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Conserved domains on  [gi|2260391634|gb|USS18871|]
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glyceraldehyde-3-phosphate dehydrogenase, partial [Atlapetes personatus personatus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GAPDH_like_C super family cl49616
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 1-32 5.68e-14

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.


The actual alignment was detected with superfamily member cd18126:

Pssm-ID: 483956  Cd Length: 165  Bit Score: 60.16  E-value: 5.68e-14
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2260391634   1 VVSCDFNGDSHSSTFDAGAGIALNDHFVKLVS 32
Cdd:cd18126   129 LVSSDFVGDPHSSIFDATATIVLGGNLVKVVA 160
 
Name Accession Description Interval E-value
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 1-32 5.68e-14

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: 60.16  E-value: 5.68e-14
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2260391634   1 VVSCDFNGDSHSSTFDAGAGIALNDHFVKLVS 32
Cdd:cd18126   129 LVSSDFVGDPHSSIFDATATIVLGGNLVKVVA 160
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-32 3.45e-11

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: 54.25  E-value: 3.45e-11
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2260391634   1 VVSCDFNGDSHSSTFDAGAGIALNDHFVKLVS 32
Cdd:COG0057   280 LVSSDFNGDPHSSIFDALQTIVIGGNLVKVLA 311
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 1-32 7.44e-09

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: 46.82  E-value: 7.44e-09
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2260391634   1 VVSCDFNGDSHSSTFDAGAGIALNDHFVKLVS 32
Cdd:pfam02800 125 LVSSDFIGDPHSSIFDAKETIVVNGNFVKVVA 156
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
1-32 9.89e-09

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 47.42  E-value: 9.89e-09
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2260391634   1 VVSCDFNGDSHSSTFDAGAGIALNDHFVKLVS 32
Cdd:PRK15425  279 VVSTDFNGEVCTSVFDAKAGIALNDNFVKLVS 310
 
Name Accession Description Interval E-value
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 1-32 5.68e-14

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: 60.16  E-value: 5.68e-14
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2260391634   1 VVSCDFNGDSHSSTFDAGAGIALNDHFVKLVS 32
Cdd:cd18126   129 LVSSDFVGDPHSSIFDATATIVLGGNLVKVVA 160
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-32 3.45e-11

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: 54.25  E-value: 3.45e-11
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2260391634   1 VVSCDFNGDSHSSTFDAGAGIALNDHFVKLVS 32
Cdd:COG0057   280 LVSSDFNGDPHSSIFDALQTIVIGGNLVKVLA 311
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 1-32 6.42e-09

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: 47.23  E-value: 6.42e-09
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2260391634   1 VVSCDFNGDSHSSTFDAGAGIALNDHFVKLVS 32
Cdd:cd18123   128 DVSSDFRGDIFESVFDAESIIAVNDNEVKLMQ 159
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 1-32 7.44e-09

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: 46.82  E-value: 7.44e-09
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2260391634   1 VVSCDFNGDSHSSTFDAGAGIALNDHFVKLVS 32
Cdd:pfam02800 125 LVSSDFIGDPHSSIFDAKETIVVNGNFVKVVA 156
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
1-32 9.89e-09

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 47.42  E-value: 9.89e-09
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2260391634   1 VVSCDFNGDSHSSTFDAGAGIALNDHFVKLVS 32
Cdd:PRK15425  279 VVSTDFNGEVCTSVFDAKAGIALNDNFVKLVS 310
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
 1-32 2.32e-08

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 46.25  E-value: 2.32e-08
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2260391634   1 VVSCDFNGDSHSSTFDAGAGIALNDHFVKLVS 32
Cdd:PLN02358  285 VVSTDFVGDNRSSIFDAKAGIALSDKFVKLVS 316
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
 1-32 9.09e-08

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 44.83  E-value: 9.09e-08
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2260391634   1 VVSCDFNGDSHSSTFDAGAGIALNDHFVKLVS 32
Cdd:PTZ00023  283 VVSSDFVHDKRSSIFDVKAGIALNDTFVKLVS 314
GAPDH_C_E4PDH cd23937
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 1-30 7.07e-03

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: 30.85  E-value: 7.07e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2260391634   1 VVSCDFNGDSHSSTFDAGAGIALNDHFVKL 30
Cdd:cd23937   129 LVSVDFNHDPHSCIVDGTQTRVSGKRLVKL 158
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
 2-30 8.83e-03

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 30.80  E-value: 8.83e-03
                          10        20
                  ....*....|....*....|....*....
gi 2260391634   2 VSCDFNGDSHSSTFDAGAGIALNDHFVKL 30
Cdd:PRK13535  283 VSIDFNHDPHSAIVDGTQTRVSGAHLIKT 311
 
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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