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Conserved domains on  [gi|378408586|gb|AFB83703|]
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glyceraldehyde-3-phosphate dehydrogenase, partial [Guignardia sansevieriae]

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
 1-206 2.33e-132

glyceraldehyde-3-phosphate dehydrogenase


The actual alignment was detected with superfamily member PLN02272:

Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 378.05  E-value: 2.33e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586   1 GQFKGEIKV-EGSDLVINGKKVRFYQERDPASIPWAETGAYYIVESTGVFTTTEKASAHLKGGAKKVVISAPSADAPMFV 79
Cdd:PLN02272 136 GNFKGTINVvDDSTLEINGKQIKVTSKRDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFV 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586  80 MGVNNETYKSDINVLSNASCTTNCLAPLAKVIHDKYTIVEGLMTTVHSYTATQKTVDGPSAKDWRGGRTAAANIIPSSTG 159
Cdd:PLN02272 216 VGVNEKTYKPNMNIVSNASCTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTG 295

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 378408586 160 AAKAVGKVIPDLNGKLTGMAFRVPTANVSVVDLTARIEKGASYEEIK 206
Cdd:PLN02272 296 AAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRLEKSASYEDVK 342
 
Name Accession Description Interval E-value
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 1-206 2.33e-132

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 378.05  E-value: 2.33e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586   1 GQFKGEIKV-EGSDLVINGKKVRFYQERDPASIPWAETGAYYIVESTGVFTTTEKASAHLKGGAKKVVISAPSADAPMFV 79
Cdd:PLN02272 136 GNFKGTINVvDDSTLEINGKQIKVTSKRDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFV 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586  80 MGVNNETYKSDINVLSNASCTTNCLAPLAKVIHDKYTIVEGLMTTVHSYTATQKTVDGPSAKDWRGGRTAAANIIPSSTG 159
Cdd:PLN02272 216 VGVNEKTYKPNMNIVSNASCTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTG 295

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 378408586 160 AAKAVGKVIPDLNGKLTGMAFRVPTANVSVVDLTARIEKGASYEEIK 206
Cdd:PLN02272 296 AAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRLEKSASYEDVK 342
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-207 2.83e-129

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: 367.03  E-value: 2.83e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586   1 GQFKGEIKVEGSDLVINGKKVRFYQERDPASIPWAETGAYYIVESTGVFTTTEKASAHLKGGAKKVVISAPSADA-PMFV 79
Cdd:COG0057   53 GRFPGEVEVEGDSLIVNGKKIKVLAERDPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIV 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586  80 MGVNNETYKSDINVLSNASCTTNCLAPLAKVIHDKYTIVEGLMTTVHSYTATQKTVDGPsAKDWRGGRTAAANIIPSSTG 159
Cdd:COG0057  133 YGVNHDDYDADHRIISNASCTTNCLAPVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTG 211

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 378408586 160 AAKAVGKVIPDLNGKLTGMAFRVPTANVSVVDLTARIEKGASYEEIKQ 207
Cdd:COG0057  212 AAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVELEKETTVEEVNA 259
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 1-205 1.59e-106

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: 309.21  E-value: 1.59e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586    1 GQFKGEIKVEGSDLVINGKKVRFY-QERDPASIPWAETGAYYIVESTGVFTTTEKASAHLKGGAKKVVISAPSADA-PMF 78
Cdd:TIGR01534  51 GRFEGEVTVDEDGLVVNGKEVISVfSERDPSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTI 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586   79 VMGVNNETYKSDINVLSNASCTTNCLAPLAKVIHDKYTIVEGLMTTVHSYTATQKTVDGPSaKDWRGGRTAAANIIPSST 158
Cdd:TIGR01534 131 VYGVNHDEYDGEERIISNASCTTNCLAPLAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPH-KDLRRARAAALNIIPTST 209

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 378408586  159 GAAKAVGKVIPDLNGKLTGMAFRVPTANVSVVDLTARIEKGASYEEI 205
Cdd:TIGR01534 210 GAAKAIGKVLPELAGKLTGMAIRVPTPNVSLVDLVVNLEKDVTVEEV 256
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 99-207 6.04e-77

