|
Name |
Accession |
Description |
Interval |
E-value |
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
1-331 |
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: 558.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 1 MSTNIAINGMGRIGRMVLRIALKN-KNLNVVAINASYPSETIAHLINYDTTHGTYDKKVEATENGIKVDNHEIKLVSDRN 79
Cdd:COG0057 1 MTIRVAINGFGRIGRLVLRALLERgPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 80 PENLPWNELDIDIVIEATGKFNHGDKAIAHINAGAKKVLLTGPSKGgEVQMIVKGVNDDKLDiNQYDIFSNASCTTNCIG 159
Cdd:COG0057 81 PAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKG-DDPTIVYGVNHDDYD-ADHRIISNASCTTNCLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 160 PVAKVLNDKFGIVNGLMTTVHAITNDQKNIDNPHKDLRRARSCNESIIPTSTGAAKALKEVLPEVEGKLHGMALRVPTKN 239
Cdd:COG0057 159 PVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 240 VSLVDLVVDLEKNVTAEEVNEAFRQ---SDLDGILDVEDAPLVSVDFNTNPNSAVLDSQSTMVMGENKVKVIAWYDNEWG 316
Cdd:COG0057 239 VSLVDLTVELEKETTVEEVNAALKEaaeGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWG 318
|
330
....*....|....*
gi 488384039 317 YSNRVVEVAEQIGEL 331
Cdd:COG0057 319 YSNRMVDLAEYMAKL 333
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-338 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 535.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 1 MSTNIAINGMGRIGRMVLRIALKNKNLNVVAINASYPSETIAHLINYDTTHGTYDKKVEATENGIKVDNHEIKLVSDRNP 80
Cdd:PRK07729 1 MKTKVAINGFGRIGRMVFRKAIKESAFEIVAINASYPSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 81 ENLPWNELDIDIVIEATGKFNHGDKAIAHINAGAKKVLLTGPSKGGEVQmIVKGVNDDKLDINQYDIFSNASCTTNCIGP 160
Cdd:PRK07729 81 KELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVT-IVVGVNEDQLDIEKHTIISNASCTTNCLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 161 VAKVLNDKFGIVNGLMTTVHAITNDQKNIDNPHKDLRRARSCNESIIPTSTGAAKALKEVLPEVEGKLHGMALRVPTKNV 240
Cdd:PRK07729 160 VVKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 241 SLVDLVVDLEKNVTAEEVNEAFRQS---DLDGILDVEDAPLVSVDFNTNPNSAVLDSQSTMVMGENKVKVIAWYDNEWGY 317
Cdd:PRK07729 240 SLVDLVVDVKRDVTVEEINEAFKTAangALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEWGY 319
|
330 340
....*....|....*....|.
gi 488384039 318 SNRVVEVAEQIGELIEKEATV 338
Cdd:PRK07729 320 SCRVVDLVTLVADELAKQENV 340
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
4-322 |
3.23e-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: 443.26 E-value: 3.23e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 4 NIAINGMGRIGRMVLRIAL--KNKNLNVVAINASYPSETIAHLINYDTTHGTYDKKVEATENGIKVDNHE-IKLVSDRNP 80
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILekPGNDLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEvISVFSERDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 81 ENLPWNELDIDIVIEATGKFNHGDKAIAHINAGAKKVLLTGPSKGgEVQMIVKGVNDDKLDiNQYDIFSNASCTTNCIGP 160
Cdd:TIGR01534 81 SDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKG-DVKTIVYGVNHDEYD-GEERIISNASCTTNCLAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 161 VAKVLNDKFGIVNGLMTTVHAITNDQKNIDNPHKDLRRARSCNESIIPTSTGAAKALKEVLPEVEGKLHGMALRVPTKNV 240
Cdd:TIGR01534 159 LAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 241 SLVDLVVDLEKNVTAEEVNEAFR---QSDLDGILDVEDAPLVSVDFNTNPNSAVLDSQSTMVMG--ENKVKVIAWYDNEW 315
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKeasEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVTGlgDSLVKVYAWYDNEW 318
|
....*..
