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Conserved domains on  [gi|672216950|gb|AIJ02554|]
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glyceraldehyde-3-phosphate dehydrogenase, partial [Bryoria sp. 1 LM-2014a]

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
PLN02272 super family cl30355
glyceraldehyde-3-phosphate dehydrogenase
 2-146 8.66e-93

glyceraldehyde-3-phosphate dehydrogenase


The actual alignment was detected with superfamily member PLN02272:

Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 274.81  E-value: 8.66e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216950   2 KDPAN*PWKDTGAYYIVESTGVFTTTEKAKAHLKGGAKKVVISAPSADAAMFVMGVNEKEYKSDIEIISNASCTTNCLAP 81
Cdd:PLN02272 163 RDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAP 242

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672216950  82 LAKVMHDNYTIIEGLMTTIHSYTATQKTVDGPSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSL 146
Cdd:PLN02272 243 LAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPEL 307
 
Name Accession Description Interval E-value
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 2-146 8.66e-93

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 274.81  E-value: 8.66e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216950   2 KDPAN*PWKDTGAYYIVESTGVFTTTEKAKAHLKGGAKKVVISAPSADAAMFVMGVNEKEYKSDIEIISNASCTTNCLAP 81
Cdd:PLN02272 163 RDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAP 242

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672216950  82 LAKVMHDNYTIIEGLMTTIHSYTATQKTVDGPSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSL 146
Cdd:PLN02272 243 LAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPEL 307
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-146 1.29e-91

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: 268.80  E-value: 1.29e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216950   1 EKDPAN*PWKDTGAYYIVESTGVFTTTEKAKAHLKGGAKKVVISAPSADA-AMFVMGVNEKEYKSDIEIISNASCTTNCL 79
Cdd:COG0057   78 ERDPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCL 157

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672216950  80 APLAKVMHDNYTIIEGLMTTIHSYTATQKTVDGPsSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSL 146
Cdd:COG0057  158 APVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPEL 223
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 1-146 8.48e-80

glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the enzyme responsible for the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. Forms exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (1.2.1.59). In some species, NAD- and NADP- utilizing forms exist, generally being responsible for reactions in the anabolic and catabolic directions respectively. Two Pfam models cover the two functional domains of this protein; pfam00044 represents the N-terminal NAD(P)-binding domain and pfam02800 represents the C-terminal catalytic domain. An additional form of gap gene is found in gamma proteobacteria and is responsible for the conversion of erythrose-4-phosphate (E4P) to 4-phospho-erythronate in the biosynthesis of pyridoxine. This pathway of pyridoxine biosynthesis appears to be limited, however, to a relatively small number of bacterial species although it is prevalent among the gamma-proteobacteria. This enzyme is described by TIGR001532. These sequences generally score between trusted and noise to this GAPDH model due to the close evolutionary relationship. There exists the possiblity that some forms of GAPDH may be bifunctional and act on E4P in species which make pyridoxine and via hydroxythreonine and lack a separate E4PDH enzyme (for instance, the GAPDH from Bacillus stearothermophilus has been shown to posess a limited E4PD activity as well as a robust GAPDH activity). There are a great number of sequences in the databases which score between trusted and noise to this model, nearly all of them due to fragmentary sequences. It seems that study of this gene has been carried out in many species utilizing PCR probes which exclude the extreme ends of the consenses used to define this model. The noise level is set relative not to E4PD, but the next closest outliers, the class II GAPDH's (found in archaea, TIGR01546) and aspartate semialdehyde dehydrogenase (ASADH, TIGR01296) both of which have highest-scoring hits around -225 to the prior model. [Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 273675 [Multi-domain]  Cd Length: 326  Bit Score: 238.33  E-value: 8.48e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216950    1 EKDPAN*PWKDTGAYYIVESTGVFTTTEKAKAHLKGGAKKVVISAPSADAA-MFVMGVNEKEYKSDIEIISNASCTTNCL 79
Cdd:TIGR01534  77 ERDPSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDVkTIVYGVNHDEYDGEERIISNASCTTNCL 156

