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Conserved domains on  [gi|1767852752|gb|QFR04591|]
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glycosomal glyceraldehyde-3-phosphate dehydrogenase, partial [Trypanosoma congolense type Savannah]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PTZ00434 super family cl30359
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 1-204 1.27e-151

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


The actual alignment was detected with superfamily member PTZ00434:

Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 424.47  E-value: 1.27e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752   1 VAKDDTLVVNGHRILCVKAQRNPADLPWGKLGVEYVIESTGLFTVKSAAEGHLRGGARKVIISAPASGGAKTFVMGVNHG 80
Cdd:PTZ00434   73 VKTDDVLVVNGHRIKCVKAQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPASGGAKTIVMGVNQH 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752  81 DYNPREHHVVSNASCTTNCLAPLVHVLVKEGFGISTGLMTTIHSYTATQKTVDGVSIKDWRGGRAAALNIIPSTTGAAKA 160
Cdd:PTZ00434  153 EYSPTEHHVVSNASCTTNCLAPIVHVLTKEGFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKA 232

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1767852752 161 VGMVIPSTQGKLTGMAFRVPTADVSVVDLTFTAARDTSIKEIDA 204
Cdd:PTZ00434  233 VGMVIPSTKGKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDA 276
 
Name Accession Description Interval E-value
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 1-204 1.27e-151

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 424.47  E-value: 1.27e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752   1 VAKDDTLVVNGHRILCVKAQRNPADLPWGKLGVEYVIESTGLFTVKSAAEGHLRGGARKVIISAPASGGAKTFVMGVNHG 80
Cdd:PTZ00434   73 VKTDDVLVVNGHRIKCVKAQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPASGGAKTIVMGVNQH 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752  81 DYNPREHHVVSNASCTTNCLAPLVHVLVKEGFGISTGLMTTIHSYTATQKTVDGVSIKDWRGGRAAALNIIPSTTGAAKA 160
Cdd:PTZ00434  153 EYSPTEHHVVSNASCTTNCLAPIVHVLTKEGFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKA 232

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1767852752 161 VGMVIPSTQGKLTGMAFRVPTADVSVVDLTFTAARDTSIKEIDA 204
Cdd:PTZ00434  233 VGMVIPSTKGKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDA 276
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 2-204 3.91e-120

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: 343.53  E-value: 3.91e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752   2 AKDDTLVVNGHRILCVkAQRNPADLPWGKLGVEYVIESTGLFTVKSAAEGHLRGGARKVIISAPASGGAKTFVMGVNHGD 81
Cdd:COG0057    61 VEGDSLIVNGKKIKVL-AERDPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDDPTIVYGVNHDD 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752  82 YNPrEHHVVSNASCTTNCLAPLVHVLvKEGFGISTGLMTTIHSYTATQKTVDGVSiKDWRGGRAAALNIIPSTTGAAKAV 161
Cdd:COG0057   140 YDA-DHRIISNASCTTNCLAPVAKVL-NDAFGIEKGLMTTIHAYTNDQNLLDAPH-KDLRRARAAALNIIPTSTGAAKAV 216

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1767852752 162 GMVIPSTQGKLTGMAFRVPTADVSVVDLTFTAARDTSIKEIDA 204
Cdd:COG0057   217 GLVLPELKGKLDGMAVRVPTPNVSLVDLTVELEKETTVEEVNA 259
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 2-204 9.78e-104

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: 301.89  E-value: 9.78e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752   2 AKDDTLVVNGHRILCVKAQRNPADLPWGKLGVEYVIESTGLFTVKSAAEGHLRGGARKVIISAPASGGAKTFVMGVNHGD 81
Cdd:TIGR01534  59 VDEDGLVVNGKEVISVFSERDPSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDVKTIVYGVNHDE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752  82 YNPrEHHVVSNASCTTNCLAPLVHVLVKEgFGISTGLMTTIHSYTATQKTVDGVSiKDWRGGRAAALNIIPSTTGAAKAV 161
Cdd:TIGR01534 139 YDG-EERIISNASCTTNCLAPLAKVLDEA-FGIVSGLMTTVHAYTNDQNLLDGPH-KDLRRARAAALNIIPTSTGAAKAI 215