gi 488384039 316 GYSNRVV 322
Cdd:TIGR01534 319 GYSNRLV 325
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
5-325 |
2.41e-137 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 392.76 E-value: 2.41e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 5 IAINGMGRIGRMVLRIALKNKNLNVVAIN-ASYPSETIAHLINYDTTHGTYDKKVEATENGIKVDNHEIKLVSDRNPENL 83
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINdLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 84 PWNElDIDIVIEATGKFNHGDKAIAHINAGAKKVLLTGPSKGGEVQMIVKGVNDDKLDINQYDIFSNASCTTNCIGPVAK 163
Cdd:NF033735 81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLNIVYGVNDHLYDPARHRIVTAASCTTNCLAPVVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 164 VLNDKFGIVNGLMTTVHAITNDQKNIDNPHKDLRRARSCNESIIPTSTGAAKALKEVLPEVEGKLHGMALRVPTKNVSLV 243
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAPHKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASLT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 244 DLVVDLEKNVTAEEVNEAFRQ---SDLDGILDVEDAPLVSVDFNTNPNSAVLDSQSTMVMGENKVKVIAWYDNEWGYSNR 320
Cdd:NF033735 240 DCVFEVERPTTVEEVNALFKAaaeGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYANR 319
|
....*
gi 488384039 321 VVEVA 325
Cdd:NF033735 320 MVDLA 324
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
153-314 |
1.46e-100 |
|
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: 293.21 E-value: 1.46e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 153 CTTNCIGPVAKVLNDKFGIVNGLMTTVHAITNDQKNIDNPHKDLRRARSCNESIIPTSTGAAKALKEVLPEVEGKLHGMA 232
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 233 LRVPTKNVSLVDLVVDLEKNVTAEEVNEAFR---QSDLDGILDVEDAPLVSVDFNTNPNSAVLDSQSTMVMGENKVKVIA 309
Cdd:cd18126 81 FRVPTPNVSVVDLTVRLEKPVTVEEVNAALKkaaEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVVA 160
|
....*
gi 488384039 310 WYDNE 314
Cdd:cd18126 161 WYDNE 165
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
160-311 |
6.18e-77 |
|
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: 232.87 E-value: 6.18e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 160 PVAKVLNDKFGIVNGLMTTVHAITNDQKNIDNPH-KDLRRARSCNESIIPTSTGAAKALKEVLPEVEGKLHGMALRVPTK 238
Cdd:pfam02800 3 PLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHhKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTP 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488384039 239 NVSLVDLVVDLEKNVTAEEVNEAFR---QSDLDGILDVEDAPLVSVDFNTNPNSAVLDSQSTMVMGENKVKVIAWY 311
Cdd:pfam02800 83 NVSVVDLVVELEKPVTVEEVNAALKeaaEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
5-153 |
1.17e-63 |
|
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: 198.93 E-value: 1.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 5 IAINGMGRIGRMVLRIALKNKNLNVVAINASYPSETIAHLINYDTTHGTYDKKVEATENGIKVDNHEIKLVSDRNPENLP 84
Cdd:smart00846 3 VGINGFGRIGRLVLRAALERPDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANLP 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488384039 85 WNELDIDIVIEATGKFNHGDKAIAHINAGAKKVLLTGPSKgGEVQMIVKGVNDDKLDINQyDIFSNASC 153
Cdd:smart00846 83 WGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSK-DADPTFVYGVNHDEYDGED-HIISNASC 149
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
1-331 |
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: 558.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 1 MSTNIAINGMGRIGRMVLRIALKN-KNLNVVAINASYPSETIAHLINYDTTHGTYDKKVEATENGIKVDNHEIKLVSDRN 79
Cdd:COG0057 1 MTIRVAINGFGRIGRLVLRALLERgPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 80 PENLPWNELDIDIVIEATGKFNHGDKAIAHINAGAKKVLLTGPSKGgEVQMIVKGVNDDKLDiNQYDIFSNASCTTNCIG 159
Cdd:COG0057 81 PAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKG-DDPTIVYGVNHDDYD-ADHRIISNASCTTNCLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 160 PVAKVLNDKFGIVNGLMTTVHAITNDQKNIDNPHKDLRRARSCNESIIPTSTGAAKALKEVLPEVEGKLHGMALRVPTKN 239