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672216950   80 APLAKVMHDNYTIIEGLMTTIHSYTATQKTVDGPsSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSL 146
Cdd:TIGR01534 157 APLAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPEL 222
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 74-146 1.56e-50

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: 158.77  E-value: 1.56e-50
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672216950  74 CTTNCLAPLAKVMHDNYTIIEGLMTTIHSYTATQKTVDGPsSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSL 146
Cdd:cd18126    1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGP-HKDLRRARAAAQNIIPTSTGAAKAVGLVIPEL 72
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
1-146 1.93e-46

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 153.17  E-value: 1.93e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216950   1 EKDPAN*PWKDtGAYYIVESTGVFTTTEKAKAHLKGGAKKVVISAP--SADAAMFVMGVNEKEYKSDIE-IISNASCTTN 77
Cdd:NF033735  74 NKDIEDTPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARHrIVTAASCTTN 152

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672216950  78 CLAPLAKVMHDNYTIIEGLMTTIHSYTATQKTVDGPsSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSL 146
Cdd:NF033735 153 CLAPVVKVIHEKIGIKHGSITTIHDITNTQTIVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPEL 220
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 79-146 3.53e-37

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: 124.63  E-value: 3.53e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672216950   79 LAPLAKVMHDNYTIIEGLMTTIHSYTATQKTVDGPSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSL 146
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPEL 68
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-74 6.43e-36

Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. N-terminal domain is a Rossmann NAD(P) binding fold.


Pssm-ID: 214851 [Multi-domain]  Cd Length: 149  Bit Score: 121.12  E-value: 6.43e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672216950     1 EKDPAN*PWKDTGAYYIVESTGVFTTTEKAKAHLKGGAKKVVISAPSADAA-MFVMGVNEKEYKSDIEIISNASC 74
Cdd:smart00846  75 ERDPANLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDADpTFVYGVNHDEYDGEDHIISNASC 149
 
Name Accession Description Interval E-value
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 2-146 8.66e-93

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 274.81  E-value: 8.66e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216950   2 KDPAN*PWKDTGAYYIVESTGVFTTTEKAKAHLKGGAKKVVISAPSADAAMFVMGVNEKEYKSDIEIISNASCTTNCLAP 81
Cdd:PLN02272 163 RDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAP 242

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672216950  82 LAKVMHDNYTIIEGLMTTIHSYTATQKTVDGPSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSL 146
Cdd:PLN02272 243 LAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPEL 307
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-146 1.29e-91

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: 268.80  E-value: 1.29e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216950   1 EKDPAN*PWKDTGAYYIVESTGVFTTTEKAKAHLKGGAKKVVISAPSADA-AMFVMGVNEKEYKSDIEIISNASCTTNCL 79
Cdd:COG0057   78 ERDPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCL 157

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672216950  80 APLAKVMHDNYTIIEGLMTTIHSYTATQKTVDGPsSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSL 146
Cdd:COG0057  158 APVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPEL 223
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 1-146 8.48e-80

glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the enzyme responsible for the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. Forms exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (1.2.1.59). In some species, NAD- and NADP- utilizing forms exist, generally being responsible for reactions in the anabolic and catabolic directions respectively. Two Pfam models cover the two functional domains of this protein; pfam00044 represents the N-terminal NAD(P)-binding domain and pfam02800 represents the C-terminal catalytic domain. An additional form of gap gene is found in gamma proteobacteria and is responsible for the conversion of erythrose-4-phosphate (E4P) to 4-phospho-erythronate in the biosynthesis of pyridoxine. This pathway of pyridoxine biosynthesis appears to be limited, however, to a relatively small number of bacterial species although it is prevalent among the gamma-proteobacteria. This enzyme is described by TIGR001532. These sequences generally score between trusted and noise to this GAPDH model due to the close evolutionary relationship. There exists the possiblity that some forms of GAPDH may be bifunctional and act on E4P in species which make pyridoxine and via hydroxythreonine and lack a separate E4PDH enzyme (for instance, the GAPDH from Bacillus stearothermophilus has been shown to posess a limited E4PD activity as well as a robust GAPDH activity). There are a great number of sequences in the databases which score between trusted and noise to this model, nearly all of them due to fragmentary sequences. It seems that study of this gene has been carried out in many species utilizing PCR probes which exclude the extreme ends of the consenses used to define this model. The noise level is set relative not to E4PD, but the next closest outliers, the class II GAPDH's (found in archaea, TIGR01546) and aspartate semialdehyde dehydrogenase (ASADH, TIGR01296) both of which have highest-scoring hits around -225 to the prior model. [Energy metabolism, Glycolysis/gluconeogenesis]