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: 228.11  E-value: 6.04e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586  99 CTTNCLAPLAKVIHDKYTIVEGLMTTVHSYTATQKTVDGPSaKDWRGGRTAAANIIPSSTGAAKAVGKVIPDLNGKLTGM 178
Cdd:cd18126    1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79

                         90       100
                 ....*....|....*....|....*....
gi 378408586 179 AFRVPTANVSVVDLTARIEKGASYEEIKQ 207
Cdd:cd18126   80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNA 108
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
1-207 1.28e-64

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 202.09  E-value: 1.28e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586   1 GQFKGEIKVEGSDLVINGKKVRFYQERDPASIPWAEtGAYYIVESTGVFTTTEKASAHLKGGAKKVVISAP--SADAPMF 78
Cdd:NF033735  49 GRWDAEVTAEEDSIVIDGKRISFSSNKDIEDTPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNI 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586  79 VMGVNNETYKSDI-NVLSNASCTTNCLAPLAKVIHDKYTIVEGLMTTVHSYTATQKTVDGPsAKDWRGGRTAAANIIPSS 157
Cdd:NF033735 128 VYGVNDHLYDPARhRIVTAASCTTNCLAPVVKVIHEKIGIKHGSITTIHDITNTQTIVDAP-HKDLRRARSCGMSLIPTT 206

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 378408586 158 TGAAKAVGKVIPDLNGKLTGMAFRVPTANVSVVDLTARIEKGASYEEIKQ 207
Cdd:NF033735 207 TGSATAITLIFPELKGKLNGHAVRVPLLNASLTDCVFEVERPTTVEEVNA 256
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 104-207 2.64e-58

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: 180.48  E-value: 2.64e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586  104 LAPLAKVIHDKYTIVEGLMTTVHSYTATQKTVDGPSAKDWRGGRTAAANIIPSSTGAAKAVGKVIPDLNGKLTGMAFRVP 183
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90       100
                  ....*....|....*....|....
gi 378408586  184 TANVSVVDLTARIEKGASYEEIKQ 207
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNA 104
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-99 6.12e-46

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: 148.85  E-value: 6.12e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586     1 GQFKGEIKVEGSDLVINGKKVRFYQERDPASIPWAETGAYYIVESTGVFTTTEKASAHLKGGAKKVVISAPSADA-PMFV 79
Cdd:smart00846  50 GRFPGTVEVEGDGLVVNGKAIKVFAERDPANLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFV 129

                           90       100
                   ....*....|....*....|
gi 378408586    80 MGVNNETYKSDINVLSNASC 99
Cdd:smart00846 130 YGVNHDEYDGEDHIISNASC 149
 
Name Accession Description Interval E-value
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 1-206 2.33e-132

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 378.05  E-value: 2.33e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586   1 GQFKGEIKV-EGSDLVINGKKVRFYQERDPASIPWAETGAYYIVESTGVFTTTEKASAHLKGGAKKVVISAPSADAPMFV 79
Cdd:PLN02272 136 GNFKGTINVvDDSTLEINGKQIKVTSKRDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFV 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586  80 MGVNNETYKSDINVLSNASCTTNCLAPLAKVIHDKYTIVEGLMTTVHSYTATQKTVDGPSAKDWRGGRTAAANIIPSSTG 159
Cdd:PLN02272 216 VGVNEKTYKPNMNIVSNASCTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTG 295

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 378408586 160 AAKAVGKVIPDLNGKLTGMAFRVPTANVSVVDLTARIEKGASYEEIK 206
Cdd:PLN02272 296 AAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRLEKSASYEDVK 342
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-207 2.83e-129

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: 367.03  E-value: 2.83e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586   1 GQFKGEIKVEGSDLVINGKKVRFYQERDPASIPWAETGAYYIVESTGVFTTTEKASAHLKGGAKKVVISAPSADA-PMFV 79
Cdd:COG0057   53 GRFPGEVEVEGDSLIVNGKKIKVLAERDPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIV 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586  80 MGVNNETYKSDINVLSNASCTTNCLAPLAKVIHDKYTIVEGLMTTVHSYTATQKTVDGPsAKDWRGGRTAAANIIPSSTG 159
Cdd:COG0057  133 YGVNHDDYDADHRIISNASCTTNCLAPVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTG 211

