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Conserved domains on  [gi|1097200711|gb|APA35783|]
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glyceraldehyde-3-phosphate dehydrogenase, partial [Ramularia asteris]

Protein Classification

type I glyceraldehyde-3-phosphate dehydrogenase( domain architecture ID 1000016)

type I glyceraldehyde-3-phosphate dehydrogenase is responsible for the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 1-139 1.61e-78

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: 229.20  E-value: 1.61e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097200711   1 IGRIVLRNAVEHGDVNVVAVNDPFIePTYAAYMLKYDSTHGVFKGTIEVDADKgLIVNGKKIRFHTERDPANIPWGESKA 80
Cdd:cd05214    11 IGRLVFRAALERDDIEVVAINDLTD-DETLAYLLKYDSVHGRFDGEVEVDDDA-LIVNGKKIKVFAERDPAELPWGELGV 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097200711  81 DYIVESTGVFTTTEKASAHLKGGAKKVVISAPSAD-APMFVMGVNNKTYTSDIPVISNAS 139
Cdd:cd05214    89 DIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDADDKIISNAS 148
 
Name Accession Description Interval E-value
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 1-139 1.61e-78

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: 229.20  E-value: 1.61e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097200711   1 IGRIVLRNAVEHGDVNVVAVNDPFIePTYAAYMLKYDSTHGVFKGTIEVDADKgLIVNGKKIRFHTERDPANIPWGESKA 80
Cdd:cd05214    11 IGRLVFRAALERDDIEVVAINDLTD-DETLAYLLKYDSVHGRFDGEVEVDDDA-LIVNGKKIKVFAERDPAELPWGELGV 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097200711  81 DYIVESTGVFTTTEKASAHLKGGAKKVVISAPSAD-APMFVMGVNNKTYTSDIPVISNAS 139
Cdd:cd05214    89 DIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDADDKIISNAS 148
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 1-141 1.58e-76

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 232.83  E-value: 1.58e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097200711   1 IGRIVLRNAVEHGDVNVVAVNDPFIEPTYAAYMLKYDSTHGVFKGTIEVDADKGLIVNGKKIRFHTERDPANIPWGESKA 80
Cdd:PLN02272   96 IGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVVDDSTLEINGKQIKVTSKRDPAEIPWGDFGA 175

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1097200711  81 DYIVESTGVFTTTEKASAHLKGGAKKVVISAPSADAPMFVMGVNNKTYTSDIPVISNASCT 141
Cdd:PLN02272  176 EYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCT 236
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-141 6.46e-71

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: 215.64  E-value: 6.46e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097200711   1 IGRIVLRNAVEHG-DVNVVAVNDPfIEPTYAAYMLKYDSTHGVFKGTIEVDADkGLIVNGKKIRFHTERDPANIPWGESK 79
Cdd:COG0057    13 IGRLVLRALLERGpDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGD-SLIVNGKKIKVLAERDPAELPWGELG 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1097200711  80 ADYIVESTGVFTTTEKASAHLKGGAKKVVISAPSADA-PMFVMGVNNKTYTSDIPVISNASCT 141
Cdd:COG0057    91 VDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCT 153
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-140 3.83e-69

Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. N-terminal domain is a Rossmann NAD(P) binding fold.


Pssm-ID: 214851 [Multi-domain]  Cd Length: 149  Bit Score: 205.09  E-value: 3.83e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097200711    1 IGRIVLRNAVEHGDVNVVAVNDPfIEPTYAAYMLKYDSTHGVFKGTIEVDADkGLIVNGKKIRFHTERDPANIPWGESKA 80
Cdd:smart00846  11 IGRLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGD-GLVVNGKAIKVFAERDPANLPWGELGV 88

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1097200711   81 DYIVESTGVFTTTEKASAHLKGGAKKVVISAPSADA-PMFVMGVNNKTYTSDIPVISNASC 140
Cdd:smart00846  89 DIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-92 5.50e-42

Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. N-terminal domain is a Rossmann NAD(P) binding fold.


Pssm-ID: 459648 [Multi-domain]  Cd Length: 101  Bit Score: 134.54  E-value: 5.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097200711   1 IGRIVLRNAVEHGDVNVVAVNDpFIEPTYAAYMLKYDSTHGVFKGTIEVDaDKGLIVNGKKIRFHTERDPANIPWGESKA 80
Cdd:pfam00044  11 IGRLVLRAALERPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAE-EDGLVVNGKKIKVFAERDPAELPWGDLGV 88

                          90
                  ....*....|..
gi 1097200711  81 DYIVESTGVFTT 92
Cdd:pfam00044  89 DVVIESTGVFTT 100
 
Name Accession Description Interval E-value
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 1-139 1.61e-78

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: 229.20  E-value: 1.61e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097200711   1 IGRIVLRNAVEHGDVNVVAVNDPFIePTYAAYMLKYDSTHGVFKGTIEVDADKgLIVNGKKIRFHTERDPANIPWGESKA 80
Cdd:cd05214    11 IGRLVFRAALERDDIEVVAINDLTD-DETLAYLLKYDSVHGRFDGEVEVDDDA-LIVNGKKIKVFAERDPAELPWGELGV 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097200711  81 DYIVESTGVFTTTEKASAHLKGGAKKVVISAPSAD-APMFVMGVNNKTYTSDIPVISNAS 139
Cdd:cd05214    89 DIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDADDKIISNAS 148
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 1-141 1.58e-76

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 232.83  E-value: 1.58e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097200711   1 IGRIVLRNAVEHGDVNVVAVNDPFIEPTYAAYMLKYDSTHGVFKGTIEVDADKGLIVNGKKIRFHTERDPANIPWGESKA 80
Cdd:PLN02272   96 IGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVVDDSTLEINGKQIKVTSKRDPAEIPWGDFGA 175

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1097200711  81 DYIVESTGVFTTTEKASAHLKGGAKKVVISAPSADAPMFVMGVNNKTYTSDIPVISNASCT 141
Cdd:PLN02272  176 EYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCT 236
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-141 6.46e-71

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: 215.64  E-value: 6.46e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097200711   1 IGRIVLRNAVEHG-DVNVVAVNDPfIEPTYAAYMLKYDSTHGVFKGTIEVDADkGLIVNGKKIRFHTERDPANIPWGESK 79
Cdd:COG0057    13 IGRLVLRALLERGpDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGD-SLIVNGKKIKVLAERDPAELPWGELG 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1097200711  80 ADYIVESTGVFTTTEKASAHLKGGAKKVVISAPSADA-PMFVMGVNNKTYTSDIPVISNASCT 141
Cdd:COG0057    91 VDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCT 153
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-140 3.83e-69

Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. N-terminal domain is a Rossmann NAD(P) binding fold.


Pssm-ID: 214851 [Multi-domain]  Cd Length: 149  Bit Score: 205.09  E-value: 3.83e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097200711    1 IGRIVLRNAVEHGDVNVVAVNDPfIEPTYAAYMLKYDSTHGVFKGTIEVDADkGLIVNGKKIRFHTERDPANIPWGESKA 80
Cdd:smart00846  11 IGRLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGD-GLVVNGKAIKVFAERDPANLPWGELGV 88

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1097200711   81 DYIVESTGVFTTTEKASAHLKGGAKKVVISAPSADA-PMFVMGVNNKTYTSDIPVISNASC 140
Cdd:smart00846  89 DIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
 1-141 6.77e-57

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 180.03  E-value: 6.77e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097200711   1 IGRIVLRNAVEHGDVNVVAVNDPFIEPTYAAYMLKYDSTHGVFKGTIEVDADKgLIVNGKKIRFHTERDPANIPWGESKA 80
Cdd:PTZ00023   13 IGRLVFRAALEREDVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGF-LMIGSKKVHVFFEKDPAAIPWGKNGV 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1097200711  81 DYIVESTGVFTTTEKASAHLKGGAKKVVISAP-SADAPMFVMGVNNKTYTSDIPVISNASCT 141
Cdd:PTZ00023   92 DVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPpKDDTPIYVMGVNHTQYDKSQRIVSNASCT 153
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
 1-141 1.96e-49

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 161.04  E-value: 1.96e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097200711   1 IGRIVLRNAVEHGDVNVVAVNDPFIEPTYAAYMLKYDSTHGVFK-GTIEVDADKGLIVNGKKIRFHTERDPANIPWGESK 79
Cdd:PLN02358   16 IGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKhHELKVKDDKTLLFGEKPVTVFGIRNPEDIPWGEAG 95

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1097200711  80 ADYIVESTGVFTTTEKASAHLKGGAKKVVISAPSADAPMFVMGVNNKTYTSDIPVISNASCT 141
Cdd:PLN02358   96 ADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCT 157
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
1-141 7.09e-43

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 144.11  E-value: 7.09e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097200711   1 IGRIVLRNAVEHGDVNVVAVNDpFIEPTYAAYMLKYDSTHGVFKGTIEVDaDKGLIVNGKKIRFHTERDPANIPWGESKA 80
Cdd:PRK15425   13 IGRIVFRAAQKRSDIEIVAIND-LLDADYMAYMLKYDSTHGRFDGTVEVK-DGHLIVNGKKIRVTAERDPANLKWDEVGV 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1097200711  81 DYIVESTGVFTTTEKASAHLKGGAKKVVISAPSAD-APMFVMGVNNKTYTSDiPVISNASCT 141
Cdd:PRK15425   91 DVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDnTPMFVKGANFDKYAGQ-DIVSNASCT 151
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-92 5.50e-42

Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. N-terminal domain is a Rossmann NAD(P) binding fold.


Pssm-ID: 459648 [Multi-domain]  Cd Length: 101  Bit Score: 134.54  E-value: 5.50e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097200711   1 IGRIVLRNAVEHGDVNVVAVNDpFIEPTYAAYMLKYDSTHGVFKGTIEVDaDKGLIVNGKKIRFHTERDPANIPWGESKA 80
Cdd:pfam00044  11 IGRLVLRAALERPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAE-EDGLVVNGKKIKVFAERDPAELPWGDLGV 88

                          90
                  ....*....|..
gi 1097200711  81 DYIVESTGVFTT 92
Cdd:pfam00044  89 DVVIESTGVFTT 100
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-141 4.14e-41

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 139.49  E-value: 4.14e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097200711   1 IGRIVLRNAVEHGDVNVVAVNDPFIEPTYAaYMLKYDSTHGVFKGTIEVDADkGLIVNGKKIRFHTERDPANIPWGESKA 80
Cdd:PRK07729   13 IGRMVFRKAIKESAFEIVAINASYPSETLA-HLIKYDTVHGKFDGTVEAFED-HLLVDGKKIRLLNNRDPKELPWTDLGI 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1097200711  81 DYIVESTGVFTTTEKASAHLKGGAKKVVISAPSADAPM-FVMGVNNKTYTSDI-PVISNASCT 141
Cdd:PRK07729   91 DIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVtIVVGVNEDQLDIEKhTIISNASCT 153
GAPDH_N_E4PDH cd17892
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 1-139 2.86e-39

N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar proteins; 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 family of proteins.


Pssm-ID: 467615 [Multi-domain]  Cd Length: 169  Bit Score: 130.08  E-value: 2.86e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097200711   1 IGRIVLRNAVEHG---DVNVVAVNDPfIEPTYAAYMLKYDSTHGVFKGTIEVDADKgLIVNGKKIRFHTERDPANIPWGE 77
Cdd:cd17892    11 IGRNVLRALYESGrraEFQVVAINEL-ADAETIAHLTKYDTTHGRFPGEVRVENDQ-LFVNGDKIRVLHEPDPENLPWRE 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1097200711  78 SKADYIVESTGVFTTTEKASAHLKGGAKKVVISAPSA---DAPMfVMGVNNKTYTSDIPVISNAS 139
Cdd:cd17892    89 LGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASndvDATI-VYGINQDLLRAEHRIVSNAS 152
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 1-141 7.51e-39