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1767852752 162 GMVIPSTQGKLTGMAFRVPTADVSVVDLTFTAARDTSIKEIDA 204
Cdd:TIGR01534 216 GKVLPELAGKLTGMAIRVPTPNVSLVDLVVNLEKDVTVEEVNA 258
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 95-204 1.22e-66

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: 201.92  E-value: 1.22e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752  95 CTTNCLAPLVHVLvKEGFGISTGLMTTIHSYTATQKTVDGVSiKDWRGGRAAALNIIPSTTGAAKAVGMVIPSTQGKLTG 174
Cdd:cd18126     1 CTTNCLAPVAKVL-NDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTG 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 1767852752 175 MAFRVPTADVSVVDLTFTAARDTSIKEIDA 204
Cdd:cd18126    79 MAFRVPTPNVSVVDLTVRLEKPVTVEEVNA 108
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
2-204 3.37e-66

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 206.32  E-value: 3.37e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752   2 AKDDTLVVNGHRIlCVKAQRNPADLPWGKlGVEYVIESTGLFTVKSAAEGHLRGGARKVIISAPA-SGGAKTFVMGVNHG 80
Cdd:NF033735   57 AEEDSIVIDGKRI-SFSSNKDIEDTPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVkEEGVLNIVYGVNDH 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752  81 DYNPREHHVVSNASCTTNCLAPLVHVlVKEGFGISTGLMTTIHSYTATQKTVDGVSiKDWRGGRAAALNIIPSTTGAAKA 160
Cdd:NF033735  135 LYDPARHRIVTAASCTTNCLAPVVKV-IHEKIGIKHGSITTIHDITNTQTIVDAPH-KDLRRARSCGMSLIPTTTGSATA 212

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1767852752 161 VGMVIPSTQGKLTGMAFRVPTADVSVVDLTFTAARDTSIKEIDA 204
Cdd:NF033735  213 ITLIFPELKGKLNGHAVRVPLLNASLTDCVFEVERPTTVEEVNA 256
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 100-204 4.78e-52

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: 164.69  E-value: 4.78e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752 100 LAPLVHVLvKEGFGISTGLMTTIHSYTATQKTVDGVSIKDWRGGRAAALNIIPSTTGAAKAVGMVIPSTQGKLTGMAFRV 179
Cdd:pfam02800   1 LAPLAKVL-NDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRV 79

                          90       100
                  ....*....|....*....|....*
gi 1767852752 180 PTADVSVVDLTFTAARDTSIKEIDA 204
Cdd:pfam02800  80 PTPNVSVVDLVVELEKPVTVEEVNA 104
 
Name Accession Description Interval E-value
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 1-204 1.27e-151

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 424.47  E-value: 1.27e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752   1 VAKDDTLVVNGHRILCVKAQRNPADLPWGKLGVEYVIESTGLFTVKSAAEGHLRGGARKVIISAPASGGAKTFVMGVNHG 80
Cdd:PTZ00434   73 VKTDDVLVVNGHRIKCVKAQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPASGGAKTIVMGVNQH 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752  81 DYNPREHHVVSNASCTTNCLAPLVHVLVKEGFGISTGLMTTIHSYTATQKTVDGVSIKDWRGGRAAALNIIPSTTGAAKA 160
Cdd:PTZ00434  153 EYSPTEHHVVSNASCTTNCLAPIVHVLTKEGFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKA 232

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1767852752 161 VGMVIPSTQGKLTGMAFRVPTADVSVVDLTFTAARDTSIKEIDA 204
Cdd:PTZ00434  233 VGMVIPSTKGKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDA 276
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 2-204 3.91e-120

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: 343.53  E-value: 3.91e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752   2 AKDDTLVVNGHRILCVkAQRNPADLPWGKLGVEYVIESTGLFTVKSAAEGHLRGGARKVIISAPASGGAKTFVMGVNHGD 81
Cdd:COG0057    61 VEGDSLIVNGKKIKVL-AERDPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDDPTIVYGVNHDD 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752  82 YNPrEHHVVSNASCTTNCLAPLVHVLvKEGFGISTGLMTTIHSYTATQKTVDGVSiKDWRGGRAAALNIIPSTTGAAKAV 161
Cdd:COG0057   140 YDA-DHRIISNASCTTNCLAPVAKVL-NDAFGIEKGLMTTIHAYTNDQNLLDAPH-KDLRRARAAALNIIPTSTGAAKAV 216

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1767852752 162 GMVIPSTQGKLTGMAFRVPTADVSVVDLTFTAARDTSIKEIDA 204
Cdd:COG0057   217 GLVLPELKGKLDGMAVRVPTPNVSLVDLTVELEKETTVEEVNA 259
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 2-204 9.78e-104

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: 301.89  E-value: 9.78e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752   2 AKDDTLVVNGHRILCVKAQRNPADLPWGKLGVEYVIESTGLFTVKSAAEGHLRGGARKVIISAPASGGAKTFVMGVNHGD 81
Cdd:TIGR01534  59 VDEDGLVVNGKEVISVFSERDPSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDVKTIVYGVNHDE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752  82 YNPrEHHVVSNASCTTNCLAPLVHVLVKEgFGISTGLMTTIHSYTATQKTVDGVSiKDWRGGRAAALNIIPSTTGAAKAV 161
Cdd:TIGR01534 139 YDG-EERIISNASCTTNCLAPLAKVLDEA-FGIVSGLMTTVHAYTNDQNLLDGPH-KDLRRARAAALNIIPTSTGAAKAI 215

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1767852752 162 GMVIPSTQGKLTGMAFRVPTADVSVVDLTFTAARDTSIKEIDA 204
Cdd:TIGR01534 216 GKVLPELAGKLTGMAIRVPTPNVSLVDLVVNLEKDVTVEEVNA 258
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 1-204 2.09e-92

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 276.35  E-value: 2.09e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752   1 VAKDDTLVVNGHRILcVKAQRNPADLPWGKLGVEYVIESTGLFTVKSAAEGHLRGGARKVIISAPaSGGAKTFVMGVNHG 80
Cdd:PLN02272  144 VVDDSTLEINGKQIK-VTSKRDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAP-SADAPMFVVGVNEK 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752  81 DYNPReHHVVSNASCTTNCLAPLVHVlVKEGFGISTGLMTTIHSYTATQKTVDGVSIKDWRGGRAAALNIIPSTTGAAKA 160
Cdd:PLN02272  222 TYKPN-MNIVSNASCTTNCLAPLAKV-VHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKA 299

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1767852752 161 VGMVIPSTQGKLTGMAFRVPTADVSVVDLTFTAARDTSIKEIDA 204
Cdd:PLN02272  300 VGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRLEKSASYEDVKA 343
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-204 7.18e-85

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 254.66  E-value: 7.18e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752   1 VAKDDTLVVNGHRILCVkAQRNPADLPWGKLGVEYVIESTGLFTVKSAAEGHLRGGARKVIISAPASGGAKTFVMGVNHG 80
Cdd:PRK07729   59 EAFEDHLLVDGKKIRLL-NNRDPKELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVTIVVGVNED 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752  81 DYNPREHHVVSNASCTTNCLAPLVHVLvKEGFGISTGLMTTIHSYTATQKTVDGVSiKDWRGGRAAALNIIPSTTGAAKA 160
Cdd:PRK07729  138 QLDIEKHTIISNASCTTNCLAPVVKVL-DEQFGIENGLMTTVHAYTNDQKNIDNPH-KDLRRARACGQSIIPTTTGAAKA 215

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1767852752 161 VGMVIPSTQGKLTGMAFRVPTADVSVVDLTFTAARDTSIKEIDA 204
Cdd:PRK07729  216 LAKVLPHLNGKLHGMALRVPTPNVSLVDLVVDVKRDVTVEEINE 259
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
 3-202 4.24e-76

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 232.03  E-value: 4.24e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752   3 KDDTLVVnGHRILCVKAQRNPADLPWGKLGVEYVIESTGLFTVKSAAEGHLRGGARKVIISAPASGGAKTFVMGVNHGDY 82
Cdd:PTZ00023   62 TDGFLMI-GSKKVHVFFEKDPAAIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKDDTPIYVMGVNHTQY 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752  83 NPREHhVVSNASCTTNCLAPLVHVlVKEGFGISTGLMTTIHSYTATQKTVDGVSI--KDWRGGRAAALNIIPSTTGAAKA 160
Cdd:PTZ00023  141 DKSQR-IVSNASCTTNCLAPLAKV-VNDKFGIVEGLMTTVHASTANQLTVDGPSKggKDWRAGRCAGVNIIPASTGAAKA 218

