NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|766431915|gb|AJR57036|]
View 

Tdh1p, partial [Saccharomyces cerevisiae YJM981]

Protein Classification

GapA superfamily protein( domain architecture ID 1903262)

GapA superfamily protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GapA super family cl43010
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 2-176 3.01e-105

Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]; Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase is part of the Pathway/BioSystem: Glycolysis


The actual alignment was detected with superfamily member COG0057:

Pssm-ID: 439827 [Multi-domain]  Cd Length: 334  Bit Score: 304.63  E-value: 3.01e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915   2 IRIAINGFGRIGRLVLRLALQR-KDIEVVAVNDPfISNDYAAYMVKYDSTHGRYKGTVSHDDKHIIIDGVKIATYQERDP 80
Cdd:COG0057    3 IRVAINGFGRIGRLVLRALLERgPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915  81 ANLPWGSLKIDVAVDSTGVFKELDTAQKHIDAGAKKVVITAPSSSA-PMFVVGVNHTKYTPDKKIVSNASCTTNCLAPLA 159
Cdd:COG0057   82 AELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAPVA 161

                        170
                 ....*....|....*..
gi 766431915 160 KVINDAFGIEEGLMTTV 176
Cdd:COG0057  162 KVLNDAFGIEKGLMTTI 178
 
Name Accession Description Interval E-value
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 2-176 3.01e-105

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: 304.63  E-value: 3.01e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915   2 IRIAINGFGRIGRLVLRLALQR-KDIEVVAVNDPfISNDYAAYMVKYDSTHGRYKGTVSHDDKHIIIDGVKIATYQERDP 80
Cdd:COG0057    3 IRVAINGFGRIGRLVLRALLERgPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915  81 ANLPWGSLKIDVAVDSTGVFKELDTAQKHIDAGAKKVVITAPSSSA-PMFVVGVNHTKYTPDKKIVSNASCTTNCLAPLA 159
Cdd:COG0057   82 AELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAPVA 161

                        170
                 ....*....|....*..
gi 766431915 160 KVINDAFGIEEGLMTTV 176
Cdd:COG0057  162 KVLNDAFGIEKGLMTTI 178
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 2-176 1.14e-90

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 270.58  E-value: 1.14e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915   2 IRIAINGFGRIGRLVLRLALQRKDIEVVAVNDPFISNDYAAYMVKYDSTHGRYKGTVSH-DDKHIIIDGVKIATYQERDP 80
Cdd:PLN02272  86 TKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDP 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915  81 ANLPWGSLKIDVAVDSTGVFKELDTAQKHIDAGAKKVVITAPSSSAPMFVVGVNHTKYTPDKKIVSNASCTTNCLAPLAK 160
Cdd:PLN02272 166 AEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLAK 245

                        170
                 ....*....|....*.
gi 766431915 161 VINDAFGIEEGLMTTV 176
Cdd:PLN02272 246 VVHEEFGILEGLMTTV 261
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 2-149 1.68e-87

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: 253.47  E-value: 1.68e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915   2 IRIAINGFGRIGRLVLRLALQRKDIEVVAVNDPFIsNDYAAYMVKYDSTHGRYKGTVSHDDKHIIIDGVKIATYQERDPA 81
Cdd:cd05214    1 IKVGINGFGRIGRLVFRAALERDDIEVVAINDLTD-DETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPA 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 766431915  82 NLPWGSLKIDVAVDSTGVFKELDTAQKHIDAGAKKVVITAPSS-SAPMFVVGVNHTKYTPDKKIVSNAS 149
Cdd:cd05214   80 ELPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKdDDPTIVMGVNHDKYDADDKIISNAS 148
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 3-176 5.72e-81

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: 242.57  E-value: 5.72e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915    3 RIAINGFGRIGRLVLRLALQRKD--IEVVAVNDPfISNDYAAYMVKYDSTHGRYKGTVSHDDKHIIIDGVKIATY-QERD 79
Cdd:TIGR01534   1 KVGINGFGRIGRLVLRRILEKPGndLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEVISVfSERD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915   80 PANLPWGSLKIDVAVDSTGVFKELDTAQKHIDAGAKKVVITAPSSSA-PMFVVGVNHTKYTPDKKIVSNASCTTNCLAPL 158
Cdd:TIGR01534  80 PSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLAPL 159

