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Conserved domains on  [gi|441467727|gb|AGC36426|]
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glyceraldehyde 3-phosphate dehydrogenase, partial [Alternaria simsimi]

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) ...
 1-120 9.81e-70

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: 206.09  E-value: 9.81e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441467727   1 EHNDVDIVAVNDPFIePHYAAYMLKYDSTHGQFKGEIKVEGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFT 80
Cdd:cd05214   21 ERDDIEVVAINDLTD-DETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAELPWGELGVDIVIESTGVFT 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 441467727  81 TTEKAKAHLKGGAKKVVISAPSAD-APMFVMGVSHETYKSD 120
Cdd:cd05214  100 TKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDAD 140
 
Name Accession Description Interval E-value
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 1-120 9.81e-70

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: 206.09  E-value: 9.81e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441467727   1 EHNDVDIVAVNDPFIePHYAAYMLKYDSTHGQFKGEIKVEGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFT 80
Cdd:cd05214   21 ERDDIEVVAINDLTD-DETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAELPWGELGVDIVIESTGVFT 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 441467727  81 TTEKAKAHLKGGAKKVVISAPSAD-APMFVMGVSHETYKSD 120
Cdd:cd05214  100 TKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDAD 140
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 3-123 1.76e-64

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 201.24  E-value: 1.76e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441467727   3 NDVDIVAVNDPFIEPHYAAYMLKYDSTHGQFKGEIKV-EGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFTT 81
Cdd:PLN02272 108 DDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDPAEIPWGDFGAEYVVESSGVFTT 187

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 441467727  82 TEKAKAHLKGGAKKVVISAPSADAPMFVMGVSHETYKSDIEV 123
Cdd:PLN02272 188 VEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNI 229
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 2-120 4.32e-59

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: 184.83  E-value: 4.32e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441467727   2 HNDVDIVAVNDPfIEPHYAAYMLKYDSTHGQFKGEIKVEGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFTT 81
Cdd:COG0057   25 GPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAELPWGELGVDVVIECTGKFTD 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 441467727  82 TEKAKAHLKGGAKKVVISAPSADA-PMFVMGVSHETYKSD 120
Cdd:COG0057  104 REKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDAD 143
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-123 7.38e-59

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: 178.13  E-value: 7.38e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441467727     1 EHNDVDIVAVNDPfIEPHYAAYMLKYDSTHGQFKGEIKVEGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFT 80
Cdd:smart00846  21 ERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANLPWGELGVDIVVECTGGFT 99

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 441467727    81 TTEKAKAHLKGGAKKVVISAPSADA-PMFVMGVSHETYKSDIEV 123
Cdd:smart00846 100 TREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHI 143
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-81 2.81e-38

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: 124.52  E-value: 2.81e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441467727    1 EHNDVDIVAVNDpFIEPHYAAYMLKYDSTHGQFKGEIKVEGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFT 80
Cdd:pfam00044  21 ERPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAELPWGDLGVDVVIESTGVFT 99


                  .
gi 441467727   81 T 81
Cdd:pfam00044 100 T 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) ...
 1-120 9.81e-70

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: 206.09  E-value: 9.81e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441467727   1 EHNDVDIVAVNDPFIePHYAAYMLKYDSTHGQFKGEIKVEGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFT 80
Cdd:cd05214   21 ERDDIEVVAINDLTD-DETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAELPWGELGVDIVIESTGVFT 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 441467727  81 TTEKAKAHLKGGAKKVVISAPSAD-APMFVMGVSHETYKSD 120
Cdd:cd05214  100 TKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDAD 140
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 3-123 1.76e-64

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 201.24  E-value: 1.76e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441467727   3 NDVDIVAVNDPFIEPHYAAYMLKYDSTHGQFKGEIKV-EGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFTT 81
Cdd:PLN02272 108 DDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDPAEIPWGDFGAEYVVESSGVFTT 187

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 441467727  82 TEKAKAHLKGGAKKVVISAPSADAPMFVMGVSHETYKSDIEV 123
Cdd:PLN02272 188 VEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNI 229
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 2-120 4.32e-59

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: 184.83  E-value: 4.32e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441467727   2 HNDVDIVAVNDPfIEPHYAAYMLKYDSTHGQFKGEIKVEGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFTT 81
Cdd:COG0057   25 GPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAELPWGELGVDVVIECTGKFTD 103