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1767852752 161 VGMVIPSTQGKLTGMAFRVPTADVSVVDLTFTAARDTSIKEI 202
Cdd:PTZ00023  219 VGKVIPELNGKLTGMAFRVPVPDVSVVDLTCKLAKPAKYEEI 260
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
 3-202 3.54e-75

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 229.61  E-value: 3.54e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752   3 KDDTLVVNGHRILCVKAQRNPADLPWGKLGVEYVIESTGLFTVKSAAEGHLRGGARKVIISAPaSGGAKTFVMGVNHGDY 82
Cdd:PLN02358   66 KDDKTLLFGEKPVTVFGIRNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAP-SKDAPMFVVGVNEHEY 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752  83 NpREHHVVSNASCTTNCLAPLVHVlVKEGFGISTGLMTTIHSYTATQKTVDGVSIKDWRGGRAAALNIIPSTTGAAKAVG 162
Cdd:PLN02358  145 K-SDLDIVSNASCTTNCLAPLAKV-INDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVG 222

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1767852752 163 MVIPSTQGKLTGMAFRVPTADVSVVDLTFTAARDTSIKEI 202
Cdd:PLN02358  223 KVLPSLNGKLTGMSFRVPTVDVSVVDLTVRLEKAATYDEI 262
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
2-203 1.03e-73

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 225.94  E-value: 1.03e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752   2 AKDDTLVVNGHRILCVkAQRNPADLPWGKLGVEYVIESTGLFTVKSAAEGHLRGGARKVIISAPASG-GAKTFVMGVNHG 80
Cdd:PRK07403   61 ADENSITVNGKTIKCV-SDRNPLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPGKGeDIGTYVVGVNHH 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752  81 DYNPREHHVVSNASCTTNCLAPLVHVLvKEGFGISTGLMTTIHSYTATQKTVDGvSIKDWRGGRAAALNIIPSTTGAAKA 160
Cdd:PRK07403  140 EYDHEDHNIISNASCTTNCLAPIAKVL-HDNFGIIKGTMTTTHSYTGDQRILDA-SHRDLRRARAAAVNIVPTSTGAAKA 217

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1767852752 161 VGMVIPSTQGKLTGMAFRVPTADVSVVDLTFTAARDTSIKEID 203
Cdd:PRK07403  218 VALVIPELKGKLNGIALRVPTPNVSVVDLVVQVEKRTITEQVN 260
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
 1-204 8.69e-68

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 212.48  E-value: 8.69e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752   1 VAKDDTLVVNGhRILCVKAQRNPADLPWGKLGVEYVIESTGLFTVKSAAEGHLRGGARKVIISAPASGGAKTFVMGVNHG 80
Cdd:PLN03096  120 PVGDDAISVDG-KVIKVVSDRNPLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKGDIPTYVVGVNAD 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752  81 DYNPREHhVVSNASCTTNCLAPLVHVLvKEGFGISTGLMTTIHSYTATQKTVDGvSIKDWRGGRAAALNIIPSTTGAAKA 160
Cdd:PLN03096  199 DYKHSDP-IISNASCTTNCLAPFVKVL-DQKFGIIKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKA 275

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1767852752 161 VGMVIPSTQGKLTGMAFRVPTADVSVVDLTFTAARDTSIKEIDA 204
Cdd:PLN03096  276 VALVLPNLKGKLNGIALRVPTPNVSVVDLVVQVEKKTFAEEVNA 319
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
3-202 3.42e-67

