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Conserved domains on  [gi|125658353|gb|ABN49093|]
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glyceraldehyde 3-phosphate dehydrogenase, partial [Ficus asperifolia]

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_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 1-121 2.93e-82

C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; Glyceraldehyde-3-phosphate dehydrogenase (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 proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily 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 (1.2.1.12), NADP (1.2.1.13) or either (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: 467676  Cd Length: 165  Bit Score: 237.74  E-value: 2.93e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125658353   1 IVEGLMTTVHSITATQKTVDGPSsKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRL 80
Cdd:cd18126   19 IEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMAFRVPTPNVSVVDLTVRL 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 125658353  81 QKAASYDEIKQAIKEESEGKLKGILGYTEDDVVSTDFVGDS 121
Cdd:cd18126   98 EKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDP 138
 
Name Accession Description Interval E-value
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 1-121 2.93e-82

C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; Glyceraldehyde-3-phosphate dehydrogenase (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 proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily 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 (1.2.1.12), NADP (1.2.1.13) or either (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: 467676  Cd Length: 165  Bit Score: 237.74  E-value: 2.93e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125658353   1 IVEGLMTTVHSITATQKTVDGPSsKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRL 80
Cdd:cd18126   19 IEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMAFRVPTPNVSVVDLTVRL 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 125658353  81 QKAASYDEIKQAIKEESEGKLKGILGYTEDDVVSTDFVGDS 121
Cdd:cd18126   98 EKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDP 138
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 1-121 3.31e-77

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 233.60  E-value: 3.31e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125658353   1 IVEGLMTTVHSITATQKTVDGPSSKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRL 80
Cdd:PLN02272 253 ILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRL 332

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 125658353  81 QKAASYDEIKQAIKEESEGKLKGILGYTEDDVVSTDFVGDS 121
Cdd:PLN02272 333 EKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDS 373
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-121 2.17e-73

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: 221.04  E-value: 2.17e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125658353   1 IVEGLMTTVHSITATQKTVDGPSsKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRL 80
Cdd:COG0057  170 IEKGLMTTIHAYTNDQNLLDAPH-KDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVEL 248

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 125658353  81 QKAASYDEIKQAIKEESEGKLKGILGYTEDDVVSTDFVGDS 121
Cdd:COG0057  249 EKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDP 289
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 1-120 6.18e-68

Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. C-terminal domain is a mixed alpha/antiparallel beta fold.


Pssm-ID: 460700  Cd Length: 158  Bit Score: 201.28  E-value: 6.18e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125658353    1 IVEGLMTTVHSITATQKTVDGPSSKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRL 80
Cdd:pfam02800  14 IKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSVVDLVVEL 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 125658353   81 QKAASYDEIKQAIKEESEGKLKGILGYTEDDVVSTDFVGD 120
Cdd:pfam02800  94 EKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGD 133
 
Name Accession Description Interval E-value
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 1-121 2.93e-82

C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; Glyceraldehyde-3-phosphate dehydrogenase (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 proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily 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 (1.2.1.12), NADP (1.2.1.13) or either (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: 467676  Cd Length: 165  Bit Score: 237.74  E-value: 2.93e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125658353   1 IVEGLMTTVHSITATQKTVDGPSsKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRL 80
Cdd:cd18126   19 IEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMAFRVPTPNVSVVDLTVRL 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 125658353  81 QKAASYDEIKQAIKEESEGKLKGILGYTEDDVVSTDFVGDS 121
Cdd:cd18126   98 EKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDP 138
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 1-121 3.31e-77

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 233.60  E-value: 3.31e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125658353   1 IVEGLMTTVHSITATQKTVDGPSSKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRL 80
Cdd:PLN02272 253 ILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRL 332

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 125658353  81 QKAASYDEIKQAIKEESEGKLKGILGYTEDDVVSTDFVGDS 121
Cdd:PLN02272 333 EKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDS 373
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-121 2.17e-73

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: 221.04  E-value: 2.17e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125658353   1 IVEGLMTTVHSITATQKTVDGPSsKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRL 80
Cdd:COG0057  170 IEKGLMTTIHAYTNDQNLLDAPH-KDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVEL 248

