|
Name |
Accession |
Description |
Interval |
E-value |
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
2-333 |
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: 615.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 2 VKVAINGFGRIGRLALRKMMEQQDKFEVVAINDLTDAKMLAHLFKYDTAQGRFNGEIEVKEGAFVVNGKEIKVTAERNPA 81
Cdd:COG0057 3 IRVAINGFGRIGRLVLRALLERGPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 82 DLPWAELGVDIVLECTGFFTSKDKAEAHIQAGAKKVVISAPATGDLKTIVFNTNSDILDGSETVISGASCTTNCLAPMAK 161
Cdd:COG0057 83 ELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDDPTIVYGVNHDDYDADHRIISNASCTTNCLAPVAK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 162 VLNDKYGIEKGLMTTIHAYTNDQNTLDGPHpkGDLRRARAAAGNIVPNTTGAAKAIGLVIPSLKGKLDGAAQRVPVVTGS 241
Cdd:COG0057 163 VLNDAFGIEKGLMTTIHAYTNDQNLLDAPH--KDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 242 ITELVCTLGKNVTVEEINAAMKEASNES----FGYTEEMLVSSDIIGISYGSLFDATQTKVMevdGKQLVKVVSWYDNEM 317
Cdd:COG0057 241 LVDLTVELEKETTVEEVNAALKEAAEGPlkgiLGYTEEPLVSSDFNGDPHSSIFDALQTIVI---GGNLVKVLAWYDNEW 317
|
330
....*....|....*.
gi 489517139 318 SYTSQLIRTLGYFAQL 333
Cdd:COG0057 318 GYSNRMVDLAEYMAKL 333
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
3-325 |
0e+00 |
|
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: 515.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 3 KVAINGFGRIGRLALRKMMEQQD-KFEVVAINDLTDAKMLAHLFKYDTAQGRFNGEIEVKEGAFVVNGKE-IKVTAERNP 80
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKPGnDLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEvISVFSERDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 81 ADLPWAELGVDIVLECTGFFTSKDKAEAHIQAGAKKVVISAPATGDLKTIVFNTNSDILDGSETVISGASCTTNCLAPMA 160
Cdd:TIGR01534 81 SDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDVKTIVYGVNHDEYDGEERIISNASCTTNCLAPLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 161 KVLNDKYGIEKGLMTTIHAYTNDQNTLDGPHpkGDLRRARAAAGNIVPNTTGAAKAIGLVIPSLKGKLDGAAQRVPVVTG 240
Cdd:TIGR01534 161 KVLDEAFGIVSGLMTTVHAYTNDQNLLDGPH--KDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 241 SITELVCTLGKNVTVEEINAAMKEAS----NESFGYTEEMLVSSDIIGISYGSLFDATQTKVMEVDGKQlVKVVSWYDNE 316
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKEASegelKGVLGYTEDELVSSDFIGSPYSSIVDATATKVTGLGDSL-VKVYAWYDNE 317
|
....*....
gi 489517139 317 MSYTSQLIR 325
Cdd:TIGR01534 318 WGYSNRLVD 326
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-324 |
1.43e-143 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 409.13 E-value: 1.43e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 1 MVKVAINGFGRIGRLALRKMMeQQDKFEVVAINDLTDAKMLAHLFKYDTAQGRFNGEIEVKEGAFVVNGKEIKVTAERNP 80
Cdd:PRK07729 2 KTKVAINGFGRIGRMVFRKAI-KESAFEIVAINASYPSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 81 ADLPWAELGVDIVLECTGFFTSKDKAEAHIQAGAKKVVISAPATGDLKTIVFNTNSDILD-GSETVISGASCTTNCLAPM 159
Cdd:PRK07729 81 KELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVTIVVGVNEDQLDiEKHTIISNASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 160 AKVLNDKYGIEKGLMTTIHAYTNDQNTLDGPHPkgDLRRARAAAGNIVPNTTGAAKAIGLVIPSLKGKLDGAAQRVPVVT 239
Cdd:PRK07729 161 VKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHK--DLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 240 GSITELVCTLGKNVTVEEINAAMKEASNES----FGYTEEMLVSSDIIGISYGSLFDATQTKVMEvdGKQlVKVVSWYDN 315
Cdd:PRK07729 239 VSLVDLVVDVKRDVTVEEINEAFKTAANGAlkgiLEFSEEPLVSIDFNTNTHSAIIDGLSTMVMG--DRK-VKVLAWYDN 315
|
....*....
gi 489517139 316 EMSYTSQLI 324
Cdd:PRK07729 316 EWGYSCRVV 324
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
4-324 |
2.75e-118 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 344.22 E-value: 2.75e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 4 VAINGFGRIGRLALRKMMEQQDkFEVVAINDL-TDAKMLAHLFKYDTAQGRFNGEIEVKEGAFVVNGKEIKVTAERNPAD 82
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPG-LEIVHINDLaGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 83 LPWAElGVDIVLECTGFFTSKDKAEAHIQAGAKKVVISAPA-TGDLKTIVFNTNSDILDGSE-TVISGASCTTNCLAPMA 160
Cdd:NF033735 80 TPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVkEEGVLNIVYGVNDHLYDPARhRIVTAASCTTNCLAPVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 161 KVLNDKYGIEKGLMTTIHAYTNDQNTLDGPHPkgDLRRARAAAGNIVPNTTGAAKAIGLVIPSLKGKLDGAAQRVPVVTG 240
Cdd:NF033735 159 KVIHEKIGIKHGSITTIHDITNTQTIVDAPHK--DLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 241 SITELVCTLGKNVTVEEINAAMKEASNES----FGYTEEMLVSSDIIGISYGSLFDATQTkvMEVDGKQlVKVVSWYDNE 316
Cdd:NF033735 237 SLTDCVFEVERPTTVEEVNALFKAAAEGPlkgiLGYEERPLVSVDYVNDPRSSIIDALST--MVVNGTQ-VKIYAWYDNE 313
|
....*...