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 209.21  E-value: 3.42e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752   3 KDDTLVVNGHRILcVKAQRNPADLPWGKLGVEYVIESTGLFTVKSAAEGHLRGGARKVIISAPASGGAKTFVMGVNHGDY 82
Cdd:PRK15425   61 KDGHLIVNGKKIR-VTAERDPANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDNTPMFVKGANFDKY 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752  83 NPREhhVVSNASCTTNCLAPLVHVlVKEGFGISTGLMTTIHSYTATQKTVDGVSIKDWRGGRAAALNIIPSTTGAAKAVG 162
Cdd:PRK15425  140 AGQD--IVSNASCTTNCLAPLAKV-INDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVG 216

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1767852752 163 MVIPSTQGKLTGMAFRVPTADVSVVDLTFTAARDTSIKEI 202
Cdd:PRK15425  217 KVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAATYEQI 256
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 95-204 1.22e-66

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: 201.92  E-value: 1.22e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752  95 CTTNCLAPLVHVLvKEGFGISTGLMTTIHSYTATQKTVDGVSiKDWRGGRAAALNIIPSTTGAAKAVGMVIPSTQGKLTG 174
Cdd:cd18126     1 CTTNCLAPVAKVL-NDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTG 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 1767852752 175 MAFRVPTADVSVVDLTFTAARDTSIKEIDA 204
Cdd:cd18126    79 MAFRVPTPNVSVVDLTVRLEKPVTVEEVNA 108
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
2-204 3.37e-66

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 206.32  E-value: 3.37e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752   2 AKDDTLVVNGHRIlCVKAQRNPADLPWGKlGVEYVIESTGLFTVKSAAEGHLRGGARKVIISAPA-SGGAKTFVMGVNHG 80
Cdd:NF033735   57 AEEDSIVIDGKRI-SFSSNKDIEDTPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVkEEGVLNIVYGVNDH 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752  81 DYNPREHHVVSNASCTTNCLAPLVHVlVKEGFGISTGLMTTIHSYTATQKTVDGVSiKDWRGGRAAALNIIPSTTGAAKA 160
Cdd:NF033735  135 LYDPARHRIVTAASCTTNCLAPVVKV-IHEKIGIKHGSITTIHDITNTQTIVDAPH-KDLRRARSCGMSLIPTTTGSATA 212

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1767852752 161 VGMVIPSTQGKLTGMAFRVPTADVSVVDLTFTAARDTSIKEIDA 204
Cdd:NF033735  213 ITLIFPELKGKLNGHAVRVPLLNASLTDCVFEVERPTTVEEVNA 256
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
 1-189 3.42e-63

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 202.05  E-value: 3.42e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752   1 VAKDDTLVVNGhRILCVKAQRNPADLPWGKLGVEYVIESTGLFTVKSAAEGHLRGGARKVIISAPASGG-AKTFVMGVNH 79
Cdd:PLN02237  135 IVDDETISVDG-KPIKVVSNRDPLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAKGAdIPTYVVGVNE 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752  80 GDYNPREHHVVSNASCTTNCLAPLVHVLvKEGFGISTGLMTTIHSYTATQKTVDGvSIKDWRGGRAAALNIIPSTTGAAK 159
Cdd:PLN02237  214 DDYDHEVANIVSNASCTTNCLAPFVKVL-DEEFGIVKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAK 291

                         170       180       190
                  ....*....|....*....|....*....|
gi 1767852752 160 AVGMVIPSTQGKLTGMAFRVPTADVSVVDL 189
Cdd:PLN02237  292 AVSLVLPQLKGKLNGIALRVPTPNVSVVDL 321
PRK08955 PRK08955
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-204 5.54e-55

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 169599 [Multi-domain]  Cd Length: 334  Bit Score: 177.62  E-value: 5.54e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752   1 VAKDDTLVVNGHRILCvKAQRNPADLPWGklGVEYVIESTGLFTVKSAAEGHLRGGARKVIISAPA-SGGAKTFVMGVNH 79
Cdd:PRK08955   60 TAEGDAIVINGKRIRT-TQNKAIADTDWS--GCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVkEEGVLNIVMGVND 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752  80 GDYNPREHHVVSNASCTTNCLAPLVHVLvKEGFGISTGLMTTIHSYTATQKTVDGVSiKDWRGGRAAALNIIPSTTGAAK 159
Cdd:PRK08955  137 HLFDPAIHPIVTAASCTTNCLAPVVKVI-HEKLGIKHGSMTTIHDLTNTQTILDAPH-KDLRRARACGMSLIPTTTGSAT 214