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 378408586 160 AAKAVGKVIPDLNGKLTGMAFRVPTANVSVVDLTARIEKGASYEEIKQ 207
Cdd:COG0057  212 AAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVELEKETTVEEVNA 259
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 1-205 1.59e-106

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: 309.21  E-value: 1.59e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586    1 GQFKGEIKVEGSDLVINGKKVRFY-QERDPASIPWAETGAYYIVESTGVFTTTEKASAHLKGGAKKVVISAPSADA-PMF 78
Cdd:TIGR01534  51 GRFEGEVTVDEDGLVVNGKEVISVfSERDPSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTI 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586   79 VMGVNNETYKSDINVLSNASCTTNCLAPLAKVIHDKYTIVEGLMTTVHSYTATQKTVDGPSaKDWRGGRTAAANIIPSST 158
Cdd:TIGR01534 131 VYGVNHDEYDGEERIISNASCTTNCLAPLAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPH-KDLRRARAAALNIIPTST 209

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 378408586  159 GAAKAVGKVIPDLNGKLTGMAFRVPTANVSVVDLTARIEKGASYEEI 205
Cdd:TIGR01534 210 GAAKAIGKVLPELAGKLTGMAIRVPTPNVSLVDLVVNLEKDVTVEEV 256
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
 1-205 1.96e-103

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 301.75  E-value: 1.96e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586   1 GQFKGEIKVEGSDLVINGKKVRFYQERDPASIPWAETGAYYIVESTGVFTTTEKASAHLKGGAKKVVISAP-SADAPMFV 79
Cdd:PTZ00023  53 GSLPAEVSVTDGFLMIGSKKVHVFFEKDPAAIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPpKDDTPIYV 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586  80 MGVNNETYKSDINVLSNASCTTNCLAPLAKVIHDKYTIVEGLMTTVHSYTATQKTVDGPS--AKDWRGGRTAAANIIPSS 157
Cdd:PTZ00023 133 MGVNHTQYDKSQRIVSNASCTTNCLAPLAKVVNDKFGIVEGLMTTVHASTANQLTVDGPSkgGKDWRAGRCAGVNIIPAS 212

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 378408586 158 TGAAKAVGKVIPDLNGKLTGMAFRVPTANVSVVDLTARIEKGASYEEI 205
Cdd:PTZ00023 213 TGAAKAVGKVIPELNGKLTGMAFRVPVPDVSVVDLTCKLAKPAKYEEI 260
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
 1-207 2.23e-100

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 293.94  E-value: 2.23e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586   1 GQFK-GEIKVEGSDLVINGKK-VRFYQERDPASIPWAETGAYYIVESTGVFTTTEKASAHLKGGAKKVVISAPSADAPMF 78
Cdd:PLN02358  56 GQWKhHELKVKDDKTLLFGEKpVTVFGIRNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMF 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586  79 VMGVNNETYKSDINVLSNASCTTNCLAPLAKVIHDKYTIVEGLMTTVHSYTATQKTVDGPSAKDWRGGRTAAANIIPSST 158
Cdd:PLN02358 136 VVGVNEHEYKSDLDIVSNASCTTNCLAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSST 215

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 378408586 159 GAAKAVGKVIPDLNGKLTGMAFRVPTANVSVVDLTARIEKGASYEEIKQ 207
Cdd:PLN02358 216 GAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRLEKAATYDEIKK 264
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
1-207 1.01e-92

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 274.30  E-value: 1.01e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586   1 GQFKGEIKVEGSDLVINGKKVRFYQERDPASIPWAETGAYYIVESTGVFTTTEKASAHLKGGAKKVVISAPSAD-APMFV 79
Cdd:PRK15425  52 GRFDGTVEVKDGHLIVNGKKIRVTAERDPANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDnTPMFV 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586  80 MGVNNETYKSDiNVLSNASCTTNCLAPLAKVIHDKYTIVEGLMTTVHSYTATQKTVDGPSAKDWRGGRTAAANIIPSSTG 159
Cdd:PRK15425 132 KGANFDKYAGQ-DIVSNASCTTNCLAPLAKVINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTG 210

