-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: 208.08  E-value: 2.20e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193620   1 VEGLMTTIHAYTGDQMTLDGPHpkGDFRRARAAAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSLTELVTVL 80
Cdd:cd18126   20 EEGLMTTVHAYTNDQKLVDGPH--KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMAFRVPTPNVSVVDLTVRL 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 308193620  81 EKEVTVDEINAAMKEASNESY----GYNTDEIVSSDIVGMTYGSLFDATQTKVM 130
Cdd:cd18126   98 EKPVTVEEVNAALKKAAEGPLkgilGYTEDPLVSSDFVGDPHSSIFDATATIVL 151
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-130 3.97e-69

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: 210.64  E-value: 3.97e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193620   1 VEGLMTTIHAYTGDQMTLDGPHpkGDFRRARAAAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSLTELVTVL 80
Cdd:COG0057  171 EKGLMTTIHAYTNDQNLLDAPH--KDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVEL 248

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 308193620  81 EKEVTVDEINAAMKEASNESY----GYNTDEIVSSDIVGMTYGSLFDATQTKVM 130
Cdd:COG0057  249 EKETTVEEVNAALKEAAEGPLkgilGYTEEPLVSSDFNGDPHSSIFDALQTIVI 302
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 1-131 1.16e-63

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: 196.73  E-value: 1.16e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193620    1 VEGLMTTIHAYTGDQMTLDGPHpkGDFRRARAAAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSLTELVTVL 80
Cdd:TIGR01534 170 VSGLMTTVHAYTNDQNLLDGPH--KDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNVSLVDLVVNL 247

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 308193620   81 EKEVTVDEINAAMKEAS----NESYGYNTDEIVSSDIVGMTYGSLFDATQTKVMT 131
Cdd:TIGR01534 248 EKDVTVEEVNAALKEASegelKGVLGYTEDELVSSDFIGSPYSSIVDATATKVTG 302
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 1-130 2.13e-58

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: 177.78  E-value: 2.13e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193620    1 VEGLMTTIHAYTGDQMTLDGPHPKgDFRRARAAAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSLTELVTVL 80
Cdd:pfam02800  15 KKGLMTTVHAYTNDQKLLDGPHHK-DLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSVVDLVVEL 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 308193620   81 EKEVTVDEINAAMKEASNESY----GYNTDEIVSSDIVGMTYGSLFDATQTKVM 130
Cdd:pfam02800  94 EKPVTVEEVNAALKEAAEGALkgilSYTEDPLVSSDFIGDPHSSIFDAKETIVV 147
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 1-130 9.54e-41

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: 133.13  E-value: 9.54e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193620   1 VEGLMTTIHAYTGDQMTLDGPHPKgDFRRARAAAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSLTELVTVL 80
Cdd:cd18123   20 KKGRMTTVHAATDTQKTVDGPSGK-DWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGMAVRVPTTLMSVHDLMVEL 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 308193620  81 EKEVTVDEINAAMKEAS--NESYGYNTDEIVSSDIVGMTYGSLFDATQTKVM 130
Cdd:cd18123   99 EKDVTYDDIKEAVKQAPegKGRLGYTEAEDVSSDFRGDIFESVFDAESIIAV 150
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 3-130 5.42e-37

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 128.32  E-value: 5.42e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193620   3 GLMTTIHAYTGDQMTLDGPHPkgDFRRARAAAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSLTELVTVLEK 82
Cdd:PRK07729 173 GLMTTVHAYTNDQKNIDNPHK--DLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNVSLVDLVVDVKR 250

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 308193620  83 EVTVDEINAAMKEASNESY----GYNTDEIVSSDIVGMTYGSLFDATQTKVM 130
Cdd:PRK07729 251 DVTVEEINEAFKTAANGALkgilEFSEEPLVSIDFNTNTHSAIIDGLSTMVM 302
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 1-124 6.64e-37

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 129.98  E-value: 6.64e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193620   1 VEGLMTTIHAYTGDQMTLDGPHPKgDFRRARAAAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSLTELVTVL 80
Cdd:PLN02272 254 LEGLMTTVHATTATQKTVDGPSMK-DWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRL 332

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 308193620  81 EKEVTVDEINAAMKEASNES----YGYNTDEIVSSDIVGMTYGSLFDA 124
Cdd:PLN02272 333 EKSASYEDVKAAIKYASEGPlkgiLGYTDEDVVSNDFVGDSRSSIFDA 380
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
 1-123 6.43e-35