gi 489517139 317 MSYTSQLI 324
Cdd:NF033735 314 WGYANRMV 321
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
151-316 |
8.45e-108 |
|
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: 311.31 E-value: 8.45e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 151 CTTNCLAPMAKVLNDKYGIEKGLMTTIHAYTNDQNTLDGPHpkGDLRRARAAAGNIVPNTTGAAKAIGLVIPSLKGKLDG 230
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH--KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 231 AAQRVPVVTGSITELVCTLGKNVTVEEINAAMKEASN----ESFGYTEEMLVSSDIIGISYGSLFDATQTKVMevdGKQL 306
Cdd:cd18126 79 MAFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEgplkGILGYTEDPLVSSDFVGDPHSSIFDATATIVL---GGNL 155
|
170
....*....|
gi 489517139 307 VKVVSWYDNE 316
Cdd:cd18126 156 VKVVAWYDNE 165
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
2-151 |
1.17e-82 |
|
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: 247.08 E-value: 1.17e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 2 VKVAINGFGRIGRLALRKMMEQQDkFEVVAINDLTDAKMLAHLFKYDTAQGRFNGEIEVKEGAFVVNGKEIKVTAERNPA 81
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPD-VEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 82 DLPWAELGVDIVLECTGFFTSKDKAEAHIQAGAKKVVISAPATGDLKTIVFNTNSDILDGSETVISGASC 151
Cdd:smart00846 80 NLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDADPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
156-313 |
9.10e-80 |
|
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: 240.19 E-value: 9.10e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 156 LAPMAKVLNDKYGIEKGLMTTIHAYTNDQNTLDGPHPKgDLRRARAAAGNIVPNTTGAAKAIGLVIPSLKGKLDGAAQRV 235
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHK-DLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 236 PVVTGSITELVCTLGKNVTVEEINAAMKEAS----NESFGYTEEMLVSSDIIGISYGSLFDATQTKVMevdGKQLVKVVS 311
Cdd:pfam02800 80 PTPNVSVVDLVVELEKPVTVEEVNAALKEAAegalKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVV---NGNFVKVVA 156
|
..
gi 489517139 312 WY 313
Cdd:pfam02800 157 WY 158
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
2-333 |
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: 615.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 2 VKVAINGFGRIGRLALRKMMEQQDKFEVVAINDLTDAKMLAHLFKYDTAQGRFNGEIEVKEGAFVVNGKEIKVTAERNPA 81
Cdd:COG0057 3 IRVAINGFGRIGRLVLRALLERGPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 82 DLPWAELGVDIVLECTGFFTSKDKAEAHIQAGAKKVVISAPATGDLKTIVFNTNSDILDGSETVISGASCTTNCLAPMAK 161
Cdd:COG0057 83 ELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDDPTIVYGVNHDDYDADHRIISNASCTTNCLAPVAK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 162 VLNDKYGIEKGLMTTIHAYTNDQNTLDGPHpkGDLRRARAAAGNIVPNTTGAAKAIGLVIPSLKGKLDGAAQRVPVVTGS 241
Cdd:COG0057 163 VLNDAFGIEKGLMTTIHAYTNDQNLLDAPH--KDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 242 ITELVCTLGKNVTVEEINAAMKEASNES----FGYTEEMLVSSDIIGISYGSLFDATQTKVMevdGKQLVKVVSWYDNEM 317
Cdd:COG0057 241 LVDLTVELEKETTVEEVNAALKEAAEGPlkgiLGYTEEPLVSSDFNGDPHSSIFDALQTIVI---GGNLVKVLAWYDNEW 317
|
330
....*....|....*.
gi 489517139 318 SYTSQLIRTLGYFAQL 333
Cdd:COG0057 318 GYSNRMVDLAEYMAKL 333
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
3-325 |
0e+00 |
|
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: 515.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 3 KVAINGFGRIGRLALRKMMEQQD-KFEVVAINDLTDAKMLAHLFKYDTAQGRFNGEIEVKEGAFVVNGKE-IKVTAERNP 80
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKPGnDLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEvISVFSERDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 81 ADLPWAELGVDIVLECTGFFTSKDKAEAHIQAGAKKVVISAPATGDLKTIVFNTNSDILDGSETVISGASCTTNCLAPMA 160
Cdd:TIGR01534 81 SDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDVKTIVYGVNHDEYDGEERIISNASCTTNCLAPLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 161 KVLNDKYGIEKGLMTTIHAYTNDQNTLDGPHpkGDLRRARAAAGNIVPNTTGAAKAIGLVIPSLKGKLDGAAQRVPVVTG 240
Cdd:TIGR01534 161 KVLDEAFGIVSGLMTTVHAYTNDQNLLDGPH--KDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 241 SITELVCTLGKNVTVEEINAAMKEAS----NESFGYTEEMLVSSDIIGISYGSLFDATQTKVMEVDGKQlVKVVSWYDNE 316
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKEASegelKGVLGYTEDELVSSDFIGSPYSSIVDATATKVTGLGDSL-VKVYAWYDNE 317
|
....*....