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 125658353  81 QKAASYDEIKQAIKEESEGKLKGILGYTEDDVVSTDFVGDS 121
Cdd:COG0057  249 EKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDP 289
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
 1-121 1.39e-72

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 219.59  E-value: 1.39e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125658353   1 IVEGLMTTVHSITATQKTVDGPSSKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRL 80
Cdd:PLN02358 174 IVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRL 253

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 125658353  81 QKAASYDEIKQAIKEESEGKLKGILGYTEDDVVSTDFVGDS 121
Cdd:PLN02358 254 EKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDN 294
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 1-120 6.18e-68

Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. C-terminal domain is a mixed alpha/antiparallel beta fold.


Pssm-ID: 460700  Cd Length: 158  Bit Score: 201.28  E-value: 6.18e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125658353    1 IVEGLMTTVHSITATQKTVDGPSSKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRL 80
Cdd:pfam02800  14 IKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSVVDLVVEL 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 125658353   81 QKAASYDEIKQAIKEESEGKLKGILGYTEDDVVSTDFVGD 120
Cdd:pfam02800  94 EKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGD 133
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
 1-120 5.11e-62

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 192.36  E-value: 5.11e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125658353   1 IVEGLMTTVHSITATQKTVDGPS--SKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTV 78
Cdd:PTZ00023 170 IVEGLMTTVHASTANQLTVDGPSkgGKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVPDVSVVDLTC 249

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 125658353  79 RLQKAASYDEIKQAIKEESEGKLKGILGYTEDDVVSTDFVGD 120
Cdd:PTZ00023 250 KLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHD 291
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
1-120 6.61e-62

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 191.87  E-value: 6.61e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125658353   1 IVEGLMTTVHSITATQKTVDGPSSKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRL 80
Cdd:PRK15425 168 IIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRL 247

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 125658353  81 QKAASYDEIKQAIKEESEGKLKGILGYTEDDVVSTDFVGD 120
Cdd:PRK15425 248 EKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGE 287
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 1-121 5.35e-57

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 180.25  E-value: 5.35e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125658353   1 IVEGLMTTVHSITATQKTVDGPSSKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRL 80
Cdd:PTZ00434 186 IETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGKLTGMSFRVPTPDVSVVDLTFRA 265

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 125658353  81 QKAASYDEIKQAIKEESEGKLKGILGYTEDDVVSTDFVGDS 121
Cdd:PTZ00434 266 TRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDN 306
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 1-120 3.23e-53

C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; Glyceraldehyde-3-phosphate dehydrogenase (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 proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily 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 (1.2.1.12), NADP (1.2.1.13) or either (1.2.1.59). GADPH family members include the ubiquitous NAD+ or NADP+ utilizing type I, type II NADP+ utilizing mainly from archaea, 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: 467673  Cd Length: 164  Bit Score: 164.33  E-value: 3.23e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125658353   1 IVEGLMTTVHSITATQKTVDGPSSKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRL 80
Cdd:cd18123   19 IKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGMAVRVPTTLMSVHDLMVEL 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 125658353  81 QKAASYDEIKQAIKEESEGklKGILGYTEDDVVSTDFVGD 120
Cdd:cd18123   99 EKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGD 136
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-121 2.43e-43

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 144.49  E-value: 2.43e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125658353   1 IVEGLMTTVHSITATQKTVDGPSsKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRL 80
Cdd:PRK07729 170 IENGLMTTVHAYTNDQKNIDNPH-KDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNVSLVDLVVDV 248

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 125658353  81 QKAASYDEIKQAIKEESEGKLKGILGYTEDDVVSTDFVGDS 121
Cdd:PRK07729 249 KRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNT 289
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
1-119 1.48e-37

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 129.26  E-value: 1.48e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125658353   1 IVEGLMTTVHSITATQKTVDGpSSKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRL 80
Cdd:PRK07403 172 IIKGTMTTTHSYTGDQRILDA-SHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTPNVSVVDLVVQV 250

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 125658353  81 QKAASYDEIKQAIKEESEGKLKGILGYTEDDVVSTDFVG 119
Cdd:PRK07403 251 EKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRG 289
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
 1-117 1.56e-34