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1767852752 160 AVGMVIPSTQGKLTGMAFRVPTADVSVVDLTFTAARDTSIKEIDA 204
Cdd:PRK08955  215 AITEIFPELKGKLNGHAVRVPLANASLTDCVFEVERDTTVEEVNA 259
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 100-204 4.78e-52

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: 164.69  E-value: 4.78e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752 100 LAPLVHVLvKEGFGISTGLMTTIHSYTATQKTVDGVSIKDWRGGRAAALNIIPSTTGAAKAVGMVIPSTQGKLTGMAFRV 179
Cdd:pfam02800   1 LAPLAKVL-NDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRV 79

                          90       100
                  ....*....|....*....|....*
gi 1767852752 180 PTADVSVVDLTFTAARDTSIKEIDA 204
Cdd:pfam02800  80 PTPNVSVVDLVVELEKPVTVEEVNA 104
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 2-94 3.52e-48

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: 154.86  E-value: 3.52e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752   2 AKDDTLVVNGHRILCVkAQRNPADLPWGKLGVEYVIESTGLFTVKSAAEGHLRGGARKVIISAPASGGAKTFVMGVNHGD 81
Cdd:cd05214    58 VDDDALIVNGKKIKVF-AERDPAELPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDDDPTIVMGVNHDK 136

                          90
                  ....*....|...
gi 1767852752  82 YNPrEHHVVSNAS 94
Cdd:cd05214   137 YDA-DDKIISNAS 148
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
 1-204 1.12e-44

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 151.36  E-value: 1.12e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752   1 VAKDDTLVVNGHRILCVKAQRNPADLPWGKLGVEYVIESTGLFTVKSAAEGHLRGGARKVIISAPASGGA-KTFVMGVNH 79
Cdd:PRK13535   60 VRQERDQLFVGDDAIRLLHERDIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSNDLdATVVYGVNH 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752  80 GDYNPrEHHVVSNASCTTNCLAPLVHVLvKEGFGISTGLMTTIHSYTATQKTVDGVSiKDWRGGRAAALNIIPSTTGAAK 159
Cdd:PRK13535  140 DQLRA-EHRIVSNASCTTNCIIPVIKLL-DDAFGIESGTVTTIHSAMNDQQVIDAYH-PDLRRTRAASQSIIPVDTKLAA 216

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1767852752 160 AVGMVIPSTQGKLTGMAFRVPTADVSVVDLTFTAARDTSIKEIDA 204
Cdd:PRK13535  217 GITRIFPQFNDRFEAISVRVPTINVTAIDLSVTVKKPVKVNEVNQ 261
PRK08289 PRK08289
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
 5-204 3.50e-44

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 236219 [Multi-domain]  Cd Length: 477  Bit Score: 153.15  E-value: 3.50e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752   5 DTLVVNGHRILCVKAQrNPADLPWGKLGVE--YVIESTGLFTVKSAAEGHLRG-GARKVIISAPASGGAKTFVMGVNHGD 81
Cdd:PRK08289  198 NAIIANGNYIQVIYAN-SPEEVDYTAYGINnaLVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGKGDIKNIVHGVNHSD 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752  82 YNPrEHHVVSNASCTTNCLAPLVHVLVKEgFGISTGLMTTIHSYTATQKTVDGVSIKDwRGGRAAALNIIPSTTGAAKAV 161
Cdd:PRK08289  277 ITD-EDKIVSAASCTTNAITPVLKAVNDK-YGIVNGHVETVHSYTNDQNLIDNYHKGD-RRGRSAPLNMVITETGAAKAV 353

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1767852752 162 GMVIPSTQGKLTGMAFRVPTADVSVVDLTFTAARDTSIKEIDA 204
Cdd:PRK08289  354 AKALPELAGKLTGNAIRVPTPNVSMAILNLNLEKETSREELNE 396
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 95-202 1.12e-39

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: 133.51  E-value: 1.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752  95 CTTNCLAPLVHVLvKEGFGISTGLMTTIHSYTATQKTVDGVSIKDWRGGRAAALNIIPSTTGAAKAVGMVIPSTQGKLTG 174
Cdd:cd18123     1 CTTNCLAPLAKAI-HDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTG 79