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 134.03  E-value: 7.51e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097200711   1 IGRIVLRNAVEHG----DVNVVAVNDPFIEPTYAAYMLKYDSTHGVFKGTIE-------VDADKGLIVNGKKIR-FHTER 68
Cdd:PTZ00434   14 IGRMVFQAICDQGligtEIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVEttksspsVKTDDVLVVNGHRIKcVKAQR 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1097200711  69 DPANIPWGESKADYIVESTGVFTTTEKASAHLKGGAKKVVISAP-SADAPMFVMGVNNKTYT-SDIPVISNASCT 141
Cdd:PTZ00434   94 NPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPaSGGAKTIVMGVNQHEYSpTEHHVVSNASCT 168
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
1-141 1.15e-34

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 122.71  E-value: 1.15e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097200711   1 IGRIVLRNAV--EHGDVNVVAVNDPfIEPTYAAYMLKYDSTHGVFKGTIEVDaDKGLIVNGKKIRFHTERDPANIPWGES 78
Cdd:PRK07403   12 IGRNFLRCWLgrENSQLELVAINDT-SDPRTNAHLLKYDSMLGKLNADISAD-ENSITVNGKTIKCVSDRNPLNLPWKEW 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1097200711  79 KADYIVESTGVFTTTEKASAHLKGGAKKVVISAP--SADAPMFVMGVNNKTYTSDI-PVISNASCT 141
Cdd:PRK07403   90 GIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPgkGEDIGTYVVGVNHHEYDHEDhNIISNASCT 155
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
 1-141 2.28e-34

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 123.12  E-value: 2.28e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097200711   1 IGRIVLR--NAVEHGDVNVVAVNDPFiEPTYAAYMLKYDSTHGVFKGTIEVDADKGLIVNGKKIRFHTERDPANIPWGES 78
Cdd:PLN03096   71 IGRNFLRcwHGRKDSPLDVVAINDTG-GVKQASHLLKYDSTLGTFDADVKPVGDDAISVDGKVIKVVSDRNPLNLPWGEL 149

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1097200711  79 KADYIVESTGVFTTTEKASAHLKGGAKKVVISAPS-ADAPMFVMGVNNKTYTSDIPVISNASCT 141
Cdd:PLN03096  150 GIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGkGDIPTYVVGVNADDYKHSDPIISNASCT 213
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
 1-141 1.25e-31

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 114.77  E-value: 1.25e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097200711   1 IGRIVLRNAVEHG---DVNVVAVNDpFIEPTYAAYMLKYDSTHGVFKGTIEVDADKgLIVNGKKIRFHTERDPANIPWGE 77
Cdd:PRK13535   12 IGRNVLRALYESGrraEITVVAINE-LADAEGMAHLLKYDTSHGRFAWDVRQERDQ-LFVGDDAIRLLHERDIASLPWRE 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1097200711  78 SKADYIVESTGVFTTTEKASAHLKGGAKKVVISAPSA---DAPMfVMGVNNKTYTSDIPVISNASCT 141
Cdd:PRK13535   90 LGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSndlDATV-VYGVNHDQLRAEHRIVSNASCT 155
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
 1-141 3.95e-30

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 112.30  E-value: 3.95e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097200711   1 IGRIVLRNAVEHGD--VNVVAVNDPF-IEPtyAAYMLKYDSTHGVFKGTIEVDADKGLIVNGKKIRFHTERDPANIPWGE 77
Cdd:PLN02237   86 IGRNFLRCWHGRKDspLDVVVVNDSGgVKN--ASHLLKYDSMLGTFKADVKIVDDETISVDGKPIKVVSNRDPLKLPWAE 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1097200711  78 SKADYIVESTGVFTTTEKASAHLKGGAKKVVISAPS--ADAPMFVMGVNNKTYTSDIP-VISNASCT 141
Cdd:PLN02237  164 LGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAkgADIPTYVVGVNEDDYDHEVAnIVSNASCT 230
PRK08955 PRK08955
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-141 3.15e-24