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 122.73  E-value: 1.56e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125658353   1 IVEGLMTTVHSITATQKTVDGpSSKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRL 80
Cdd:PLN03096 230 IIKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQV 308

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 125658353  81 QKAASYDEIKQAIKEESEGKLKGILGYTEDDVVSTDF 117
Cdd:PLN03096 309 EKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDF 345
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
 1-117 1.66e-32

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 118.08  E-value: 1.66e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125658353   1 IVEGLMTTVHSITATQKTVDGpSSKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRL 80
Cdd:PLN02237 247 IVKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTPNVSVVDLVVNV 325

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 125658353  81 QKAA-SYDEIKQAIKEESEGKLKGILGYTEDDVVSTDF 117
Cdd:PLN02237 326 EKKGiTAEDVNAAFRKAADGPLKGILAVCDVPLVSVDF 363
PRK08289 PRK08289
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
 1-121 1.96e-32

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 236219 [Multi-domain]  Cd Length: 477  Bit Score: 118.10  E-value: 1.96e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125658353   1 IVEGLMTTVHSITATQKTVDGPSSKDwRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRL 80
Cdd:PRK08289 307 IVNGHVETVHSYTNDQNLIDNYHKGD-RRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNAIRVPTPNVSMAILNLNL 385

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 125658353  81 QKAASYDEIKQAIKEES-EGKLKGILGYTED-DVVSTDFVGDS 121
Cdd:PRK08289 386 EKETSREELNEYLRQMSlHSPLQNQIDYTDStEVVSSDFVGSR 428
GAPDH_C_E4PDH cd23937
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 4-121 3.79e-32

C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar proteins; D-erythrose-4-phosphate dehydrogenase (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 superfamily of proteins.


Pssm-ID: 467686  Cd Length: 165  Bit Score: 110.97  E-value: 3.79e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125658353   4 GLMTTVHSITATQKTVDGpSSKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRLQKA 83
Cdd:cd23937   22 GTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAIAVRVPTINVTAMDLSVTLKKD 100

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 125658353  84 ASYDEIKQAIKEESEGKLKGILGYTEDDVVSTDFVGDS 121
Cdd:cd23937  101 VTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDP 138
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 1-121 4.40e-29

C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) superfamily of proteins; GAPDH-like C-terminal catalytic domains are typically associated with a classic N-terminal Rossmann fold NAD(P)-binding domain. This superfamily includes the C-terminal domains of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), aspartate beta-semialdehyde dehydrogenase (ASADH), acetaldehyde dehydrogenase (ALDH) and USG-1 homolog proteins.


Pssm-ID: 467672 [Multi-domain]  Cd Length: 166  Bit Score: 102.98  E-value: 4.40e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125658353   1 IVEGLMTTVHSITATQKTVDGPSSKDWrgGRAASFNIIPSSTGAAKAVGKVLPSLN--GKLTGMSFRVPTVDVSVVDLTV 78
Cdd:cd18122   19 IEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIGkpIKVDGIAVRVPATLGHLVTVTV 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 125658353  79 RLQKAASYDEIKQAIKEESEGKLKGILGYTEDDVVSTDFVGDS 121
Cdd:cd18122   97 KLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGV 139
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
 1-117 1.94e-26

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 100.13  E-value: 1.94e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125658353   1 IVEGLMTTVHSITATQKTVDGPSSkDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRL 80
Cdd:PRK13535 172 IESGTVTTIHSAMNDQQVIDAYHP-DLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPTINVTAIDLSVTV 250

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 125658353  81 QKAASYDEIKQAIKEESEGKLKGILGYTEDDVVSTDF 117
Cdd:PRK13535 251 KKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDF 287
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
 24-121 5.84e-20

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 83.00  E-value: 5.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125658353  24 SKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRLQKAASYDEIKQAIKEESEGKLKG 103
Cdd:PTZ00353 195 SQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVKKGCAIDMLVRTKQPVSKEVVDSALAEAASDRLNG 274

                         90
                 ....*....|....*...
gi 125658353 104 ILGYTEDDVVSTDFVGDS 121
Cdd:PTZ00353 275 VLCISKRDMISVDCIPNG 292
 
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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