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Conserved domains on  [gi|2473904382|gb|WFD50133|]
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glyceraldehyde 3-phosphate dehydrogenase, partial [Alternaria sp. 'section Eureka']

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) ...
 1-128 2.63e-74

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: 218.03  E-value: 2.63e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473904382   1 IEHNDVDIVAVNDPFIePHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVF 80
Cdd:cd05214    20 LERDDIEVVAINDLTD-DETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAELPWGELGVDIVIESTGVF 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2473904382  81 TTTEKAKAHLKGGAKKVVISAPSAD-APMFVMGVNHETYKSDIEVLSNA 128
Cdd:cd05214    99 TTKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDADDKIISNA 147
 
Name Accession Description Interval E-value
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 1-128 2.63e-74

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: 218.03  E-value: 2.63e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473904382   1 IEHNDVDIVAVNDPFIePHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVF 80
Cdd:cd05214    20 LERDDIEVVAINDLTD-DETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAELPWGELGVDIVIESTGVF 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2473904382  81 TTTEKAKAHLKGGAKKVVISAPSAD-APMFVMGVNHETYKSDIEVLSNA 128
Cdd:cd05214    99 TTKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDADDKIISNA 147
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 4-128 4.15e-69

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 213.18  E-value: 4.15e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473904382   4 NDVDIVAVNDPFIEPHYAAYMLKYDSTHGQFKGEIKV-DGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFTT 82
Cdd:PLN02272  108 DDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDPAEIPWGDFGAEYVVESSGVFTT 187

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2473904382  83 TEKAKAHLKGGAKKVVISAPSADAPMFVMGVNHETYKSDIEVLSNA 128
Cdd:PLN02272  188 VEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNA 233
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 3-128 2.24e-63

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: 196.00  E-value: 2.24e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473904382   3 HNDVDIVAVNDPfIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFTT 82
Cdd:COG0057    25 GPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAELPWGELGVDVVIECTGKFTD 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2473904382  83 TEKAKAHLKGGAKKVVISAPSADA-PMFVMGVNHETYKSDIEVLSNA 128
Cdd:COG0057   104 REKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNA 150
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-128 4.92e-63

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: 188.91  E-value: 4.92e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473904382    1 IEHNDVDIVAVNDPfIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVF 80
Cdd:smart00846  20 LERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANLPWGELGVDIVVECTGGF 98

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2473904382   81 TTTEKAKAHLKGGAKKVVISAPSADA-PMFVMGVNHETYKSDIEVLSNA 128
Cdd:smart00846  99 TTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNA 147
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-82 3.21e-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: 3.21e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473904382   1 IEHNDVDIVAVNDpFIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVF 80
Cdd:pfam00044  20 LERPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAELPWGDLGVDVVIESTGVF 98


                  ..
gi 2473904382  81 TT 82
Cdd:pfam00044  99 TT 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) ...
 1-128 2.63e-74

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: 218.03  E-value: 2.63e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473904382   1 IEHNDVDIVAVNDPFIePHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVF 80
Cdd:cd05214    20 LERDDIEVVAINDLTD-DETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAELPWGELGVDIVIESTGVF 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2473904382  81 TTTEKAKAHLKGGAKKVVISAPSAD-APMFVMGVNHETYKSDIEVLSNA 128
Cdd:cd05214    99 TTKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDADDKIISNA 147
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 4-128 4.15e-69

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 213.18  E-value: 4.15e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473904382   4 NDVDIVAVNDPFIEPHYAAYMLKYDSTHGQFKGEIKV-DGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFTT 82
Cdd:PLN02272  108 DDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDPAEIPWGDFGAEYVVESSGVFTT 187

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2473904382  83 TEKAKAHLKGGAKKVVISAPSADAPMFVMGVNHETYKSDIEVLSNA 128
Cdd:PLN02272  188 VEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNA 233
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 3-128 2.24e-63

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: 196.00  E-value: 2.24e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473904382   3 HNDVDIVAVNDPfIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFTT 82
Cdd:COG0057    25 GPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAELPWGELGVDVVIECTGKFTD 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2473904382  83 TEKAKAHLKGGAKKVVISAPSADA-PMFVMGVNHETYKSDIEVLSNA 128
Cdd:COG0057   104 REKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNA 150
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-128 4.92e-63

