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Conserved domains on  [gi|371560600|gb|AEX37080|]
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glyceraldehyde-3-phosphate dehydrogenase, partial [Sphingomonas sp. 624]

Protein Classification

type I glyceraldehyde-3-phosphate dehydrogenase( domain architecture ID 1903262)

type I glyceraldehyde-3-phosphate dehydrogenase catalyzes the NAD-dependent oxidative phosphorylation of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GapA super family cl43010
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-127 8.80e-43

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


The actual alignment was detected with superfamily member COG0057:

Pssm-ID: 439827 [Multi-domain]  Cd Length: 334  Bit Score: 143.61  E-value: 8.80e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560600   1 LNDAIPIERGLDESIHRYTTDQKIIDYTRTDVGRARAAGRSMIPTTPAPARAVGEVLPELNDKRGWLAVRGPTTNVWMTD 80
Cdd:COG0057  164 LNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVD 243

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 371560600  81 MTFTPKRETSSDGVNQLLKAGAEGsPLKGVLANSKDRLASIDYNGHP 127
Cdd:COG0057  244 LTVELEKETTVEEVNAALKEAAEG-PLKGILGYTEEPLVSSDFNGDP 289
 
Name Accession Description Interval E-value
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-127 8.80e-43

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: 143.61  E-value: 8.80e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560600   1 LNDAIPIERGLDESIHRYTTDQKIIDYTRTDVGRARAAGRSMIPTTPAPARAVGEVLPELNDKRGWLAVRGPTTNVWMTD 80
Cdd:COG0057  164 LNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVD 243

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 371560600  81 MTFTPKRETSSDGVNQLLKAGAEGsPLKGVLANSKDRLASIDYNGHP 127
Cdd:COG0057  244 LTVELEKETTVEEVNAALKEAAEG-PLKGILGYTEEPLVSSDFNGDP 289
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 1-127 3.66e-40

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: 132.19  E-value: 3.66e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560600   1 LNDAIPIERGLDESIHRYTTDQKIIDYTRTDVGRARAAGRSMIPTTPAPARAVGEVLPELNDKRGWLAVRGPTTNVWMTD 80
Cdd:cd18126   13 LNDNFGIEEGLMTTVHAYTNDQKLVDGPHKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMAFRVPTPNVSVVD 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 371560600  81 MTFTPKRETSSDGVNQLLKAGAEGsPLKGVLANSKDRLASIDYNGHP 127
Cdd:cd18126   93 LTVRLEKPVTVEEVNAALKKAAEG-PLKGILGYTEDPLVSSDFVGDP 138
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 1-133 8.56e-35

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: 118.46  E-value: 8.56e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560600    1 LNDAIPIERGLDESIHRYTTDQKIID-YTRTDVGRARAAGRSMIPTTPAPARAVGEVLPELNDKRGWLAVRGPTTNVWMT 79
Cdd:pfam02800   8 LNDNFGIKKGLMTTVHAYTNDQKLLDgPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSVV 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 371560600   80 DMTFTPKRETSSDGVNQLLKAGAEGsPLKGVLANSKDRLASIDYNGHPGNFTVD 133
Cdd:pfam02800  88 DLVVELEKPVTVEEVNAALKEAAEG-ALKGILSYTEDPLVSSDFIGDPHSSIFD 140
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-133 4.77e-34

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 121.38  E-value: 4.77e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560600   1 LNDAIPIERGLDESIHRYTTDQKIIDYTRTDVGRARAAGRSMIPTTPAPARAVGEVLPELNDKRGWLAVRGPTTNVWMTD 80
Cdd:PRK07729 164 LDEQFGIENGLMTTVHAYTNDQKNIDNPHKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNVSLVD 243

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 371560600  81 MTFTPKRETSSDGVNQLLKAGAEGSpLKGVLANSKDRLASIDYNGHPGNFTVD 133
Cdd:PRK07729 244 LVVDVKRDVTVEEINEAFKTAANGA-LKGILEFSEEPLVSIDFNTNTHSAIID 295
 
Name Accession Description Interval E-value
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-127 8.80e-43

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: 143.61  E-value: 8.80e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560600   1 LNDAIPIERGLDESIHRYTTDQKIIDYTRTDVGRARAAGRSMIPTTPAPARAVGEVLPELNDKRGWLAVRGPTTNVWMTD 80
Cdd:COG0057  164 LNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVD 243

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 371560600  81 MTFTPKRETSSDGVNQLLKAGAEGsPLKGVLANSKDRLASIDYNGHP 127
Cdd:COG0057  244 LTVELEKETTVEEVNAALKEAAEG-PLKGILGYTEEPLVSSDFNGDP 289
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 1-127 3.66e-40

