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Conserved domains on  [gi|1958682051|ref|XP_038949894|]
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glyceraldehyde-3-phosphate dehydrogenase-like [Rattus norvegicus]

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
 1-289 1.17e-180

glyceraldehyde-3-phosphate dehydrogenase


The actual alignment was detected with superfamily member PLN02272:

Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 504.39  E-value: 1.17e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051   1 MVYMFQYDSTHDKFNGTVKAGNEK-LVINGKPITIFQERDPANIKWGDAGAEYVMESTGIFTTVEKAGAHLKGGAKRVII 79
Cdd:PLN02272  125 MAYMFKYDSTHGNFKGTINVVDDStLEINGKQIKVTSKRDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVI 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051  80 SAPSVDAPMFVMGVNHRKYDNFLKIVRNASCTTNCLAPLTKVIHDNFVILEGLMTTVHAITATQKTVNGSSGKLWCDGCG 159
Cdd:PLN02272  205 SAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRG 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 160 AAQNIIPASTGAAKAVGKVISELNGKLTGMGFRVPTPNVSIVDLTCRLEKPAKYDDIKMVMKQVSEGPLKGILGYTEDKV 239
Cdd:PLN02272  285 ASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDV 364

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958682051 240 VSCDFKSNSHSSTFDAGAGIALNDKFVKLISWYDNEYGYSNRVVDLMAYM 289
Cdd:PLN02272  365 VSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYSNRVLDLIEHM 414
 
Name Accession Description Interval E-value
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 1-289 1.17e-180

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 504.39  E-value: 1.17e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051   1 MVYMFQYDSTHDKFNGTVKAGNEK-LVINGKPITIFQERDPANIKWGDAGAEYVMESTGIFTTVEKAGAHLKGGAKRVII 79
Cdd:PLN02272  125 MAYMFKYDSTHGNFKGTINVVDDStLEINGKQIKVTSKRDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVI 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051  80 SAPSVDAPMFVMGVNHRKYDNFLKIVRNASCTTNCLAPLTKVIHDNFVILEGLMTTVHAITATQKTVNGSSGKLWCDGCG 159
Cdd:PLN02272  205 SAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRG 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 160 AAQNIIPASTGAAKAVGKVISELNGKLTGMGFRVPTPNVSIVDLTCRLEKPAKYDDIKMVMKQVSEGPLKGILGYTEDKV 239
Cdd:PLN02272  285 ASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDV 364

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958682051 240 VSCDFKSNSHSSTFDAGAGIALNDKFVKLISWYDNEYGYSNRVVDLMAYM 289
Cdd:PLN02272  365 VSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYSNRVLDLIEHM 414
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-293 6.24e-170

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: 473.73  E-value: 6.24e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051   1 MVYMFQYDSTHDKFNGTVKAGNEKLVINGKPITIFQERDPANIKWGDAGAEYVMESTGIFTTVEKAGAHLKGGAKRVIIS 80
Cdd:COG0057    42 LAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLIS 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051  81 APSVDA-PMFVMGVNHRKYDNFLKIVRNASCTTNCLAPLTKVIHDNFVILEGLMTTVHAITATQKTVNGSSGKLWcDGCG 159
Cdd:COG0057   122 APAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAPVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLR-RARA 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 160 AAQNIIPASTGAAKAVGKVISELNGKLTGMGFRVPTPNVSIVDLTCRLEKPAKYDDIKMVMKQVSEGPLKGILGYTEDKV 239
Cdd:COG0057   201 AALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPL 280

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958682051 240 VSCDFKSNSHSSTFDAGAGIALNDKFVKLISWYDNEYGYSNRVVDLMAYMVSKE 293
Cdd:COG0057   281 VSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGYSNRMVDLAEYMAKLL 334
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 1-284 2.67e-139

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: 395.88  E-value: 2.67e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051   1 MVYMFQYDSTHDKFNGTVKAGNEKLVINGKPIT-IFQERDPANIKWGDAGAEYVMESTGIFTTVEKAGAHLKGGAKRVII 79
Cdd:TIGR01534  40 LAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEVIsVFSERDPSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051  80 SAPSVDA-PMFVMGVNHRKYDNFLKIVRNASCTTNCLAPLTKVIHDNFVILEGLMTTVHAITATQKTVNGSSGKlWCDGC 158
Cdd:TIGR01534 120 SAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLAPLAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKD-LRRAR 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 159 GAAQNIIPASTGAAKAVGKVISELNGKLTGMGFRVPTPNVSIVDLTCRLEKPAKYDDIKMVMKQVSEGPLKGILGYTEDK 238
Cdd:TIGR01534 199 AAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNVSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDE 278

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1958682051 239 VVSCDFKSNSHSSTFDAGAGIA--LNDKFVKLISWYDNEYGYSNRVVD 284
Cdd:TIGR01534 279 LVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNEWGYSNRLVD 326
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 110-275 1.31e-106

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: 306.69  E-value: 1.31e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 110 CTTNCLAPLTKVIHDNFVILEGLMTTVHAITATQKTVNGSSgKLWCDGCGAAQNIIPASTGAAKAVGKVISELNGKLTGM 189
Cdd:cd18126     1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 190 GFRVPTPNVSIVDLTCRLEKPAKYDDIKMVMKQVSEGPLKGILGYTEDKVVSCDFKSNSHSSTFDAGAGIALNDKFVKLI 269
Cdd:cd18126    80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159


                  ....*.
gi 1958682051 270 SWYDNE 275
Cdd:cd18126   160 AWYDNE 165
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
6-285 3.28e-88

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 266.03  E-value: 3.28e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051   6 QYDSTHDKFNGTVKAGNEKLVINGKPITIFQERDPANIKWGDaGAEYVMESTGIFTTVEKAGAHLKGGAKRVIISAP--S 83
Cdd:NF033735   43 EFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDTPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkE 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051  84 VDAPMFVMGVNHRKYD-NFLKIVRNASCTTNCLAPLTKVIHDNFVILEGLMTTVHAITATQKTVNGSSGKL-WCDGCGaa 161
Cdd:NF033735  122 EGVLNIVYGVNDHLYDpARHRIVTAASCTTNCLAPVVKVIHEKIGIKHGSITTIHDITNTQTIVDAPHKDLrRARSCG-- 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 162 QNIIPASTGAAKAVGKVISELNGKLTGMGFRVPTPNVSIVDLTCRLEKPAKYDDIKMVMKQVSEGPLKGILGYTEDKVVS 241
Cdd:NF033735  200 MSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASLTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVS 279

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958682051 242 CDFKSNSHSSTFDAGAGIALNDKFVKLISWYDNEYGYSNRVVDL 285
Cdd:NF033735  280 VDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYANRMVDL 323
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 115-272 5.02e-78

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: 234.02  E-value: 5.02e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 115 LAPLTKVIHDNFVILEGLMTTVHAITATQKTVNGSSGKLWCDGCGAAQNIIPASTGAAKAVGKVISELNGKLTGMGFRVP 194
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958682051 195 TPNVSIVDLTCRLEKPAKYDDIKMVMKQVSEGPLKGILGYTEDKVVSCDFKSNSHSSTFDAGAGIALNDKFVKLISWY 272
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-110 2.50e-55

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: 175.82  E-value: 2.50e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051    1 MVYMFQYDSTHDKFNGTVKAGNEKLVINGKPITIFQERDPANIKWGDAGAEYVMESTGIFTTVEKAGAHLKGGAKRVIIS 80
Cdd:smart00846  39 LAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIIS 118

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1958682051   81 APSVDA-PMFVMGVNHRKYDNFLKIVRNASC 110
Cdd:smart00846 119 APSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
 
Name Accession Description Interval E-value
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 1-289 1.17e-180

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 504.39  E-value: 1.17e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051   1 MVYMFQYDSTHDKFNGTVKAGNEK-LVINGKPITIFQERDPANIKWGDAGAEYVMESTGIFTTVEKAGAHLKGGAKRVII 79
Cdd:PLN02272  125 MAYMFKYDSTHGNFKGTINVVDDStLEINGKQIKVTSKRDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVI 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051  80 SAPSVDAPMFVMGVNHRKYDNFLKIVRNASCTTNCLAPLTKVIHDNFVILEGLMTTVHAITATQKTVNGSSGKLWCDGCG 159
Cdd:PLN02272  205 SAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRG 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 160 AAQNIIPASTGAAKAVGKVISELNGKLTGMGFRVPTPNVSIVDLTCRLEKPAKYDDIKMVMKQVSEGPLKGILGYTEDKV 239
Cdd:PLN02272  285 ASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDV 364

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958682051 240 VSCDFKSNSHSSTFDAGAGIALNDKFVKLISWYDNEYGYSNRVVDLMAYM 289
Cdd:PLN02272  365 VSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYSNRVLDLIEHM 414
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-293 6.24e-170

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: 473.73  E-value: 6.24e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051   1 MVYMFQYDSTHDKFNGTVKAGNEKLVINGKPITIFQERDPANIKWGDAGAEYVMESTGIFTTVEKAGAHLKGGAKRVIIS 80
Cdd:COG0057    42 LAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLIS 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051  81 APSVDA-PMFVMGVNHRKYDNFLKIVRNASCTTNCLAPLTKVIHDNFVILEGLMTTVHAITATQKTVNGSSGKLWcDGCG 159
Cdd:COG0057   122 APAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAPVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLR-RARA 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 160 AAQNIIPASTGAAKAVGKVISELNGKLTGMGFRVPTPNVSIVDLTCRLEKPAKYDDIKMVMKQVSEGPLKGILGYTEDKV 239
Cdd:COG0057   201 AALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPL 280

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958682051 240 VSCDFKSNSHSSTFDAGAGIALNDKFVKLISWYDNEYGYSNRVVDLMAYMVSKE 293
Cdd:COG0057   281 VSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGYSNRMVDLAEYMAKLL 334
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
 1-293 9.87e-148

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 417.70  E-value: 9.87e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051   1 MVYMFQYDSTHDKFNGTVKAGNEKLVINGKPITIFQERDPANIKWGDAGAEYVMESTGIFTTVEKAGAHLKGGAKRVIIS 80
Cdd:PTZ00023   42 MCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKDPAAIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMS 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051  81 AP-SVDAPMFVMGVNHRKYDNFLKIVRNASCTTNCLAPLTKVIHDNFVILEGLMTTVHAITATQKTVNGSS--GKLWCDG 157
Cdd:PTZ00023  122 APpKDDTPIYVMGVNHTQYDKSQRIVSNASCTTNCLAPLAKVVNDKFGIVEGLMTTVHASTANQLTVDGPSkgGKDWRAG 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 158 CGAAQNIIPASTGAAKAVGKVISELNGKLTGMGFRVPTPNVSIVDLTCRLEKPAKYDDIKMVMKQVSEGPLKGILGYTED 237
Cdd:PTZ00023  202 RCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVPDVSVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDD 281

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958682051 238 KVVSCDFKSNSHSSTFDAGAGIALNDKFVKLISWYDNEYGYSNRVVDLMAYMVSKE 293
Cdd:PTZ00023  282 EVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDNEWGYSNRLLDLAHYITQKY 337
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 1-284 2.67e-139

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: 395.88  E-value: 2.67e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051   1 MVYMFQYDSTHDKFNGTVKAGNEKLVINGKPIT-IFQERDPANIKWGDAGAEYVMESTGIFTTVEKAGAHLKGGAKRVII 79
Cdd:TIGR01534  40 LAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEVIsVFSERDPSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051  80 SAPSVDA-PMFVMGVNHRKYDNFLKIVRNASCTTNCLAPLTKVIHDNFVILEGLMTTVHAITATQKTVNGSSGKlWCDGC 158
Cdd:TIGR01534 120 SAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLAPLAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKD-LRRAR 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 159 GAAQNIIPASTGAAKAVGKVISELNGKLTGMGFRVPTPNVSIVDLTCRLEKPAKYDDIKMVMKQVSEGPLKGILGYTEDK 238
Cdd:TIGR01534 199 AAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNVSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDE 278

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1958682051 239 VVSCDFKSNSHSSTFDAGAGIA--LNDKFVKLISWYDNEYGYSNRVVD 284
Cdd:TIGR01534 279 LVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNEWGYSNRLVD 326
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
 1-289 3.06e-133

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 380.99  E-value: 3.06e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051   1 MVYMFQYDSTHDKF-NGTVKAGNEKLVING-KPITIFQERDPANIKWGDAGAEYVMESTGIFTTVEKAGAHLKGGAKRVI 78
Cdd:PLN02358   45 MTYMFKYDSVHGQWkHHELKVKDDKTLLFGeKPVTVFGIRNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVV 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051  79 ISAPSVDAPMFVMGVNHRKYDNFLKIVRNASCTTNCLAPLTKVIHDNFVILEGLMTTVHAITATQKTVNGSSGKLWCDGC 158
Cdd:PLN02358  125 ISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCTTNCLAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGR 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 159 GAAQNIIPASTGAAKAVGKVISELNGKLTGMGFRVPTPNVSIVDLTCRLEKPAKYDDIKMVMKQVSEGPLKGILGYTEDK 238
Cdd:PLN02358  205 AASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDD 284

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958682051 239 VVSCDFKSNSHSSTFDAGAGIALNDKFVKLISWYDNEYGYSNRVVDLMAYM 289
Cdd:PLN02358  285 VVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEWGYSSRVVDLIVHM 335
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
1-289 2.55e-129

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 370.99  E-value: 2.55e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051   1 MVYMFQYDSTHDKFNGTVKAGNEKLVINGKPITIFQERDPANIKWGDAGAEYVMESTGIFTTVEKAGAHLKGGAKRVIIS 80
Cdd:PRK15425   41 MAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMT 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051  81 APSVD-APMFVMGVNHRKYDNfLKIVRNASCTTNCLAPLTKVIHDNFVILEGLMTTVHAITATQKTVNGSSGKLWCDGCG 159
Cdd:PRK15425  121 GPSKDnTPMFVKGANFDKYAG-QDIVSNASCTTNCLAPLAKVINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRG 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 160 AAQNIIPASTGAAKAVGKVISELNGKLTGMGFRVPTPNVSIVDLTCRLEKPAKYDDIKMVMKQVSEGPLKGILGYTEDKV 239
Cdd:PRK15425  200 ASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDV 279

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958682051 240 VSCDFKSNSHSSTFDAGAGIALNDKFVKLISWYDNEYGYSNRVVDLMAYM 289
Cdd:PRK15425  280 VSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYSNKVLDLIAHI 329
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-292 8.19e-110

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 321.69  E-value: 8.19e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051   1 MVYMFQYDSTHDKFNGTVKAGNEKLVINGKPITIFQERDPANIKWGDAGAEYVMESTGIFTTVEKAGAHLKGGAKRVIIS 80
Cdd:PRK07729   41 LAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDPKELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILT 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051  81 APSVDAPM-FVMGVNHRKYD-NFLKIVRNASCTTNCLAPLTKVIHDNFVILEGLMTTVHAITATQKTVNGSSGKLW-CDG 157
Cdd:PRK07729  121 APGKNEDVtIVVGVNEDQLDiEKHTIISNASCTTNCLAPVVKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHKDLRrARA 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 158 CGaaQNIIPASTGAAKAVGKVISELNGKLTGMGFRVPTPNVSIVDLTCRLEKPAKYDDIKMVMKQVSEGPLKGILGYTED 237
Cdd:PRK07729  201 CG--QSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNVSLVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEE 278

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958682051 238 KVVSCDFKSNSHSSTFDAGAGIALNDKFVKLISWYDNEYGYSNRVVDLMAYMVSK 292
Cdd:PRK07729  279 PLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEWGYSCRVVDLVTLVADE 333
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 3-293 3.62e-108

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 318.15  E-value: 3.62e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051   3 YMFQYDSTHDKFNGTVKAGNEK--------LVINGKPITIFQ-ERDPANIKWGDAGAEYVMESTGIFTTVEKAGAHLKGG 73
Cdd:PTZ00434   49 YQMKYDTVHGRPKYTVETTKSSpsvktddvLVVNGHRIKCVKaQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGG 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051  74 AKRVIISAP-SVDAPMFVMGVNHRKYD-NFLKIVRNASCTTNCLAPLTKVI-HDNFVILEGLMTTVHAITATQKTVNGSS 150
Cdd:PTZ00434  129 AKKVVISAPaSGGAKTIVMGVNQHEYSpTEHHVVSNASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVS 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 151 GKLWCDGCGAAQNIIPASTGAAKAVGKVISELNGKLTGMGFRVPTPNVSIVDLTCRLEKPAKYDDIKMVMKQVSEGPLKG 230
Cdd:PTZ00434  209 VKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKG 288

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958682051 231 ILGYTEDKVVSCDFKSNSHSSTFDAGAGIALN----DKFVKLISWYDNEYGYSNRVVDLMAYMVSKE 293
Cdd:PTZ00434  289 ILGFTDDELVSADFINDNRSSIYDSKATLQNNlpgeRRFFKIVSWYDNEWGYSHRVVDLVRYMAAKD 355
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 110-275 1.31e-106

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: 306.69  E-value: 1.31e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 110 CTTNCLAPLTKVIHDNFVILEGLMTTVHAITATQKTVNGSSgKLWCDGCGAAQNIIPASTGAAKAVGKVISELNGKLTGM 189
Cdd:cd18126     1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 190 GFRVPTPNVSIVDLTCRLEKPAKYDDIKMVMKQVSEGPLKGILGYTEDKVVSCDFKSNSHSSTFDAGAGIALNDKFVKLI 269
Cdd:cd18126    80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159


                  ....*.
gi 1958682051 270 SWYDNE 275
Cdd:cd18126   160 AWYDNE 165
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
3-292 2.07e-99

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 294.89  E-value: 2.07e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051   3 YMFQYDSTHDKFNGTVKAGNEKLVINGKPITIFQERDPANIKWGDAGAEYVMESTGIFTTVEKAGAHLKGGAKRVIISAP 82
Cdd:PRK07403   44 HLLKYDSMLGKLNADISADENSITVNGKTIKCVSDRNPLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAP 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051  83 --SVDAPMFVMGVNHRKYD-NFLKIVRNASCTTNCLAPLTKVIHDNFVILEGLMTTVHAITATQKTVNGSSGKLWcDGCG 159
Cdd:PRK07403  124 gkGEDIGTYVVGVNHHEYDhEDHNIISNASCTTNCLAPIAKVLHDNFGIIKGTMTTTHSYTGDQRILDASHRDLR-RARA 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 160 AAQNIIPASTGAAKAVGKVISELNGKLTGMGFRVPTPNVSIVDLTCRLEKPAKYDDIKMVMKQVSEGPLKGILGYTEDKV 239
Cdd:PRK07403  203 AAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTPNVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPL 282

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958682051 240 VSCDFKSNSHSSTFDAGAGIALNDKFVKLISWYDNEYGYSNRVVDLMAYMVSK 292
Cdd:PRK07403  283 VSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYDNEWGYSQRVVDLAELVARK 335
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
 3-285 1.12e-89

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 272.19  E-value: 1.12e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051   3 YMFQYDSTHDKFNGTVKA-GNEKLVINGKPITIFQERDPANIKWGDAGAEYVMESTGIFTTVEKAGAHLKGGAKRVIISA 81
Cdd:PLN03096  103 HLLKYDSTLGTFDADVKPvGDDAISVDGKVIKVVSDRNPLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITA 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051  82 PSV-DAPMFVMGVNHRKYDNFLKIVRNASCTTNCLAPLTKVIHDNFVILEGLMTTVHAITATQKTVNGSSGKLWcDGCGA 160
Cdd:PLN03096  183 PGKgDIPTYVVGVNADDYKHSDPIISNASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLR-RARAA 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 161 AQNIIPASTGAAKAVGKVISELNGKLTGMGFRVPTPNVSIVDLTCRLEKPAKYDDIKMVMKQVSEGPLKGILGYTEDKVV 240
Cdd:PLN03096  262 ALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLV 341

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1958682051 241 SCDFKSNSHSSTFDAGAGIALNDKFVKLISWYDNEYGYSNRVVDL 285
Cdd:PLN03096  342 SVDFRCSDVSSTIDSSLTMVMGDDMVKVVAWYDNEWGYSQRVVDL 386
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
 3-292 2.70e-88

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 270.23  E-value: 2.70e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051   3 YMFQYDSTHDKFNGTVK-AGNEKLVINGKPITIFQERDPANIKWGDAGAEYVMESTGIFTTVEKAGAHLKGGAKRVIISA 81
Cdd:PLN02237  118 HLLKYDSMLGTFKADVKiVDDETISVDGKPIKVVSNRDPLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITA 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051  82 PS--VDAPMFVMGVNHRKYDN-FLKIVRNASCTTNCLAPLTKVIHDNFVILEGLMTTVHAITATQKTVNGSSGKLWcDGC 158
Cdd:PLN02237  198 PAkgADIPTYVVGVNEDDYDHeVANIVSNASCTTNCLAPFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDASHRDLR-RAR 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 159 GAAQNIIPASTGAAKAVGKVISELNGKLTGMGFRVPTPNVSIVDLTCRLEKPA-KYDDIKMVMKQVSEGPLKGILGYTED 237
Cdd:PLN02237  277 AAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTPNVSVVDLVVNVEKKGiTAEDVNAAFRKAADGPLKGILAVCDV 356

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958682051 238 KVVSCDFKSNSHSSTFDAGAGIALNDKFVKLISWYDNEYGYSNRVVDLmAYMVSK 292
Cdd:PLN02237  357 PLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVAWYDNEWGYSQRVVDL-AHLVAA 410
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
6-285 3.28e-88

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 266.03  E-value: 3.28e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051   6 QYDSTHDKFNGTVKAGNEKLVINGKPITIFQERDPANIKWGDaGAEYVMESTGIFTTVEKAGAHLKGGAKRVIISAP--S 83
Cdd:NF033735   43 EFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDTPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkE 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051  84 VDAPMFVMGVNHRKYD-NFLKIVRNASCTTNCLAPLTKVIHDNFVILEGLMTTVHAITATQKTVNGSSGKL-WCDGCGaa 161
Cdd:NF033735  122 EGVLNIVYGVNDHLYDpARHRIVTAASCTTNCLAPVVKVIHEKIGIKHGSITTIHDITNTQTIVDAPHKDLrRARSCG-- 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 162 QNIIPASTGAAKAVGKVISELNGKLTGMGFRVPTPNVSIVDLTCRLEKPAKYDDIKMVMKQVSEGPLKGILGYTEDKVVS 241
Cdd:NF033735  200 MSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASLTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVS 279

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958682051 242 CDFKSNSHSSTFDAGAGIALNDKFVKLISWYDNEYGYSNRVVDL 285
Cdd:NF033735  280 VDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYANRMVDL 323
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 110-275 1.05e-80

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: 240.98  E-value: 1.05e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 110 CTTNCLAPLTKVIHDNFVILEGLMTTVHAITATQKTVNGSSGKLWCDGCGAAQNIIPASTGAAKAVGKVISELNGKLTGM 189
Cdd:cd18123     1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 190 GFRVPTPNVSIVDLTCRLEKPAKYDDIKMVMKQVSEGplKGILGYTEDKVVSCDFKSNSHSSTFDAGAGIALNDKFVKLI 269
Cdd:cd18123    81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLM 158


                  ....*.
gi 1958682051 270 SWYDNE 275
Cdd:cd18123   159 QWYDNE 164
PRK08955 PRK08955
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-286 4.28e-78

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 169599 [Multi-domain]  Cd Length: 334  Bit Score: 240.40  E-value: 4.28e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051   1 MVYMFQYDSTHDKFNGTVKAGNEKLVINGKPITIFQERDPANIKWgdAGAEYVMESTGIFTTVEKAGAHLKGGAKRVIIS 80
Cdd:PRK08955   42 LAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKAIADTDW--SGCDVVIEASGVMKTKALLQAYLDQGVKRVVVT 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051  81 APSVDAPMF--VMGVNHRKYDNFL-KIVRNASCTTNCLAPLTKVIHDNFVILEGLMTTVHAITATQKTVNGSSGKLW-CD 156
Cdd:PRK08955  120 APVKEEGVLniVMGVNDHLFDPAIhPIVTAASCTTNCLAPVVKVIHEKLGIKHGSMTTIHDLTNTQTILDAPHKDLRrAR 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 157 GCGaaQNIIPASTGAAKAVGKVISELNGKLTGMGFRVPTPNVSIVDLTCRLEKPAKYDDIKMVMKQVSEGPLKGILGYTE 236
Cdd:PRK08955  200 ACG--MSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLANASLTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEE 277

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958682051 237 DKVVSCDFKSNSHSSTFDAGAGIALNDKFVKLISWYDNEYGYSNRVVDLM 286
Cdd:PRK08955  278 RPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNEWGYANRTAELA 327
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 115-272 5.02e-78

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: 234.02  E-value: 5.02e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 115 LAPLTKVIHDNFVILEGLMTTVHAITATQKTVNGSSGKLWCDGCGAAQNIIPASTGAAKAVGKVISELNGKLTGMGFRVP 194
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958682051 195 TPNVSIVDLTCRLEKPAKYDDIKMVMKQVSEGPLKGILGYTEDKVVSCDFKSNSHSSTFDAGAGIALNDKFVKLISWY 272
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
PRK08289 PRK08289
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
 6-289 1.51e-69

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 236219 [Multi-domain]  Cd Length: 477  Bit Score: 222.88  E-value: 1.51e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051   6 QYDSTHDKFNGTVKAG--NEKLVINGKPITIFQERDPANI---KWG--DAgaeYVMESTGIFTTVEKAGAHLKG-GAKRV 77
Cdd:PRK08289  179 RRDSVHGPFNGTITVDeeNNAIIANGNYIQVIYANSPEEVdytAYGinNA---LVVDNTGKWRDEEGLSQHLKSkGVAKV 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051  78 IISAPSV-DAPMFVMGVNHRKYDNFLKIVRNASCTTNCLAPLTKVIHDNFVILEGLMTTVHAITATQKTV-NGSSGklwc 155
Cdd:PRK08289  256 LLTAPGKgDIKNIVHGVNHSDITDEDKIVSAASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIdNYHKG---- 331

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 156 D--GCGAAQNIIPASTGAAKAVGKVISELNGKLTGMGFRVPTPNVSIVDLTCRLEKPAKYDDIKMVMKQVS-EGPLKGIL 232
Cdd:PRK08289  332 DrrGRSAPLNMVITETGAAKAVAKALPELAGKLTGNAIRVPTPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQI 411

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958682051 233 GYTEDK-VVSCDFKSNSHSSTFDAGAGIAlNDKFVKLISWYDNEYGYSNRVVDLMAYM 289
Cdd:PRK08289  412 DYTDSTeVVSSDFVGSRHAGVVDSQATIV-NGNRAVLYVWYDNEFGYSCQVVRVMEQM 468
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
 1-284 1.77e-69

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 218.39  E-value: 1.77e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051   1 MVYMFQYDSTHDKFNGTVKAGNEKLVINGKPITIFQERDPANIKWGDAGAEYVMESTGIFTTVEKAGAHLKGGAKRVIIS 80
Cdd:PRK13535   43 MAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHERDIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFS 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051  81 APS---VDAPMfVMGVNHRKYDNFLKIVRNASCTTNCLAPLTKVIHDNFVILEGLMTTVHAITATQKTVNGSSGKLWcDG 157
Cdd:PRK13535  123 HPGsndLDATV-VYGVNHDQLRAEHRIVSNASCTTNCIIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHPDLR-RT 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 158 CGAAQNIIPASTGAAKAVGKVISELNGKLTGMGFRVPTPNVSIVDLTCRLEKPAKYDDIKMVMKQVSEGPLKGILGYTED 237
Cdd:PRK13535  201 RAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPTINVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTEL 280

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1958682051 238 KVVSCDFKSNSHSSTFDAGAGIALNDKFVKLISWYDNEYGYSNRVVD 284
Cdd:PRK13535  281 PLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNEWGFANRMLD 327
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 1-109 4.00e-59

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: 186.06  E-value: 4.00e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051   1 MVYMFQYDSTHDKFNGTVKAGNEKLVINGKPITIFQERDPANIKWGDAGAEYVMESTGIFTTVEKAGAHLKGGAKRVIIS 80
Cdd:cd05214    39 LAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAELPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIIS 118

                          90       100       110
                  ....*....|....*....|....*....|
gi 1958682051  81 APSVD-APMFVMGVNHRKYDNFLKIVRNAS 109
Cdd:cd05214   119 APAKDdDPTIVMGVNHDKYDADDKIISNAS 148
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-110 2.50e-55

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: 175.82  E-value: 2.50e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051    1 MVYMFQYDSTHDKFNGTVKAGNEKLVINGKPITIFQERDPANIKWGDAGAEYVMESTGIFTTVEKAGAHLKGGAKRVIIS 80
Cdd:smart00846  39 LAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIIS 118

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1958682051   81 APSVDA-PMFVMGVNHRKYDNFLKIVRNASC 110
Cdd:smart00846 119 APSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
GAPDH_C_E4PDH cd23937
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 110-275 9.03e-42

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: 141.78  E-value: 9.03e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 110 CTTNCLAPLTKVIHDNFVILEGLMTTVHAITATQKTVNGSSGKLWCDGCgAAQNIIPASTGAAKAVGKVISELNGKLTGM 189
Cdd:cd23937     1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDAYHPDLRRTRA-ASQSIIPVDTKLARGIERILPHLAGRFEAI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 190 GFRVPTPNVSIVDLTCRLEKPAKYDDIKMVMKQVSEGPLKGILGYTEDKVVSCDFKSNSHSSTFDAGAGIALNDKFVKLI 269
Cdd:cd23937    80 AVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLL 159


                  ....*.
gi 1958682051 270 SWYDNE 275
Cdd:cd23937   160 VWCDNE 165
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 110-275 5.14e-39

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: 134.57  E-value: 5.14e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 110 CTTNCLAPLTKVIHDNFVILEGLMTTVHAITATQKTVNGSSGKLWCDGcgAAQNIIPASTGAAKAVGKVISELN--GKLT 187
Cdd:cd18122     1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSEVRA--IIPNIPKNETKHAPETGKVLGEIGkpIKVD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 188 GMGFRVPTPNVSIVDLTCRLEKPAKYDDIKMVMKQVSEGPLKGILGYTEDKVVSCDFKSNSHSSTFDAGAGIALNDKFVK 267
Cdd:cd18122    79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLK 158


                  ....*...
gi 1958682051 268 LISWYDNE 275
Cdd:cd18122   159 VFSAVDNE 166
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
 1-289 3.76e-37

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 135.00  E-value: 3.76e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051   1 MVYMFQYDSTHDKFNGT-VKAGNEKLVING-KPITIFQERDPANIKWGDAGAEYVMESTGIFTTVEKAGAHLKGGAKRVI 78
Cdd:PTZ00353   42 IAYVLEQESPLSAPDGAsIRVVGEQIVLNGtQKIRVSAKHDLVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVF 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051  79 ISAPSVDAPMFVMGVNHRKYDNFLKIVRNASCTTNCLAPLTKVIHDNFVILEGLMTTVHAITATQKTVNGS-SGKLWCDG 157
Cdd:PTZ00353  122 VAGQSADAPTVMAGSNDERLSASLPVCCAGAPIAVALAPVIRALHEVYGVEECSYTAIHGMQPQEPIAARSkNSQDWRQT 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051 158 CGAAQNIIPASTGAAKAVGKVISELNGKLTGMGFRVPTPNVSIVDLTCRLEKPAKYDDIKMVMKQVSEGPLKGILGYTED 237
Cdd:PTZ00353  202 RVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVKKGCAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKR 281

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958682051 238 KVVSCDFKSNShSSTFDAGAGIALND-KFVKLISWYDNEYGYSNRVVDLMAYM 289
Cdd:PTZ00353  282 DMISVDCIPNG-KLCYDATSSSSSREgEVHKMVLWFDVECYYAARLLSLVKQL 333
GAPDH_N_E4PDH cd17892
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 1-109 3.37e-30

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: 111.59  E-value: 3.37e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958682051   1 MVYMFQYDSTHDKFNGTVKAGNEKLVINGKPITIFQERDPANIKWGDAGAEYVMESTGIFTTVEKAGAHLKGGAKRVIIS 80
Cdd:cd17892    42 IAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPDPENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFS 121

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1958682051  81 APS---VDAPMfVMGVNHRKYDNFLKIVRNAS 109
Cdd:cd17892   122 HPAsndVDATI-VYGINQDLLRAEHRIVSNAS 152
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-62 4.17e-28

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: 104.11  E-value: 4.17e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958682051   1 MVYMFQYDSTHDKFNGTVKAGNEKLVINGKPITIFQERDPANIKWGDAGAEYVMESTGIFTT 62
Cdd:pfam00044  39 LAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAELPWGDLGVDVVIESTGVFTT 100
GAPDH-like_N cd05192
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ...
 51-114 8.89e-06

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: 43.88  E-value: 8.89e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958682051  51 EYVMESTGIFTTVEKAGAHLKGGAKRVIISAPSV-DAPMFVMGVNHRKYDNFLKIVRNASCTTNC 114
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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