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Conserved domains on  [gi|166864058|gb|ABZ01783|]
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glyceraldehyde 3-phosphate dehydrogenase, partial [Actinidia callosa var. discolor]

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 ...
 1-132 1.30e-87

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: 251.99  E-value: 1.30e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166864058   1 IVEGLMTTVHSITATQKTVDGPSsKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGTSFRVPTVDVSVVDLTVRL 80
Cdd:cd18126   19 IEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMAFRVPTPNVSVVDLTVRL 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 166864058  81 EKKATYQQIKDAIKEESEGKLKGILGYTEDDVVSTDFVGDSRSSIFDAKAGI 132
Cdd:cd18126   98 EKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATI 149
 
Name Accession Description Interval E-value
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 1-132 1.30e-87

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: 251.99  E-value: 1.30e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166864058   1 IVEGLMTTVHSITATQKTVDGPSsKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGTSFRVPTVDVSVVDLTVRL 80
Cdd:cd18126   19 IEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMAFRVPTPNVSVVDLTVRL 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 166864058  81 EKKATYQQIKDAIKEESEGKLKGILGYTEDDVVSTDFVGDSRSSIFDAKAGI 132
Cdd:cd18126   98 EKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATI 149
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 1-132 3.97e-84

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 252.09  E-value: 3.97e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166864058   1 IVEGLMTTVHSITATQKTVDGPSSKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGTSFRVPTVDVSVVDLTVRL 80
Cdd:PLN02272 253 ILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRL 332

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 166864058  81 EKKATYQQIKDAIKEESEGKLKGILGYTEDDVVSTDFVGDSRSSIFDAKAGI 132
Cdd:PLN02272 333 EKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGI 384
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-132 1.99e-78

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: 234.52  E-value: 1.99e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166864058   1 IVEGLMTTVHSITATQKTVDGPSsKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGTSFRVPTVDVSVVDLTVRL 80
Cdd:COG0057  170 IEKGLMTTIHAYTNDQNLLDAPH-KDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVEL 248

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 166864058  81 EKKATYQQIKDAIKEESEGKLKGILGYTEDDVVSTDFVGDSRSSIFDAKAGI 132
Cdd:COG0057  249 EKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTI 300
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 1-132 1.04e-72

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: 213.99  E-value: 1.04e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166864058    1 IVEGLMTTVHSITATQKTVDGPSSKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGTSFRVPTVDVSVVDLTVRL 80
Cdd:pfam02800  14 IKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSVVDLVVEL 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 166864058   81 EKKATYQQIKDAIKEESEGKLKGILGYTEDDVVSTDFVGDSRSSIFDAKAGI 132
Cdd:pfam02800  94 EKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETI 145
 
Name Accession Description Interval E-value
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 1-132 1.30e-87

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: 251.99  E-value: 1.30e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166864058   1 IVEGLMTTVHSITATQKTVDGPSsKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGTSFRVPTVDVSVVDLTVRL 80
Cdd:cd18126   19 IEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMAFRVPTPNVSVVDLTVRL 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 166864058  81 EKKATYQQIKDAIKEESEGKLKGILGYTEDDVVSTDFVGDSRSSIFDAKAGI 132
Cdd:cd18126   98 EKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATI 149
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 1-132 3.97e-84

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 252.09  E-value: 3.97e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166864058   1 IVEGLMTTVHSITATQKTVDGPSSKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGTSFRVPTVDVSVVDLTVRL 80
Cdd:PLN02272 253 ILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRL 332

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 166864058  81 EKKATYQQIKDAIKEESEGKLKGILGYTEDDVVSTDFVGDSRSSIFDAKAGI 132
Cdd:PLN02272 333 EKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGI 384
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-132 1.99e-78

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: 234.52  E-value: 1.99e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166864058   1 IVEGLMTTVHSITATQKTVDGPSsKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGTSFRVPTVDVSVVDLTVRL 80
Cdd:COG0057  170 IEKGLMTTIHAYTNDQNLLDAPH-KDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVEL 248

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 166864058  81 EKKATYQQIKDAIKEESEGKLKGILGYTEDDVVSTDFVGDSRSSIFDAKAGI 132
Cdd:COG0057  249 EKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTI 300
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
 1-132 7.68e-78

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 233.46  E-value: 7.68e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166864058   1 IVEGLMTTVHSITATQKTVDGPSSKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGTSFRVPTVDVSVVDLTVRL 80
Cdd:PLN02358 174 IVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRL 253

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 166864058  81 EKKATYQQIKDAIKEESEGKLKGILGYTEDDVVSTDFVGDSRSSIFDAKAGI 132
Cdd:PLN02358 254 EKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGI 305
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 1-132 1.04e-72

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: 213.99  E-value: 1.04e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166864058    1 IVEGLMTTVHSITATQKTVDGPSSKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGTSFRVPTVDVSVVDLTVRL 80
Cdd:pfam02800  14 IKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSVVDLVVEL 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 166864058   81 EKKATYQQIKDAIKEESEGKLKGILGYTEDDVVSTDFVGDSRSSIFDAKAGI 132
Cdd:pfam02800  94 EKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETI 145
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
 1-132 2.76e-67

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 206.22  E-value: 2.76e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166864058   1 IVEGLMTTVHSITATQKTVDGPS--SKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGTSFRVPTVDVSVVDLTV 78
Cdd:PTZ00023 170 IVEGLMTTVHASTANQLTVDGPSkgGKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVPDVSVVDLTC 249

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 166864058  79 RLEKKATYQQIKDAIKEESEGKLKGILGYTEDDVVSTDFVGDSRSSIFDAKAGI 132
Cdd:PTZ00023 250 KLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGI 303
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
1-132 2.01e-64

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 198.80  E-value: 2.01e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166864058   1 IVEGLMTTVHSITATQKTVDGPSSKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGTSFRVPTVDVSVVDLTVRL 80
Cdd:PRK15425 168 IIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRL 247

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 166864058  81 EKKATYQQIKDAIKEESEGKLKGILGYTEDDVVSTDFVGDSRSSIFDAKAGI 132
Cdd:PRK15425 248 EKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGI 299
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 1-130 1.06e-60

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 190.27  E-value: 1.06e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166864058   1 IVEGLMTTVHSITATQKTVDGPSSKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGTSFRVPTVDVSVVDLTVRL 80
Cdd:PTZ00434 186 IETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGKLTGMSFRVPTPDVSVVDLTFRA 265

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 166864058  81 EKKATYQQIKDAIKEESEGKLKGILGYTEDDVVSTDFVGDSRSSIFDAKA 130
Cdd:PTZ00434 266 TRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKA 315
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 1-132 1.17e-56

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: 173.57  E-value: 1.17e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166864058   1 IVEGLMTTVHSITATQKTVDGPSSKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGTSFRVPTVDVSVVDLTVRL 80
Cdd:cd18123   19 IKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGMAVRVPTTLMSVHDLMVEL 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 166864058  81 EKKATYQQIKDAIKEESEGklKGILGYTEDDVVSTDFVGDSRSSIFDAKAGI 132
Cdd:cd18123   99 EKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIFESVFDAESII 148
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-127 8.19e-45

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 148.73  E-value: 8.19e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166864058   1 IVEGLMTTVHSITATQKTVDGPSsKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGTSFRVPTVDVSVVDLTVRL 80
Cdd:PRK07729 170 IENGLMTTVHAYTNDQKNIDNPH-KDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNVSLVDLVVDV 248

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 166864058  81 EKKATYQQIKDAIKEESEGKLKGILGYTEDDVVSTDFVGDSRSSIFD 127
Cdd:PRK07729 249 KRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIID 295
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
1-128 3.89e-41

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 139.27  E-value: 3.89e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166864058   1 IVEGLMTTVHSITATQKTVDGpSSKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGTSFRVPTVDVSVVDLTVRL 80
Cdd:PRK07403 172 IIKGTMTTTHSYTGDQRILDA-SHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTPNVSVVDLVVQV 250

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 166864058  81 EKKATYQQIKDAIKEESEGKLKGILGYTEDDVVSTDFVGDSRSSIFDA 128
Cdd:PRK07403 251 EKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDA 298
GAPDH_C_E4PDH cd23937
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 4-128 3.08e-36

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: 121.75  E-value: 3.08e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166864058   4 GLMTTVHSITATQKTVDGpSSKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGTSFRVPTVDVSVVDLTVRLEKK 83
Cdd:cd23937   22 GTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAIAVRVPTINVTAMDLSVTLKKD 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 166864058  84 ATYQQIKDAIKEESEGKLKGILGYTEDDVVSTDFVGDSRSSIFDA 128
Cdd:cd23937  101 VTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDG 145
PRK08289 PRK08289
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
 1-132 9.10e-36

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 236219 [Multi-domain]  Cd Length: 477  Bit Score: 127.73  E-value: 9.10e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166864058   1 IVEGLMTTVHSITATQKTVDGPSSKDwRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGTSFRVPTVDVSVVDLTVRL 80
Cdd:PRK08289 307 IVNGHVETVHSYTNDQNLIDNYHKGD-RRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNAIRVPTPNVSMAILNLNL 385

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 166864058  81 EKKATYQQIKDAIKEES-EGKLKGILGYTED-DVVSTDFVGDSRSSIFDAKAGI 132
Cdd:PRK08289 386 EKETSREELNEYLRQMSlHSPLQNQIDYTDStEVVSSDFVGSRHAGVVDSQATI 439
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
 1-128 8.21e-35

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 123.89  E-value: 8.21e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166864058   1 IVEGLMTTVHSITATQKTVDGpSSKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGTSFRVPTVDVSVVDLTVRL 80
Cdd:PLN03096 230 IIKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQV 308

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 166864058  81 EKKATYQQIKDAIKEESEGKLKGILGYTEDDVVSTDFVGDSRSSIFDA 128
Cdd:PLN03096 309 EKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDS 356
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
 1-128 3.89e-34

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 122.70  E-value: 3.89e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166864058   1 IVEGLMTTVHSITATQKTVDGpSSKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGTSFRVPTVDVSVVDLTVRL 80
Cdd:PLN02237 247 IVKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTPNVSVVDLVVNV 325

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 166864058  81 EKKA-TYQQIKDAIKEESEGKLKGILGYTEDDVVSTDFVGDSRSSIFDA 128
Cdd:PLN02237 326 EKKGiTAEDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDA 374
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 1-132 4.36e-31

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: 108.76  E-value: 4.36e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166864058   1 IVEGLMTTVHSITATQKTVDGPSSKDWrgGRAASFNIIPSSTGAAKAVGKVLPALN--GKLTGTSFRVPTVDVSVVDLTV 78
Cdd:cd18122   19 IEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIGkpIKVDGIAVRVPATLGHLVTVTV 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 166864058  79 RLEKKATYQQIKDAIKEESEGKLKGILGYTEDDVVSTDFVGDSRSSIFDAKAGI 132
Cdd:cd18122   97 KLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREF 150
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
 1-127 1.93e-27

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 103.21  E-value: 1.93e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166864058   1 IVEGLMTTVHSITATQKTVDGPSSkDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGTSFRVPTVDVSVVDLTVRL 80
Cdd:PRK13535 172 IESGTVTTIHSAMNDQQVIDAYHP-DLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPTINVTAIDLSVTV 250

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 166864058  81 EKKATYQQIKDAIKEESEGKLKGILGYTEDDVVSTDFVGDSRSSIFD 127
Cdd:PRK13535 251 KKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVD 297
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
 24-130 8.80e-19

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 80.30  E-value: 8.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166864058  24 SKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGTSFRVPTVDVSVVDLTVRLEKKATYQQIKDAIKEESEGKLKG 103
Cdd:PTZ00353 195 SQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVKKGCAIDMLVRTKQPVSKEVVDSALAEAASDRLNG 274

                         90       100
                 ....*....|....*....|....*..
gi 166864058 104 ILGYTEDDVVSTDFVGDSRsSIFDAKA 130
Cdd:PTZ00353 275 VLCISKRDMISVDCIPNGK-LCYDATS 300
 
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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