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: 132.19  E-value: 3.66e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560600   1 LNDAIPIERGLDESIHRYTTDQKIIDYTRTDVGRARAAGRSMIPTTPAPARAVGEVLPELNDKRGWLAVRGPTTNVWMTD 80
Cdd:cd18126   13 LNDNFGIEEGLMTTVHAYTNDQKLVDGPHKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMAFRVPTPNVSVVD 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 371560600  81 MTFTPKRETSSDGVNQLLKAGAEGsPLKGVLANSKDRLASIDYNGHP 127
Cdd:cd18126   93 LTVRLEKPVTVEEVNAALKKAAEG-PLKGILGYTEDPLVSSDFVGDP 138
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 1-133 8.56e-35

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: 118.46  E-value: 8.56e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560600    1 LNDAIPIERGLDESIHRYTTDQKIID-YTRTDVGRARAAGRSMIPTTPAPARAVGEVLPELNDKRGWLAVRGPTTNVWMT 79
Cdd:pfam02800   8 LNDNFGIKKGLMTTVHAYTNDQKLLDgPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSVV 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 371560600   80 DMTFTPKRETSSDGVNQLLKAGAEGsPLKGVLANSKDRLASIDYNGHPGNFTVD 133
Cdd:pfam02800  88 DLVVELEKPVTVEEVNAALKEAAEG-ALKGILSYTEDPLVSSDFIGDPHSSIFD 140
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-133 4.77e-34

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 121.38  E-value: 4.77e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560600   1 LNDAIPIERGLDESIHRYTTDQKIIDYTRTDVGRARAAGRSMIPTTPAPARAVGEVLPELNDKRGWLAVRGPTTNVWMTD 80
Cdd:PRK07729 164 LDEQFGIENGLMTTVHAYTNDQKNIDNPHKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNVSLVD 243

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 371560600  81 MTFTPKRETSSDGVNQLLKAGAEGSpLKGVLANSKDRLASIDYNGHPGNFTVD 133
Cdd:PRK07729 244 LVVDVKRDVTVEEINEAFKTAANGA-LKGILEFSEEPLVSIDFNTNTHSAIID 295
PRK08955 PRK08955
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-145 3.59e-31

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 169599 [Multi-domain]  Cd Length: 334  Bit Score: 113.67  E-value: 3.59e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560600   1 LNDAIPIERGLDESIHRYTTDQKIIDYTRTDVGRARAAGRSMIPTTPAPARAVGEVLPELNDKRGWLAVRGPTTNVWMTD 80
Cdd:PRK08955 164 IHEKLGIKHGSMTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLANASLTD 243

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 371560600  81 MTFTPKRETSSDGVNQLLKAGAEGsPLKGVLANSKDRLASIDYNGHPGNFTVDTFEAAGIGGSVV 145
Cdd:PRK08955 244 CVFEVERDTTVEEVNALLKEAAEG-ELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQV 307
GAPDH_C_E4PDH cd23937
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 1-133 3.09e-28

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: 101.72  E-value: 3.09e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560600   1 LNDAIPIERGLDESIHRYTTDQKIIDYTRTDVGRARAAGRSMIPTTPAPARAVGEVLPELNDKRGWLAVRGPTTNVWMTD 80
Cdd:cd23937   13 LDEAFGIESGTITTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAIAVRVPTINVTAMD 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 371560600  81 MTFTPKRETSSDGVNQLLKAGAEGsPLKGVLANSKDRLASIDYNGHPGNFTVD 133
Cdd:cd23937   93 LSVTLKKDVTAEEVNRVLRQASQG-RLKGILGYTEEPLVSVDFNHDPHSCIVD 144
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
1-145 6.89e-28

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 104.99  E-value: 6.89e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560600   1 LNDAIPIERGLDESIHRYTTDQKIIDYTRTDVGRARAAGRSMIPTTPAPARAVGEVLPELNDKRGWLAVRGPTTNVWMTD 80
Cdd:PRK07403 166 LHDNFGIIKGTMTTTHSYTGDQRILDASHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTPNVSVVD 245

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 371560600  81 MTFTPKRETSSDGVNQLLKAGAEGsPLKGVLANSKDRLASIDYNGHPGNFTVDTFEAAGIGGSVV 145
Cdd:PRK07403 246 LVVQVEKRTITEQVNEVLKDASEG-PLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMV 309
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
 1-133 5.45e-22

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 89.35  E-value: 5.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560600   1 LNDAIPIERGLDESIHRYTTDQKIIDYTRTDVGRARAAGRSMIPTTPAPARAVGEVLPELNDKRGWLAVRGPTTNVWMTD 80
Cdd:PRK13535 166 LDDAFGIESGTVTTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPTINVTAID 245