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: 188.91  E-value: 4.92e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473904382    1 IEHNDVDIVAVNDPfIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVF 80
Cdd:smart00846  20 LERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANLPWGELGVDIVVECTGGF 98

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2473904382   81 TTTEKAKAHLKGGAKKVVISAPSADA-PMFVMGVNHETYKSDIEVLSNA 128
Cdd:smart00846  99 TTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNA 147
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
 1-128 1.06e-50

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 163.85  E-value: 1.06e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473904382   1 IEHNDVDIVAVNDPFIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVF 80
Cdd:PTZ00023   22 LEREDVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKDPAAIPWGKNGVDVVCESTGVF 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2473904382  81 TTTEKAKAHLKGGAKKVVISAP-SADAPMFVMGVNHETYKSDIEVLSNA 128
Cdd:PTZ00023  102 LTKEKAQAHLKGGAKKVIMSAPpKDDTPIYVMGVNHTQYDKSQRIVSNA 150
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
 1-128 7.83e-46

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 151.41  E-value: 7.83e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473904382   1 IEHNDVDIVAVNDPFIEPHYAAYMLKYDSTHGQFK-GEIKV-DGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTG 78
Cdd:PLN02358   25 LQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKhHELKVkDDKTLLFGEKPVTVFGIRNPEDIPWGEAGADFVVESTG 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2473904382  79 VFTTTEKAKAHLKGGAKKVVISAPSADAPMFVMGVNHETYKSDIEVLSNA 128
Cdd:PLN02358  105 VFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNA 154
GAPDH_N_E4PDH cd17892
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 4-128 4.11e-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: 128.92  E-value: 4.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473904382   4 NDVDIVAVNDPfIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFTTT 83
Cdd:cd17892    26 AEFQVVAINEL-ADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPDPENLPWRELGIDLVLECTGVFGSR 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2473904382  84 EKAKAHLKGGAKKVVISAPSA---DAPMfVMGVNHETYKSDIEVLSNA 128
Cdd:cd17892   105 EDAERHLAAGAKKVLFSHPASndvDATI-VYGINQDLLRAEHRIVSNA 151
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-82 3.21e-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: 3.21e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473904382   1 IEHNDVDIVAVNDpFIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVF 80
Cdd:pfam00044  20 LERPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAELPWGDLGVDVVIESTGVF 98


                  ..
gi 2473904382  81 TT 82
Cdd:pfam00044  99 TT 100
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
2-128 6.31e-38

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 130.62  E-value: 6.31e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473904382   2 EHNDVDIVAVNDpFIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFT 81
Cdd:PRK15425   23 KRSDIEIVAIND-LLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPANLKWDEVGVDVVAEATGLFL 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2473904382  82 TTEKAKAHLKGGAKKVVISAPSAD-APMFVMGVNHETYKSDiEVLSNA 128
Cdd:PRK15425  102 TDETARKHITAGAKKVVMTGPSKDnTPMFVKGANFDKYAGQ-DIVSNA 148
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
2-128 1.01e-35

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 125.02  E-value: 1.01e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473904382   2 EHNDVDIVAVNDPfIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFT 81
Cdd:PRK07403   24 ENSQLELVAINDT-SDPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDRNPLNLPWKEWGIDLIIESTGVFV 102

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2473904382  82 TTEKAKAHLKGGAKKVVISAP--SADAPMFVMGVNHETYKSDI-EVLSNA 128
Cdd:PRK07403  103 TKEGASKHIQAGAKKVLITAPgkGEDIGTYVVGVNHHEYDHEDhNIISNA 152
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 4-128 1.12e-32

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 117.46  E-value: 1.12e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473904382   4 NDVDIVAVNDPFIEPHYAAYMLKYDSTHGQFKGEIKV--------DGNNLTVNGKTIR-FHMEKDPANIPWSETGAYYVV 74
Cdd:PTZ00434   30 TEIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVETtksspsvkTDDVLVVNGHRIKcVKAQRNPADLPWGKLGVDYVI 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2473904382  75 ESTGVFTTTEKAKAHLKGGAKKVVISAP-SADAPMFVMGVNHETYK-SDIEVLSNA 128
Cdd:PTZ00434  110 ESTGLFTDKLAAEGHLKGGAKKVVISAPaSGGAKTIVMGVNQHEYSpTEHHVVSNA 165
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-128 6.03e-32