Pssm-ID: 273675 [Multi-domain]  Cd Length: 326  Bit Score: 238.33  E-value: 8.48e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216950    1 EKDPAN*PWKDTGAYYIVESTGVFTTTEKAKAHLKGGAKKVVISAPSADAA-MFVMGVNEKEYKSDIEIISNASCTTNCL 79
Cdd:TIGR01534  77 ERDPSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDVkTIVYGVNHDEYDGEERIISNASCTTNCL 156

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672216950   80 APLAKVMHDNYTIIEGLMTTIHSYTATQKTVDGPsSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSL 146
Cdd:TIGR01534 157 APLAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPEL 222
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
 2-146 1.09e-74

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 226.14  E-value: 1.09e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216950   2 KDPAN*PWKDTGAYYIVESTGVFTTTEKAKAHLKGGAKKVVISAPSADAAMFVMGVNEKEYKSDIEIISNASCTTNCLAP 81
Cdd:PLN02358  84 RNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCTTNCLAP 163

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672216950  82 LAKVMHDNYTIIEGLMTTIHSYTATQKTVDGPSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSL 146
Cdd:PLN02358 164 LAKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSL 228
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
 1-146 8.05e-72

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 218.55  E-value: 8.05e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216950   1 EKDPAN*PWKDTGAYYIVESTGVFTTTEKAKAHLKGGAKKVVISAPSADAA-MFVMGVNEKEYKSDIEIISNASCTTNCL 79
Cdd:PTZ00023  78 EKDPAAIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKDDTpIYVMGVNHTQYDKSQRIVSNASCTTNCL 157

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672216950  80 APLAKVMHDNYTIIEGLMTTIHSYTATQKTVDGPS--SKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSL 146
Cdd:PTZ00023 158 APLAKVVNDKFGIVEGLMTTVHASTANQLTVDGPSkgGKDWRAGRCAGVNIIPASTGAAKAVGKVIPEL 226
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 1-145 1.11e-64

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 201.05  E-value: 1.11e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216950   1 EKDPAN*PWKDTGAYYIVESTGVFTTTEKAKAHLKGGAKKVVISAP-SADAAMFVMGVNEKEYK-SDIEIISNASCTTNC 78
Cdd:PTZ00434  92 QRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPaSGGAKTIVMGVNQHEYSpTEHHVVSNASCTTNC 171

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672216950  79 LAPLAKVM-HDNYTIIEGLMTTIHSYTATQKTVDGPSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPS 145
Cdd:PTZ00434 172 LAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPS 239
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
1-146 2.07e-60

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 189.17  E-value: 2.07e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216950   1 EKDPAN*PWKDTGAYYIVESTGVFTTTEKAKAHLKGGAKKVVISAPSAD-AAMFVMGVNEKEYKSDiEIISNASCTTNCL 79
Cdd:PRK15425  77 ERDPANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDnTPMFVKGANFDKYAGQ-DIVSNASCTTNCL 155

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672216950  80 APLAKVMHDNYTIIEGLMTTIHSYTATQKTVDGPSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSL 146
Cdd:PRK15425 156 APLAKVINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPEL 222
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-146 3.85e-57