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 371560600  81 MTFTPKRETSSDGVNQLLKAGAEGSpLKGVLANSKDRLASIDYNGHPGNFTVD 133
Cdd:PRK13535 246 LSVTVKKPVKVNEVNQLLQKAAQGA-FHGIVDYTELPLVSIDFNHDPHSAIVD 297
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
 1-134 8.66e-22

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 89.22  E-value: 8.66e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560600   1 LNDAIPIERGLDESIHRYTTDQKIIDYTRTDVGRARAAGRSMIPTTPAPARAVGEVLPELNDKRGWLAVRGPTTNVWMTD 80
Cdd:PLN03096 224 LDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVD 303

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 371560600  81 MTFTPKRETSSDGVNQLLKAGAEGsPLKGVLANSKDRLASIDYNGHPGNFTVDT 134
Cdd:PLN03096 304 LVVQVEKKTFAEEVNAAFRDAAEK-ELKGILAVCDEPLVSVDFRCSDVSSTIDS 356
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
 1-134 6.99e-20

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 84.18  E-value: 6.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560600   1 LNDAIPIERGLDESIHRYTTDQKIIDYTRTDVGRARAAGRSMIPTTPAPARAVGEVLPELNDKRGWLAVRGPTTNVWMTD 80
Cdd:PLN02237 241 LDEEFGIVKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTPNVSVVD 320

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 371560600  81 MTF-TPKRETSSDGVNQLLKAGAEGsPLKGVLANSKDRLASIDYNGHPGNFTVDT 134
Cdd:PLN02237 321 LVVnVEKKGITAEDVNAAFRKAADG-PLKGILAVCDVPLVSVDFRCSDVSSTIDA 374
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 7-123 1.50e-18

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 80.10  E-value: 1.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560600   7 IERGLDESIHRYTTDQKIID-YTRTDVGRARAAGRSMIPTTPAPARAVGEVLPELNDKRGWLAVRGPTTNVWMTDMTFTP 85
Cdd:PTZ00434 186 IETGLMTTIHSYTATQKTVDgVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGKLTGMSFRVPTPDVSVVDLTFRA 265

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 371560600  86 KRETSSDGVNQLLKAGAEGSpLKGVLANSKDRLASIDY 123
Cdd:PTZ00434 266 TRDTSIQEIDAAIKRASQTY-MKGILGFTDDELVSADF 302
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 1-133 1.53e-17

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: 74.19  E-value: 1.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560600   1 LNDAIPIERGLDESIHRYTTDQKIIDYTRTDVGRA-RAAGRSMIPTTPAPARAVGEVLPELNDKRGWLAVRGPTTNVWMT 79
Cdd:cd18123   13 IHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRAsRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGMAVRVPTTLMSVH 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 371560600  80 DMTFTPKRETSSDGVNQLLKAGAEGsplKGVLANSKDRLASIDYNGHPGNFTVD 133
Cdd:cd18123   93 DLMVELEKDVTYDDIKEAVKQAPEG---KGRLGYTEAEDVSSDFRGDIFESVFD 143
PRK08289 PRK08289
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
 1-109 3.63e-17

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 236219 [Multi-domain]  Cd Length: 477  Bit Score: 76.50  E-value: 3.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560600   1 LNDAIPIERGLDESIHRYTTDQKIID-YTRTDvGRARAAGRSMIPTTPAPARAVGEVLPELNDKRGWLAVRGPTTNVWMT 79
Cdd:PRK08289 301 VNDKYGIVNGHVETVHSYTNDQNLIDnYHKGD-RRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNAIRVPTPNVSMA 379

                         90       100       110
                 ....*....|....*....|....*....|
gi 371560600  80 DMTFTPKRETSSDGVNQLLKAGAEGSPLKG 109
Cdd:PRK08289 380 ILNLNLEKETSREELNEYLRQMSLHSPLQN 409
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
 1-123 9.72e-15

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 69.48  E-value: 9.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560600   1 LNDAIPIERGLDESIHRYTTDQKIIDYTR---TDVGRARAAGRSMIPTTPAPARAVGEVLPELNDKRGWLAVRGPTTNVW 77
Cdd:PTZ00023 164 VNDKFGIVEGLMTTVHASTANQLTVDGPSkggKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVPDVS 243

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 371560600  78 MTDMTFTPKRETSSDGVNQLLKAGAEGsPLKGVLANSKDRLASIDY 123
Cdd:PTZ00023 244 VVDLTCKLAKPAKYEEIVAAVKKAAEG-PLKGILGYTDDEVVSSDF 288
 
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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