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 378408586 160 AAKAVGKVIPDLNGKLTGMAFRVPTANVSVVDLTARIEKGASYEEIKQ 207
Cdd:PRK15425 211 AAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAATYEQIKA 258
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 14-205 5.82e-83

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 250.36  E-value: 5.82e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586  14 LVINGKKVRFYQ-ERDPASIPWAETGAYYIVESTGVFTTTEKASAHLKGGAKKVVISAP-SADAPMFVMGVNNETYK-SD 90
Cdd:PTZ00434  79 LVVNGHRIKCVKaQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPaSGGAKTIVMGVNQHEYSpTE 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586  91 INVLSNASCTTNCLAPLAKVI-HDKYTIVEGLMTTVHSYTATQKTVDGPSAKDWRGGRTAAANIIPSSTGAAKAVGKVIP 169
Cdd:PTZ00434 159 HHVVSNASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIP 238

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 378408586 170 DLNGKLTGMAFRVPTANVSVVDLTARIEKGASYEEI 205
Cdd:PTZ00434 239 STKGKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEI 274
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-207 5.57e-82

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 247.34  E-value: 5.57e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586   1 GQFKGEIKVEGSDLVINGKKVRFYQERDPASIPWAETGAYYIVESTGVFTTTEKASAHLKGGAKKVVISAPSADAPM-FV 79
Cdd:PRK07729  52 GKFDGTVEAFEDHLLVDGKKIRLLNNRDPKELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVtIV 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586  80 MGVNNETYKSDIN-VLSNASCTTNCLAPLAKVIHDKYTIVEGLMTTVHSYTATQKTVDGPSaKDWRGGRTAAANIIPSST 158
Cdd:PRK07729 132 VGVNEDQLDIEKHtIISNASCTTNCLAPVVKVLDEQFGIENGLMTTVHAYTNDQKNIDNPH-KDLRRARACGQSIIPTTT 210

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 378408586 159 GAAKAVGKVIPDLNGKLTGMAFRVPTANVSVVDLTARIEKGASYEEIKQ 207
Cdd:PRK07729 211 GAAKALAKVLPHLNGKLHGMALRVPTPNVSLVDLVVDVKRDVTVEEINE 259
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
1-207 3.42e-79

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 239.81  E-value: 3.42e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586   1 GQFKGEIKVEGSDLVINGKKVRFYQERDPASIPWAETGAYYIVESTGVFTTTEKASAHLKGGAKKVVISAP--SADAPMF 78
Cdd:PRK07403  53 GKLNADISADENSITVNGKTIKCVSDRNPLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPgkGEDIGTY 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586  79 VMGVNNETYKSDI-NVLSNASCTTNCLAPLAKVIHDKYTIVEGLMTTVHSYTATQKTVDGpSAKDWRGGRTAAANIIPSS 157
Cdd:PRK07403 133 VVGVNHHEYDHEDhNIISNASCTTNCLAPIAKVLHDNFGIIKGTMTTTHSYTGDQRILDA-SHRDLRRARAAAVNIVPTS 211

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 378408586 158 TGAAKAVGKVIPDLNGKLTGMAFRVPTANVSVVDLTARIEKGASYEEIKQ 207
Cdd:PRK07403 212 TGAAKAVALVIPELKGKLNGIALRVPTPNVSVVDLVVQVEKRTITEQVNE 261
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 99-207 6.04e-77

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: 228.11  E-value: 6.04e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586  99 CTTNCLAPLAKVIHDKYTIVEGLMTTVHSYTATQKTVDGPSaKDWRGGRTAAANIIPSSTGAAKAVGKVIPDLNGKLTGM 178
Cdd:cd18126    1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79

                         90       100
                 ....*....|....*....|....*....
gi 378408586 179 AFRVPTANVSVVDLTARIEKGASYEEIKQ 207
Cdd:cd18126   80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNA 108
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
 1-207 1.09e-71