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 115.22  E-value: 6.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473904382   1 IEHNDVDIVAVNDPFiEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVF 80
Cdd:PRK07729   22 IKESAFEIVAINASY-PSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDPKELPWTDLGIDIVIEATGKF 100

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2473904382  81 TTTEKAKAHLKGGAKKVVISAPSADAPM-FVMGVNHETYKSDIE-VLSNA 128
Cdd:PRK07729  101 NSKEKAILHVEAGAKKVILTAPGKNEDVtIVVGVNEDQLDIEKHtIISNA 150
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
 6-128 2.01e-30

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 111.95  E-value: 2.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473904382   6 VDIVAVNDPFiEPHYAAYMLKYDSTHGQFKGEIKVDGNN-LTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFTTTE 84
Cdd:PLN03096   87 LDVVAINDTG-GVKQASHLLKYDSTLGTFDADVKPVGDDaISVDGKVIKVVSDRNPLNLPWGELGIDLVIEGTGVFVDRE 165

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2473904382  85 KAKAHLKGGAKKVVISAPS-ADAPMFVMGVNHETYKSDIEVLSNA 128
Cdd:PLN03096  166 GAGKHIQAGAKKVLITAPGkGDIPTYVVGVNADDYKHSDPIISNA 210
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
 3-128 1.01e-28

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 106.68  E-value: 1.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473904382   3 HNDVDIVAVNDpFIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFTT 82
Cdd:PRK13535   26 RAEITVVAINE-LADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHERDIASLPWRELGVDVVLDCTGVYGS 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2473904382  83 TEKAKAHLKGGAKKVVISAPSA---DAPMfVMGVNHETYKSDIEVLSNA 128
Cdd:PRK13535  105 REDGEAHIAAGAKKVLFSHPGSndlDATV-VYGVNHDQLRAEHRIVSNA 152
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
 6-128 6.11e-28

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 105.75  E-value: 6.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473904382   6 VDIVAVNDPF-IEPhyAAYMLKYDSTHGQFKGEIK-VDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFTTT 83
Cdd:PLN02237  102 LDVVVVNDSGgVKN--ASHLLKYDSMLGTFKADVKiVDDETISVDGKPIKVVSNRDPLKLPWAELGIDIVIEGTGVFVDG 179

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2473904382  84 EKAKAHLKGGAKKVVISAPS--ADAPMFVMGVNHETYKSDI-EVLSNA 128
Cdd:PLN02237  180 PGAGKHIQAGAKKVIITAPAkgADIPTYVVGVNEDDYDHEVaNIVSNA 227
PRK08955 PRK08955
glyceraldehyde-3-phosphate dehydrogenase; Validated
 5-122 3.61e-23

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 169599 [Multi-domain]  Cd Length: 334  Bit Score: 91.72  E-value: 3.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473904382   5 DVDIVAVNDPFIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSetGAYYVVESTGVFTTTE 84
Cdd:PRK08955   26 ELEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKAIADTDWS--GCDVVIEASGVMKTKA 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2473904382  85 KAKAHLKGGAKKVVISAPSADAPMF--VMGVNHETYKSDI 122
Cdd:PRK08955  104 LLQAYLDQGVKRVVVTAPVKEEGVLniVMGVNDHLFDPAI 143
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
 6-124 2.77e-21

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 86.85  E-value: 2.77e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2473904382   6 VDIVAVNDPFIEPHYAAYMLKYDSTH-GQFKGEIKVDGNNLTVNG-KTIRFHMEKDPANIPWSETGAYYVVESTGVFTTT 83
Cdd:PTZ00353   27 VTVVAVNDASVSIAYIAYVLEQESPLsAPDGASIRVVGEQIVLNGtQKIRVSAKHDLVEIAWRDYGVQYVVECTGLYSTR 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2473904382  84 EKAKAHLKGGAKKVVISAPSADAPMFVMGVNHETYKSDIEV 124
Cdd:PTZ00353  107 SRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDERLSASLPV 147
GAPDH-like_N cd05192
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ...
 72-128 4.71e-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: 50.43  E-value: 4.71e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2473904382  72 YVVESTGVFTTTEKAKAHLKGGAKKVVISAPS-ADAPMFVMGVNHETYKSDIEVLSNA 128
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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