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 123.02  E-value: 6.43e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193620   1 VEGLMTTIHAYTGDQMTLDGPHPKG-DFRRARAAAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSLTELVTV 79
Cdd:PTZ00023 171 VEGLMTTVHASTANQLTVDGPSKGGkDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVPDVSVVDLTCK 250

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 308193620  80 LEKEVTVDEINAAMKEASNESY----GYNTDEIVSSDIVGMTYGSLFD 123
Cdd:PTZ00023 251 LAKPAKYEEIVAAVKKAAEGPLkgilGYTDDEVVSSDFVHDKRSSIFD 298
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
1-130 5.04e-34

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 120.78  E-value: 5.04e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193620   1 VEGLMTTIHAYTGDQMTLDGPHPkgDFRRARAAAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSLTELVTVL 80
Cdd:PRK07403 173 IKGTMTTTHSYTGDQRILDASHR--DLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTPNVSVVDLVVQV 250

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 308193620  81 EKEVTVDEINAAMKEASNESY----GYNTDEIVSSDIVGMTYGSLFDATQTKVM 130
Cdd:PRK07403 251 EKRTITEQVNEVLKDASEGPLkgilEYSDLPLVSSDYRGTDASSIVDASLTMVM 304
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
1-124 1.31e-29

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 109.05  E-value: 1.31e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193620   1 VEGLMTTIHAYTGDQMTLDGPHPKgDFRRARAAAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSLTELVTVL 80
Cdd:PRK15425 169 IEGLMTTVHATTATQKTVDGPSHK-DWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRL 247

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 308193620  81 EKEVTVDEINAAMKEASNESY----GYNTDEIVSSDIVGMTYGSLFDA 124
Cdd:PRK15425 248 EKAATYEQIKAAVKAAAEGEMkgvlGYTEDDVVSTDFNGEVCTSVFDA 295
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
 1-124 2.08e-29

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 108.65  E-value: 2.08e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193620   1 VEGLMTTIHAYTGDQMTLDGPHPKgDFRRARAAAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSLTELVTVL 80
Cdd:PLN02358 175 VEGLMTTVHSITATQKTVDGPSMK-DWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRL 253

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 308193620  81 EKEVTVDEINAAMKEASNES----YGYNTDEIVSSDIVGMTYGSLFDA 124
Cdd:PLN02358 254 EKAATYDEIKKAIKEESEGKlkgiLGYTEDDVVSTDFVGDNRSSIFDA 301
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 3-127 2.91e-29

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 108.60  E-value: 2.91e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193620   3 GLMTTIHAYTGDQMTLDGPHPKgDFRRARAAAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSLTELVTVLEK 82
Cdd:PTZ00434 189 GLMTTIHSYTATQKTVDGVSVK-DWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGKLTGMSFRVPTPDVSVVDLTFRATR 267

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 308193620  83 EVTVDEINAAMKEASnESY-----GYNTDEIVSSDIVGMTYGSLFDATQT 127
Cdd:PTZ00434 268 DTSIQEIDAAIKRAS-QTYmkgilGFTDDELVSADFINDNRSSIYDSKAT 316
PRK08289 PRK08289
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
 1-129 3.60e-28

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 236219 [Multi-domain]  Cd Length: 477  Bit Score: 106.93  E-value: 3.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193620   1 VEGLMTTIHAYTGDQMTLDGPHpKGDfRRARAAAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSLTELVTVL 80
Cdd:PRK08289 308 VNGHVETVHSYTNDQNLIDNYH-KGD-RRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNAIRVPTPNVSMAILNLNL 385

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 308193620  81 EKEVTVDEINAAMKEASNESY-----GY-NTDEIVSSDIVGMTYGSLFDATQTKV 129
Cdd:PRK08289 386 EKETSREELNEYLRQMSLHSPlqnqiDYtDSTEVVSSDFVGSRHAGVVDSQATIV 440
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
 1-130 8.56e-28

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 105.01  E-value: 8.56e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193620   1 VEGLMTTIHAYTGDQMTLDGPHPkgDFRRARAAAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSLTELVTVL 80
Cdd:PLN03096 231 IKGTMTTTHSYTGDQRLLDASHR--DLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQV 308