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 181.09  E-value: 3.85e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216950   1 EKDPAN*PWKDTGAYYIVESTGVFTTTEKAKAHLKGGAKKVVISAPSADA-AMFVMGVNEKEYKSDIE-IISNASCTTNC 78
Cdd:PRK07729  77 NRDPKELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEdVTIVVGVNEDQLDIEKHtIISNASCTTNC 156

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672216950  79 LAPLAKVMHDNYTIIEGLMTTIHSYTATQKTVDGPsSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSL 146
Cdd:PRK07729 157 LAPVVKVLDEQFGIENGLMTTVHAYTNDQKNIDNP-HKDLRRARACGQSIIPTTTGAAKALAKVLPHL 223
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
1-146 6.10e-57

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 180.49  E-value: 6.10e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216950   1 EKDPAN*PWKDTGAYYIVESTGVFTTTEKAKAHLKGGAKKVVISAP--SADAAMFVMGVNEKEYKSDI-EIISNASCTTN 77
Cdd:PRK07403  78 DRNPLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPgkGEDIGTYVVGVNHHEYDHEDhNIISNASCTTN 157

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672216950  78 CLAPLAKVMHDNYTIIEGLMTTIHSYTATQKTVDGpSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSL 146
Cdd:PRK07403 158 CLAPIAKVLHDNFGIIKGTMTTTHSYTGDQRILDA-SHRDLRRARAAAVNIVPTSTGAAKAVALVIPEL 225
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
 1-146 9.71e-52

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 168.57  E-value: 9.71e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216950   1 EKDPAN*PWKDTGAYYIVESTGVFTTTEKAKAHLKGGAKKVVISAPS-ADAAMFVMGVNEKEYKSDIEIISNASCTTNCL 79
Cdd:PLN03096 138 DRNPLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGkGDIPTYVVGVNADDYKHSDPIISNASCTTNCL 217

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672216950  80 APLAKVMHDNYTIIEGLMTTIHSYTATQKTVDGpSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSL 146
Cdd:PLN03096 218 APFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVALVLPNL 283
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 74-146 1.56e-50

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: 158.77  E-value: 1.56e-50
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672216950  74 CTTNCLAPLAKVMHDNYTIIEGLMTTIHSYTATQKTVDGPsSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSL 146
Cdd:cd18126    1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGP-HKDLRRARAAAQNIIPTSTGAAKAVGLVIPEL 72
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
 1-146 6.24e-48

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 160.07  E-value: 6.24e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216950   1 EKDPAN*PWKDTGAYYIVESTGVFTTTEKAKAHLKGGAKKVVISAPS--ADAAMFVMGVNEKEYKSDI-EIISNASCTTN 77
Cdd:PLN02237 153 NRDPLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAkgADIPTYVVGVNEDDYDHEVaNIVSNASCTTN 232

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672216950  78 CLAPLAKVMHDNYTIIEGLMTTIHSYTATQKTVDGpSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSL 146
Cdd:PLN02237 233 CLAPFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVSLVLPQL 300
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
1-146 1.93e-46

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 153.17  E-value: 1.93e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216950   1 EKDPAN*PWKDtGAYYIVESTGVFTTTEKAKAHLKGGAKKVVISAP--SADAAMFVMGVNEKEYKSDIE-IISNASCTTN 77
Cdd:NF033735  74 NKDIEDTPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARHrIVTAASCTTN 152

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672216950  78 CLAPLAKVMHDNYTIIEGLMTTIHSYTATQKTVDGPsSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSL 146
Cdd:NF033735 153 CLAPVVKVIHEKIGIKHGSITTIHDITNTQTIVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPEL 220
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 1-73 1.30e-39

N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; GAPDH plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (EC 1.2.1.59). The family corresponds to the ubiquitous NAD+ or NADP+ utilizing type I GAPDH and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose.