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 169599 [Multi-domain]  Cd Length: 334  Bit Score: 95.18  E-value: 3.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097200711   1 IGRIVLRNAVEHGDVNVVAVNDPFIEPTYAAYMLKYDSTHGVFKGTIEVDADkGLIVNGKKIRFHTERDPANIPWgeSKA 80
Cdd:PRK08955   13 IGRLALRAAWDWPELEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTAEGD-AIVINGKRIRTTQNKAIADTDW--SGC 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1097200711  81 DYIVESTGVFTTTEKASAHLKGGAKKVVISAPSADAPMF--VMGVNNKTYTSDI-PVISNASCT 141
Cdd:PRK08955   90 DVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLniVMGVNDHLFDPAIhPIVTAASCT 153
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
 1-139 3.64e-22

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 89.55  E-value: 3.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097200711   1 IGRIVLRNAVEHGDVNVVAVNDPFIEPTYAAYMLKYDSTHGVFKGT-IEVDADKGLIVNGKKIRFHTERDPANIPWGESK 79
Cdd:PTZ00353   13 VGKAVLFASLTDPLVTVVAVNDASVSIAYIAYVLEQESPLSAPDGAsIRVVGEQIVLNGTQKIRVSAKHDLVEIAWRDYG 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097200711  80 ADYIVESTGVFTTTEKASAHLKGGAKKVVISAPSADAPMFVMGVNNKTYTSDIPVISNAS 139
Cdd:PTZ00353   93 VQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDERLSASLPVCCAGA 152
PRK08289 PRK08289
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
 31-141 8.71e-22

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 236219 [Multi-domain]  Cd Length: 477  Bit Score: 89.60  E-value: 8.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1097200711  31 AYMLKYDSTHGVFKGTIEVDAD-KGLIVNGKKIRFHTERDPANIpwgeskaDY---------IVESTGVFTTTEKASAHL 100
Cdd:PRK08289  175 ASLLRRDSVHGPFNGTITVDEEnNAIIANGNYIQVIYANSPEEV-------DYtayginnalVVDNTGKWRDEEGLSQHL 247

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1097200711 101 KG-GAKKVVISAPS-ADAPMFVMGVNNKTYTSDIPVISNASCT 141
Cdd:PRK08289  248 KSkGVAKVLLTAPGkGDIKNIVHGVNHSDITDEDKIVSAASCT 290
GAPDH-like_N cd05192
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ...
 81-138 5.50e-07

N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like family; The GAPDH-like family includes glyceraldehyde-3-phosphate dehydrogenase (GAPDH), native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs), 2,4-diaminopentanoate dehydrogenase (DAPDH), meso-diaminopimelate D-dehydrogenase (meso-DAPDH), and dihydrodipicolinate reductase (DHDPR). 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. nat-AmDHs catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. They play important roles in the efficient asymmetric synthesis of alpha-chiral amines. DAPDH is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). DHDPR catalyzes the NAD(P)H-dependent reduction of 2,3-dihydrodipicolinate (DHDP) to 2,3,4,5-tetrahydrodipicolinate (THDP). It could also function as a dehydratase in addition to the role of a nucleotide dependent reductase. The model corresponds to the N-terminal NAD(P)-binding domain of GAPDH-like family proteins. It contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft.


Pssm-ID: 467613 [Multi-domain]  Cd Length: 109  Bit Score: 45.04  E-value: 5.50e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1097200711  81 DYIVESTGVFTTTEKASAHLKGGAKKVVISAPS-ADAPMFVMGVNNKTYTSDIPVISNA 138
Cdd:cd05192    35 DVVIECTGSFTDDDNAEKHIKAGGKKAVITAPEkGDIPTIVVVLNELAKSAGATVVSNA 93
 
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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