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Conserved domains on  [gi|510947029|gb|AGN53499|]
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glyceraldehyde-3-phosphate dehydrogenase, partial [Alternaria dianthicola]

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) ...
 1-136 1.85e-79

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: 231.51  E-value: 1.85e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510947029   1 RIVFRNAIEHNDVDIVAVNDPFIePHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYV 80
Cdd:cd05214   13 RLVFRAALERDDIEVVAINDLTD-DETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAELPWGELGVDIV 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 510947029  81 VESTGVFTTTEKAKAHLKGGAKKVVISAPSAD-APMFVMGVNHETYKSDIEVLSNAS 136
Cdd:cd05214   92 IESTGVFTTKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDADDKIISNAS 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) ...
 1-136 1.85e-79

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: 231.51  E-value: 1.85e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510947029   1 RIVFRNAIEHNDVDIVAVNDPFIePHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYV 80
Cdd:cd05214   13 RLVFRAALERDDIEVVAINDLTD-DETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAELPWGELGVDIV 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 510947029  81 VESTGVFTTTEKAKAHLKGGAKKVVISAPSAD-APMFVMGVNHETYKSDIEVLSNAS 136
Cdd:cd05214   92 IESTGVFTTKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDADDKIISNAS 148
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 1-136 2.38e-72

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 222.04  E-value: 2.38e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510947029   1 RIVFRNAIEHNDVDIVAVNDPFIEPHYAAYMLKYDSTHGQFKGEIKV-DGNNLTVNGKTIRFHMEKDPANIPWSETGAYY 79
Cdd:PLN02272  98 RLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDPAEIPWGDFGAEY 177

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 510947029  80 VVESTGVFTTTEKAKAHLKGGAKKVVISAPSADAPMFVMGVNHETYKSDIEVLSNAS 136
Cdd:PLN02272 178 VVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNAS 234
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-136 5.65e-68

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: 207.94  E-value: 5.65e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510947029   1 RIVFRNAIEH-NDVDIVAVNDPfIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYY 79
Cdd:COG0057   15 RLVLRALLERgPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAELPWGELGVDV 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 510947029  80 VVESTGVFTTTEKAKAHLKGGAKKVVISAPSADA-PMFVMGVNHETYKSDIEVLSNAS 136
Cdd:COG0057   94 VIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNAS 151
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-136 1.85e-67

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: 200.47  E-value: 1.85e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510947029     1 RIVFRNAIEHNDVDIVAVNDPfIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYV 80
Cdd:smart00846  13 RLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANLPWGELGVDIV 91

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 510947029    81 VESTGVFTTTEKAKAHLKGGAKKVVISAPSADA-PMFVMGVNHETYKSDIEVLSNAS 136
Cdd:smart00846  92 VECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNAS 148
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-89 9.09e-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: 133.77  E-value: 9.09e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510947029    1 RIVFRNAIEHNDVDIVAVNDpFIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYV 80
Cdd:pfam00044  13 RLVLRAALERPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAELPWGDLGVDVV 91


                  ....*....
gi 510947029   81 VESTGVFTT 89
Cdd:pfam00044  92 IESTGVFTT 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) ...
 1-136 1.85e-79

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: 231.51  E-value: 1.85e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510947029   1 RIVFRNAIEHNDVDIVAVNDPFIePHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYV 80
Cdd:cd05214   13 RLVFRAALERDDIEVVAINDLTD-DETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAELPWGELGVDIV 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 510947029  81 VESTGVFTTTEKAKAHLKGGAKKVVISAPSAD-APMFVMGVNHETYKSDIEVLSNAS 136
Cdd:cd05214   92 IESTGVFTTKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDADDKIISNAS 148
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 1-136 2.38e-72

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 222.04  E-value: 2.38e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510947029   1 RIVFRNAIEHNDVDIVAVNDPFIEPHYAAYMLKYDSTHGQFKGEIKV-DGNNLTVNGKTIRFHMEKDPANIPWSETGAYY 79
Cdd:PLN02272  98 RLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDPAEIPWGDFGAEY 177

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 510947029  80 VVESTGVFTTTEKAKAHLKGGAKKVVISAPSADAPMFVMGVNHETYKSDIEVLSNAS 136
Cdd:PLN02272 178 VVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNAS 234
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-136 5.65e-68

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: 207.94  E-value: 5.65e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510947029   1 RIVFRNAIEH-NDVDIVAVNDPfIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYY 79
Cdd:COG0057   15 RLVLRALLERgPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAELPWGELGVDV 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 510947029  80 VVESTGVFTTTEKAKAHLKGGAKKVVISAPSADA-PMFVMGVNHETYKSDIEVLSNAS 136
Cdd:COG0057   94 VIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNAS 151
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-136 1.85e-67