gi 489517139 317 MSYTSQLIR 325
Cdd:TIGR01534 318 WGYSNRLVD 326
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-324 |
1.43e-143 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 409.13 E-value: 1.43e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 1 MVKVAINGFGRIGRLALRKMMeQQDKFEVVAINDLTDAKMLAHLFKYDTAQGRFNGEIEVKEGAFVVNGKEIKVTAERNP 80
Cdd:PRK07729 2 KTKVAINGFGRIGRMVFRKAI-KESAFEIVAINASYPSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 81 ADLPWAELGVDIVLECTGFFTSKDKAEAHIQAGAKKVVISAPATGDLKTIVFNTNSDILD-GSETVISGASCTTNCLAPM 159
Cdd:PRK07729 81 KELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVTIVVGVNEDQLDiEKHTIISNASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 160 AKVLNDKYGIEKGLMTTIHAYTNDQNTLDGPHPkgDLRRARAAAGNIVPNTTGAAKAIGLVIPSLKGKLDGAAQRVPVVT 239
Cdd:PRK07729 161 VKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHK--DLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 240 GSITELVCTLGKNVTVEEINAAMKEASNES----FGYTEEMLVSSDIIGISYGSLFDATQTKVMEvdGKQlVKVVSWYDN 315
Cdd:PRK07729 239 VSLVDLVVDVKRDVTVEEINEAFKTAANGAlkgiLEFSEEPLVSIDFNTNTHSAIIDGLSTMVMG--DRK-VKVLAWYDN 315
|
....*....
gi 489517139 316 EMSYTSQLI 324
Cdd:PRK07729 316 EWGYSCRVV 324
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
1-324 |
2.68e-120 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 349.98 E-value: 2.68e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 1 MVKVAINGFGRIGRLALRKMMEQQD-KFEVVAINDLTDAKMLAHLFKYDTAQGRFNGEIEVKEGAFVVNGKEIKVTAERN 79
Cdd:PRK07403 1 MIRVAINGFGRIGRNFLRCWLGRENsQLELVAINDTSDPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 80 PADLPWAELGVDIVLECTGFFTSKDKAEAHIQAGAKKVVISAPATG-DLKTIVFNTNSDILDGSE-TVISGASCTTNCLA 157
Cdd:PRK07403 81 PLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPGKGeDIGTYVVGVNHHEYDHEDhNIISNASCTTNCLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 158 PMAKVLNDKYGIEKGLMTTIHAYTNDQNTLDGPHPkgDLRRARAAAGNIVPNTTGAAKAIGLVIPSLKGKLDGAAQRVPV 237
Cdd:PRK07403 161 PIAKVLHDNFGIIKGTMTTTHSYTGDQRILDASHR--DLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 238 VTGSITELVCTLGKNVTVEEINAAMKEASNESF----GYTEEMLVSSDIIGISYGSLFDATQTKVMevdGKQLVKVVSWY 313
Cdd:PRK07403 239 PNVSVVDLVVQVEKRTITEQVNEVLKDASEGPLkgilEYSDLPLVSSDYRGTDASSIVDASLTMVM---GGDMVKVIAWY 315
|
330
....*....|.
gi 489517139 314 DNEMSYTSQLI 324
Cdd:PRK07403 316 DNEWGYSQRVV 326
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
4-324 |
2.75e-118 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 344.22 E-value: 2.75e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 4 VAINGFGRIGRLALRKMMEQQDkFEVVAINDL-TDAKMLAHLFKYDTAQGRFNGEIEVKEGAFVVNGKEIKVTAERNPAD 82
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPG-LEIVHINDLaGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 83 LPWAElGVDIVLECTGFFTSKDKAEAHIQAGAKKVVISAPA-TGDLKTIVFNTNSDILDGSE-TVISGASCTTNCLAPMA 160
Cdd:NF033735 80 TPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVkEEGVLNIVYGVNDHLYDPARhRIVTAASCTTNCLAPVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 161 KVLNDKYGIEKGLMTTIHAYTNDQNTLDGPHPkgDLRRARAAAGNIVPNTTGAAKAIGLVIPSLKGKLDGAAQRVPVVTG 240
Cdd:NF033735 159 KVIHEKIGIKHGSITTIHDITNTQTIVDAPHK--DLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 241 SITELVCTLGKNVTVEEINAAMKEASNES----FGYTEEMLVSSDIIGISYGSLFDATQTkvMEVDGKQlVKVVSWYDNE 316
Cdd:NF033735 237 SLTDCVFEVERPTTVEEVNALFKAAAEGPlkgiLGYEERPLVSVDYVNDPRSSIIDALST--MVVNGTQ-VKIYAWYDNE 313
|
....*...