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 222.50  E-value: 1.09e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586   1 GQFKGEIKVEGSD-LVINGKKVRFYQERDPASIPWAETGAYYIVESTGVFTTTEKASAHLKGGAKKVVISAPS-ADAPMF 78
Cdd:PLN03096 112 GTFDADVKPVGDDaISVDGKVIKVVSDRNPLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGkGDIPTY 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586  79 VMGVNNETYKSDINVLSNASCTTNCLAPLAKVIHDKYTIVEGLMTTVHSYTATQKTVDGpSAKDWRGGRTAAANIIPSST 158
Cdd:PLN03096 192 VVGVNADDYKHSDPIISNASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTST 270

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 378408586 159 GAAKAVGKVIPDLNGKLTGMAFRVPTANVSVVDLTARIEKGASYEEIKQ 207
Cdd:PLN03096 271 GAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQVEKKTFAEEVNA 319
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
 1-205 1.28e-68

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 216.31  E-value: 1.28e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586   1 GQFKGEIK-VEGSDLVINGKKVRFYQERDPASIPWAETGAYYIVESTGVFTTTEKASAHLKGGAKKVVISAPS--ADAPM 77
Cdd:PLN02237 127 GTFKADVKiVDDETISVDGKPIKVVSNRDPLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAkgADIPT 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586  78 FVMGVNNETYKSDI-NVLSNASCTTNCLAPLAKVIHDKYTIVEGLMTTVHSYTATQKTVDGpSAKDWRGGRTAAANIIPS 156
Cdd:PLN02237 207 YVVGVNEDDYDHEVaNIVSNASCTTNCLAPFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPT 285

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 378408586 157 STGAAKAVGKVIPDLNGKLTGMAFRVPTANVSVVDLTARIEK-GASYEEI 205
Cdd:PLN02237 286 STGAAKAVSLVLPQLKGKLNGIALRVPTPNVSVVDLVVNVEKkGITAEDV 335
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
1-207 1.28e-64

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 202.09  E-value: 1.28e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586   1 GQFKGEIKVEGSDLVINGKKVRFYQERDPASIPWAEtGAYYIVESTGVFTTTEKASAHLKGGAKKVVISAP--SADAPMF 78
Cdd:NF033735  49 GRWDAEVTAEEDSIVIDGKRISFSSNKDIEDTPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNI 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586  79 VMGVNNETYKSDI-NVLSNASCTTNCLAPLAKVIHDKYTIVEGLMTTVHSYTATQKTVDGPsAKDWRGGRTAAANIIPSS 157
Cdd:NF033735 128 VYGVNDHLYDPARhRIVTAASCTTNCLAPVVKVIHEKIGIKHGSITTIHDITNTQTIVDAP-HKDLRRARSCGMSLIPTT 206

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 378408586 158 TGAAKAVGKVIPDLNGKLTGMAFRVPTANVSVVDLTARIEKGASYEEIKQ 207
Cdd:NF033735 207 TGSATAITLIFPELKGKLNGHAVRVPLLNASLTDCVFEVERPTTVEEVNA 256
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 104-207 2.64e-58

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: 180.48  E-value: 2.64e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586  104 LAPLAKVIHDKYTIVEGLMTTVHSYTATQKTVDGPSAKDWRGGRTAAANIIPSSTGAAKAVGKVIPDLNGKLTGMAFRVP 183
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90       100
                  ....*....|....*....|....
gi 378408586  184 TANVSVVDLTARIEKGASYEEIKQ 207
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNA 104
PRK08955 PRK08955
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-207 1.84e-55

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 169599 [Multi-domain]  Cd Length: 334  Bit Score: 179.16  E-value: 1.84e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586   1 GQFKGEIKVEGSDLVINGKKVRFYQERDPASIPWaeTGAYYIVESTGVFTTTEKASAHLKGGAKKVVISAPSADAPMF-- 78
Cdd:PRK08955  53 GRWHHEVTAEGDAIVINGKRIRTTQNKAIADTDW--SGCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLni 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586  79 VMGVNNETYKSDIN-VLSNASCTTNCLAPLAKVIHDKYTIVEGLMTTVHSYTATQKTVDGPSaKDWRGGRTAAANIIPSS 157
Cdd:PRK08955 131 VMGVNDHLFDPAIHpIVTAASCTTNCLAPVVKVIHEKLGIKHGSMTTIHDLTNTQTILDAPH-KDLRRARACGMSLIPTT 209

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 378408586 158 TGAAKAVGKVIPDLNGKLTGMAFRVPTANVSVVDLTARIEKGASYEEIKQ 207
Cdd:PRK08955 210 TGSATAITEIFPELKGKLNGHAVRVPLANASLTDCVFEVERDTTVEEVNA 259
PRK08289 PRK08289
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
 1-205 1.88e-55

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 236219 [Multi-domain]  Cd Length: 477  Bit Score: 182.81  E-value: 1.88e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586   1 GQFKGEIKV--EGSDLVINGKKVRFYQERDPASIPWAETGAY--YIVESTGVFTTTEKASAHLKG-GAKKVVISAPS-AD 74
Cdd:PRK08289 185 GPFNGTITVdeENNAIIANGNYIQVIYANSPEEVDYTAYGINnaLVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGkGD 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586  75 APMFVMGVNNETYKSDINVLSNASCTTNCLAPLAKVIHDKYTIVEGLMTTVHSYTATQKTVDGPSAKDwRGGRTAAANII 154
Cdd:PRK08289 265 IKNIVHGVNHSDITDEDKIVSAASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKGD-RRGRSAPLNMV 343

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 378408586 155 PSSTGAAKAVGKVIPDLNGKLTGMAFRVPTANVSVVDLTARIEKGASYEEI 205
Cdd:PRK08289 344 ITETGAAKAVAKALPELAGKLTGNAIRVPTPNVSMAILNLNLEKETSREEL 394
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 99-206 1.28e-54

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: 171.65  E-value: 1.28e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586  99 CTTNCLAPLAKVIHDKYTIVEGLMTTVHSYTATQKTVDGPSAKDWRGGRTAAANIIPSSTGAAKAVGKVIPDLNGKLTGM 178
Cdd:cd18123    1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80

                         90       100
                 ....*....|....*....|....*...
gi 378408586 179 AFRVPTANVSVVDLTARIEKGASYEEIK 206
Cdd:cd18123   81 AVRVPTTLMSVHDLMVELEKDVTYDDIK 108
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 1-98 2.32e-53

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: 168.34  E-value: 2.32e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586   1 GQFKGEIKVEGSDLVINGKKVRFYQERDPASIPWAETGAYYIVESTGVFTTTEKASAHLKGGAKKVVISAPSAD-APMFV 79
Cdd:cd05214   50 GRFDGEVEVDDDALIVNGKKIKVFAERDPAELPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDdDPTIV 129

                         90
                 ....*....|....*....
gi 378408586  80 MGVNNETYKSDINVLSNAS 98
Cdd:cd05214  130 MGVNHDKYDADDKIISNAS 148
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
 1-207 3.53e-48

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 160.22  E-value: 3.53e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586   1 GQFKGEIKVEGSDLVINGKKVRFYQERDPASIPWAETGAYYIVESTGVFTTTEKASAHLKGGAKKVVISAPSA---DAPM 77
Cdd:PRK13535  54 GRFAWDVRQERDQLFVGDDAIRLLHERDIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSndlDATV 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586  78 fVMGVNNETYKSDINVLSNASCTTNCLAPLAKVIHDKYTIVEGLMTTVHSYTATQKTVDGpSAKDWRGGRTAAANIIPSS 157
Cdd:PRK13535 134 -VYGVNHDQLRAEHRIVSNASCTTNCIIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVD 211

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 378408586 158 TGAAKAVGKVIPDLNGKLTGMAFRVPTANVSVVDLTARIEKGASYEEIKQ 207
Cdd:PRK13535 212 TKLAAGITRIFPQFNDRFEAISVRVPTINVTAIDLSVTVKKPVKVNEVNQ 261
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-99 6.12e-46