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: 200.47  E-value: 1.85e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510947029     1 RIVFRNAIEHNDVDIVAVNDPfIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYV 80
Cdd:smart00846  13 RLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANLPWGELGVDIV 91

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 510947029    81 VESTGVFTTTEKAKAHLKGGAKKVVISAPSADA-PMFVMGVNHETYKSDIEVLSNAS 136
Cdd:smart00846  92 VECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNAS 148
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
 1-136 1.60e-55

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 176.56  E-value: 1.60e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510947029   1 RIVFRNAIEHNDVDIVAVNDPFIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYV 80
Cdd:PTZ00023  15 RLVFRAALEREDVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKDPAAIPWGKNGVDVV 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 510947029  81 VESTGVFTTTEKAKAHLKGGAKKVVISAP-SADAPMFVMGVNHETYKSDIEVLSNAS 136
Cdd:PTZ00023  95 CESTGVFLTKEKAQAHLKGGAKKVIMSAPpKDDTPIYVMGVNHTQYDKSQRIVSNAS 151
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
 1-136 2.99e-48

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 157.96  E-value: 2.99e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510947029   1 RIVFRNAIEHNDVDIVAVNDPFIEPHYAAYMLKYDSTHGQFK-GEIKV-DGNNLTVNGKTIRFHMEKDPANIPWSETGAY 78
Cdd:PLN02358  18 RLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKhHELKVkDDKTLLFGEKPVTVFGIRNPEDIPWGEAGAD 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 510947029  79 YVVESTGVFTTTEKAKAHLKGGAKKVVISAPSADAPMFVMGVNHETYKSDIEVLSNAS 136
Cdd:PLN02358  98 FVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNAS 155
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
1-136 3.19e-42

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 142.18  E-value: 3.19e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510947029   1 RIVFRNAIEHNDVDIVAVNDpFIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYV 80
Cdd:PRK15425  15 RIVFRAAQKRSDIEIVAIND-LLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPANLKWDEVGVDVV 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 510947029  81 VESTGVFTTTEKAKAHLKGGAKKVVISAPSAD-APMFVMGVNHETYKSDiEVLSNAS 136
Cdd:PRK15425  94 AEATGLFLTDETARKHITAGAKKVVMTGPSKDnTPMFVKGANFDKYAGQ-DIVSNAS 149
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-89 9.09e-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: 133.77  E-value: 9.09e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510947029    1 RIVFRNAIEHNDVDIVAVNDpFIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYV 80
Cdd:pfam00044  13 RLVLRAALERPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAELPWGDLGVDVV 91


                  ....*....
gi 510947029   81 VESTGVFTT 89
Cdd:pfam00044  92 IESTGVFTT 100
GAPDH_N_E4PDH cd17892
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 11-136 1.18e-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: 130.85  E-value: 1.18e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510947029  11 NDVDIVAVNDPfIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFTTT 90
Cdd:cd17892   26 AEFQVVAINEL-ADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPDPENLPWRELGIDLVLECTGVFGSR 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 510947029  91 EKAKAHLKGGAKKVVISAPSA---DAPMfVMGVNHETYKSDIEVLSNAS 136
Cdd:cd17892  105 EDAERHLAAGAKKVLFSHPASndvDATI-VYGINQDLLRAEHRIVSNAS 152
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-136 2.23e-37

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 129.86  E-value: 2.23e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510947029   1 RIVFRNAIEHNDVDIVAVNDPFiEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYV 80
Cdd:PRK07729  15 RMVFRKAIKESAFEIVAINASY-PSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDPKELPWTDLGIDIV 93

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 510947029  81 VESTGVFTTTEKAKAHLKGGAKKVVISAPSADAPM-FVMGVNHETYKSDIE-VLSNAS 136
Cdd:PRK07729  94 IEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVtIVVGVNEDQLDIEKHtIISNAS 151
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
9-136 2.49e-36

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 126.95  E-value: 2.49e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510947029   9 EHNDVDIVAVNDPfIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFT 88
Cdd:PRK07403  24 ENSQLELVAINDT-SDPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDRNPLNLPWKEWGIDLIIESTGVFV 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 510947029  89 TTEKAKAHLKGGAKKVVISAP--SADAPMFVMGVNHETYKSDI-EVLSNAS 136
Cdd:PRK07403 103 TKEGASKHIQAGAKKVLITAPgkGEDIGTYVVGVNHHEYDHEDhNIISNAS 153
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 1-136 1.31e-33