                         170
                  ....*....|....*...
gi 766431915  159 AKVINDAFGIEEGLMTTV 176
Cdd:TIGR01534 160 AKVLDEAFGIVSGLMTTV 177
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 2-150 1.58e-79

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: 232.83  E-value: 1.58e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915     2 IRIAINGFGRIGRLVLRLALQRKDIEVVAVNDPfISNDYAAYMVKYDSTHGRYKGTVSHDDKHIIIDGVKIATYQERDPA 81
Cdd:smart00846   1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPA 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915    82 NLPWGSLKIDVAVDSTGVFKELDTAQKHIDAGAKKVVITAPSSSA-PMFVVGVNHTKYTPDKKIVSNASC 150
Cdd:smart00846  80 NLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
4-176 1.43e-61

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 193.23  E-value: 1.43e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915   4 IAINGFGRIGRLVLRLALQRKDIEVVAVNDPFISNDYAAYMVKYDSTHGRYKGTVSHDDKHIIIDGVKIATYQERDPANL 83
Cdd:NF033735   1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915  84 PWGSlKIDVAVDSTGVFKELDTAQKHIDAGAKKVVITAP--SSSAPMFVVGVNHTKYTPDK-KIVSNASCTTNCLAPLAK 160
Cdd:NF033735  81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARhRIVTAASCTTNCLAPVVK 159

                        170
                 ....*....|....*.
gi 766431915 161 VINDAFGIEEGLMTTV 176
Cdd:NF033735 160 VIHEKIGIKHGSITTI 175
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 2-101 1.08e-54

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: 168.05  E-value: 1.08e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915    2 IRIAINGFGRIGRLVLRLALQRKDIEVVAVNDpFISNDYAAYMVKYDSTHGRYKGTVSHDDKHIIIDGVKIATYQERDPA 81
Cdd:pfam00044   1 VKVGINGFGRIGRLVLRAALERPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPA 79

                          90       100
                  ....*....|....*....|
gi 766431915   82 NLPWGSLKIDVAVDSTGVFK 101
Cdd:pfam00044  80 ELPWGDLGVDVVIESTGVFT 99
 
Name Accession Description Interval E-value
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 2-176 3.01e-105

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: 304.63  E-value: 3.01e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915   2 IRIAINGFGRIGRLVLRLALQR-KDIEVVAVNDPfISNDYAAYMVKYDSTHGRYKGTVSHDDKHIIIDGVKIATYQERDP 80
Cdd:COG0057    3 IRVAINGFGRIGRLVLRALLERgPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915  81 ANLPWGSLKIDVAVDSTGVFKELDTAQKHIDAGAKKVVITAPSSSA-PMFVVGVNHTKYTPDKKIVSNASCTTNCLAPLA 159
Cdd:COG0057   82 AELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAPVA 161

                        170
                 ....*....|....*..
gi 766431915 160 KVINDAFGIEEGLMTTV 176
Cdd:COG0057  162 KVLNDAFGIEKGLMTTI 178
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 2-176 1.14e-90

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 270.58  E-value: 1.14e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915   2 IRIAINGFGRIGRLVLRLALQRKDIEVVAVNDPFISNDYAAYMVKYDSTHGRYKGTVSH-DDKHIIIDGVKIATYQERDP 80
Cdd:PLN02272  86 TKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDP 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915  81 ANLPWGSLKIDVAVDSTGVFKELDTAQKHIDAGAKKVVITAPSSSAPMFVVGVNHTKYTPDKKIVSNASCTTNCLAPLAK 160
Cdd:PLN02272 166 AEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLAK 245

                        170
                 ....*....|....*.
gi 766431915 161 VINDAFGIEEGLMTTV 176
Cdd:PLN02272 246 VVHEEFGILEGLMTTV 261
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 2-149 1.68e-87

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: 253.47  E-value: 1.68e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915   2 IRIAINGFGRIGRLVLRLALQRKDIEVVAVNDPFIsNDYAAYMVKYDSTHGRYKGTVSHDDKHIIIDGVKIATYQERDPA 81
Cdd:cd05214    1 IKVGINGFGRIGRLVFRAALERDDIEVVAINDLTD-DETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPA 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 766431915  82 NLPWGSLKIDVAVDSTGVFKELDTAQKHIDAGAKKVVITAPSS-SAPMFVVGVNHTKYTPDKKIVSNAS 149
Cdd:cd05214   80 ELPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKdDDPTIVMGVNHDKYDADDKIISNAS 148
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 3-176 5.72e-81