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: 148.85  E-value: 6.12e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586     1 GQFKGEIKVEGSDLVINGKKVRFYQERDPASIPWAETGAYYIVESTGVFTTTEKASAHLKGGAKKVVISAPSADA-PMFV 79
Cdd:smart00846  50 GRFPGTVEVEGDGLVVNGKAIKVFAERDPANLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFV 129

                           90       100
                   ....*....|....*....|
gi 378408586    80 MGVNNETYKSDINVLSNASC 99
Cdd:smart00846 130 YGVNHDEYDGEDHIISNASC 149
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
 4-207 7.02e-36

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 128.45  E-value: 7.02e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586   4 KGEIKVEGSDLVING-KKVRFYQERDPASIPWAETGAYYIVESTGVFTTTEKASAHLKGGAKKVVISAPSADAPMFVMGV 82
Cdd:PTZ00353  57 GASIRVVGEQIVLNGtQKIRVSAKHDLVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSADAPTVMAGS 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586  83 NNETYKSDINVLSNASCTTNCLAPLAKVIHDKYTIVEGLMTTVHSyTATQKTVDGPSA--KDWRGGRTAAANIIPSSTGA 160
Cdd:PTZ00353 137 NDERLSASLPVCCAGAPIAVALAPVIRALHEVYGVEECSYTAIHG-MQPQEPIAARSKnsQDWRQTRVAIDAIAPYRDNG 215

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 378408586 161 AKAVGKVIPDLNGKLTGMAFRVPTANVSVVDLTARIEKGASYEEIKQ 207
Cdd:PTZ00353 216 AETVCKLLPHLVGRISGSAFQVPVKKGCAIDMLVRTKQPVSKEVVDS 262
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 99-207 1.33e-29

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: 107.61  E-value: 1.33e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586  99 CTTNCLAPLAKVIHDKYTIVEGLMTTVHSYTATQKTVDGPSAKDWrgGRTAAANIIPSSTGAAKAVGKVIPDLN--GKLT 176
Cdd:cd18122    1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIGkpIKVD 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 378408586 177 GMAFRVPTANVSVVDLTARIEKGASYEEIKQ 207
Cdd:cd18122   79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAE 109
GAPDH_N_E4PDH cd17892
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 1-98 2.67e-27

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: 101.57  E-value: 2.67e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586   1 GQFKGEIKVEGSDLVINGKKVRFYQERDPASIPWAETGAYYIVESTGVFTTTEKASAHLKGGAKKVVISAPSA---DAPM 77
Cdd:cd17892   53 GRFPGEVRVENDQLFVNGDKIRVLHEPDPENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASndvDATI 132

                         90       100
                 ....*....|....*....|.
gi 378408586  78 fVMGVNNETYKSDINVLSNAS 98
Cdd:cd17892  133 -VYGINQDLLRAEHRIVSNAS 152
GAPDH_C_E4PDH cd23937
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 99-207 6.07e-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: 92.86  E-value: 6.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378408586  99 CTTNCLAPLAKVIHDKYTIVEGLMTTVHSYTATQKTVDGpSAKDWRGGRTAAANIIPSSTGAAKAVGKVIPDLNGKLTGM 178
Cdd:cd23937    1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAI 79

                         90       100
                 ....*....|....*....|....*....
gi 378408586 179 AFRVPTANVSVVDLTARIEKGASYEEIKQ 207
Cdd:cd23937   80 AVRVPTINVTAMDLSVTLKKDVTAEEVNR 108
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-51 2.03e-18

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: 76.76  E-value: 2.03e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 378408586    1 GQFKGEIKVEGSDLVINGKKVRFYQERDPASIPWAETGAYYIVESTGVFTT 51
Cdd:pfam00044  50 GRFPGEVEAEEDGLVVNGKKIKVFAERDPAELPWGDLGVDVVIESTGVFTT 100
GAPDH-like_N cd05192
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ...
 41-103 2.94e-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: 47.35  E-value: 2.94e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 378408586  41 YIVESTGVFTTTEKASAHLKGGAKKVVISAPS-ADAPMFVMGVNNETYKSDINVLSNASCTTNC 103
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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