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 120.16  E-value: 1.31e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510947029   1 RIVFRNAIEH----NDVDIVAVNDPFIEPHYAAYMLKYDSTHGQFKGEIKV--------DGNNLTVNGKTIR-FHMEKDP 67
Cdd:PTZ00434  16 RMVFQAICDQgligTEIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVETtksspsvkTDDVLVVNGHRIKcVKAQRNP 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510947029  68 ANIPWSETGAYYVVESTGVFTTTEKAKAHLKGGAKKVVISAP-SADAPMFVMGVNHETYK-SDIEVLSNAS 136
Cdd:PTZ00434  96 ADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPaSGGAKTIVMGVNQHEYSpTEHHVVSNAS 166
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
 13-136 5.05e-31

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 113.87  E-value: 5.05e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510947029  13 VDIVAVNDPFiEPHYAAYMLKYDSTHGQFKGEIKVDGNN-LTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFTTTE 91
Cdd:PLN03096  87 LDVVAINDTG-GVKQASHLLKYDSTLGTFDADVKPVGDDaISVDGKVIKVVSDRNPLNLPWGELGIDLVIEGTGVFVDRE 165

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 510947029  92 KAKAHLKGGAKKVVISAPS-ADAPMFVMGVNHETYKSDIEVLSNAS 136
Cdd:PLN03096 166 GAGKHIQAGAKKVLITAPGkGDIPTYVVGVNADDYKHSDPIISNAS 211
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
 1-136 2.16e-29

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 108.61  E-value: 2.16e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510947029   1 RIVFRNAIE---HNDVDIVAVNDpFIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGA 77
Cdd:PRK13535  14 RNVLRALYEsgrRAEITVVAINE-LADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHERDIASLPWRELGV 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 510947029  78 YYVVESTGVFTTTEKAKAHLKGGAKKVVISAPSA---DAPMfVMGVNHETYKSDIEVLSNAS 136
Cdd:PRK13535  93 DVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSndlDATV-VYGVNHDQLRAEHRIVSNAS 153
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
 13-136 1.47e-28

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 108.06  E-value: 1.47e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510947029  13 VDIVAVNDPF-IEPhyAAYMLKYDSTHGQFKGEIK-VDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFTTT 90
Cdd:PLN02237 102 LDVVVVNDSGgVKN--ASHLLKYDSMLGTFKADVKiVDDETISVDGKPIKVVSNRDPLKLPWAELGIDIVIEGTGVFVDG 179

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 510947029  91 EKAKAHLKGGAKKVVISAPS--ADAPMFVMGVNHETYKSDI-EVLSNAS 136
Cdd:PLN02237 180 PGAGKHIQAGAKKVIITAPAkgADIPTYVVGVNEDDYDHEVaNIVSNAS 228
PRK08955 PRK08955
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-129 3.50e-25

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 169599 [Multi-domain]  Cd Length: 334  Bit Score: 97.49  E-value: 3.50e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510947029   1 RIVFRNAIEHNDVDIVAVNDPFIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSetGAYYV 80
Cdd:PRK08955  15 RLALRAAWDWPELEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKAIADTDWS--GCDVV 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 510947029  81 VESTGVFTTTEKAKAHLKGGAKKVVISAPSADAPMF--VMGVNHETYKSDI 129
Cdd:PRK08955  93 IEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLniVMGVNDHLFDPAI 143
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
 13-136 3.12e-21

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 86.85  E-value: 3.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510947029  13 VDIVAVNDPFIEPHYAAYMLKYDSTH-GQFKGEIKVDGNNLTVNG-KTIRFHMEKDPANIPWSETGAYYVVESTGVFTTT 90
Cdd:PTZ00353  27 VTVVAVNDASVSIAYIAYVLEQESPLsAPDGASIRVVGEQIVLNGtQKIRVSAKHDLVEIAWRDYGVQYVVECTGLYSTR 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 510947029  91 EKAKAHLKGGAKKVVISAPSADAPMFVMGVNHETYKSDIEVLSNAS 136
Cdd:PTZ00353 107 SRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDERLSASLPVCCAGA 152
GAPDH-like_N cd05192
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ...
 79-135 6.29e-09

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: 50.04  E-value: 6.29e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 510947029  79 YVVESTGVFTTTEKAKAHLKGGAKKVVISAPS-ADAPMFVMGVNHETYKSDIEVLSNA 135
Cdd:cd05192   36 VVIECTGSFTDDDNAEKHIKAGGKKAVITAPEkGDIPTIVVVLNELAKSAGATVVSNA 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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