gi 489517139 317 MSYTSQLI 324
Cdd:NF033735 314 WGYANRMV 321
|
|
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
2-334 |
1.33e-117 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 346.07 E-value: 1.33e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 2 VKVAINGFGRIGRLALRkMMEQQDKFEVVAIND-LTDAKMLAHLFKYDTAQGRFNGEIEV-KEGAFVVNGKEIKVTAERN 79
Cdd:PLN02272 86 TKIGINGFGRIGRLVLR-IATSRDDIEVVAVNDpFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRD 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 80 PADLPWAELGVDIVLECTGFFTSKDKAEAHIQAGAKKVVISAPaTGDLKTIVFNTNSDILDGSETVISGASCTTNCLAPM 159
Cdd:PLN02272 165 PAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAP-SADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 160 AKVLNDKYGIEKGLMTTIHAYTNDQNTLDGPHPKgDLRRARAAAGNIVPNTTGAAKAIGLVIPSLKGKLDGAAQRVPVVT 239
Cdd:PLN02272 244 AKVVHEEFGILEGLMTTVHATTATQKTVDGPSMK-DWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPN 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 240 GSITELVCTLGKNVTVEEINAAMKEASNES----FGYTEEMLVSSDIIGISYGSLFDATQTKVMEvdgKQLVKVVSWYDN 315
Cdd:PLN02272 323 VSVVDLTCRLEKSASYEDVKAAIKYASEGPlkgiLGYTDEDVVSNDFVGDSRSSIFDAKAGIGLS---ASFMKLVSWYDN 399
|
330
....*....|....*....
gi 489517139 316 EMSYTSQLIRTLGYFAQLA 334
Cdd:PLN02272 400 EWGYSNRVLDLIEHMALVA 418
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
1-326 |
1.12e-111 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 327.78 E-value: 1.12e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 1 MVKVAINGFGRIGRLALRKMME--QQDKFEVVAINDLTDAKMLAHLFKYDTAQGRFNGEIEVKEGAFVVNGKEIKVTAER 78
Cdd:PRK13535 1 TIRVAINGFGRIGRNVLRALYEsgRRAEITVVAINELADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 79 NPADLPWAELGVDIVLECTGFFTSKDKAEAHIQAGAKKVVISAPATGDL-KTIVFNTNSDILDGSETVISGASCTTNCLA 157
Cdd:PRK13535 81 DIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSNDLdATVVYGVNHDQLRAEHRIVSNASCTTNCII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 158 PMAKVLNDKYGIEKGLMTTIHAYTNDQNTLDGPHPkgDLRRARAAAGNIVPNTTGAAKAIGLVIPSLKGKLDGAAQRVPV 237
Cdd:PRK13535 161 PVIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHP--DLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 238 VTGSITELVCTLGKNVTVEEINAAMKEASNESF----GYTEEMLVSSDIIGISYGSLFDATQTKvmeVDGKQLVKVVSWY 313
Cdd:PRK13535 239 INVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFhgivDYTELPLVSIDFNHDPHSAIVDGTQTR---VSGAHLIKTLVWC 315
|
330
....*....|...
gi 489517139 314 DNEMSYTSQLIRT 326
Cdd:PRK13535 316 DNEWGFANRMLDT 328
|
|
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
2-324 |
1.48e-111 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 327.56 E-value: 1.48e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 2 VKVAINGFGRIGRLALRKMMEQQDkFEVVAIND-LTDAKMLAHLFKYDTAQGRFNGEIEVKEGAFVVNGKEIKVTAERNP 80
Cdd:PTZ00023 3 VKLGINGFGRIGRLVFRAALERED-VEVVAINDpFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 81 ADLPWAELGVDIVLECTGFFTSKDKAEAHIQAGAKKVVISAPATGDLKTIVFNTNSDILDGSETVISGASCTTNCLAPMA 160
Cdd:PTZ00023 82 AAIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKDDTPIYVMGVNHTQYDKSQRIVSNASCTTNCLAPLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 161 KVLNDKYGIEKGLMTTIHAYTNDQNTLDGPHPKG-DLRRARAAAGNIVPNTTGAAKAIGLVIPSLKGKLDGAAQRVPVVT 239
Cdd:PTZ00023 162 KVVNDKFGIVEGLMTTVHASTANQLTVDGPSKGGkDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVPD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 240 GSITELVCTLGKNVTVEEINAAMKEASNES----FGYTEEMLVSSDIIGISYGSLFDaTQTKVMEVDgkQLVKVVSWYDN 315
Cdd:PTZ00023 242 VSVVDLTCKLAKPAKYEEIVAAVKKAAEGPlkgiLGYTDDEVVSSDFVHDKRSSIFD-VKAGIALND--TFVKLVSWYDN 318
|
....*....
gi 489517139 316 EMSYTSQLI 324
Cdd:PTZ00023 319 EWGYSNRLL 327
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
2-324 |
6.48e-111 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 328.04 E-value: 6.48e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 2 VKVAINGFGRIGRLALRKMMEQQDK-FEVVAINDLTDAKMLAHLFKYDTAQGRFNGEIE-VKEGAFVVNGKEIKVTAERN 79
Cdd:PLN03096 61 IKVAINGFGRIGRNFLRCWHGRKDSpLDVVAINDTGGVKQASHLLKYDSTLGTFDADVKpVGDDAISVDGKVIKVVSDRN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 80 PADLPWAELGVDIVLECTGFFTSKDKAEAHIQAGAKKVVISAPATGDLKTIVFNTNSDILDGSETVISGASCTTNCLAPM 159
Cdd:PLN03096 141 PLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKGDIPTYVVGVNADDYKHSDPIISNASCTTNCLAPF 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 160 AKVLNDKYGIEKGLMTTIHAYTNDQNTLDGPHPkgDLRRARAAAGNIVPNTTGAAKAIGLVIPSLKGKLDGAAQRVPVVT 239
Cdd:PLN03096 221 VKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHR--DLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPN 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 240 GSITELVCTLGKNVTVEEINAAMKEASNES----FGYTEEMLVSSDIIGISYGSLFDATQTKVMevdGKQLVKVVSWYDN 315
Cdd:PLN03096 299 VSVVDLVVQVEKKTFAEEVNAAFRDAAEKElkgiLAVCDEPLVSVDFRCSDVSSTIDSSLTMVM---GDDMVKVVAWYDN 375
|
....*....
gi 489517139 316 EMSYTSQLI 324
Cdd:PLN03096 376 EWGYSQRVV 384
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
2-331 |
4.51e-110 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 324.70 E-value: 4.51e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 2 VKVAINGFGRIGRLALRKMMEQQ---DKFEVVAINDL-TDAKMLAHLFKYDTAQGRFNGEIEV--------KEGAFVVNG 69
Cdd:PTZ00434 4 IKVGINGFGRIGRMVFQAICDQGligTEIDVVAVVDMsTNAEYFAYQMKYDTVHGRPKYTVETtksspsvkTDDVLVVNG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 70 KEIK-VTAERNPADLPWAELGVDIVLECTGFFTSKDKAEAHIQAGAKKVVISAPATGDLKTIVFNTNSDILDGSE-TVIS 147
Cdd:PTZ00434 84 HRIKcVKAQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPASGGAKTIVMGVNQHEYSPTEhHVVS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 148 GASCTTNCLAPMAKVL-NDKYGIEKGLMTTIHAYTNDQNTLDGPHPKgDLRRARAAAGNIVPNTTGAAKAIGLVIPSLKG 226
Cdd:PTZ00434 164 NASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSVK-DWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 227 KLDGAAQRVPVVTGSITELVCTLGKNVTVEEINAAMKEASN----ESFGYTEEMLVSSDIIGISYGSLFDATQTKVMEVD 302
Cdd:PTZ00434 243 KLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQtymkGILGFTDDELVSADFINDNRSSIYDSKATLQNNLP 322
|
330 340 350
....*....|....*....|....*....|
gi 489517139 303 G-KQLVKVVSWYDNEMSYTSQLIRTLGYFA 331
Cdd:PTZ00434 323 GeRRFFKIVSWYDNEWGYSHRVVDLVRYMA 352
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
151-316 |
8.45e-108 |
|
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: 311.31 E-value: 8.45e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 151 CTTNCLAPMAKVLNDKYGIEKGLMTTIHAYTNDQNTLDGPHpkGDLRRARAAAGNIVPNTTGAAKAIGLVIPSLKGKLDG 230
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH--KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 231 AAQRVPVVTGSITELVCTLGKNVTVEEINAAMKEASN----ESFGYTEEMLVSSDIIGISYGSLFDATQTKVMevdGKQL 306
Cdd:cd18126 79 MAFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEgplkGILGYTEDPLVSSDFVGDPHSSIFDATATIVL---GGNL 155
|
170
....*....|
gi 489517139 307 VKVVSWYDNE 316
Cdd:cd18126 156 VKVVAWYDNE 165
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
2-324 |
2.15e-106 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 318.00 E-value: 2.15e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 2 VKVAINGFGRIGRLALRKMMEQQDK-FEVVAINDLTDAKMLAHLFKYDTAQGRFNGEIEVKEGAFV-VNGKEIKVTAERN 79
Cdd:PLN02237 76 LKVAINGFGRIGRNFLRCWHGRKDSpLDVVVVNDSGGVKNASHLLKYDSMLGTFKADVKIVDDETIsVDGKPIKVVSNRD 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 80 PADLPWAELGVDIVLECTGFFTSKDKAEAHIQAGAKKVVISAPATG-DLKTIVFNTNSDILDGS-ETVISGASCTTNCLA 157
Cdd:PLN02237 156 PLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAKGaDIPTYVVGVNEDDYDHEvANIVSNASCTTNCLA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 158 PMAKVLNDKYGIEKGLMTTIHAYTNDQNTLDGPHPkgDLRRARAAAGNIVPNTTGAAKAIGLVIPSLKGKLDGAAQRVPV 237
Cdd:PLN02237 236 PFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDASHR--DLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPT 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 238 VTGSITELVCTL-GKNVTVEEINAAMKEASNES----FGYTEEMLVSSDIIGISYGSLFDATQTKVMevdGKQLVKVVSW 312
Cdd:PLN02237 314 PNVSVVDLVVNVeKKGITAEDVNAAFRKAADGPlkgiLAVCDVPLVSVDFRCSDVSSTIDASLTMVM---GDDMVKVVAW 390
|
330
....*....|..
gi 489517139 313 YDNEMSYTSQLI 324
Cdd:PLN02237 391 YDNEWGYSQRVV 402
|
|
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
2-328 |
3.87e-103 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 305.89 E-value: 3.87e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 2 VKVAINGFGRIGRLALRKMMEQQDkFEVVAINDLT-DAKMLAHLFKYDTAQGRFNGEIEVKEGAFVVNGKEIKVTAERNP 80
Cdd:PRK08955 3 IKVGINGFGRIGRLALRAAWDWPE-LEFVQINDPAgDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 81 ADLPWAelGVDIVLECTGFFTSKDKAEAHIQAGAKKVVISAPATGD-LKTIVFNTNSDILDGSE-TVISGASCTTNCLAP 158
Cdd:PRK08955 82 ADTDWS--GCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEgVLNIVMGVNDHLFDPAIhPIVTAASCTTNCLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 159 MAKVLNDKYGIEKGLMTTIHAYTNDQNTLDGPHPkgDLRRARAAAGNIVPNTTGAAKAIGLVIPSLKGKLDGAAQRVPVV 238
Cdd:PRK08955 160 VVKVIHEKLGIKHGSMTTIHDLTNTQTILDAPHK--DLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 239 TGSITELVCTLGKNVTVEEINAAMKEASNESF----GYTEEMLVSSDIIGISYGSLFDATQTKVmeVDGKQlVKVVSWYD 314
Cdd:PRK08955 238 NASLTDCVFEVERDTTVEEVNALLKEAAEGELkgilGYEERPLVSIDYKTDPRSSIVDALSTMV--VNGTQ-VKLYAWYD 314
|
330
....*....|....*..
gi 489517139 315 NEMSY---TSQLIRTLG 328
Cdd:PRK08955 315 NEWGYanrTAELARKVG 331
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
2-332 |
1.11e-101 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 302.42 E-value: 1.11e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 2 VKVAINGFGRIGRLALRKMMEQQDkFEVVAINDLTDAKMLAHLFKYDTAQGRFNGEIEVKEGAFVVNGKEIKVTAERNPA 81
Cdd:PRK15425 3 IKVGINGFGRIGRIVFRAAQKRSD-IEIVAINDLLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 82 DLPWAELGVDIVLECTGFFTSKDKAEAHIQAGAKKVVISAPATGDLKTIVFNTNSDILDGSEtVISGASCTTNCLAPMAK 161
Cdd:PRK15425 82 NLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDNTPMFVKGANFDKYAGQD-IVSNASCTTNCLAPLAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 162 VLNDKYGIEKGLMTTIHAYTNDQNTLDGPHPKgDLRRARAAAGNIVPNTTGAAKAIGLVIPSLKGKLDGAAQRVPVVTGS 241
Cdd:PRK15425 161 VINDNFGIIEGLMTTVHATTATQKTVDGPSHK-DWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 242 ITELVCTLGKNVTVEEINAAMKEASNES----FGYTEEMLVSSDIIGISYGSLFDATQTKVMEvdgKQLVKVVSWYDNEM 317
Cdd:PRK15425 240 VVDLTVRLEKAATYEQIKAAVKAAAEGEmkgvLGYTEDDVVSTDFNGEVCTSVFDAKAGIALN---DNFVKLVSWYDNET 316
|
330
....*....|....*
gi 489517139 318 SYTSQLIRTLGYFAQ 332
Cdd:PRK15425 317 GYSNKVLDLIAHISK 331
|
|
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
2-324 |
2.49e-92 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 278.53 E-value: 2.49e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 2 VKVAINGFGRIGRLALRKMMeQQDKFEVVAIND-LTDAKMLAHLFKYDTAQGRF-NGEIEVK-EGAFVVNGKEIKVTAER 78
Cdd:PLN02358 6 IRIGINGFGRIGRLVARVVL-QRDDVELVAVNDpFITTEYMTYMFKYDSVHGQWkHHELKVKdDKTLLFGEKPVTVFGIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 79 NPADLPWAELGVDIVLECTGFFTSKDKAEAHIQAGAKKVVISAPATgDLKTIVFNTNSDILDGSETVISGASCTTNCLAP 158
Cdd:PLN02358 85 NPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSK-DAPMFVVGVNEHEYKSDLDIVSNASCTTNCLAP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 159 MAKVLNDKYGIEKGLMTTIHAYTNDQNTLDGPHPKgDLRRARAAAGNIVPNTTGAAKAIGLVIPSLKGKLDGAAQRVPVV 238
Cdd:PLN02358 164 LAKVINDRFGIVEGLMTTVHSITATQKTVDGPSMK-DWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 239 TGSITELVCTLGKNVTVEEINAAMKEASNES----FGYTEEMLVSSDIIGISYGSLFDATQTKVMEvdgKQLVKVVSWYD 314
Cdd:PLN02358 243 DVSVVDLTVRLEKAATYDEIKKAIKEESEGKlkgiLGYTEDDVVSTDFVGDNRSSIFDAKAGIALS---DKFVKLVSWYD 319
|
330
....*....|
gi 489517139 315 NEMSYTSQLI 324
Cdd:PLN02358 320 NEWGYSSRVV 329
|
|
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
4-333 |
4.24e-90 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 277.57 E-value: 4.24e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 4 VAINGFGRIGRLALRKMMEQQ---DKFEVVAI-------NDLtdAKMlAHLFKYDTAQGRFNGEIEVKE--GAFVVNGKE 71
Cdd:PRK08289 130 VVLYGFGRIGRLLARLLIEKTgggNGLRLRAIvvrkgseGDL--EKR-ASLLRRDSVHGPFNGTITVDEenNAIIANGNY 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 72 IKVTAERNPADLPWAELGVD--IVLECTGFFTSKDKAEAHIQA-GAKKVVISAPATGDLKTIVFNTNSDILDGSETVISG 148
Cdd:PRK08289 207 IQVIYANSPEEVDYTAYGINnaLVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGKGDIKNIVHGVNHSDITDEDKIVSA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 149 ASCTTNCLAPMAKVLNDKYGIEKGLMTTIHAYTNDQNTLDGPHpKGDlRRARAAAGNIVPNTTGAAKAIGLVIPSLKGKL 228
Cdd:PRK08289 287 ASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYH-KGD-RRGRSAPLNMVITETGAAKAVAKALPELAGKL 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 229 DGAAQRVPVVTGSITELVCTLGKNVTVEEINAAMKEASNES-----FGYTEEM-LVSSDIIGISYGSLFDATQTKvmeVD 302
Cdd:PRK08289 365 TGNAIRVPTPNVSMAILNLNLEKETSREELNEYLRQMSLHSplqnqIDYTDSTeVVSSDFVGSRHAGVVDSQATI---VN 441
|
330 340 350
....*....|....*....|....*....|.
gi 489517139 303 GKQLVKVVsWYDNEMSYTSQLIRTLGYFAQL 333
Cdd:PRK08289 442 GNRAVLYV-WYDNEFGYSCQVVRVMEQMAGV 471
|
|
| GAPDH_I_N |
cd05214 |
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
2-150 |
7.09e-89 |
|
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: 263.48 E-value: 7.09e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 2 VKVAINGFGRIGRLALRKMMEQQDkFEVVAINDLTDAKMLAHLFKYDTAQGRFNGEIEVKEGAFVVNGKEIKVTAERNPA 81
Cdd:cd05214 1 IKVGINGFGRIGRLVFRAALERDD-IEVVAINDLTDDETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPA 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489517139 82 DLPWAELGVDIVLECTGFFTSKDKAEAHIQAGAKKVVISAPATGDLKTIVFNTNSDILDGSETVISGAS 150
Cdd:cd05214 80 ELPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDDDPTIVMGVNHDKYDADDKIISNAS 148
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
2-151 |
1.17e-82 |
|
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: 247.08 E-value: 1.17e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 2 VKVAINGFGRIGRLALRKMMEQQDkFEVVAINDLTDAKMLAHLFKYDTAQGRFNGEIEVKEGAFVVNGKEIKVTAERNPA 81
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPD-VEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 82 DLPWAELGVDIVLECTGFFTSKDKAEAHIQAGAKKVVISAPATGDLKTIVFNTNSDILDGSETVISGASC 151
Cdd:smart00846 80 NLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDADPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
156-313 |
9.10e-80 |
|
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: 240.19 E-value: 9.10e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 156 LAPMAKVLNDKYGIEKGLMTTIHAYTNDQNTLDGPHPKgDLRRARAAAGNIVPNTTGAAKAIGLVIPSLKGKLDGAAQRV 235
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHK-DLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 236 PVVTGSITELVCTLGKNVTVEEINAAMKEAS----NESFGYTEEMLVSSDIIGISYGSLFDATQTKVMevdGKQLVKVVS 311
Cdd:pfam02800 80 PTPNVSVVDLVVELEKPVTVEEVNAALKEAAegalKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVV---NGNFVKVVA 156
|
..
gi 489517139 312 WY 313
Cdd:pfam02800 157 WY 158
|
|
| GAPDH_N_E4PDH |
cd17892 |
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
2-150 |
1.96e-66 |
|
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: 206.35 E-value: 1.96e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 2 VKVAINGFGRIGRLALRKMME--QQDKFEVVAINDLTDAKMLAHLFKYDTAQGRFNGEIEVKEGAFVVNGKEIKVTAERN 79
Cdd:cd17892 1 YRVAINGYGRIGRNVLRALYEsgRRAEFQVVAINELADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489517139 80 PADLPWAELGVDIVLECTGFFTSKDKAEAHIQAGAKKVVISAPATGDLK-TIVFNTNSDILDGSETVISGAS 150
Cdd:cd17892 81 PENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASNDVDaTIVYGINQDLLRAEHRIVSNAS 152
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
151-316 |
2.66e-62 |
|
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: 195.91 E-value: 2.66e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 151 CTTNCLAPMAKVLNDKYGIEKGLMTTIHAYTNDQNTLDGPHPKgDLRRARAAAGNIVPNTTGAAKAIGLVIPSLKGKLDG 230
Cdd:cd18123 1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGK-DWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 231 AAQRVPVVTGSITELVCTLGKNVTVEEINAAMKEAS--NESFGYTEEMLVSSDIIGISYGSLFDATQTKVMEvdgKQLVK 308
Cdd:cd18123 80 MAVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPegKGRLGYTEAEDVSSDFRGDIFESVFDAESIIAVN---DNEVK 156
|
....*...
gi 489517139 309 VVSWYDNE 316
Cdd:cd18123 157 LMQWYDNE 164
|
|
| Gp_dh_N |
pfam00044 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
2-103 |
7.07e-59 |
|
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: 184.61 E-value: 7.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 2 VKVAINGFGRIGRLALRKMMEQQDkFEVVAINDLTDAKMLAHLFKYDTAQGRFNGEIEVKEGAFVVNGKEIKVTAERNPA 81
Cdd:pfam00044 1 VKVGINGFGRIGRLVLRAALERPD-IEVVAINDLTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPA 79
|
90 100
....*....|....*....|..
gi 489517139 82 DLPWAELGVDIVLECTGFFTSK 103
Cdd:pfam00044 80 ELPWGDLGVDVVIESTGVFTTK 101
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
151-316 |
2.93e-50 |
|
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: 164.90 E-value: 2.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 151 CTTNCLAPMAKVLNDKYGIEKGLMTTIHAYTNDQNTLDGPHPkgDLRRARAAAGNIVPNTTGAAKAIGLVIPSLKGKLDG 230
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDAYHP--DLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 231 AAQRVPVVTGSITELVCTLGKNVTVEEINAAMKEASNESF----GYTEEMLVSSDIIGISYGSLFDATQTKvmeVDGKQL 306
Cdd:cd23937 79 IAVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLkgilGYTEEPLVSVDFNHDPHSCIVDGTQTR---VSGKRL 155
|
170
....*....|
gi 489517139 307 VKVVSWYDNE 316
Cdd:cd23937 156 VKLLVWCDNE 165
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
2-324 |
4.39e-42 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 149.26 E-value: 4.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 2 VKVAINGFGRIGRLALRKMMEQQdKFEVVAINDLT-DAKMLAHLFKYDTAQGRFNG-EIEVKEGAFVVNGKE-IKVTAER 78
Cdd:PTZ00353 3 ITVGINGFGPVGKAVLFASLTDP-LVTVVAVNDASvSIAYIAYVLEQESPLSAPDGaSIRVVGEQIVLNGTQkIRVSAKH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 79 NPADLPWAELGVDIVLECTGFFTSKDKAEAHIQAGAKKVVISApATGDLKTIVFNTNSDILDGSETVISGASCTTNCLAP 158
Cdd:PTZ00353 82 DLVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAG-QSADAPTVMAGSNDERLSASLPVCCAGAPIAVALAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 159 MAKVLNDKYGIEKGLMTTIHAYTNDQNTLDGPHPKGDLRRARAAAGNIVPNTTGAAKAIGLVIPSLKGKLDGAAQRVPVV 238
Cdd:PTZ00353 161 VIRALHEVYGVEECSYTAIHGMQPQEPIAARSKNSQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 239 TGSITELVCTLGKNVTVEEINAAMKEASNESFG----YTEEMLVSSDIIGISyGSLFDATQTKVMEvDGKqLVKVVSWYD 314
Cdd:PTZ00353 241 KGCAIDMLVRTKQPVSKEVVDSALAEAASDRLNgvlcISKRDMISVDCIPNG-KLCYDATSSSSSR-EGE-VHKMVLWFD 317
|
330
....*....|
gi 489517139 315 NEMSYTSQLI 324
Cdd:PTZ00353 318 VECYYAARLL 327
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
151-316 |
3.34e-38 |
|
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: 133.80 E-value: 3.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 151 CTTNCLAPMAKVLNDKYGIEKGLMTTIHAYTNDQNTLDGPHPKGDlrrARAAAGNIVPNTTGAAKAIGLVIPSL--KGKL 228
Cdd:cd18122 1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE---VRAIIPNIPKNETKHAPETGKVLGEIgkPIKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 229 DGAAQRVPVVTGSITELVCTLGKNVTVEEINAAMKEASNESFGYTEEML----VSSDIIGISYGSLFDATQTKVMevdGK 304
Cdd:cd18122 78 DGIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLtyakVSTRSVGGVYGVPVGRQREFAF---DD 154
|
170
....*....|..
gi 489517139 305 QLVKVVSWYDNE 316
Cdd:cd18122 155 NKLKVFSAVDNE 166
|
|
| GAPDH-like_N |
cd05192 |
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ... |
2-155 |
5.35e-19 |
|
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: 80.86 E-value: 5.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 2 VKVAINGFGRIGRLALRkMMEQQDKFEVVAINDLTDakmlahlfkydtaqgrfngeievkegafvvngkeikvtaernpa 81
Cdd:cd05192 1 IRVAINGFGRIGRIVFR-AIADQDDLDVVAINDRRD-------------------------------------------- 35
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489517139 82 dlpwaelgvdIVLECTGFFTSKDKAEAHIQAGAKKVVISAPATGDLKTIVFNTNSDILDGSETVISGASCTTNC 155
Cdd:cd05192 36 ----------VVIECTGSFTDDDNAEKHIKAGGKKAVITAPEKGDIPTIVVVLNELAKSAGATVVSNANETSYS 99
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| nat-AmDH_N_like |
cd24146 |
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ... |
2-120 |
2.11e-03 |
|
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.
Pssm-ID: 467616 [Multi-domain] Cd Length: 157 Bit Score: 38.29 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489517139 2 VKVAINGFGRIGRLALRKMMEQQDkFEVVAINDLTDAKmlahlfkydtaQGRFNGEIEVKEgafvvnGKEIKVTAerNPA 81
Cdd:cd24146 1 IRVVVWGLGAMGRGIARYLLEKPG-LEIVGAVDRDPAK-----------VGKDLGELGGGA------PLGVKVTD--DLD 60
|
90 100 110
....*....|....*....|....*....|....*....
gi 489517139 82 DLpWAELGVDIVLECTGFFTSKDKAEAHIQAGAKKVVIS 120
Cdd:cd24146 61 AV-LAATKPDVVVHATTSFLADVAPQIERLLEAGLNVIT 98
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