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Conserved domains on  [gi|2393307764|gb|WAJ62847|]
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glyceraldehyde-3-phosphate dehydrogenase, partial [Alternaria solani]

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
 1-190 7.46e-116

glyceraldehyde-3-phosphate dehydrogenase


The actual alignment was detected with superfamily member PLN02272:

Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 335.29  E-value: 7.46e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764   1 RIVFRNAIEHNDVDIVAVNDPFIEPHYAAYMLKYDSTHGQFKGEIKV-DGNNLTVNGKTIRFHMEKDPANIPWSETGAYY 79
Cdd:PLN02272   98 RLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDPAEIPWGDFGAEY 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764  80 VVESTGVFTTTEKAKAHLKGGAKKVVISAPSADAPMFVMGVNHETYKSDIEVLSNASCTTNCLAPLAKVVHDKFTIIEGL 159
Cdd:PLN02272  178 VVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLAKVVHEEFGILEGL 257

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2393307764 160 MTTIHSYTATQKVVDGPSAKDWRGGRTAAQN 190
Cdd:PLN02272  258 MTTVHATTATQKTVDGPSMKDWRGGRGASQN 288
 
Name Accession Description Interval E-value
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 1-190 7.46e-116

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 335.29  E-value: 7.46e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764   1 RIVFRNAIEHNDVDIVAVNDPFIEPHYAAYMLKYDSTHGQFKGEIKV-DGNNLTVNGKTIRFHMEKDPANIPWSETGAYY 79
Cdd:PLN02272   98 RLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDPAEIPWGDFGAEY 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764  80 VVESTGVFTTTEKAKAHLKGGAKKVVISAPSADAPMFVMGVNHETYKSDIEVLSNASCTTNCLAPLAKVVHDKFTIIEGL 159
Cdd:PLN02272  178 VVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLAKVVHEEFGILEGL 257

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2393307764 160 MTTIHSYTATQKVVDGPSAKDWRGGRTAAQN 190
Cdd:PLN02272  258 MTTVHATTATQKTVDGPSMKDWRGGRGASQN 288
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-190 1.51e-109

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: 316.18  E-value: 1.51e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764   1 RIVFRNAIEH-NDVDIVAVNDPfIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYY 79
Cdd:COG0057    15 RLVLRALLERgPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAELPWGELGVDV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764  80 VVESTGVFTTTEKAKAHLKGGAKKVVISAPSADA-PMFVMGVNHETYKSDIEVLSNASCTTNCLAPLAKVVHDKFTIIEG 158
Cdd:COG0057    94 VIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAPVAKVLNDAFGIEKG 173

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2393307764 159 LMTTIHSYTATQKVVDGPsAKDWRGGRTAAQN 190
Cdd:COG0057   174 LMTTIHAYTNDQNLLDAP-HKDLRRARAAALN 204
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 1-190 1.15e-90

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: 267.99  E-value: 1.15e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764   1 RIVFRNAIE--HNDVDIVAVNDPfIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGK-TIRFHMEKDPANIPWSETGA 77
Cdd:TIGR01534  12 RLVLRRILEkpGNDLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKeVISVFSERDPSDLPWKALGV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764  78 YYVVESTGVFTTTEKAKAHLKGGAKKVVISAPSADA-PMFVMGVNHETYKSDIEVLSNASCTTNCLAPLAKVVHDKFTII 156
Cdd:TIGR01534  91 DIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLAPLAKVLDEAFGIV 170

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2393307764 157 EGLMTTIHSYTATQKVVDGPSaKDWRGGRTAAQN 190
Cdd:TIGR01534 171 SGLMTTVHAYTNDQNLLDGPH-KDLRRARAAALN 203
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 1-136 4.25e-80

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: 235.37  E-value: 4.25e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764   1 RIVFRNAIEHNDVDIVAVNDPFIePHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYV 80
Cdd:cd05214    13 RLVFRAALERDDIEVVAINDLTD-DETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAELPWGELGVDIV 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2393307764  81 VESTGVFTTTEKAKAHLKGGAKKVVISAPSAD-APMFVMGVNHETYKSDIEVLSNAS 136
Cdd:cd05214    92 IESTGVFTTKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDADDKIISNAS 148
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-137 2.40e-69

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: 207.40  E-value: 2.40e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764    1 RIVFRNAIEHNDVDIVAVNDPfIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYV 80
Cdd:smart00846  13 RLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANLPWGELGVDIV 91

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2393307764   81 VESTGVFTTTEKAKAHLKGGAKKVVISAPSADA-PMFVMGVNHETYKSDIEVLSNASC 137
Cdd:smart00846  92 VECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
1-190 2.96e-62

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 195.54  E-value: 2.96e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764   1 RIVFRNAIEHNDVDIVAVNDPFIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSEtGAYYV 80
Cdd:NF033735   11 RLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDTPWGD-GVDVV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764  81 VESTGVFTTTEKAKAHLKGGAKKVVISAP--SADAPMFVMGVNHETYKSDIE-VLSNASCTTNCLAPLAKVVHDKFTIIE 157
Cdd:NF033735   90 IECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARHrIVTAASCTTNCLAPVVKVIHEKIGIKH 169

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2393307764 158 GLMTTIHSYTATQKVVDGPsAKDWRGGRTAAQN 190
Cdd:NF033735  170 GSITTIHDITNTQTIVDAP-HKDLRRARSCGMS 201
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-89 1.13e-41

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: 135.69  E-value: 1.13e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764   1 RIVFRNAIEHNDVDIVAVNDpFIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYV 80
Cdd:pfam00044  13 RLVLRAALERPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAELPWGDLGVDVV 91


                  ....*....
gi 2393307764  81 VESTGVFTT 89
Cdd:pfam00044  92 IESTGVFTT 100
 
Name Accession Description Interval E-value
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 1-190 7.46e-116

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 335.29  E-value: 7.46e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764   1 RIVFRNAIEHNDVDIVAVNDPFIEPHYAAYMLKYDSTHGQFKGEIKV-DGNNLTVNGKTIRFHMEKDPANIPWSETGAYY 79
Cdd:PLN02272   98 RLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDPAEIPWGDFGAEY 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764  80 VVESTGVFTTTEKAKAHLKGGAKKVVISAPSADAPMFVMGVNHETYKSDIEVLSNASCTTNCLAPLAKVVHDKFTIIEGL 159
Cdd:PLN02272  178 VVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLAKVVHEEFGILEGL 257

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2393307764 160 MTTIHSYTATQKVVDGPSAKDWRGGRTAAQN 190
Cdd:PLN02272  258 MTTVHATTATQKTVDGPSMKDWRGGRGASQN 288
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-190 1.51e-109

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: 316.18  E-value: 1.51e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764   1 RIVFRNAIEH-NDVDIVAVNDPfIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYY 79
Cdd:COG0057    15 RLVLRALLERgPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAELPWGELGVDV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764  80 VVESTGVFTTTEKAKAHLKGGAKKVVISAPSADA-PMFVMGVNHETYKSDIEVLSNASCTTNCLAPLAKVVHDKFTIIEG 158
Cdd:COG0057    94 VIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAPVAKVLNDAFGIEKG 173

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2393307764 159 LMTTIHSYTATQKVVDGPsAKDWRGGRTAAQN 190
Cdd:COG0057   174 LMTTIHAYTNDQNLLDAP-HKDLRRARAAALN 204
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 1-190 1.15e-90

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: 267.99  E-value: 1.15e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764   1 RIVFRNAIE--HNDVDIVAVNDPfIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGK-TIRFHMEKDPANIPWSETGA 77
Cdd:TIGR01534  12 RLVLRRILEkpGNDLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKeVISVFSERDPSDLPWKALGV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764  78 YYVVESTGVFTTTEKAKAHLKGGAKKVVISAPSADA-PMFVMGVNHETYKSDIEVLSNASCTTNCLAPLAKVVHDKFTII 156
Cdd:TIGR01534  91 DIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLAPLAKVLDEAFGIV 170

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2393307764 157 EGLMTTIHSYTATQKVVDGPSaKDWRGGRTAAQN 190
Cdd:TIGR01534 171 SGLMTTVHAYTNDQNLLDGPH-KDLRRARAAALN 203
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
 1-190 1.35e-89

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 265.55  E-value: 1.35e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764   1 RIVFRNAIEHNDVDIVAVNDPFIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYV 80
Cdd:PTZ00023   15 RLVFRAALEREDVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKDPAAIPWGKNGVDVV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764  81 VESTGVFTTTEKAKAHLKGGAKKVVISAP-SADAPMFVMGVNHETYKSDIEVLSNASCTTNCLAPLAKVVHDKFTIIEGL 159
Cdd:PTZ00023   95 CESTGVFLTKEKAQAHLKGGAKKVIMSAPpKDDTPIYVMGVNHTQYDKSQRIVSNASCTTNCLAPLAKVVNDKFGIVEGL 174

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2393307764 160 MTTIHSYTATQKVVDGPS--AKDWRGGRTAAQN 190
Cdd:PTZ00023  175 MTTVHASTANQLTVDGPSkgGKDWRAGRCAGVN 207
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
 1-190 3.13e-83

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 249.64  E-value: 3.13e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764   1 RIVFRNAIEHNDVDIVAVNDPFIEPHYAAYMLKYDSTHGQFK-GEIKV-DGNNLTVNGKTIRFHMEKDPANIPWSETGAY 78
Cdd:PLN02358   18 RLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKhHELKVkDDKTLLFGEKPVTVFGIRNPEDIPWGEAGAD 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764  79 YVVESTGVFTTTEKAKAHLKGGAKKVVISAPSADAPMFVMGVNHETYKSDIEVLSNASCTTNCLAPLAKVVHDKFTIIEG 158
Cdd:PLN02358   98 FVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCTTNCLAPLAKVINDRFGIVEG 177

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2393307764 159 LMTTIHSYTATQKVVDGPSAKDWRGGRTAAQN 190
Cdd:PLN02358  178 LMTTVHSITATQKTVDGPSMKDWRGGRAASFN 209
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 1-136 4.25e-80

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: 235.37  E-value: 4.25e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764   1 RIVFRNAIEHNDVDIVAVNDPFIePHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYV 80
Cdd:cd05214    13 RLVFRAALERDDIEVVAINDLTD-DETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAELPWGELGVDIV 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2393307764  81 VESTGVFTTTEKAKAHLKGGAKKVVISAPSAD-APMFVMGVNHETYKSDIEVLSNAS 136
Cdd:cd05214    92 IESTGVFTTKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDADDKIISNAS 148
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
1-190 3.98e-77

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 233.86  E-value: 3.98e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764   1 RIVFRNAIEHNDVDIVAVNDpFIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYV 80
Cdd:PRK15425   15 RIVFRAAQKRSDIEIVAIND-LLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPANLKWDEVGVDVV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764  81 VESTGVFTTTEKAKAHLKGGAKKVVISAPSAD-APMFVMGVNHETYKSDiEVLSNASCTTNCLAPLAKVVHDKFTIIEGL 159
Cdd:PRK15425   94 AEATGLFLTDETARKHITAGAKKVVMTGPSKDnTPMFVKGANFDKYAGQ-DIVSNASCTTNCLAPLAKVINDNFGIIEGL 172

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2393307764 160 MTTIHSYTATQKVVDGPSAKDWRGGRTAAQN 190
Cdd:PRK15425  173 MTTVHATTATQKTVDGPSHKDWRGGRGASQN 203
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-137 2.40e-69

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: 207.40  E-value: 2.40e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764    1 RIVFRNAIEHNDVDIVAVNDPfIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYV 80
Cdd:smart00846  13 RLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANLPWGELGVDIV 91

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2393307764   81 VESTGVFTTTEKAKAHLKGGAKKVVISAPSADA-PMFVMGVNHETYKSDIEVLSNASC 137
Cdd:smart00846  92 VECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 1-190 7.39e-65

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 203.36  E-value: 7.39e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764   1 RIVFRNAIEH----NDVDIVAVNDPFIEPHYAAYMLKYDSTHGQFKGEIKV--------DGNNLTVNGKTIR-FHMEKDP 67
Cdd:PTZ00434   16 RMVFQAICDQgligTEIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVETtksspsvkTDDVLVVNGHRIKcVKAQRNP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764  68 ANIPWSETGAYYVVESTGVFTTTEKAKAHLKGGAKKVVISAP-SADAPMFVMGVNHETYK-SDIEVLSNASCTTNCLAPL 145
Cdd:PTZ00434   96 ADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPaSGGAKTIVMGVNQHEYSpTEHHVVSNASCTTNCLAPI 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2393307764 146 AKV-VHDKFTIIEGLMTTIHSYTATQKVVDGPSAKDWRGGRTAAQN 190
Cdd:PTZ00434  176 VHVlTKEGFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVN 221
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-189 4.05e-64

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 200.73  E-value: 4.05e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764   1 RIVFRNAIEHNDVDIVAVNDPFiEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYV 80
Cdd:PRK07729   15 RMVFRKAIKESAFEIVAINASY-PSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDPKELPWTDLGIDIV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764  81 VESTGVFTTTEKAKAHLKGGAKKVVISAPSADAPM-FVMGVNHETYKSDIE-VLSNASCTTNCLAPLAKVVHDKFTIIEG 158
Cdd:PRK07729   94 IEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVtIVVGVNEDQLDIEKHtIISNASCTTNCLAPVVKVLDEQFGIENG 173

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2393307764 159 LMTTIHSYTATQKVVDGPSaKDWRGGRTAAQ 189
Cdd:PRK07729  174 LMTTVHAYTNDQKNIDNPH-KDLRRARACGQ 203
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
9-190 1.56e-63

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 199.36  E-value: 1.56e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764   9 EHNDVDIVAVNDPfIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFT 88
Cdd:PRK07403   24 ENSQLELVAINDT-SDPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDRNPLNLPWKEWGIDLIIESTGVFV 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764  89 TTEKAKAHLKGGAKKVVISAP--SADAPMFVMGVNHETYKSDI-EVLSNASCTTNCLAPLAKVVHDKFTIIEGLMTTIHS 165
Cdd:PRK07403  103 TKEGASKHIQAGAKKVLITAPgkGEDIGTYVVGVNHHEYDHEDhNIISNASCTTNCLAPIAKVLHDNFGIIKGTMTTTHS 182

                         170       180
                  ....*....|....*....|....*
gi 2393307764 166 YTATQKVVDGpSAKDWRGGRTAAQN 190
Cdd:PRK07403  183 YTGDQRILDA-SHRDLRRARAAAVN 206
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
1-190 2.96e-62

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 195.54  E-value: 2.96e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764   1 RIVFRNAIEHNDVDIVAVNDPFIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSEtGAYYV 80
Cdd:NF033735   11 RLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDTPWGD-GVDVV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764  81 VESTGVFTTTEKAKAHLKGGAKKVVISAP--SADAPMFVMGVNHETYKSDIE-VLSNASCTTNCLAPLAKVVHDKFTIIE 157
Cdd:NF033735   90 IECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARHrIVTAASCTTNCLAPVVKVIHEKIGIKH 169

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2393307764 158 GLMTTIHSYTATQKVVDGPsAKDWRGGRTAAQN 190
Cdd:NF033735  170 GSITTIHDITNTQTIVDAP-HKDLRRARSCGMS 201
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
 13-190 1.44e-55

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 180.51  E-value: 1.44e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764  13 VDIVAVNDPFiEPHYAAYMLKYDSTHGQFKGEIKVDGNN-LTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFTTTE 91
Cdd:PLN03096   87 LDVVAINDTG-GVKQASHLLKYDSTLGTFDADVKPVGDDaISVDGKVIKVVSDRNPLNLPWGELGIDLVIEGTGVFVDRE 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764  92 KAKAHLKGGAKKVVISAPS-ADAPMFVMGVNHETYKSDIEVLSNASCTTNCLAPLAKVVHDKFTIIEGLMTTIHSYTATQ 170
Cdd:PLN03096  166 GAGKHIQAGAKKVLITAPGkGDIPTYVVGVNADDYKHSDPIISNASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQ 245

                         170       180
                  ....*....|....*....|
gi 2393307764 171 KVVDGpSAKDWRGGRTAAQN 190
Cdd:PLN03096  246 RLLDA-SHRDLRRARAAALN 264
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
 13-190 3.25e-52

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 172.78  E-value: 3.25e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764  13 VDIVAVNDPF-IEPhyAAYMLKYDSTHGQFKGEIK-VDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFTTT 90
Cdd:PLN02237  102 LDVVVVNDSGgVKN--ASHLLKYDSMLGTFKADVKiVDDETISVDGKPIKVVSNRDPLKLPWAELGIDIVIEGTGVFVDG 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764  91 EKAKAHLKGGAKKVVISAPS--ADAPMFVMGVNHETYKSDI-EVLSNASCTTNCLAPLAKVVHDKFTIIEGLMTTIHSYT 167
Cdd:PLN02237  180 PGAGKHIQAGAKKVIITAPAkgADIPTYVVGVNEDDYDHEVaNIVSNASCTTNCLAPFVKVLDEEFGIVKGTMTTTHSYT 259

                         170       180
                  ....*....|....*....|...
gi 2393307764 168 ATQKVVDGpSAKDWRGGRTAAQN 190
Cdd:PLN02237  260 GDQRLLDA-SHRDLRRARAAALN 281
PRK08955 PRK08955
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-185 3.07e-48

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 169599 [Multi-domain]  Cd Length: 334  Bit Score: 159.90  E-value: 3.07e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764   1 RIVFRNAIEHNDVDIVAVNDPFIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSetGAYYV 80
Cdd:PRK08955   15 RLALRAAWDWPELEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKAIADTDWS--GCDVV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764  81 VESTGVFTTTEKAKAHLKGGAKKVVISAPSADAPMF--VMGVNHETYKSDI-EVLSNASCTTNCLAPLAKVVHDKFTIIE 157
Cdd:PRK08955   93 IEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLniVMGVNDHLFDPAIhPIVTAASCTTNCLAPVVKVIHEKLGIKH 172

                         170       180
                  ....*....|....*....|....*...
gi 2393307764 158 GLMTTIHSYTATQKVVDGPSaKDWRGGR 185
Cdd:PRK08955  173 GSMTTIHDLTNTQTILDAPH-KDLRRAR 199
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
 1-189 6.19e-48

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 159.07  E-value: 6.19e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764   1 RIVFRNAIE---HNDVDIVAVNDpFIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGA 77
Cdd:PRK13535   14 RNVLRALYEsgrRAEITVVAINE-LADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHERDIASLPWRELGV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764  78 YYVVESTGVFTTTEKAKAHLKGGAKKVVISAPSA---DAPMfVMGVNHETYKSDIEVLSNASCTTNCLAPLAKVVHDKFT 154
Cdd:PRK13535   93 DVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSndlDATV-VYGVNHDQLRAEHRIVSNASCTTNCIIPVIKLLDDAFG 171

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2393307764 155 IIEGLMTTIHSYTATQKVVDGpSAKDWRGGRTAAQ 189
Cdd:PRK13535  172 IESGTVTTIHSAMNDQQVIDA-YHPDLRRTRAASQ 205
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-89 1.13e-41

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: 135.69  E-value: 1.13e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764   1 RIVFRNAIEHNDVDIVAVNDpFIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYV 80
Cdd:pfam00044  13 RLVLRAALERPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAELPWGDLGVDVV 91


                  ....*....
gi 2393307764  81 VESTGVFTT 89
Cdd:pfam00044  92 IESTGVFTT 100
GAPDH_N_E4PDH cd17892
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 11-136 2.73e-39

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: 132.01  E-value: 2.73e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764  11 NDVDIVAVNDPfIEPHYAAYMLKYDSTHGQFKGEIKVDGNNLTVNGKTIRFHMEKDPANIPWSETGAYYVVESTGVFTTT 90
Cdd:cd17892    26 AEFQVVAINEL-ADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPDPENLPWRELGIDLVLECTGVFGSR 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2393307764  91 EKAKAHLKGGAKKVVISAPSA---DAPMfVMGVNHETYKSDIEVLSNAS 136
Cdd:cd17892   105 EDAERHLAAGAKKVLFSHPASndvDATI-VYGINQDLLRAEHRIVSNAS 152
PRK08289 PRK08289
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
 29-190 5.46e-38

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 236219 [Multi-domain]  Cd Length: 477  Bit Score: 135.82  E-value: 5.46e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764  29 AYMLKYDSTHGQFKGEIKVDGNN--LTVNGKTIRFHMEKDPANIPWSETGAY--YVVESTGVFTTTEKAKAHLKG-GAKK 103
Cdd:PRK08289  175 ASLLRRDSVHGPFNGTITVDEENnaIIANGNYIQVIYANSPEEVDYTAYGINnaLVVDNTGKWRDEEGLSQHLKSkGVAK 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764 104 VVISAPS-ADAPMFVMGVNHETYKSDIEVLSNASCTTNCLAPLAKVVHDKFTIIEGLMTTIHSYTATQKVVDGPSAKDwR 182
Cdd:PRK08289  255 VLLTAPGkGDIKNIVHGVNHSDITDEDKIVSAASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKGD-R 333


                  ....*...
gi 2393307764 183 GGRTAAQN 190
Cdd:PRK08289  334 RGRSAPLN 341
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 137-190 1.11e-33

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: 117.56  E-value: 1.11e-33
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2393307764 137 CTTNCLAPLAKVVHDKFTIIEGLMTTIHSYTATQKVVDGPSaKDWRGGRTAAQN 190
Cdd:cd18126     1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQN 53
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
 13-190 6.16e-27

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 104.19  E-value: 6.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764  13 VDIVAVNDPFIEPHYAAYMLKYDSTH-GQFKGEIKVDGNNLTVNG-KTIRFHMEKDPANIPWSETGAYYVVESTGVFTTT 90
Cdd:PTZ00353   27 VTVVAVNDASVSIAYIAYVLEQESPLsAPDGASIRVVGEQIVLNGtQKIRVSAKHDLVEIAWRDYGVQYVVECTGLYSTR 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2393307764  91 EKAKAHLKGGAKKVVISAPSADAPMFVMGVNHETYKSDIEVLSNASCTTNCLAPLAKVVHDKFTIIEGLMTTIHSyTATQ 170
Cdd:PTZ00353  107 SRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDERLSASLPVCCAGAPIAVALAPVIRALHEVYGVEECSYTAIHG-MQPQ 185

                         170       180
                  ....*....|....*....|..
gi 2393307764 171 KVVDGPSA--KDWRGGRTAAQN 190
Cdd:PTZ00353  186 EPIAARSKnsQDWRQTRVAIDA 207
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 142-190 2.82e-23

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: 90.34  E-value: 2.82e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2393307764 142 LAPLAKVVHDKFTIIEGLMTTIHSYTATQKVVDGPSAKDWRGGRTAAQN 190
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPN 49
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 137-190 6.97e-23

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: 89.60  E-value: 6.97e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2393307764 137 CTTNCLAPLAKVVHDKFTIIEGLMTTIHSYTATQKVVDGPSAKDWRGGRTAAQN 190
Cdd:cd18123     1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNN 54
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 137-190 8.42e-11

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: 57.91  E-value: 8.42e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2393307764 137 CTTNCLAPLAKVVHDKFTIIEGLMTTIHSYTATQKVVDGPSAKDWrgGRTAAQN 190
Cdd:cd18122     1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPN 52
GAPDH-like_N cd05192
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ...
 79-141 5.82e-09

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


Pssm-ID: 467613 [Multi-domain]  Cd Length: 109  Bit Score: 51.59  E-value: 5.82e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2393307764  79 YVVESTGVFTTTEKAKAHLKGGAKKVVISAPS-ADAPMFVMGVNHETYKSDIEVLSNASCTTNC 141
Cdd:cd05192    36 VVIECTGSFTDDDNAEKHIKAGGKKAVITAPEkGDIPTIVVVLNELAKSAGATVVSNANETSYS 99
GAPDH_C_E4PDH cd23937
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 137-189 4.11e-08

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: 50.49  E-value: 4.11e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2393307764 137 CTTNCLAPLAKVVHDKFTIIEGLMTTIHSYTATQKVVDGpSAKDWRGGRTAAQ 189
Cdd:cd23937     1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDA-YHPDLRRTRAASQ 52
 
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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