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 308193620  81 EKEVTVDEINAAMKEASNESYG---YNTDE-IVSSDIVGMTYGSLFDATQTKVM 130
Cdd:PLN03096 309 EKKTFAEEVNAAFRDAAEKELKgilAVCDEpLVSVDFRCSDVSSTIDSSLTMVM 362
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 1-130 2.69e-26

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: 96.43  E-value: 2.69e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193620   1 VEGLMTTIHAYTGDQMTLDGPHpkgDFRRARAAAANIVPNSTGAAKAIGLVIPELN--GKLDGAAQRVPVPTGSLTELVT 78
Cdd:cd18122   20 EEILVVTVQAVSGAGPKTKGPI---LKSEVRAIIPNIPKNETKHAPETGKVLGEIGkpIKVDGIAVRVPATLGHLVTVTV 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 308193620  79 VLEKEVTVDEINAAMKEASNESYGYNTDE----IVSSDIVGMTYGSLFDATQTKVM 130
Cdd:cd18122   97 KLEKTATLEQIAEAVAEAVEEVQISAEDGltyaKVSTRSVGGVYGVPVGRQREFAF 152
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
 1-130 3.12e-26

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 101.52  E-value: 3.12e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193620   1 VEGLMTTIHAYTGDQMTLDGPHPkgDFRRARAAAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSLTELVTVL 80
Cdd:PLN02237 248 VKGTMTTTHSYTGDQRLLDASHR--DLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTPNVSVVDLVVNV 325

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 308193620  81 EKE-VTVDEINAAMKEASNESYGYNTD----EIVSSDIVGMTYGSLFDATQTKVM 130
Cdd:PLN02237 326 EKKgITAEDVNAAFRKAADGPLKGILAvcdvPLVSVDFRCSDVSSTIDASLTMVM 380
PRK08955 PRK08955
glyceraldehyde-3-phosphate dehydrogenase; Validated
 3-129 2.57e-25

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 169599 [Multi-domain]  Cd Length: 334  Bit Score: 97.49  E-value: 2.57e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193620   3 GLMTTIHAYTGDQMTLDGPHPkgDFRRARAAAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSLTELVTVLEK 82
Cdd:PRK08955 173 GSMTTIHDLTNTQTILDAPHK--DLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLANASLTDCVFEVER 250

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 308193620  83 EVTVDEINAAMKEASNES----YGYNTDEIVSSDIVGMTYGSLFDATQTKV 129
Cdd:PRK08955 251 DTTVEEVNALLKEAAEGElkgiLGYEERPLVSIDYKTDPRSSIVDALSTMV 301
GAPDH_C_E4PDH cd23937
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 3-129 7.60e-21

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: 82.46  E-value: 7.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193620   3 GLMTTIHAYTGDQMTLDGPHPkgDFRRARAAAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSLTELVTVLEK 82
Cdd:cd23937   22 GTITTIHSAMNDQQVIDAYHP--DLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAIAVRVPTINVTAMDLSVTLKK 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 308193620  83 EVTVDEINAAMKEASNESY----GYNTDEIVSSDIVGMTYGSLFDATQTKV 129
Cdd:cd23937  100 DVTAEEVNRVLRQASQGRLkgilGYTEEPLVSVDFNHDPHSCIVDGTQTRV 150
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
 3-129 1.23e-13

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 65.85  E-value: 1.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193620   3 GLMTTIHAYTGDQMTLDGPHPkgDFRRARAAAANIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSLTELVTVLEK 82
Cdd:PRK13535 175 GTVTTIHSAMNDQQVIDAYHP--DLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPTINVTAIDLSVTVKK 252

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 308193620  83 EVTVDEINAAMKEASNESY----GYNTDEIVSSDIVGMTYGSLFDATQTKV 129
Cdd:PRK13535 253 PVKVNEVNQLLQKAAQGAFhgivDYTELPLVSIDFNHDPHSAIVDGTQTRV 303
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
 36-115 2.32e-05

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 42.17  E-value: 2.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308193620  36 NIVPNSTGAAKAIGLVIPELNGKLDGAAQRVPVPTGSLTELVTVLEKEVTVDEINAAMKEASNESYG----YNTDEIVSS 111
Cdd:PTZ00353 207 AIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVKKGCAIDMLVRTKQPVSKEVVDSALAEAASDRLNgvlcISKRDMISV 286


                 ....
gi 308193620 112 DIVG 115
Cdd:PTZ00353 287 DCIP 290
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH