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Conserved domains on  [gi|47779479|gb|AAT38666|]
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glyceraldehyde 3-phosphate dehydrogenase, partial [Leccinum palustre]

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
 1-225 4.88e-136

glyceraldehyde-3-phosphate dehydrogenase


The actual alignment was detected with superfamily member PLN02272:

Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 388.06  E-value: 4.88e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479    1 IVAVNDPFIDLEYMVYMFKYDSVHGRFKGDVHA-KDGKLYINGKAITVYAERDPANIKWGGVGAEYVVESTGVFTTIEKA 79
Cdd:PLN02272 112 VVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDPAEIPWGDFGAEYVVESSGVFTTVEKA 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479   80 GAHLKGGAKKVIISAPSADAPMFVCGVNLDKYDPKYTVISNASCTTNCLAPLAKV*********GLMSTIHATTATQKTV 159
Cdd:PLN02272 192 SAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQKTV 271

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47779479  160 DGPSAKDWRGGRAVNGNIIPSSTGAAKAVGKVIPTLNGKLTGLAFRVPTNDVSVVDLVVRLEKSAS 225
Cdd:PLN02272 272 DGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRLEKSAS 337
 
Name Accession Description Interval E-value
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 1-225 4.88e-136

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 388.06  E-value: 4.88e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479    1 IVAVNDPFIDLEYMVYMFKYDSVHGRFKGDVHA-KDGKLYINGKAITVYAERDPANIKWGGVGAEYVVESTGVFTTIEKA 79
Cdd:PLN02272 112 VVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDPAEIPWGDFGAEYVVESSGVFTTVEKA 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479   80 GAHLKGGAKKVIISAPSADAPMFVCGVNLDKYDPKYTVISNASCTTNCLAPLAKV*********GLMSTIHATTATQKTV 159
Cdd:PLN02272 192 SAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQKTV 271

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47779479  160 DGPSAKDWRGGRAVNGNIIPSSTGAAKAVGKVIPTLNGKLTGLAFRVPTNDVSVVDLVVRLEKSAS 225
Cdd:PLN02272 272 DGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRLEKSAS 337
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-225 2.79e-125

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: 357.40  E-value: 2.79e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479   1 IVAVNDPfIDLEYMVYMFKYDSVHGRFKGDVHAKDGKLYINGKAITVYAERDPANIKWGGVGAEYVVESTGVFTTIEKAG 80
Cdd:COG0057  30 VVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAELPWGELGVDVVIECTGKFTDREKAS 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479  81 AHLKGGAKKVIISAPSADA-PMFVCGVNLDKYDPKYTVISNASCTTNCLAPLAKV*********GLMSTIHATTATQKTV 159
Cdd:COG0057 109 AHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAPVAKVLNDAFGIEKGLMTTIHAYTNDQNLL 188

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47779479 160 DGPsAKDWRGGRAVNGNIIPSSTGAAKAVGKVIPTLNGKLTGLAFRVPTNDVSVVDLVVRLEKSAS 225
Cdd:COG0057 189 DAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVELEKETT 253
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 1-225 4.64e-108

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: 313.83  E-value: 4.64e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479     1 IVAVNDPfIDLEYMVYMFKYDSVHGRFKGDVHAKDGKLYINGKAITVYA-ERDPANIKWGGVGAEYVVESTGVFTTIEKA 79
Cdd:TIGR01534  28 VVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEVISVFsERDPSDLPWKALGVDIVIECTGKFRDKEKL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479    80 GAHLKGGAKKVIISAPSADA-PMFVCGVNLDKYDPKYTVISNASCTTNCLAPLAKV*********GLMSTIHATTATQKT 158
Cdd:TIGR01534 107 EKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLAPLAKVLDEAFGIVSGLMTTVHAYTNDQNL 186

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47779479   159 VDGPSaKDWRGGRAVNGNIIPSSTGAAKAVGKVIPTLNGKLTGLAFRVPTNDVSVVDLVVRLEKSAS 225
Cdd:TIGR01534 187 LDGPH-KDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNVSLVDLVVNLEKDVT 252
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 1-122 5.00e-73

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: 218.80  E-value: 5.00e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479   1 IVAVNDPFIDlEYMVYMFKYDSVHGRFKGDVHAKDGKLYINGKAITVYAERDPANIKWGGVGAEYVVESTGVFTTIEKAG 80
Cdd:cd05214  27 VVAINDLTDD-ETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAELPWGELGVDIVIESTGVFTTKEKAS 105

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 47779479  81 AHLKGGAKKVIISAPSAD-APMFVCGVNLDKYDPKYTVISNAS 122
Cdd:cd05214 106 AHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDADDKIISNAS 148
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-123 1.91e-62

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: 191.61  E-value: 1.91e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479      1 IVAVNDPfIDLEYMVYMFKYDSVHGRFKGDVHAKDGKLYINGKAITVYAERDPANIKWGGVGAEYVVESTGVFTTIEKAG 80
Cdd:smart00846  27 VVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANLPWGELGVDIVVECTGGFTTREKAS 105

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 47779479     81 AHLKGGAKKVIISAPSADA-PMFVCGVNLDKYDPKYTVISNASC 123
Cdd:smart00846 106 AHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
1-225 2.46e-60

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 192.07  E-value: 2.46e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479    1 IVAVNDPFIDLEYMVYMFKYDSVHGRFKGDVHAKDGKLYINGKAITVYAERDPANIKWGGvGAEYVVESTGVFTTIEKAG 80
Cdd:NF033735  25 IVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDTPWGD-GVDVVIECTGKFKTPEKLQ 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479   81 AHLKGGAKKVIISAP--SADAPMFVCGVNLDKYDP-KYTVISNASCTTNCLAPLAKV*********GLMSTIHATTATQK 157
Cdd:NF033735 104 PYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPaRHRIVTAASCTTNCLAPVVKVIHEKIGIKHGSITTIHDITNTQT 183

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47779479  158 TVDGPsAKDWRGGRAVNGNIIPSSTGAAKAVGKVIPTLNGKLTGLAFRVPTNDVSVVDLVVRLEKSAS 225
Cdd:NF033735 184 IVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASLTDCVFEVERPTT 250
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 128-225 2.58e-43

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: 143.12  E-value: 2.58e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479   128 LAPLAKV*********GLMSTIHATTATQKTVDGPSAKDWRGGRAVNGNIIPSSTGAAKAVGKVIPTLNGKLTGLAFRVP 207
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90
                  ....*....|....*...
gi 47779479   208 TNDVSVVDLVVRLEKSAS 225
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVT 98
 
Name Accession Description Interval E-value
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 1-225 4.88e-136

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 388.06  E-value: 4.88e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479    1 IVAVNDPFIDLEYMVYMFKYDSVHGRFKGDVHA-KDGKLYINGKAITVYAERDPANIKWGGVGAEYVVESTGVFTTIEKA 79
Cdd:PLN02272 112 VVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDPAEIPWGDFGAEYVVESSGVFTTVEKA 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479   80 GAHLKGGAKKVIISAPSADAPMFVCGVNLDKYDPKYTVISNASCTTNCLAPLAKV*********GLMSTIHATTATQKTV 159
Cdd:PLN02272 192 SAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQKTV 271

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47779479  160 DGPSAKDWRGGRAVNGNIIPSSTGAAKAVGKVIPTLNGKLTGLAFRVPTNDVSVVDLVVRLEKSAS 225
Cdd:PLN02272 272 DGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRLEKSAS 337
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-225 2.79e-125

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: 357.40  E-value: 2.79e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479   1 IVAVNDPfIDLEYMVYMFKYDSVHGRFKGDVHAKDGKLYINGKAITVYAERDPANIKWGGVGAEYVVESTGVFTTIEKAG 80
Cdd:COG0057  30 VVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAELPWGELGVDVVIECTGKFTDREKAS 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479  81 AHLKGGAKKVIISAPSADA-PMFVCGVNLDKYDPKYTVISNASCTTNCLAPLAKV*********GLMSTIHATTATQKTV 159
Cdd:COG0057 109 AHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAPVAKVLNDAFGIEKGLMTTIHAYTNDQNLL 188

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47779479 160 DGPsAKDWRGGRAVNGNIIPSSTGAAKAVGKVIPTLNGKLTGLAFRVPTNDVSVVDLVVRLEKSAS 225
Cdd:COG0057 189 DAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVELEKETT 253
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
 1-224 3.74e-108

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 314.47  E-value: 3.74e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479    1 IVAVNDPFIDLEYMVYMFKYDSVHGRFKGDVHAKDGKLYINGKAITVYAERDPANIKWGGVGAEYVVESTGVFTTIEKAG 80
Cdd:PTZ00023  29 VVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKDPAAIPWGKNGVDVVCESTGVFLTKEKAQ 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479   81 AHLKGGAKKVIISAP-SADAPMFVCGVNLDKYDPKYTVISNASCTTNCLAPLAKV*********GLMSTIHATTATQKTV 159
Cdd:PTZ00023 109 AHLKGGAKKVIMSAPpKDDTPIYVMGVNHTQYDKSQRIVSNASCTTNCLAPLAKVVNDKFGIVEGLMTTVHASTANQLTV 188

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47779479  160 DGPS--AKDWRGGRAVNGNIIPSSTGAAKAVGKVIPTLNGKLTGLAFRVPTNDVSVVDLVVRLEKSA 224
Cdd:PTZ00023 189 DGPSkgGKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVPDVSVVDLTCKLAKPA 255
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 1-225 4.64e-108

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: 313.83  E-value: 4.64e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479     1 IVAVNDPfIDLEYMVYMFKYDSVHGRFKGDVHAKDGKLYINGKAITVYA-ERDPANIKWGGVGAEYVVESTGVFTTIEKA 79
Cdd:TIGR01534  28 VVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEVISVFsERDPSDLPWKALGVDIVIECTGKFRDKEKL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479    80 GAHLKGGAKKVIISAPSADA-PMFVCGVNLDKYDPKYTVISNASCTTNCLAPLAKV*********GLMSTIHATTATQKT 158
Cdd:TIGR01534 107 EKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLAPLAKVLDEAFGIVSGLMTTVHAYTNDQNL 186

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47779479   159 VDGPSaKDWRGGRAVNGNIIPSSTGAAKAVGKVIPTLNGKLTGLAFRVPTNDVSVVDLVVRLEKSAS 225
Cdd:TIGR01534 187 LDGPH-KDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNVSLVDLVVNLEKDVT 252
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
 1-225 1.65e-101

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 297.79  E-value: 1.65e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479    1 IVAVNDPFIDLEYMVYMFKYDSVHGRFK-GDVHAKDGKLYING-KAITVYAERDPANIKWGGVGAEYVVESTGVFTTIEK 78
Cdd:PLN02358  32 LVAVNDPFITTEYMTYMFKYDSVHGQWKhHELKVKDDKTLLFGeKPVTVFGIRNPEDIPWGEAGADFVVESTGVFTDKDK 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479   79 AGAHLKGGAKKVIISAPSADAPMFVCGVNLDKYDPKYTVISNASCTTNCLAPLAKV*********GLMSTIHATTATQKT 158
Cdd:PLN02358 112 AAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCTTNCLAPLAKVINDRFGIVEGLMTTVHSITATQKT 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47779479  159 VDGPSAKDWRGGRAVNGNIIPSSTGAAKAVGKVIPTLNGKLTGLAFRVPTNDVSVVDLVVRLEKSAS 225
Cdd:PLN02358 192 VDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRLEKAAT 258
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
1-225 1.24e-95

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 282.39  E-value: 1.24e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479    1 IVAVNDpFIDLEYMVYMFKYDSVHGRFKGDVHAKDGKLYINGKAITVYAERDPANIKWGGVGAEYVVESTGVFTTIEKAG 80
Cdd:PRK15425  29 IVAIND-LLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPANLKWDEVGVDVVAEATGLFLTDETAR 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479   81 AHLKGGAKKVIISAPSAD-APMFVCGVNLDKYDPKyTVISNASCTTNCLAPLAKV*********GLMSTIHATTATQKTV 159
Cdd:PRK15425 108 KHITAGAKKVVMTGPSKDnTPMFVKGANFDKYAGQ-DIVSNASCTTNCLAPLAKVINDNFGIIEGLMTTVHATTATQKTV 186

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47779479  160 DGPSAKDWRGGRAVNGNIIPSSTGAAKAVGKVIPTLNGKLTGLAFRVPTNDVSVVDLVVRLEKSAS 225
Cdd:PRK15425 187 DGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAAT 252
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 1-225 2.06e-87

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 262.68  E-value: 2.06e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479    1 IVAVNDPFIDLEYMVYMFKYDSVHGRFKGDVH--------AKDGKLYINGKAI-TVYAERDPANIKWGGVGAEYVVESTG 71
Cdd:PTZ00434  34 VVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVEttksspsvKTDDVLVVNGHRIkCVKAQRNPADLPWGKLGVDYVIESTG 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479   72 VFTTIEKAGAHLKGGAKKVIISAP-SADAPMFVCGVNLDKYDPK-YTVISNASCTTNCLAPLAKV*****-****GLMST 148
Cdd:PTZ00434 114 LFTDKLAAEGHLKGGAKKVVISAPaSGGAKTIVMGVNQHEYSPTeHHVVSNASCTTNCLAPIVHVLTKEGfGIETGLMTT 193

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47779479  149 IHATTATQKTVDGPSAKDWRGGRAVNGNIIPSSTGAAKAVGKVIPTLNGKLTGLAFRVPTNDVSVVDLVVRLEKSAS 225
Cdd:PTZ00434 194 IHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGKLTGMSFRVPTPDVSVVDLTFRATRDTS 270
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-222 1.79e-83

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 251.97  E-value: 1.79e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479    1 IVAVNDPFiDLEYMVYMFKYDSVHGRFKGDVHAKDGKLYINGKAITVYAERDPANIKWGGVGAEYVVESTGVFTTIEKAG 80
Cdd:PRK07729  29 IVAINASY-PSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDPKELPWTDLGIDIVIEATGKFNSKEKAI 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479   81 AHLKGGAKKVIISAPSADAPM-FVCGVNLDKYDP-KYTVISNASCTTNCLAPLAKV*********GLMSTIHATTATQKT 158
Cdd:PRK07729 108 LHVEAGAKKVILTAPGKNEDVtIVVGVNEDQLDIeKHTIISNASCTTNCLAPVVKVLDEQFGIENGLMTTVHAYTNDQKN 187

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47779479  159 VDGPSaKDWRGGRAVNGNIIPSSTGAAKAVGKVIPTLNGKLTGLAFRVPTNDVSVVDLVVRLEK 222
Cdd:PRK07729 188 IDNPH-KDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNVSLVDLVVDVKR 250
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 1-122 5.00e-73

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: 218.80  E-value: 5.00e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479   1 IVAVNDPFIDlEYMVYMFKYDSVHGRFKGDVHAKDGKLYINGKAITVYAERDPANIKWGGVGAEYVVESTGVFTTIEKAG 80
Cdd:cd05214  27 VVAINDLTDD-ETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAELPWGELGVDIVIESTGVFTTKEKAS 105

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 47779479  81 AHLKGGAKKVIISAPSAD-APMFVCGVNLDKYDPKYTVISNAS 122
Cdd:cd05214 106 AHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDADDKIISNAS 148
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
1-223 8.88e-70

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 216.70  E-value: 8.88e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479    1 IVAVNDPfIDLEYMVYMFKYDSVHGRFKGDVHAKDGKLYINGKAITVYAERDPANIKWGGVGAEYVVESTGVFTTIEKAG 80
Cdd:PRK07403  30 LVAINDT-SDPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDRNPLNLPWKEWGIDLIIESTGVFVTKEGAS 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479   81 AHLKGGAKKVIISAP--SADAPMFVCGVNLDKYD-PKYTVISNASCTTNCLAPLAKV*********GLMSTIHATTATQK 157
Cdd:PRK07403 109 KHIQAGAKKVLITAPgkGEDIGTYVVGVNHHEYDhEDHNIISNASCTTNCLAPIAKVLHDNFGIIKGTMTTTHSYTGDQR 188

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47779479  158 TVDGpSAKDWRGGRAVNGNIIPSSTGAAKAVGKVIPTLNGKLTGLAFRVPTNDVSVVDLVVRLEKS 223
Cdd:PRK07403 189 ILDA-SHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTPNVSVVDLVVQVEKR 253
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
 1-222 1.40e-66

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 210.17  E-value: 1.40e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479    1 IVAVNDPFiDLEYMVYMFKYDSVHGRFKGDVHAK-DGKLYINGKAITVYAERDPANIKWGGVGAEYVVESTGVFTTIEKA 79
Cdd:PLN03096  89 VVAINDTG-GVKQASHLLKYDSTLGTFDADVKPVgDDAISVDGKVIKVVSDRNPLNLPWGELGIDLVIEGTGVFVDREGA 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479   80 GAHLKGGAKKVIISAPS-ADAPMFVCGVNLDKYDPKYTVISNASCTTNCLAPLAKV*********GLMSTIHATTATQKT 158
Cdd:PLN03096 168 GKHIQAGAKKVLITAPGkGDIPTYVVGVNADDYKHSDPIISNASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRL 247

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47779479  159 VDGpSAKDWRGGRAVNGNIIPSSTGAAKAVGKVIPTLNGKLTGLAFRVPTNDVSVVDLVVRLEK 222
Cdd:PLN03096 248 LDA-SHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQVEK 310
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
 16-222 7.03e-63

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 202.05  E-value: 7.03e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479   16 YMFKYDSVHGRFKGDVHAKDGK-LYINGKAITVYAERDPANIKWGGVGAEYVVESTGVFTTIEKAGAHLKGGAKKVIISA 94
Cdd:PLN02237 118 HLLKYDSMLGTFKADVKIVDDEtISVDGKPIKVVSNRDPLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITA 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479   95 PS--ADAPMFVCGVNLDKYDPKYT-VISNASCTTNCLAPLAKV*********GLMSTIHATTATQKTVDGpSAKDWRGGR 171
Cdd:PLN02237 198 PAkgADIPTYVVGVNEDDYDHEVAnIVSNASCTTNCLAPFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDA-SHRDLRRAR 276

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 47779479  172 AVNGNIIPSSTGAAKAVGKVIPTLNGKLTGLAFRVPTNDVSVVDLVVRLEK 222
Cdd:PLN02237 277 AAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTPNVSVVDLVVNVEK 327
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-123 1.91e-62

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: 191.61  E-value: 1.91e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479      1 IVAVNDPfIDLEYMVYMFKYDSVHGRFKGDVHAKDGKLYINGKAITVYAERDPANIKWGGVGAEYVVESTGVFTTIEKAG 80
Cdd:smart00846  27 VVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANLPWGELGVDIVVECTGGFTTREKAS 105

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 47779479     81 AHLKGGAKKVIISAPSADA-PMFVCGVNLDKYDPKYTVISNASC 123
Cdd:smart00846 106 AHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
1-225 2.46e-60

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 192.07  E-value: 2.46e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479    1 IVAVNDPFIDLEYMVYMFKYDSVHGRFKGDVHAKDGKLYINGKAITVYAERDPANIKWGGvGAEYVVESTGVFTTIEKAG 80
Cdd:NF033735  25 IVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDTPWGD-GVDVVIECTGKFKTPEKLQ 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479   81 AHLKGGAKKVIISAP--SADAPMFVCGVNLDKYDP-KYTVISNASCTTNCLAPLAKV*********GLMSTIHATTATQK 157
Cdd:NF033735 104 PYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPaRHRIVTAASCTTNCLAPVVKVIHEKIGIKHGSITTIHDITNTQT 183

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47779479  158 TVDGPsAKDWRGGRAVNGNIIPSSTGAAKAVGKVIPTLNGKLTGLAFRVPTNDVSVVDLVVRLEKSAS 225
Cdd:NF033735 184 IVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASLTDCVFEVERPTT 250
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 123-225 4.44e-59

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: 183.43  E-value: 4.44e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479 123 CTTNCLAPLAKV*********GLMSTIHATTATQKTVDGPSaKDWRGGRAVNGNIIPSSTGAAKAVGKVIPTLNGKLTGL 202
Cdd:cd18126   1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79

                        90       100
                ....*....|....*....|...
gi 47779479 203 AFRVPTNDVSVVDLVVRLEKSAS 225
Cdd:cd18126  80 AFRVPTPNVSVVDLTVRLEKPVT 102
PRK08955 PRK08955
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-225 5.68e-52

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 169599 [Multi-domain]  Cd Length: 334  Bit Score: 170.68  E-value: 5.68e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479    1 IVAVNDPFIDLEYMVYMFKYDSVHGRFKGDVHAKDGKLYINGKAITVYAERDPANIKWGGvgAEYVVESTGVFTTIEKAG 80
Cdd:PRK08955  29 FVQINDPAGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKAIADTDWSG--CDVVIEASGVMKTKALLQ 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479   81 AHLKGGAKKVIISAPSADAPMF--VCGVNLDKYDP-KYTVISNASCTTNCLAPLAKV*********GLMSTIHATTATQK 157
Cdd:PRK08955 107 AYLDQGVKRVVVTAPVKEEGVLniVMGVNDHLFDPaIHPIVTAASCTTNCLAPVVKVIHEKLGIKHGSMTTIHDLTNTQT 186

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47779479  158 TVDGPSaKDWRGGRAVNGNIIPSSTGAAKAVGKVIPTLNGKLTGLAFRVPTNDVSVVDLVVRLEKSAS 225
Cdd:PRK08955 187 ILDAPH-KDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLANASLTDCVFEVERDTT 253
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
 1-223 7.55e-50

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 165.23  E-value: 7.55e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479    1 IVAVNDpFIDLEYMVYMFKYDSVHGRFKGDVHAKDGKLYINGKAITVYAERDPANIKWGGVGAEYVVESTGVFTTIEKAG 80
Cdd:PRK13535  31 VVAINE-LADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHERDIASLPWRELGVDVVLDCTGVYGSREDGE 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479   81 AHLKGGAKKVIISAPSA---DAPMfVCGVNLDKYDPKYTVISNASCTTNCLAPLAKV*********GLMSTIHATTATQK 157
Cdd:PRK13535 110 AHIAAGAKKVLFSHPGSndlDATV-VYGVNHDQLRAEHRIVSNASCTTNCIIPVIKLLDDAFGIESGTVTTIHSAMNDQQ 188

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47779479  158 TVDGpSAKDWRGGRAVNGNIIPSSTGAAKAVGKVIPTLNGKLTGLAFRVPTNDVSVVDLVVRLEKS 223
Cdd:PRK13535 189 VIDA-YHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPTINVTAIDLSVTVKKP 253
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 128-225 2.58e-43

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: 143.12  E-value: 2.58e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479   128 LAPLAKV*********GLMSTIHATTATQKTVDGPSAKDWRGGRAVNGNIIPSSTGAAKAVGKVIPTLNGKLTGLAFRVP 207
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90
                  ....*....|....*...
gi 47779479   208 TNDVSVVDLVVRLEKSAS 225
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVT 98
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 123-225 1.48e-42

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: 141.60  E-value: 1.48e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479 123 CTTNCLAPLAKV*********GLMSTIHATTATQKTVDGPSAKDWRGGRAVNGNIIPSSTGAAKAVGKVIPTLNGKLTGL 202
Cdd:cd18123   1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80

                        90       100
                ....*....|....*....|...
gi 47779479 203 AFRVPTNDVSVVDLVVRLEKSAS 225
Cdd:cd18123  81 AVRVPTTLMSVHDLMVELEKDVT 103
PRK08289 PRK08289
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
 10-225 3.47e-42

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 236219 [Multi-domain]  Cd Length: 477  Bit Score: 148.53  E-value: 3.47e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479   10 DLEYMVYMFKYDSVHGRFKG--DVHAKDGKLYINGKAITVYAERDPANIKWG--GVGAEYVVESTGVFTTIEKAGAHLKG 85
Cdd:PRK08289 170 DLEKRASLLRRDSVHGPFNGtiTVDEENNAIIANGNYIQVIYANSPEEVDYTayGINNALVVDNTGKWRDEEGLSQHLKS 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479   86 -GAKKVIISAPS-ADAPMFVCGVNLDKYDPKYTVISNASCTTNCLAPLAKV*********GLMSTIHATTATQKTVDGPS 163
Cdd:PRK08289 250 kGVAKVLLTAPGkGDIKNIVHGVNHSDITDEDKIVSAASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYH 329

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47779479  164 AKDwRGGRAVNGNIIPSSTGAAKAVGKVIPTLNGKLTGLAFRVPTNDVSVVDLVVRLEKSAS 225
Cdd:PRK08289 330 KGD-RRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNAIRVPTPNVSMAILNLNLEKETS 390
GAPDH_N_E4PDH cd17892
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 1-122 6.94e-37

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: 127.00  E-value: 6.94e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479   1 IVAVNDPfIDLEYMVYMFKYDSVHGRFKGDVHAKDGKLYINGKAITVYAERDPANIKWGGVGAEYVVESTGVFTTIEKAG 80
Cdd:cd17892  30 VVAINEL-ADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPDPENLPWRELGIDLVLECTGVFGSREDAE 108

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 47779479  81 AHLKGGAKKVIISAPSA---DAPMfVCGVNLDKYDPKYTVISNAS 122
Cdd:cd17892 109 RHLAAGAKKVLFSHPASndvDATI-VYGINQDLLRAEHRIVSNAS 152
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-75 2.92e-36

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


Pssm-ID: 459648 [Multi-domain]  Cd Length: 101  Bit Score: 122.98  E-value: 2.92e-36
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47779479     1 IVAVNDpFIDLEYMVYMFKYDSVHGRFKGDVHAKDGKLYINGKAITVYAERDPANIKWGGVGAEYVVESTGVFTT 75
Cdd:pfam00044  27 VVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAELPWGDLGVDVVIESTGVFTT 100
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
 1-225 8.39e-35

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 126.53  E-value: 8.39e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479    1 IVAVNDPFIDLEYMVYMFKYDSVHGRFKG-DVHAKDGKLYING-KAITVYAERDPANIKWGGVGAEYVVESTGVFTTIEK 78
Cdd:PTZ00353  29 VVAVNDASVSIAYIAYVLEQESPLSAPDGaSIRVVGEQIVLNGtQKIRVSAKHDLVEIAWRDYGVQYVVECTGLYSTRSR 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479   79 AGAHLKGGAKKVIISAPSADAPMFVCGVNLDKYDPKYTVISNASCTTNCLAPLAKV*********GLMSTIHATTAtQKT 158
Cdd:PTZ00353 109 CWGHVTGGAKGVFVAGQSADAPTVMAGSNDERLSASLPVCCAGAPIAVALAPVIRALHEVYGVEECSYTAIHGMQP-QEP 187

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47779479  159 VDGPSA--KDWRGGRAVNGNIIPSSTGAAKAVGKVIPTLNGKLTGLAFRVPTNDVSVVDLVVRLEKSAS 225
Cdd:PTZ00353 188 IAARSKnsQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVKKGCAIDMLVRTKQPVS 256
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 123-225 1.38e-20

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: 84.88  E-value: 1.38e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479 123 CTTNCLAPLAKV*********GLMSTIHATTATQKTVDGPSAKDWrgGRAVNGNIIPSSTGAAKAVGKVIPTLN--GKLT 200
Cdd:cd18122   1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIGkpIKVD 78

                        90       100
                ....*....|....*....|....*
gi 47779479 201 GLAFRVPTNDVSVVDLVVRLEKSAS 225
Cdd:cd18122  79 GIAVRVPATLGHLVTVTVKLEKTAT 103
GAPDH_C_E4PDH cd23937
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 123-225 1.17e-18

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: 79.77  E-value: 1.17e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47779479 123 CTTNCLAPLAKV*********GLMSTIHATTATQKTVDGpSAKDWRGGRAVNGNIIPSSTGAAKAVGKVIPTLNGKLTGL 202
Cdd:cd23937   1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAI 79

                        90       100
                ....*....|....*....|...
gi 47779479 203 AFRVPTNDVSVVDLVVRLEKSAS 225
Cdd:cd23937  80 AVRVPTINVTAMDLSVTLKKDVT 102
GAPDH-like_N cd05192
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ...
 64-127 5.18e-07

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


Pssm-ID: 467613 [Multi-domain]  Cd Length: 109  Bit Score: 46.96  E-value: 5.18e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47779479  64 EYVVESTGVFTTIEKAGAHLKGGAKKVIISAPS-ADAPMFVCGVNLDKYDPKYTVISNASCTTNC 127
Cdd:cd05192  35 DVVIECTGSFTDDDNAEKHIKAGGKKAVITAPEkGDIPTIVVVLNELAKSAGATVVSNANETSYS 99
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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