Pssm-ID: 467614 [Multi-domain]  Cd Length: 164  Bit Score: 130.98  E-value: 1.30e-39
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672216950   1 EKDPAN*PWKDTGAYYIVESTGVFTTTEKAKAHLKGGAKKVVISAPSADAA-MFVMGVNEKEYKSDIEIISNAS 73
Cdd:cd05214   75 ERDPAELPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDDDpTIVMGVNHDKYDADDKIISNAS 148
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
 1-144 1.10e-37

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 130.56  E-value: 1.10e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216950   1 EKDPAN*PWKDTGAYYIVESTGVFTTTEKAKAHLKGGAKKVVISAPSA---DAAMfVMGVNEKEYKSDIEIISNASCTTN 77
Cdd:PRK13535  79 ERDIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSndlDATV-VYGVNHDQLRAEHRIVSNASCTTN 157

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672216950  78 CLAPLAKVMHDNYTIIEGLMTTIHSYTATQKTVDGPSSkDWRGGRTAAQNIIPSSTGAAKAVGKVIP 144
Cdd:PRK13535 158 CIIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHP-DLRRTRAASQSIIPVDTKLAAGITRIFP 223
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 79-146 3.53e-37

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: 124.63  E-value: 3.53e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672216950   79 LAPLAKVMHDNYTIIEGLMTTIHSYTATQKTVDGPSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSL 146
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPEL 68
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-74 6.43e-36

Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. N-terminal domain is a Rossmann NAD(P) binding fold.


Pssm-ID: 214851 [Multi-domain]  Cd Length: 149  Bit Score: 121.12  E-value: 6.43e-36
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672216950     1 EKDPAN*PWKDTGAYYIVESTGVFTTTEKAKAHLKGGAKKVVISAPSADAA-MFVMGVNEKEYKSDIEIISNASC 74
Cdd:smart00846  75 ERDPANLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDADpTFVYGVNHDEYDGEDHIISNASC 149
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 74-146 1.69e-35

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: 120.41  E-value: 1.69e-35
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672216950  74 CTTNCLAPLAKVMHDNYTIIEGLMTTIHSYTATQKTVDGPSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSL 146
Cdd:cd18123    1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPEL 73
PRK08955 PRK08955
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-146 2.67e-35

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 169599 [Multi-domain]  Cd Length: 334  Bit Score: 124.46  E-value: 2.67e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216950   1 EKDPAN*PWkdTGAYYIVESTGVFTTTEKAKAHLKGGAKKVVISAPSAD--AAMFVMGVNEKEYKSDI-EIISNASCTTN 77
Cdd:PRK08955  78 NKAIADTDW--SGCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEegVLNIVMGVNDHLFDPAIhPIVTAASCTTN 155

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672216950  78 CLAPLAKVMHDNYTIIEGLMTTIHSYTATQKTVDGPsSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSL 146
Cdd:PRK08955 156 CLAPVVKVIHEKLGIKHGSMTTIHDLTNTQTILDAP-HKDLRRARACGMSLIPTTTGSATAITEIFPEL 223
PRK08289 PRK08289
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
 17-146 5.76e-34

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 236219 [Multi-domain]  Cd Length: 477  Bit Score: 123.49  E-value: 5.76e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216950  17 IVESTGVFTTTEKAKAHLKG-GAKKVVISAPS-ADAAMFVMGVNEKEYKSDIEIISNASCTTNCLAPLAKVMHDNYTIIE 94
Cdd:PRK08289 230 VVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGkGDIKNIVHGVNHSDITDEDKIVSAASCTTNAITPVLKAVNDKYGIVN 309

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 672216950  95 GLMTTIHSYTATQKTVDGPSSKDwRGGRTAAQNIIPSSTGAAKAVGKVIPSL 146
Cdd:PRK08289 310 GHVETVHSYTNDQNLIDNYHKGD-RRGRSAPLNMVITETGAAKAVAKALPEL 360
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
 3-146 5.01e-25

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 97.64  E-value: 5.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216950   3 DPAN*PWKDTGAYYIVESTGVFTTTEKAKAHLKGGAKKVVISAPSADAAMFVMGVNEKEYKSDIEIISNASCTTNCLAPL 82
Cdd:PTZ00353  82 DLVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDERLSASLPVCCAGAPIAVALAPV 161

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672216950  83 AKVMHDNYTIIEGLMTTIHSyTATQKTVDGPS--SKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSL 146
Cdd:PTZ00353 162 IRALHEVYGVEECSYTAIHG-MQPQEPIAARSknSQDWRQTRVAIDAIAPYRDNGAETVCKLLPHL 226
GAPDH_N_E4PDH cd17892
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 1-73 3.85e-19

N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar proteins; E4PDH (EC 1.2.1.72), also called E4P dehydrogenase, catalyzes the NAD-dependent conversion of D-erythrose 4-phosphate (E4P) to 4-phosphoerythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose. This enzyme activity appears to have evolved from glyceraldehyde-3-phosphate dehydrogenase (GADPH), whose substrate differs only in the lack of one carbon relative to E4P. E4PDH proteins contain an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal GADPH-like catalytic domain and are members of the GAPDH family of proteins.


Pssm-ID: 467615 [Multi-domain]  Cd Length: 169  Bit Score: 78.46  E-value: 3.85e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672216950   1 EKDPAN*PWKDTGAYYIVESTGVFTTTEKAKAHLKGGAKKVVISAPSA---DAAMfVMGVNEKEYKSDIEIISNAS 73
Cdd:cd17892   78 EPDPENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASndvDATI-VYGINQDLLRAEHRIVSNAS 152
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 74-146 2.23e-17

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: 74.09  E-value: 2.23e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672216950  74 CTTNCLAPLAKVMHDNYTIIEGLMTTIHSYTATQKTVDGPSSKDWrgGRTAAQNIIPSSTGAAKAVGKVIPSL 146
Cdd:cd18122    1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEI 71
GAPDH_C_E4PDH cd23937
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 74-146 5.38e-14

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: 65.13  E-value: 5.38e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672216950  74 CTTNCLAPLAKVMHDNYTIIEGLMTTIHSYTATQKTVDGpSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSL 146
Cdd:cd23937    1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLARGIERILPHL 72
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-26 1.39e-07

Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. N-terminal domain is a Rossmann NAD(P) binding fold.


Pssm-ID: 459648 [Multi-domain]  Cd Length: 101  Bit Score: 46.71  E-value: 1.39e-07
                          10        20
                  ....*....|....*....|....*.
gi 672216950    1 EKDPAN*PWKDTGAYYIVESTGVFTT 26
Cdd:pfam00044  75 ERDPAELPWGDLGVDVVIESTGVFTT 100
GAPDH-like_N cd05192
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ...
 16-78 2.77e-07

N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like family; The GAPDH-like family includes glyceraldehyde-3-phosphate dehydrogenase (GAPDH), native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs), 2,4-diaminopentanoate dehydrogenase (DAPDH), meso-diaminopimelate D-dehydrogenase (meso-DAPDH), and dihydrodipicolinate reductase (DHDPR). GAPDH plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. nat-AmDHs catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. They play important roles in the efficient asymmetric synthesis of alpha-chiral amines. DAPDH is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). DHDPR catalyzes the NAD(P)H-dependent reduction of 2,3-dihydrodipicolinate (DHDP) to 2,3,4,5-tetrahydrodipicolinate (THDP). It could also function as a dehydratase in addition to the role of a nucleotide dependent reductase. The model corresponds to the N-terminal NAD(P)-binding domain of GAPDH-like family proteins. It contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft.


Pssm-ID: 467613 [Multi-domain]  Cd Length: 109  Bit Score: 46.19  E-value: 2.77e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672216950  16 YIVESTGVFTTTEKAKAHLKGGAKKVVISAPSADAAMF-VMGVNEKEYKSDIEIISNASCTTNC 78
Cdd:cd05192   36 VVIECTGSFTDDDNAEKHIKAGGKKAVITAPEKGDIPTiVVVLNELAKSAGATVVSNANETSYS 99
 
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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