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 441467727  82 TEKAKAHLKGGAKKVVISAPSADA-PMFVMGVSHETYKSD 120
Cdd:COG0057  104 REKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDAD 143
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-123 7.38e-59

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: 178.13  E-value: 7.38e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441467727     1 EHNDVDIVAVNDPfIEPHYAAYMLKYDSTHGQFKGEIKVEGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFT 80
Cdd:smart00846  21 ERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANLPWGELGVDIVVECTGGFT 99

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 441467727    81 TTEKAKAHLKGGAKKVVISAPSADA-PMFVMGVSHETYKSDIEV 123
Cdd:smart00846 100 TREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHI 143
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
 1-119 1.75e-47

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 155.38  E-value: 1.75e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441467727   1 EHNDVDIVAVNDPFIEPHYAAYMLKYDSTHGQFKGEIKVEGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFT 80
Cdd:PTZ00023  23 EREDVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKDPAAIPWGKNGVDVVCESTGVFL 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 441467727  81 TTEKAKAHLKGGAKKVVISAP-SADAPMFVMGVSHETYKS 119
Cdd:PTZ00023 103 TKEKAQAHLKGGAKKVIMSAPpKDDTPIYVMGVNHTQYDK 142
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
 1-123 3.11e-42

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 141.78  E-value: 3.11e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441467727   1 EHNDVDIVAVNDPFIEPHYAAYMLKYDSTHGQFK-GEIKVEGNNLTVNG-KTIRFHMEKDPANIPWSETGAYYVVESTGV 78
Cdd:PLN02358  26 QRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKhHELKVKDDKTLLFGeKPVTVFGIRNPEDIPWGEAGADFVVESTGV 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 441467727  79 FTTTEKAKAHLKGGAKKVVISAPSADAPMFVMGVSHETYKSDIEV 123
Cdd:PLN02358 106 FTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDI 150
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-81 2.81e-38

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: 124.52  E-value: 2.81e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441467727    1 EHNDVDIVAVNDpFIEPHYAAYMLKYDSTHGQFKGEIKVEGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFT 80
Cdd:pfam00044  21 ERPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAELPWGDLGVDVVIESTGVFT 99


                  .
gi 441467727   81 T 81
Cdd:pfam00044 100 T 100
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
1-117 9.26e-37

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 127.16  E-value: 9.26e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441467727   1 EHNDVDIVAVNDpFIEPHYAAYMLKYDSTHGQFKGEIKVEGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFT 80
Cdd:PRK15425  23 KRSDIEIVAIND-LLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPANLKWDEVGVDVVAEATGLFL 101

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 441467727  81 TTEKAKAHLKGGAKKVVISAPSAD-APMFVMGVSHETY 117
Cdd:PRK15425 102 TDETARKHITAGAKKVVMTGPSKDnTPMFVKGANFDKY 139
GAPDH_N_E4PDH cd17892
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 3-120 7.05e-36

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: 120.45  E-value: 7.05e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441467727   3 NDVDIVAVNDPfIEPHYAAYMLKYDSTHGQFKGEIKVEGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFTTT 82
Cdd:cd17892   26 AEFQVVAINEL-ADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPDPENLPWRELGIDLVLECTGVFGSR 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 441467727  83 EKAKAHLKGGAKKVVISAPSA---DAPMfVMGVSHETYKSD 120
Cdd:cd17892  105 EDAERHLAAGAKKVLFSHPASndvDATI-VYGINQDLLRAE 144
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
1-121 8.40e-33

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 116.93  E-value: 8.40e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441467727   1 EHNDVDIVAVNDPfIEPHYAAYMLKYDSTHGQFKGEIKVEGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFT 80
Cdd:PRK07403  24 ENSQLELVAINDT-SDPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDRNPLNLPWKEWGIDLIIESTGVFV 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 441467727  81 TTEKAKAHLKGGAKKVVISAP--SADAPMFVMGVSHETYKSDI 121
Cdd:PRK07403 103 TKEGASKHIQAGAKKVLITAPgkGEDIGTYVVGVNHHEYDHED 145
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 3-117 6.96e-31

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 112.46  E-value: 6.96e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441467727   3 NDVDIVAVNDPFIEPHYAAYMLKYDSTHGQFKGEIKV--------EGNNLTVNGKTIR-FHMEKDPANIPWSETGAYYVV 73
Cdd:PTZ00434  30 TEIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVETtksspsvkTDDVLVVNGHRIKcVKAQRNPADLPWGKLGVDYVI 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 441467727  74 ESTGVFTTTEKAKAHLKGGAKKVVISAP-SADAPMFVMGVSHETY 117
Cdd:PTZ00434 110 ESTGLFTDKLAAEGHLKGGAKKVVISAPaSGGAKTIVMGVNQHEY 154
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 3-120 1.34e-29

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 108.67  E-value: 1.34e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441467727   3 NDVDIVAVNDPFiEPHYAAYMLKYDSTHGQFKGEIKVEGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFTTT 82
Cdd:PRK07729  25 SAFEIVAINASY-PSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDPKELPWTDLGIDIVIEATGKFNSK 103

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 441467727  83 EKAKAHLKGGAKKVVISAPSADAPM-FVMGVSHETYKSD 120
Cdd:PRK07729 104 EKAILHVEAGAKKVILTAPGKNEDVtIVVGVNEDQLDIE 142
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
 5-120 7.78e-28

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 105.01  E-value: 7.78e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441467727   5 VDIVAVNDPFiEPHYAAYMLKYDSTHGQFKGEIKVEGNN-LTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFTTTE 83
Cdd:PLN03096  87 LDVVAINDTG-GVKQASHLLKYDSTLGTFDADVKPVGDDaISVDGKVIKVVSDRNPLNLPWGELGIDLVIEGTGVFVDRE 165

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 441467727  84 KAKAHLKGGAKKVVISAPS-ADAPMFVMGVSHETYKSD 120
Cdd:PLN03096 166 GAGKHIQAGAKKVLITAPGkGDIPTYVVGVNADDYKHS 203
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
 5-121 1.41e-25

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 99.20  E-value: 1.41e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441467727   5 VDIVAVNDPF-IEPhyAAYMLKYDSTHGQFKGEIK-VEGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFTTT 82
Cdd:PLN02237 102 LDVVVVNDSGgVKN--ASHLLKYDSMLGTFKADVKiVDDETISVDGKPIKVVSNRDPLKLPWAELGIDIVIEGTGVFVDG 179

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 441467727  83 EKAKAHLKGGAKKVVISAPS--ADAPMFVMGVSHETYKSDI 121
Cdd:PLN02237 180 PGAGKHIQAGAKKVIITAPAkgADIPTYVVGVNEDDYDHEV 220
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
 2-120 2.46e-25

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 97.43  E-value: 2.46e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441467727   2 HNDVDIVAVNDpFIEPHYAAYMLKYDSTHGQFKGEIKVEGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFTT 81
Cdd:PRK13535  26 RAEITVVAINE-LADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHERDIASLPWRELGVDVVLDCTGVYGS 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 441467727  82 TEKAKAHLKGGAKKVVISAPSA---DAPMfVMGVSHETYKSD 120
Cdd:PRK13535 105 REDGEAHIAAGAKKVLFSHPGSndlDATV-VYGVNHDQLRAE 145
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
 5-123 1.20e-20

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 84.93  E-value: 1.20e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 441467727   5 VDIVAVNDPFIEPHYAAYMLKYDSTH-GQFKGEIKVEGNNLTVNG-KTIRFHMEKDPANIPWSETGAYYVVESTGVFTTT 82
Cdd:PTZ00353  27 VTVVAVNDASVSIAYIAYVLEQESPLsAPDGASIRVVGEQIVLNGtQKIRVSAKHDLVEIAWRDYGVQYVVECTGLYSTR 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 441467727  83 EKAKAHLKGGAKKVVISAPSADAPMFVMGVSHETYKSDIEV 123
Cdd:PTZ00353 107 SRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDERLSASLPV 147
GAPDH-like_N cd05192
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ...
 71-118 1.46e-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: 46.19  E-value: 1.46e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 441467727  71 YVVESTGVFTTTEKAKAHLKGGAKKVVISAPS-ADAPMFVMGVSHETYK 118
Cdd:cd05192   36 VVIECTGSFTDDDNAEKHIKAGGKKAVITAPEkGDIPTIVVVLNELAKS 84
 
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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