                          90       100
                  ....*....|....*....|....*...
gi 1767852752 175 MAFRVPTADVSVVDLTFTAARDTSIKEI 202
Cdd:cd18123    80 MAVRVPTTLMSVHDLMVELEKDVTYDDI 107
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
 4-189 8.68e-25

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 99.18  E-value: 8.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752   4 DDTLVVNGHRILCVKAQRNPADLPWGKLGVEYVIESTGLFTVKSAAEGHLRGGARKVIISApASGGAKTFVMGVNHGDYN 83
Cdd:PTZ00353   64 GEQIVLNGTQKIRVSAKHDLVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAG-QSADAPTVMAGSNDERLS 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752  84 pREHHVVSNASCTTNCLAPLVHVLVKEgFGISTGLMTTIHSyTATQKTVDGVSI--KDWRGGRAAALNIIPSTTGAAKAV 161
Cdd:PTZ00353  143 -ASLPVCCAGAPIAVALAPVIRALHEV-YGVEECSYTAIHG-MQPQEPIAARSKnsQDWRQTRVAIDAIAPYRDNGAETV 219

                         170       180
                  ....*....|....*....|....*...
gi 1767852752 162 GMVIPSTQGKLTGMAFRVPTADVSVVDL 189
Cdd:PTZ00353  220 CKLLPHLVGRISGSAFQVPVKKGCAIDM 247
GAPDH_C_E4PDH cd23937
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 95-204 1.27e-24

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: 94.79  E-value: 1.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752  95 CTTNCLAPLVHVLvKEGFGISTGLMTTIHSYTATQKTVDGvSIKDWRGGRAAALNIIPSTTGAAKAVGMVIPSTQGKLTG 174
Cdd:cd23937     1 CTTNCIVPVIKVL-DEAFGIESGTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEA 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 1767852752 175 MAFRVPTADVSVVDLTFTAARDTSIKEIDA 204
Cdd:cd23937    79 IAVRVPTINVTAMDLSVTLKKDVTAEEVNR 108
GAPDH_N_E4PDH cd17892
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 4-94 5.63e-22

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: 87.71  E-value: 5.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752   4 DDTLVVNGHRILcVKAQRNPADLPWGKLGVEYVIESTGLFTVKSAAEGHLRGGARKVIISAPASGGAK-TFVMGVNHGDY 82
Cdd:cd17892    63 NDQLFVNGDKIR-VLHEPDPENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASNDVDaTIVYGINQDLL 141

                          90
                  ....*....|..
gi 1767852752  83 NPrEHHVVSNAS 94
Cdd:cd17892   142 RA-EHRIVSNAS 152
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 95-204 5.32e-19

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: 79.87  E-value: 5.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1767852752  95 CTTNCLAPLVHVLVKEgFGISTGLMTTIHSYTATQKTVDGVSIKDWrgGRAAALNIIPSTTGAAKAVGMVIP--STQGKL 172
Cdd:cd18122     1 CTTTGLIPAAKALNDK-FGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGeiGKPIKV 77

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1767852752 173 TGMAFRVPTADVSVVDLTFTAARDTSIKEIDA 204
Cdd:cd18122    78 DGIAVRVPATLGHLVTVTVKLEKTATLEQIAE 109
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-44 1.84e-15

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: 68.67  E-value: 1.84e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1767852752   1 VAKDDTLVVNGHRILCVkAQRNPADLPWGKLGVEYVIESTGLFT 44
Cdd:pfam00044  57 EAEEDGLVVNGKKIKVF-AERDPAELPWGDLGVDVVIESTGVFT 99
GAPDH-like_N cd05192
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ...
 34-99 6.66e-09

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: 51.59  E-value: 6.66e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1767852752  34 EYVIESTGLFTVKSAAEGHLRGGARKVIISAPASGGAKTFVMGVNHGDYNPrEHHVVSNASCTTNC 99
Cdd:cd05192    35 DVVIECTGSFTDDDNAEKHIKAGGKKAVITAPEKGDIPTIVVVLNELAKSA-GATVVSNANETSYS 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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