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: 242.57  E-value: 5.72e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915    3 RIAINGFGRIGRLVLRLALQRKD--IEVVAVNDPfISNDYAAYMVKYDSTHGRYKGTVSHDDKHIIIDGVKIATY-QERD 79
Cdd:TIGR01534   1 KVGINGFGRIGRLVLRRILEKPGndLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEVISVfSERD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915   80 PANLPWGSLKIDVAVDSTGVFKELDTAQKHIDAGAKKVVITAPSSSA-PMFVVGVNHTKYTPDKKIVSNASCTTNCLAPL 158
Cdd:TIGR01534  80 PSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLAPL 159

                         170
                  ....*....|....*...
gi 766431915  159 AKVINDAFGIEEGLMTTV 176
Cdd:TIGR01534 160 AKVLDEAFGIVSGLMTTV 177
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 2-150 1.58e-79

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: 232.83  E-value: 1.58e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915     2 IRIAINGFGRIGRLVLRLALQRKDIEVVAVNDPfISNDYAAYMVKYDSTHGRYKGTVSHDDKHIIIDGVKIATYQERDPA 81
Cdd:smart00846   1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPA 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915    82 NLPWGSLKIDVAVDSTGVFKELDTAQKHIDAGAKKVVITAPSSSA-PMFVVGVNHTKYTPDKKIVSNASC 150
Cdd:smart00846  80 NLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
 2-176 2.66e-79

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 238.97  E-value: 2.66e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915   2 IRIAINGFGRIGRLVLRLALQRKDIEVVAVNDPFISNDYAAYMVKYDSTHGRYKGTVSHDDKHIIIDGVKIATYQERDPA 81
Cdd:PTZ00023   3 VKLGINGFGRIGRLVFRAALEREDVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKDPA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915  82 NLPWGSLKIDVAVDSTGVFKELDTAQKHIDAGAKKVVITAPSS-SAPMFVVGVNHTKYTPDKKIVSNASCTTNCLAPLAK 160
Cdd:PTZ00023  83 AIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKdDTPIYVMGVNHTQYDKSQRIVSNASCTTNCLAPLAK 162

                        170
                 ....*....|....*.
gi 766431915 161 VINDAFGIEEGLMTTV 176
Cdd:PTZ00023 163 VVNDKFGIVEGLMTTV 178
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-176 1.64e-70

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 216.53  E-value: 1.64e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915   1 MIRIAINGFGRIGRLVLRLALQRKDIEVVAVNDPFISnDYAAYMVKYDSTHGRYKGTVSHDDKHIIIDGVKIATYQERDP 80
Cdd:PRK07729   2 KTKVAINGFGRIGRMVFRKAIKESAFEIVAINASYPS-ETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915  81 ANLPWGSLKIDVAVDSTGVFKELDTAQKHIDAGAKKVVITAPSSSAPM-FVVGVNHTKYTPDKK-IVSNASCTTNCLAPL 158
Cdd:PRK07729  81 KELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVtIVVGVNEDQLDIEKHtIISNASCTTNCLAPV 160

                        170
                 ....*....|....*...
gi 766431915 159 AKVINDAFGIEEGLMTTV 176
Cdd:PRK07729 161 VKVLDEQFGIENGLMTTV 178
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
 2-176 1.01e-67

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 209.58  E-value: 1.01e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915   2 IRIAINGFGRIGRLVLRLALQRKDIEVVAVNDPFISNDYAAYMVKYDSTHGRYKGT--VSHDDKHIIIDGVKIATYQERD 79
Cdd:PLN02358   6 IRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKHHelKVKDDKTLLFGEKPVTVFGIRN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915  80 PANLPWGSLKIDVAVDSTGVFKELDTAQKHIDAGAKKVVITAPSSSAPMFVVGVNHTKYTPDKKIVSNASCTTNCLAPLA 159
Cdd:PLN02358  86 PEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCTTNCLAPLA 165

                        170
                 ....*....|....*..
gi 766431915 160 KVINDAFGIEEGLMTTV 176
Cdd:PLN02358 166 KVINDRFGIVEGLMTTV 182
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
2-176 1.36e-67

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 208.82  E-value: 1.36e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915   2 IRIAINGFGRIGRLVLRLALQRKDIEVVAVNDpFISNDYAAYMVKYDSTHGRYKGTVSHDDKHIIIDGVKIATYQERDPA 81
Cdd:PRK15425   3 IKVGINGFGRIGRIVFRAAQKRSDIEIVAIND-LLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915  82 NLPWGSLKIDVAVDSTGVFKELDTAQKHIDAGAKKVVITAPSS-SAPMFVVGVNHTKYTpDKKIVSNASCTTNCLAPLAK 160
Cdd:PRK15425  82 NLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKdNTPMFVKGANFDKYA-GQDIVSNASCTTNCLAPLAK 160

                        170
                 ....*....|....*.
gi 766431915 161 VINDAFGIEEGLMTTV 176
Cdd:PRK15425 161 VINDNFGIIEGLMTTV 176
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
4-176 1.43e-61

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 193.23  E-value: 1.43e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915   4 IAINGFGRIGRLVLRLALQRKDIEVVAVNDPFISNDYAAYMVKYDSTHGRYKGTVSHDDKHIIIDGVKIATYQERDPANL 83
Cdd:NF033735   1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915  84 PWGSlKIDVAVDSTGVFKELDTAQKHIDAGAKKVVITAP--SSSAPMFVVGVNHTKYTPDK-KIVSNASCTTNCLAPLAK 160
Cdd:NF033735  81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARhRIVTAASCTTNCLAPVVK 159

                        170
                 ....*....|....*.
gi 766431915 161 VINDAFGIEEGLMTTV 176
Cdd:NF033735 160 VIHEKIGIKHGSITTI 175
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
 1-176 3.31e-61

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 192.58  E-value: 3.31e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915   1 MIRIAINGFGRIGRLVLRlAL----QRKDIEVVAVNDpFISNDYAAYMVKYDSTHGRYKGTVSHDDKHIIIDGVKIATYQ 76
Cdd:PRK13535   1 TIRVAINGFGRIGRNVLR-ALyesgRRAEITVVAINE-LADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915  77 ERDPANLPWGSLKIDVAVDSTGVFKELDTAQKHIDAGAKKVVITAPSSS--APMFVVGVNHTKYTPDKKIVSNASCTTNC 154
Cdd:PRK13535  79 ERDIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSNdlDATVVYGVNHDQLRAEHRIVSNASCTTNC 158

                        170       180
                 ....*....|....*....|..
gi 766431915 155 LAPLAKVINDAFGIEEGLMTTV 176
Cdd:PRK13535 159 IIPVIKLLDDAFGIESGTVTTI 180
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
1-175 3.13e-60

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 190.12  E-value: 3.13e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915   1 MIRIAINGFGRIGRLVLRLALQRKD--IEVVAVNDpfiSND--YAAYMVKYDSTHGRYKGTVSHDDKHIIIDGVKIATYQ 76
Cdd:PRK07403   1 MIRVAINGFGRIGRNFLRCWLGRENsqLELVAIND---TSDprTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915  77 ERDPANLPWGSLKIDVAVDSTGVFKELDTAQKHIDAGAKKVVITAPSSSAPM--FVVGVNHTKYTPDK-KIVSNASCTTN 153
Cdd:PRK07403  78 DRNPLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPGKGEDIgtYVVGVNHHEYDHEDhNIISNASCTTN 157

                        170       180
                 ....*....|....*....|..
gi 766431915 154 CLAPLAKVINDAFGIEEGLMTT 175
Cdd:PRK07403 158 CLAPIAKVLHDNFGIIKGTMTT 179
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
 2-175 2.48e-57

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 184.36  E-value: 2.48e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915   2 IRIAINGFGRIGRLVLRLALQRKD--IEVVAVNDPFiSNDYAAYMVKYDSTHGRYKGTVS-HDDKHIIIDGVKIATYQER 78
Cdd:PLN03096  61 IKVAINGFGRIGRNFLRCWHGRKDspLDVVAINDTG-GVKQASHLLKYDSTLGTFDADVKpVGDDAISVDGKVIKVVSDR 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915  79 DPANLPWGSLKIDVAVDSTGVFKELDTAQKHIDAGAKKVVITAPSSSA-PMFVVGVNHTKYTPDKKIVSNASCTTNCLAP 157
Cdd:PLN03096 140 NPLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKGDiPTYVVGVNADDYKHSDPIISNASCTTNCLAP 219

                        170
                 ....*....|....*...
gi 766431915 158 LAKVINDAFGIEEGLMTT 175
Cdd:PLN03096 220 FVKVLDQKFGIIKGTMTT 237
E4PD_g-proteo TIGR01532
erythrose-4-phosphate dehydrogenase; This model represents the small clade of dehydrogenases ...
 3-176 1.18e-55

erythrose-4-phosphate dehydrogenase; This model represents the small clade of dehydrogenases in gamma-proteobacteria 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. This enzyme activity appears to have evolved from glyceraldehyde-3-phosphate dehydrogenase, whose substrate differs only in the lack of one carbon relative to E4P. Accordingly, this model is very close to the corresponding models for GAPDH, and those sequences which hit above trusted here invariably hit between trusted and noise to the GAPDH model (TIGR01534). Similarly, it may be found that there are species outside of the gamma proteobacteria which synthesize pyridoxine and have more than one aparrent GAPDH gene of which one may have E4PD activity - this may necessitate a readjustment of these models. Alternatively, some of the GAPDH enzymes may prove to be bifunctional in certain species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]


Pssm-ID: 130595  Cd Length: 325  Bit Score: 178.16  E-value: 1.18e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915    3 RIAINGFGRIGRLVLRlAL----QRKDIEVVAVNDpFISNDYAAYMVKYDSTHGRYKGTVSHDDKHIIIDGVKIATYQER 78
Cdd:TIGR01532   1 RVAINGFGRIGRNVLR-ALyesgRRAEITVVAINE-LADAAGMAHLLKYDTSHGRFAWEVRQDRDQLFVGDDAIRVLHER 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915   79 DPANLPWGSLKIDVAVDSTGVFKELDTAQKHIDAGAKKVVITAPSSS--APMFVVGVNHTKYTPDKKIVSNASCTTNCLA 156
Cdd:TIGR01532  79 SLQSLPWRELGVDLVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGASdlDATIVYGVNQDQLRAEHRIVSNASCTTNCIV 158

                         170       180
                  ....*....|....*....|
gi 766431915  157 PLAKVINDAFGIEEGLMTTV 176
Cdd:TIGR01532 159 PVIKLLDDAYGIESGTITTI 178
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 2-176 7.80e-55

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 177.17  E-value: 7.80e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915   2 IRIAINGFGRIGRLVLRL----ALQRKDIEVVAVNDPFISNDYAAYMVKYDSTHGRYKGTVS--------HDDKHIIIDG 69
Cdd:PTZ00434   4 IKVGINGFGRIGRMVFQAicdqGLIGTEIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVEttksspsvKTDDVLVVNG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915  70 VKIATYQ-ERDPANLPWGSLKIDVAVDSTGVFKELDTAQKHIDAGAKKVVITAPSS-SAPMFVVGVNHTKYTP-DKKIVS 146
Cdd:PTZ00434  84 HRIKCVKaQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPASgGAKTIVMGVNQHEYSPtEHHVVS 163

                        170       180       190
                 ....*....|....*....|....*....|.
gi 766431915 147 NASCTTNCLAPLAKVI-NDAFGIEEGLMTTV 176
Cdd:PTZ00434 164 NASCTTNCLAPIVHVLtKEGFGIETGLMTTI 194
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 2-101 1.08e-54

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: 168.05  E-value: 1.08e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915    2 IRIAINGFGRIGRLVLRLALQRKDIEVVAVNDpFISNDYAAYMVKYDSTHGRYKGTVSHDDKHIIIDGVKIATYQERDPA 81
Cdd:pfam00044   1 VKVGINGFGRIGRLVLRAALERPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPA 79

                          90       100
                  ....*....|....*....|
gi 766431915   82 NLPWGSLKIDVAVDSTGVFK 101
Cdd:pfam00044  80 ELPWGDLGVDVVIESTGVFT 99
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
 2-175 6.96e-54

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 176.63  E-value: 6.96e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915   2 IRIAINGFGRIGRLVLRLALQRKD--IEVVAVNDPFISNDyAAYMVKYDSTHGRYKGTVS-HDDKHIIIDGVKIATYQER 78
Cdd:PLN02237  76 LKVAINGFGRIGRNFLRCWHGRKDspLDVVVVNDSGGVKN-ASHLLKYDSMLGTFKADVKiVDDETISVDGKPIKVVSNR 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915  79 DPANLPWGSLKIDVAVDSTGVFKELDTAQKHIDAGAKKVVITAPSSSA--PMFVVGVNHTKYTPD-KKIVSNASCTTNCL 155
Cdd:PLN02237 155 DPLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAKGAdiPTYVVGVNEDDYDHEvANIVSNASCTTNCL 234

                        170       180
                 ....*....|....*....|
gi 766431915 156 APLAKVINDAFGIEEGLMTT 175
Cdd:PLN02237 235 APFVKVLDEEFGIVKGTMTT 254
GAPDH_N_E4PDH cd17892
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 2-149 1.12e-52

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: 165.52  E-value: 1.12e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915   2 IRIAINGFGRIGRLVLRlAL----QRKDIEVVAVNDPfISNDYAAYMVKYDSTHGRYKGTVSHDDKHIIIDGVKIATYQE 77
Cdd:cd17892    1 YRVAINGYGRIGRNVLR-ALyesgRRAEFQVVAINEL-ADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHE 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 766431915  78 RDPANLPWGSLKIDVAVDSTGVFKELDTAQKHIDAGAKKVVITAPSSSA--PMFVVGVNHTKYTPDKKIVSNAS 149
Cdd:cd17892   79 PDPENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASNDvdATIVYGINQDLLRAEHRIVSNAS 152
PRK08955 PRK08955
glyceraldehyde-3-phosphate dehydrogenase; Validated
 2-176 1.01e-51

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 169599 [Multi-domain]  Cd Length: 334  Bit Score: 168.37  E-value: 1.01e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915   2 IRIAINGFGRIGRLVLRLALQRKDIEVVAVNDPFISNDYAAYMVKYDSTHGRYKGTVSHDDKHIIIDGVKIATYQERDPA 81
Cdd:PRK08955   3 IKVGINGFGRIGRLALRAAWDWPELEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKAIA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915  82 NLPWGslKIDVAVDSTGVFKELDTAQKHIDAGAKKVVITAP--SSSAPMFVVGVNHTKYTPDK-KIVSNASCTTNCLAPL 158
Cdd:PRK08955  83 DTDWS--GCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPvkEEGVLNIVMGVNDHLFDPAIhPIVTAASCTTNCLAPV 160

                        170
                 ....*....|....*...
gi 766431915 159 AKVINDAFGIEEGLMTTV 176
Cdd:PRK08955 161 VKVIHEKLGIKHGSMTTI 178
PRK08289 PRK08289
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
 8-176 1.13e-33

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 236219 [Multi-domain]  Cd Length: 477  Bit Score: 123.88  E-value: 1.13e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915   8 GFGRIGRLVLRLALQR---------KDIEVVAVNDpfisNDYA--AYMVKYDSTHGRYKGTVSHDDKH--IIIDGVKIAT 74
Cdd:PRK08289 134 GFGRIGRLLARLLIEKtgggnglrlRAIVVRKGSE----GDLEkrASLLRRDSVHGPFNGTITVDEENnaIIANGNYIQV 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915  75 YQERDPANLPWGSLKIDVA--VDSTGVFKELDTAQKHIDA-GAKKVVITAPSSSA-PMFVVGVNHTKYTPDKKIVSNASC 150
Cdd:PRK08289 210 IYANSPEEVDYTAYGINNAlvVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGKGDiKNIVHGVNHSDITDEDKIVSAASC 289

                        170       180
                 ....*....|....*....|....*.
gi 766431915 151 TTNCLAPLAKVINDAFGIEEGLMTTV 176
Cdd:PRK08289 290 TTNAITPVLKAVNDKYGIVNGHVETV 315
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
 2-170 1.84e-20

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 86.47  E-value: 1.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915   2 IRIAINGFGRIGRLVLRLALQRKDIEVVAVNDPFISNDYAAYMVKYDSTHGRYKGT-VSHDDKHIIIDGV-KIATYQERD 79
Cdd:PTZ00353   3 ITVGINGFGPVGKAVLFASLTDPLVTVVAVNDASVSIAYIAYVLEQESPLSAPDGAsIRVVGEQIVLNGTqKIRVSAKHD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915  80 PANLPWGSLKIDVAVDSTGVFKELDTAQKHIDAGAKKVVITAPSSSAPMFVVGVNHTKYTPDKKIVSNASCTTNCLAPLA 159
Cdd:PTZ00353  83 LVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDERLSASLPVCCAGAPIAVALAPVI 162

                        170
                 ....*....|.
gi 766431915 160 KVINDAFGIEE 170
Cdd:PTZ00353 163 RALHEVYGVEE 173
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 150-176 6.52e-16

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: 70.95  E-value: 6.52e-16
                         10        20
                 ....*....|....*....|....*..
gi 766431915 150 CTTNCLAPLAKVINDAFGIEEGLMTTV 176
Cdd:cd18126    1 CTTNCLAPVAKVLNDNFGIEEGLMTTV 27
GAPDH-like_N cd05192
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ...
 2-154 7.96e-15

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: 66.61  E-value: 7.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915   2 IRIAINGFGRIGRLVLRLALQRKDIEVVAVNDpfisndyaaymvkydsthgrykgtvshddkhiiidgvkiatyqerdpa 81
Cdd:cd05192    1 IRVAINGFGRIGRIVFRAIADQDDLDVVAIND------------------------------------------------ 32

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 766431915  82 nlpwgslKIDVAVDSTGVFKELDTAQKHIDAGAKKVVITAPSSSA-PMFVVGVNHTKYTPDKKIVSNASCTTNC 154
Cdd:cd05192   33 -------RRDVVIECTGSFTDDDNAEKHIKAGGKKAVITAPEKGDiPTIVVVLNELAKSAGATVVSNANETSYS 99
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 150-176 1.46e-09

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


Pssm-ID: 467673  Cd Length: 164  Bit Score: 54.16  E-value: 1.46e-09
                         10        20
                 ....*....|....*....|....*..
gi 766431915 150 CTTNCLAPLAKVINDAFGIEEGLMTTV 176
Cdd:cd18123    1 CTTNCLAPLAKAIHDSFGIKKGRMTTV 27
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 155-176 2.60e-07

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: 47.97  E-value: 2.60e-07
                          10        20
                  ....*....|....*....|..
gi 766431915  155 LAPLAKVINDAFGIEEGLMTTV 176
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTV 22
GAPDH_C_E4PDH cd23937
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 150-176 1.78e-06

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: 45.48  E-value: 1.78e-06
                         10        20
                 ....*....|....*....|....*..
gi 766431915 150 CTTNCLAPLAKVINDAFGIEEGLMTTV 176
Cdd:cd23937    1 CTTNCIVPVIKVLDEAFGIESGTITTI 27
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 150-176 2.72e-05

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: 42.51  E-value: 2.72e-05
                         10        20
                 ....*....|....*....|....*..
gi 766431915 150 CTTNCLAPLAKVINDAFGIEEGLMTTV 176
Cdd:cd18122    1 CTTTGLIPAAKALNDKFGIEEILVVTV 27
nat-AmDH_N_like cd24146
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ...
 2-128 1.14e-04

N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, 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). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.


Pssm-ID: 467616 [Multi-domain]  Cd Length: 157  Bit Score: 40.60  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915   2 IRIAINGFGRIGRLVLRLALQRKDIEVVAVNDpfISNDYAaymvkydsthGRYKGTVSHDDKhiiiDGVKIATyqerDPA 81
Cdd:cd24146    1 IRVVVWGLGAMGRGIARYLLEKPGLEIVGAVD--RDPAKV----------GKDLGELGGGAP----LGVKVTD----DLD 60

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 766431915  82 NLpWGSLKIDVAVDSTG--VFKELDTAQKHIDAGaKKVVITAPSSSAPM 128
Cdd:cd24146   61 AV-LAATKPDVVVHATTsfLADVAPQIERLLEAG-LNVITTCEELFYPW 107
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 3-44 1.17e-04

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240644 [Multi-domain]  Cd Length: 330  Bit Score: 41.39  E-value: 1.17e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 766431915   3 RIAINGFGRIGRLVLRLaLQRKDIEVVaVNDPFISNDYAAYM 44
Cdd:cd12167  152 TVGIVGFGRIGRAVVEL-LRPFGLRVL-VYDPYLPAAEAAAL 191
DapB_N pfam01113
Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the ...
 2-31 3.38e-04

Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the alpha,beta-unsaturated cyclic imine, dihydro-dipicolinate. This reaction is the second committed step in the biosynthesis of L-lysine and its precursor meso-diaminopimelate, which are critical for both protein and cell wall biosynthesis. The N-terminal domain of DapB binds the dinucleotide NADPH.


Pssm-ID: 460069 [Multi-domain]  Cd Length: 121  Bit Score: 38.75  E-value: 3.38e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 766431915    2 IRIAINGF-GRIGRLVLRLALQRKDIEVVAV 31
Cdd:pfam01113   1 IKIAVAGAsGRMGRELIKAVLEAPDLELVAA 31
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-34 4.28e-04

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 39.52  E-value: 4.28e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 766431915   1 MIRIAINGFGRIGRLVLRLALQRKDIEVVAVNDP 34
Cdd:COG0673    3 KLRVGIIGAGGIGRAHAPALAALPGVELVAVADR 36
DHDPR_N cd02274
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; ...
 2-33 4.69e-04

N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; DHDPR (EC 1.17.1.8), also called 4-hydroxy-tetrahydrodipicolinate reductase, or HTPA reductase, is a product of an essential gene referred to as dapB. It catalyzes the NAD(P)H-dependent reduction of 2,3-dihydrodipicolinate (DHDP) to 2,3,4,5-tetrahydrodipicolinate (THDP). DHDPR could also function as a dehydratase in addition to the role of a nucleotide dependent reductase. DHDPR is a component of the biosynthetic pathway that generates meso-diaminopimelate, a component of bacterial cell walls, and the amino acid L-lysine in various bacteria, archaea, cyanobacteria and higher plants. The enzyme is a homotetramer where each monomer is composed of two domains, an N-terminal NAD(P)-binding domain which forms a Rossmann fold, and a C-terminal substrate-binding domain that forms an open, mixed alpha-beta sandwich.


Pssm-ID: 467611 [Multi-domain]  Cd Length: 139  Bit Score: 38.31  E-value: 4.69e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 766431915   2 IRIAINGF-GRIGRLVLRLALQRKDIEVVAVND 33
Cdd:cd02274    1 IKVAVAGAtGRMGRELVKAILEAPDLELVGAVD 33
Asd COG0136
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ...
 89-169 5.46e-04

Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; Aspartate-semialdehyde dehydrogenase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439906 [Multi-domain]  Cd Length: 333  Bit Score: 39.24  E-value: 5.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766431915  89 KIDVAVDSTG--VFKELdtAQKHIDAGAkkVVITApsSSA-------PMFVVGVNH---TKYTPdKKIVSNASCTTNCLA 156
Cdd:COG0136   62 GVDIALFSAGgsVSKEY--APKAAAAGA--VVIDN--SSAfrmdpdvPLVVPEVNPealADHLP-KGIIANPNCSTIQML 134

                         90
                 ....*....|...
gi 766431915 157 PLAKVINDAFGIE 169
Cdd:COG0136  135 VALKPLHDAAGIK 147
meso-DAPDH_N cd02270
N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and ...
 2-31 8.47e-04

N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and similar proteins; Meso-DAPDH (EC 1.4.1.16), also called diaminopimelate dehydrogenase, or meso-DAP dehydrogenase, probably plays a role in lysine biosynthesis. It catalyzes the reversible NADP(H)-dependent reductive amination of L-2-amino-6-oxopimelate, the acyclic form of L-tetrahydrodipicolinate, to generate the meso compound, D,L-2,6-diaminopimelate. DAPDH is a homodimer which is highly specific for meso-DAP and NADP(+) as substrates. Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.


Pssm-ID: 467610 [Multi-domain]  Cd Length: 151  Bit Score: 37.94  E-value: 8.47e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 766431915   2 IRIAINGFGRIGRLVLRLALQRKDIEVVAV 31
Cdd:cd02270    1 IRVAIVGYGNLGRGVEEAIQANPDMELVGV 30
PRK04207 PRK04207
type II glyceraldehyde-3-phosphate dehydrogenase;
1-44 1.05e-03

type II glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 179786 [Multi-domain]  Cd Length: 341  Bit Score: 38.66  E-value: 1.05e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 766431915   1 MIRIAINGFGRIGRLVLRLALQRKDIEVVAVNDpfISNDYAAYM 44
Cdd:PRK04207   1 MIKVGVNGYGTIGKRVADAVAAQPDMELVGVAK--TKPDYEARV 42
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH