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Conserved domains on  [gi|1276317824|ref|NP_001344872|]
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glyceraldehyde-3-phosphate dehydrogenase isoform 4 [Homo sapiens]

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
 2-314 0e+00

glyceraldehyde-3-phosphate dehydrogenase


The actual alignment was detected with superfamily member PLN02272:

Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 561.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824   2 GKVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMA-------------------ENGKLVINGNPITIFQER 62
Cdd:PLN02272   84 GKTKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAymfkydsthgnfkgtinvvDDSTLEINGKQIKVTSKR 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824  63 DPSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAPL 142
Cdd:PLN02272  164 DPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPL 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 143 AKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANV 222
Cdd:PLN02272  244 AKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNV 323

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 223 SVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGY 302
Cdd:PLN02272  324 SVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGY 403

                         330
                  ....*....|..
gi 1276317824 303 SNRVVDLMAHMA 314
Cdd:PLN02272  404 SNRVLDLIEHMA 415
 
Name Accession Description Interval E-value
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 2-314 0e+00

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 561.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824   2 GKVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMA-------------------ENGKLVINGNPITIFQER 62
Cdd:PLN02272   84 GKTKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAymfkydsthgnfkgtinvvDDSTLEINGKQIKVTSKR 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824  63 DPSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAPL 142
Cdd:PLN02272  164 DPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPL 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 143 AKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANV 222
Cdd:PLN02272  244 AKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNV 323

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 223 SVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGY 302
Cdd:PLN02272  324 SVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGY 403

                         330
                  ....*....|..
gi 1276317824 303 SNRVVDLMAHMA 314
Cdd:PLN02272  404 SNRVLDLIEHMA 415
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 3-317 0e+00

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: 539.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824   3 KVKVGVNGFGRIGRLVTRAAFNSGK-VDIVAINDPfIDLNYMA------------------ENGKLVINGNPITIFQERD 63
Cdd:COG0057     2 TIRVAINGFGRIGRLVLRALLERGPdIEVVAINDL-GDAETLAhllkydsvhgrfpgevevEGDSLIVNGKKIKVLAERD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824  64 PSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPSADA-PMFVMGVNHEKYDNSLKIISNASCTTNCLAPL 142
Cdd:COG0057    81 PAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAPV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 143 AKVIHDNFGIVEGLMTTVHAITATQKTVDGPsGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANV 222
Cdd:COG0057   161 AKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 223 SVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGY 302
Cdd:COG0057   240 SLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGY 319

                         330
                  ....*....|....*
gi 1276317824 303 SNRVVDLMAHMASKE 317
Cdd:COG0057   320 SNRMVDLAEYMAKLL 334
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 5-308 2.26e-157

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: 442.49  E-value: 2.26e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824   5 KVGVNGFGRIGRLVTRAAFNSG--KVDIVAINDPfIDLNYMA------------------ENGKLVINGNPIT-IFQERD 63
Cdd:TIGR01534   1 KVGINGFGRIGRLVLRRILEKPgnDLEVVAINDL-TDLEKLAyllkydsvhgrfegevtvDEDGLVVNGKEVIsVFSERD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824  64 PSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPSADA-PMFVMGVNHEKYDNSLKIISNASCTTNCLAPL 142
Cdd:TIGR01534  80 PSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLAPL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 143 AKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKlWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANV 222
Cdd:TIGR01534 160 AKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKD-LRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 223 SVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIA--LNDHFVKLISWYDNEF 300
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNEW 318


                  ....*...
gi 1276317824 301 GYSNRVVD 308
Cdd:TIGR01534 319 GYSNRLVD 326
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 134-299 5.53e-120

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: 341.74  E-value: 5.53e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 134 CTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSgKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGM 213
Cdd:cd18126     1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 214 AFRVPTANVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLI 293
Cdd:cd18126    80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159


                  ....*.
gi 1276317824 294 SWYDNE 299
Cdd:cd18126   160 AWYDNE 165
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
6-309 7.01e-111

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 324.58  E-value: 7.01e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824   6 VGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFID-------LNY-----------MAENGKLVINGNPITIFQERDPSKI 67
Cdd:NF033735    1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDaatlahlLEFdsvhgrwdaevTAEEDSIVIDGKRISFSSNKDIEDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824  68 KWGDaGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAP--SADAPMFVMGVNHEKYDNSL-KIISNASCTTNCLAPLAK 144
Cdd:NF033735   81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARhRIVTAASCTTNCLAPVVK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 145 VIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLwRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANVSV 224
Cdd:NF033735  160 VIHEKIGIKHGSITTIHDITNTQTIVDAPHKDL-RRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 225 VDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGYSN 304
Cdd:NF033735  239 TDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYAN 318


                  ....*
gi 1276317824 305 RVVDL 309
Cdd:NF033735  319 RMVDL 323
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 139-296 1.75e-90

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: 266.77  E-value: 1.75e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 139 LAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVP 218
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1276317824 219 TANVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWY 296
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 4-134 4.89e-66

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: 203.94  E-value: 4.89e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824    4 VKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPfIDLNYMA------------------ENGKLVINGNPITIFQERDPS 65
Cdd:smart00846   1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDL-TDPEYLAyllkydsvhgrfpgtvevEGDGLVVNGKAIKVFAERDPA 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824   66 KIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPSADA-PMFVMGVNHEKYDNSLKIISNASC 134
Cdd:smart00846  80 NLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
 
Name Accession Description Interval E-value
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 2-314 0e+00

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 561.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824   2 GKVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMA-------------------ENGKLVINGNPITIFQER 62
Cdd:PLN02272   84 GKTKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAymfkydsthgnfkgtinvvDDSTLEINGKQIKVTSKR 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824  63 DPSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAPL 142
Cdd:PLN02272  164 DPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPL 243

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 143 AKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANV 222
Cdd:PLN02272  244 AKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNV 323

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 223 SVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGY 302
Cdd:PLN02272  324 SVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGY 403

                         330
                  ....*....|..
gi 1276317824 303 SNRVVDLMAHMA 314
Cdd:PLN02272  404 SNRVLDLIEHMA 415
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 3-317 0e+00

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: 539.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824   3 KVKVGVNGFGRIGRLVTRAAFNSGK-VDIVAINDPfIDLNYMA------------------ENGKLVINGNPITIFQERD 63
Cdd:COG0057     2 TIRVAINGFGRIGRLVLRALLERGPdIEVVAINDL-GDAETLAhllkydsvhgrfpgevevEGDSLIVNGKKIKVLAERD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824  64 PSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPSADA-PMFVMGVNHEKYDNSLKIISNASCTTNCLAPL 142
Cdd:COG0057    81 PAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAPV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 143 AKVIHDNFGIVEGLMTTVHAITATQKTVDGPsGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANV 222
Cdd:COG0057   161 AKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 223 SVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGY 302
Cdd:COG0057   240 SLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGY 319

                         330
                  ....*....|....*
gi 1276317824 303 SNRVVDLMAHMASKE 317
Cdd:COG0057   320 SNRMVDLAEYMAKLL 334
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
 4-317 5.71e-171

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 477.40  E-value: 5.71e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824   4 VKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMA------------------ENGKLVINGNPITIFQERDPS 65
Cdd:PTZ00023    3 VKLGINGFGRIGRLVFRAALEREDVEVVAINDPFMTLDYMCyllkydsvhgslpaevsvTDGFLMIGSKKVHVFFEKDPA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824  66 KIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAP-SADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAPLAK 144
Cdd:PTZ00023   83 AIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPpKDDTPIYVMGVNHTQYDKSQRIVSNASCTTNCLAPLAK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 145 VIHDNFGIVEGLMTTVHAITATQKTVDGPS--GKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANV 222
Cdd:PTZ00023  163 VVNDKFGIVEGLMTTVHASTANQLTVDGPSkgGKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVPDV 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 223 SVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGY 302
Cdd:PTZ00023  243 SVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDNEWGY 322

                         330
                  ....*....|....*
gi 1276317824 303 SNRVVDLMAHMASKE 317
Cdd:PTZ00023  323 SNRLLDLAHYITQKY 337
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 5-308 2.26e-157

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: 442.49  E-value: 2.26e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824   5 KVGVNGFGRIGRLVTRAAFNSG--KVDIVAINDPfIDLNYMA------------------ENGKLVINGNPIT-IFQERD 63
Cdd:TIGR01534   1 KVGINGFGRIGRLVLRRILEKPgnDLEVVAINDL-TDLEKLAyllkydsvhgrfegevtvDEDGLVVNGKEVIsVFSERD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824  64 PSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPSADA-PMFVMGVNHEKYDNSLKIISNASCTTNCLAPL 142
Cdd:TIGR01534  80 PSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLAPL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 143 AKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKlWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANV 222
Cdd:TIGR01534 160 AKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKD-LRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 223 SVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIA--LNDHFVKLISWYDNEF 300
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNEW 318


                  ....*...
gi 1276317824 301 GYSNRVVD 308
Cdd:TIGR01534 319 GYSNRLVD 326
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
 3-314 1.82e-151

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 428.37  E-value: 1.82e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824   3 KVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMA--------------------ENGKLVINGNPITIFQER 62
Cdd:PLN02358    5 KIRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTymfkydsvhgqwkhhelkvkDDKTLLFGEKPVTVFGIR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824  63 DPSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAPL 142
Cdd:PLN02358   85 NPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCTTNCLAPL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 143 AKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANV 222
Cdd:PLN02358  165 AKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDV 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 223 SVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGY 302
Cdd:PLN02358  245 SVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEWGY 324

                         330
                  ....*....|..
gi 1276317824 303 SNRVVDLMAHMA 314
Cdd:PLN02358  325 SSRVVDLIVHMS 336
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
4-314 5.74e-142

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 403.73  E-value: 5.74e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824   4 VKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDpFIDLNYMA------------------ENGKLVINGNPITIFQERDPS 65
Cdd:PRK15425    3 IKVGINGFGRIGRIVFRAAQKRSDIEIVAIND-LLDADYMAymlkydsthgrfdgtvevKDGHLIVNGKKIRVTAERDPA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824  66 KIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPSAD-APMFVMGVNHEKYDNSlKIISNASCTTNCLAPLAK 144
Cdd:PRK15425   82 NLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDnTPMFVKGANFDKYAGQ-DIVSNASCTTNCLAPLAK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 145 VIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANVSV 224
Cdd:PRK15425  161 VINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 225 VDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGYSN 304
Cdd:PRK15425  241 VDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYSN 320

                         330
                  ....*....|
gi 1276317824 305 RVVDLMAHMA 314
Cdd:PRK15425  321 KVLDLIAHIS 330
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 3-316 5.68e-128

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 368.68  E-value: 5.68e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824   3 KVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPF-----------------IDLNYMAENGKLVINGNPITIFQERDPS 65
Cdd:PRK07729    2 KTKVAINGFGRIGRMVFRKAIKESAFEIVAINASYpsetlahlikydtvhgkFDGTVEAFEDHLLVDGKKIRLLNNRDPK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824  66 KIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPSADAPM-FVMGVNHEKYD-NSLKIISNASCTTNCLAPLA 143
Cdd:PRK07729   82 ELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVtIVVGVNEDQLDiEKHTIISNASCTTNCLAPVV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 144 KVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLwRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANVS 223
Cdd:PRK07729  162 KVLDEQFGIENGLMTTVHAYTNDQKNIDNPHKDL-RRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNVS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 224 VVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGYS 303
Cdd:PRK07729  241 LVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEWGYS 320

                         330
                  ....*....|...
gi 1276317824 304 NRVVDLMAHMASK 316
Cdd:PRK07729  321 CRVVDLVTLVADE 333
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 1-317 6.51e-122

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 353.98  E-value: 6.51e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824   1 MGKVKVGVNGFGRIGRLVTRAAFNSG----KVDIVAINDPFIDLNYMAENGK--------------------------LV 50
Cdd:PTZ00434    1 MAPIKVGINGFGRIGRMVFQAICDQGligtEIDVVAVVDMSTNAEYFAYQMKydtvhgrpkytvettksspsvktddvLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824  51 INGNPITIFQ-ERDPSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAP-SADAPMFVMGVNHEKYD-NSLK 127
Cdd:PTZ00434   81 VNGHRIKCVKaQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPaSGGAKTIVMGVNQHEYSpTEHH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 128 IISNASCTTNCLAPLAKVI-HDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPEL 206
Cdd:PTZ00434  161 VVSNASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPST 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 207 NGKLTGMAFRVPTANVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALN 286
Cdd:PTZ00434  241 KGKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKATLQNN 320

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1276317824 287 ----DHFVKLISWYDNEFGYSNRVVDLMAHMASKE 317
Cdd:PTZ00434  321 lpgeRRFFKIVSWYDNEWGYSHRVVDLVRYMAAKD 355
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 134-299 5.53e-120

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: 341.74  E-value: 5.53e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 134 CTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSgKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGM 213
Cdd:cd18126     1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 214 AFRVPTANVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLI 293
Cdd:cd18126    80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159


                  ....*.
gi 1276317824 294 SWYDNE 299
Cdd:cd18126   160 AWYDNE 165
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
6-309 7.01e-111

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 324.58  E-value: 7.01e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824   6 VGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFID-------LNY-----------MAENGKLVINGNPITIFQERDPSKI 67
Cdd:NF033735    1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDaatlahlLEFdsvhgrwdaevTAEEDSIVIDGKRISFSSNKDIEDT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824  68 KWGDaGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAP--SADAPMFVMGVNHEKYDNSL-KIISNASCTTNCLAPLAK 144
Cdd:NF033735   81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARhRIVTAASCTTNCLAPVVK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 145 VIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLwRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANVSV 224
Cdd:NF033735  160 VIHEKIGIKHGSITTIHDITNTQTIVDAPHKDL-RRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 225 VDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFGYSN 304
Cdd:NF033735  239 TDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYAN 318


                  ....*
gi 1276317824 305 RVVDL 309
Cdd:NF033735  319 RMVDL 323
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
4-316 1.92e-109

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 321.47  E-value: 1.92e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824   4 VKVGVNGFGRIGRLVTRAAF--NSGKVDIVAINDPF-----------------IDLNYMAENGKLVINGNPITIFQERDP 64
Cdd:PRK07403    2 IRVAINGFGRIGRNFLRCWLgrENSQLELVAINDTSdprtnahllkydsmlgkLNADISADENSITVNGKTIKCVSDRNP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824  65 SKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAP--SADAPMFVMGVNHEKYD-NSLKIISNASCTTNCLAP 141
Cdd:PRK07403   82 LNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPgkGEDIGTYVVGVNHHEYDhEDHNIISNASCTTNCLAP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 142 LAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLwRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTAN 221
Cdd:PRK07403  162 IAKVLHDNFGIIKGTMTTTHSYTGDQRILDASHRDL-RRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTPN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 222 VSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFG 301
Cdd:PRK07403  241 VSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYDNEWG 320

                         330
                  ....*....|....*
gi 1276317824 302 YSNRVVDLMAHMASK 316
Cdd:PRK07403  321 YSQRVVDLAELVARK 335
PRK08955 PRK08955
glyceraldehyde-3-phosphate dehydrogenase; Validated
 3-310 1.33e-99

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 169599 [Multi-domain]  Cd Length: 334  Bit Score: 296.26  E-value: 1.33e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824   3 KVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFID-------LNY-----------MAENGKLVINGNPITIFQERDP 64
Cdd:PRK08955    2 TIKVGINGFGRIGRLALRAAWDWPELEFVQINDPAGDaatlahlLEFdsvhgrwhhevTAEGDAIVINGKRIRTTQNKAI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824  65 SKIKWgdAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPSADAPMF--VMGVNHEKYDNSL-KIISNASCTTNCLAP 141
Cdd:PRK08955   82 ADTDW--SGCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLniVMGVNDHLFDPAIhPIVTAASCTTNCLAP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 142 LAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLwRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTAN 221
Cdd:PRK08955  160 VVKVIHEKLGIKHGSMTTIHDLTNTQTILDAPHKDL-RRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLAN 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 222 VSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFG 301
Cdd:PRK08955  239 ASLTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNEWG 318


                  ....*....
gi 1276317824 302 YSNRVVDLM 310
Cdd:PRK08955  319 YANRTAELA 327
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
 3-316 5.44e-98

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 296.04  E-value: 5.44e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824   3 KVKVGVNGFGRIGRLVTRA--AFNSGKVDIVAINDP------------------FIDLNYMAENGKLVINGNPITIFQER 62
Cdd:PLN02237   75 KLKVAINGFGRIGRNFLRCwhGRKDSPLDVVVVNDSggvknashllkydsmlgtFKADVKIVDDETISVDGKPIKVVSNR 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824  63 DPSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPS--ADAPMFVMGVNHEKYDNSL-KIISNASCTTNCL 139
Cdd:PLN02237  155 DPLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAkgADIPTYVVGVNEDDYDHEVaNIVSNASCTTNCL 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 140 APLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLwRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPT 219
Cdd:PLN02237  235 APFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDASHRDL-RRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPT 313

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 220 ANVSVVDLTCRLEKPA-KYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDN 298
Cdd:PLN02237  314 PNVSVVDLVVNVEKKGiTAEDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVAWYDN 393

                         330
                  ....*....|....*...
gi 1276317824 299 EFGYSNRVVDLMAHMASK 316
Cdd:PLN02237  394 EWGYSQRVVDLAHLVAAK 411
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
 3-316 4.01e-97

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 292.22  E-value: 4.01e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824   3 KVKVGVNGFGRIGRLVTRA--AFNSGKVDIVAINDP------------------FIDLNYMAENGKLVINGNPITIFQER 62
Cdd:PLN03096   60 KIKVAINGFGRIGRNFLRCwhGRKDSPLDVVAINDTggvkqashllkydstlgtFDADVKPVGDDAISVDGKVIKVVSDR 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824  63 DPSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPS-ADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAP 141
Cdd:PLN03096  140 NPLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGkGDIPTYVVGVNADDYKHSDPIISNASCTTNCLAP 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 142 LAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLwRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTAN 221
Cdd:PLN03096  220 FVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDL-RRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPN 298

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 222 VSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNEFG 301
Cdd:PLN03096  299 VSVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAWYDNEWG 378

                         330
                  ....*....|....*
gi 1276317824 302 YSNRVVDLMAHMASK 316
Cdd:PLN03096  379 YSQRVVDLADIVANK 393
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 134-299 9.02e-95

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: 277.96  E-value: 9.02e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 134 CTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGM 213
Cdd:cd18123     1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 214 AFRVPTANVSVVDLTCRLEKPAKYDDIKKVVKQASEGplKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLI 293
Cdd:cd18123    81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLM 158


                  ....*.
gi 1276317824 294 SWYDNE 299
Cdd:cd18123   159 QWYDNE 164
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 139-296 1.75e-90

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: 266.77  E-value: 1.75e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 139 LAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVP 218
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1276317824 219 TANVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWY 296
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
 4-314 2.51e-86

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 262.69  E-value: 2.51e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824   4 VKVGVNGFGRIGRLVTRAAFNSGK---VDIVAINDpFIDLNYMA------------------ENGKLVINGNPITIFQER 62
Cdd:PRK13535    2 IRVAINGFGRIGRNVLRALYESGRraeITVVAINE-LADAEGMAhllkydtshgrfawdvrqERDQLFVGDDAIRLLHER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824  63 DPSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPSA---DAPMfVMGVNHEKYDNSLKIISNASCTTNCL 139
Cdd:PRK13535   81 DIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSndlDATV-VYGVNHDQLRAEHRIVSNASCTTNCI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 140 APLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLwRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPT 219
Cdd:PRK13535  160 IPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHPDL-RRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPT 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 220 ANVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLISWYDNE 299
Cdd:PRK13535  239 INVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNE 318

                         330
                  ....*....|....*
gi 1276317824 300 FGYSNRVVDLMAHMA 314
Cdd:PRK13535  319 WGFANRMLDTTLAMA 333
PRK08289 PRK08289
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
 10-314 1.57e-76

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 236219 [Multi-domain]  Cd Length: 477  Bit Score: 241.75  E-value: 1.57e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824  10 GFGRIGRLVTR----AAFNSGKVDIVAI-------ND---------------PF-----IDlnymAENGKLVINGNPITI 58
Cdd:PRK08289  134 GFGRIGRLLARllieKTGGGNGLRLRAIvvrkgseGDlekrasllrrdsvhgPFngtitVD----EENNAIIANGNYIQV 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824  59 FQERDPSKI---KWG--DAgaeYVVESTGVFTTMEKAGAHLQG-GAKRVIISAPS-ADAPMFVMGVNHEKYDNSLKIISN 131
Cdd:PRK08289  210 IYANSPEEVdytAYGinNA---LVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGkGDIKNIVHGVNHSDITDEDKIVSA 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 132 ASCTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSgKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLT 211
Cdd:PRK08289  287 ASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYH-KGDRRGRSAPLNMVITETGAAKAVAKALPELAGKLT 365

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 212 GMAFRVPTANVSVVDLTCRLEKPAKYDDIKKVVKQAS-EGPLKGILGYTE-HQVVSSDFNSDTHSSTFDAGAGIALNDHF 289
Cdd:PRK08289  366 GNAIRVPTPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQIDYTDsTEVVSSDFVGSRHAGVVDSQATIVNGNRA 445

                         330       340
                  ....*....|....*....|....*
gi 1276317824 290 VkLISWYDNEFGYSNRVVDLMAHMA 314
Cdd:PRK08289  446 V-LYVWYDNEFGYSCQVVRVMEQMA 469
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 4-133 4.19e-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: 222.65  E-value: 4.19e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824   4 VKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDlNYMA------------------ENGKLVINGNPITIFQERDPS 65
Cdd:cd05214     1 IKVGINGFGRIGRLVFRAALERDDIEVVAINDLTDD-ETLAyllkydsvhgrfdgevevDDDALIVNGKKIKVFAERDPA 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276317824  66 KIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPSAD-APMFVMGVNHEKYDNSLKIISNAS 133
Cdd:cd05214    80 ELPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDADDKIISNAS 148
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 4-134 4.89e-66

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: 203.94  E-value: 4.89e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824    4 VKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPfIDLNYMA------------------ENGKLVINGNPITIFQERDPS 65
Cdd:smart00846   1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDL-TDPEYLAyllkydsvhgrfpgtvevEGDGLVVNGKAIKVFAERDPA 79

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824   66 KIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPSADA-PMFVMGVNHEKYDNSLKIISNASC 134
Cdd:smart00846  80 NLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
 4-313 4.10e-53

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 177.38  E-value: 4.10e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824   4 VKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFIDLNYMA-----------ENG--------KLVINGNP-ITIFQERD 63
Cdd:PTZ00353    3 ITVGINGFGPVGKAVLFASLTDPLVTVVAVNDASVSIAYIAyvleqesplsaPDGasirvvgeQIVLNGTQkIRVSAKHD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824  64 PSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPSADAPMFVMGVNHEKYDNSLKIISNASCTTNCLAPLA 143
Cdd:PTZ00353   83 LVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDERLSASLPVCCAGAPIAVALAPVI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 144 KVIHDNFGIVEGLMTTVHAITATQKT-VDGPSGKLWRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTANV 222
Cdd:PTZ00353  163 RALHEVYGVEECSYTAIHGMQPQEPIaARSKNSQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVKKG 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 223 SVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDThSSTFDAGAGIALNDHFV-KLISWYDNEFG 301
Cdd:PTZ00353  243 CAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCIPNG-KLCYDATSSSSSREGEVhKMVLWFDVECY 321

                         330
                  ....*....|..
gi 1276317824 302 YSNRVVDLMAHM 313
Cdd:PTZ00353  322 YAARLLSLVKQL 333
GAPDH_C_E4PDH cd23937
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 134-299 7.76e-51

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: 165.67  E-value: 7.76e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 134 CTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLwRDGRGALQNIIPASTGAAKAVGKVIPELNGKLTGM 213
Cdd:cd23937     1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDAYHPDL-RRTRAASQSIIPVDTKLARGIERILPHLAGRFEAI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 214 AFRVPTANVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVKLI 293
Cdd:cd23937    80 AVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLL 159


                  ....*.
gi 1276317824 294 SWYDNE 299
Cdd:cd23937   160 VWCDNE 165
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 134-299 5.17e-47

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: 156.14  E-value: 5.17e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 134 CTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWrdGRGALQNIIPASTGAAKAVGKVIPELN--GKLT 211
Cdd:cd18122     1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIGkpIKVD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824 212 GMAFRVPTANVSVVDLTCRLEKPAKYDDIKKVVKQASEGPLKGILGYTEHQVVSSDFNSDTHSSTFDAGAGIALNDHFVK 291
Cdd:cd18122    79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLK 158


                  ....*...
gi 1276317824 292 LISWYDNE 299
Cdd:cd18122   159 VFSAVDNE 166
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 4-86 4.62e-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: 125.29  E-value: 4.62e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824   4 VKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDpFIDLNYMA------------------ENGKLVINGNPITIFQERDPS 65
Cdd:pfam00044   1 VKVGINGFGRIGRLVLRAALERPDIEVVAIND-LTDPETLAyllkydsvhgrfpgeveaEEDGLVVNGKKIKVFAERDPA 79

                          90       100
                  ....*....|....*....|.
gi 1276317824  66 KIKWGDAGAEYVVESTGVFTT 86
Cdd:pfam00044  80 ELPWGDLGVDVVIESTGVFTT 100
GAPDH_N_E4PDH cd17892
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 4-133 2.55e-34

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: 123.15  E-value: 2.55e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824   4 VKVGVNGFGRIGRLVTRAAFNSGK---VDIVAINDPfIDLNYMA------------------ENGKLVINGNPITIFQER 62
Cdd:cd17892     1 YRVAINGYGRIGRNVLRALYESGRraeFQVVAINEL-ADAETIAhltkydtthgrfpgevrvENDQLFVNGDKIRVLHEP 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1276317824  63 DPSKIKWGDAGAEYVVESTGVFTTMEKAGAHLQGGAKRVIISAPSA---DAPMfVMGVNHEKYDNSLKIISNAS 133
Cdd:cd17892    80 DPENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASndvDATI-VYGINQDLLRAEHRIVSNAS 152
GAPDH-like_N cd05192
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ...
 4-138 3.28e-14

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: 67.76  E-value: 3.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317824   4 VKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPfidlnymaengklvingnpitifqerdpskikwgdagAEYVVESTGV 83
Cdd:cd05192     1 IRVAINGFGRIGRIVFRAIADQDDLDVVAINDR-------------------------------------RDVVIECTGS 43

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1276317824  84 FTTMEKAGAHLQGGAKRVIISAPS-ADAPMFVMGVNHEKYDNSLKIISNASCTTNC 138
Cdd:cd05192    44 FTDDDNAEKHIKAGGKKAVITAPEkGDIPTIVVVLNELAKSAGATVVSNANETSYS 99
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-39 5.55e-03

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 37.98  E-value: 5.55e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1276317824   1 MGKVKVGVNGFGRIGRLVTRAAFNSGKVDIVAINDPFID 39
Cdd:COG0673     1 MDKLRVGIIGAGGIGRAHAPALAALPGVELVAVADRDPE 39
 
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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