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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651624576   1 VEHNDVDIVAVNDPFIePHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVF 80
Cdd:cd05214    20 LERDDIEVVAINDLTD-DETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAELPWGELGVDIVIESTGVF 98

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2651624576  81 TTTEKAKAHLKGGAKKVVISAPSAD-APMFVMG 112
Cdd:cd05214    99 TTKEKASAHLKAGAKKVIISAPAKDdDPTIVMG 131

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651624576   1 VEHNDVDIVAVNDPFIePHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVF 80
Cdd:cd05214    20 LERDDIEVVAINDLTD-DETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAELPWGELGVDIVIESTGVF 98

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2651624576  81 TTTEKAKAHLKGGAKKVVISAPSAD-APMFVMG 112
Cdd:cd05214    99 TTKEKASAHLKAGAKKVIISAPAKDdDPTIVMG 131

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651624576    1 VEHNDVDIVAVNDPfIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVF 80
Cdd:smart00846  20 LERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANLPWGELGVDIVVECTGGF 98

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2651624576   81 TTTEKAKAHLKGGAKKVVISAPSADA-PMFVMG 112
Cdd:smart00846  99 TTREKASAHLKAGAKKVIISAPSKDAdPTFVYG 131

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651624576   2 EHNDVDIVAVNDpFIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFT 81
Cdd:pfam00044  21 ERPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAELPWGDLGVDVVIESTGVFT 99

                  .
gi 2651624576  82 T 82
Cdd:pfam00044 100 T 100

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651624576   1 VEHNDVDIVAVNDPFIePHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVF 80
Cdd:cd05214    20 LERDDIEVVAINDLTD-DETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAELPWGELGVDIVIESTGVF 98

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2651624576  81 TTTEKAKAHLKGGAKKVVISAPSAD-APMFVMG 112
Cdd:cd05214    99 TTKEKASAHLKAGAKKVIISAPAKDdDPTIVMG 131

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651624576    1 VEHNDVDIVAVNDPfIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVF 80
Cdd:smart00846  20 LERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANLPWGELGVDIVVECTGGF 98

                           90       100       110
                   ....*....|....*....|....*....|...
gi 2651624576   81 TTTEKAKAHLKGGAKKVVISAPSADA-PMFVMG 112
Cdd:smart00846  99 TTREKASAHLKAGAKKVIISAPSKDAdPTFVYG 131

glyceraldehyde-3-phosphate dehydrogenase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651624576   2 EHNDVDIVAVNDPFIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFT 81
Cdd:PTZ00023   23 EREDVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKDPAAIPWGKNGVDVVCESTGVFL 102

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2651624576  82 TTEKAKAHLKGGAKKVVISAP-SADAPMFVMG 112
Cdd:PTZ00023  103 TKEKAQAHLKGGAKKVIMSAPpKDDTPIYVMG 134

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651624576   2 EHNDVDIVAVNDpFIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFT 81
Cdd:pfam00044  21 ERPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAELPWGDLGVDVVIESTGVFT 99

                  .
gi 2651624576  82 T 82
Cdd:pfam00044 100 T 100

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651624576   4 NDVDIVAVNDPfIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFTTT 83
Cdd:cd17892    26 AEFQVVAINEL-ADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPDPENLPWRELGIDLVLECTGVFGSR 104

                          90       100
                  ....*....|....*....|..
gi 2651624576  84 EKAKAHLKGGAKKVVISAPSAD 105
Cdd:cd17892   105 EDAERHLAAGAKKVLFSHPASN 126

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651624576   4 NDVDIVAVNDPFIEPHYAAYMLKYDSTHGQFKGEIKV--------DGNNLTVNGKTIR-FHMEKDPANIPWSETGAYYVV 74
Cdd:PTZ00434   30 TEIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVETtksspsvkTDDVLVVNGHRIKcVKAQRNPADLPWGKLGVDYVI 109

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2651624576  75 ESTGVFTTTEKAKAHLKGGAKKVVISAP-SADAPMFVMG 112
Cdd:PTZ00434  110 ESTGLFTDKLAAEGHLKGGAKKVVISAPaSGGAKTIVMG 148

glyceraldehyde-3-phosphate dehydrogenase A; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651624576   6 VDIVAVNDPFiEPHYAAYMLKYDSTHGQFKGEIKVDGNN-LTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFTTTE 84
Cdd:PLN03096   87 LDVVAINDTG-GVKQASHLLKYDSTLGTFDADVKPVGDDaISVDGKVIKVVSDRNPLNLPWGELGIDLVIEGTGVFVDRE 165

                          90       100
                  ....*....|....*....|....*....
gi 2651624576  85 KAKAHLKGGAKKVVISAPS-ADAPMFVMG 112
Cdd:PLN03096  166 GAGKHIQAGAKKVLITAPGkGDIPTYVVG 194

erythrose 4-phosphate dehydrogenase; Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2651624576   3 HNDVDIVAVNDpFIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFTT 82
Cdd:PRK13535   26 RAEITVVAINE-LADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHERDIASLPWRELGVDVVLDCTGVYGS 104

                          90       100
                  ....*....|....*....|..
gi 2651624576  83 TEKAKAHLKGGAKKVVISAPSA 104
Cdd:PRK13535  105 REDGEAHIAAGAKKVLFSHPGS 126

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.

                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2651624576  72 YVVESTGVFTTTEKAKAHLKGGAKKVVISAPSADAPMF 109
Cdd:cd05192    36 VVIECTGSFTDDDNAEKHIKAGGKKAVITAPEKGDIPT 73