Cdd:COG0057 159 PVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 240 VSLVDLVVDLEKNVTAEEVNEAFRQ---SDLDGILDVEDAPLVSVDFNTNPNSAVLDSQSTMVMGENKVKVIAWYDNEWG 316
Cdd:COG0057 239 VSLVDLTVELEKETTVEEVNAALKEaaeGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWG 318
|
330
....*....|....*
gi 488384039 317 YSNRVVEVAEQIGEL 331
Cdd:COG0057 319 YSNRMVDLAEYMAKL 333
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-338 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 535.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 1 MSTNIAINGMGRIGRMVLRIALKNKNLNVVAINASYPSETIAHLINYDTTHGTYDKKVEATENGIKVDNHEIKLVSDRNP 80
Cdd:PRK07729 1 MKTKVAINGFGRIGRMVFRKAIKESAFEIVAINASYPSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 81 ENLPWNELDIDIVIEATGKFNHGDKAIAHINAGAKKVLLTGPSKGGEVQmIVKGVNDDKLDINQYDIFSNASCTTNCIGP 160
Cdd:PRK07729 81 KELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVT-IVVGVNEDQLDIEKHTIISNASCTTNCLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 161 VAKVLNDKFGIVNGLMTTVHAITNDQKNIDNPHKDLRRARSCNESIIPTSTGAAKALKEVLPEVEGKLHGMALRVPTKNV 240
Cdd:PRK07729 160 VVKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 241 SLVDLVVDLEKNVTAEEVNEAFRQS---DLDGILDVEDAPLVSVDFNTNPNSAVLDSQSTMVMGENKVKVIAWYDNEWGY 317
Cdd:PRK07729 240 SLVDLVVDVKRDVTVEEINEAFKTAangALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEWGY 319
|
330 340
....*....|....*....|.
gi 488384039 318 SNRVVEVAEQIGELIEKEATV 338
Cdd:PRK07729 320 SCRVVDLVTLVADELAKQENV 340
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
4-322 |
3.23e-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: 443.26 E-value: 3.23e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 4 NIAINGMGRIGRMVLRIAL--KNKNLNVVAINASYPSETIAHLINYDTTHGTYDKKVEATENGIKVDNHE-IKLVSDRNP 80
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILekPGNDLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEvISVFSERDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 81 ENLPWNELDIDIVIEATGKFNHGDKAIAHINAGAKKVLLTGPSKGgEVQMIVKGVNDDKLDiNQYDIFSNASCTTNCIGP 160
Cdd:TIGR01534 81 SDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKG-DVKTIVYGVNHDEYD-GEERIISNASCTTNCLAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 161 VAKVLNDKFGIVNGLMTTVHAITNDQKNIDNPHKDLRRARSCNESIIPTSTGAAKALKEVLPEVEGKLHGMALRVPTKNV 240
Cdd:TIGR01534 159 LAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 241 SLVDLVVDLEKNVTAEEVNEAFR---QSDLDGILDVEDAPLVSVDFNTNPNSAVLDSQSTMVMG--ENKVKVIAWYDNEW 315
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKeasEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVTGlgDSLVKVYAWYDNEW 318
|
....*..
gi 488384039 316 GYSNRVV 322
Cdd:TIGR01534 319 GYSNRLV 325
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
5-325 |
2.41e-137 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 392.76 E-value: 2.41e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 5 IAINGMGRIGRMVLRIALKNKNLNVVAIN-ASYPSETIAHLINYDTTHGTYDKKVEATENGIKVDNHEIKLVSDRNPENL 83
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINdLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 84 PWNElDIDIVIEATGKFNHGDKAIAHINAGAKKVLLTGPSKGGEVQMIVKGVNDDKLDINQYDIFSNASCTTNCIGPVAK 163
Cdd:NF033735 81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLNIVYGVNDHLYDPARHRIVTAASCTTNCLAPVVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 164 VLNDKFGIVNGLMTTVHAITNDQKNIDNPHKDLRRARSCNESIIPTSTGAAKALKEVLPEVEGKLHGMALRVPTKNVSLV 243
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAPHKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASLT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 244 DLVVDLEKNVTAEEVNEAFRQ---SDLDGILDVEDAPLVSVDFNTNPNSAVLDSQSTMVMGENKVKVIAWYDNEWGYSNR 320
Cdd:NF033735 240 DCVFEVERPTTVEEVNALFKAaaeGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYANR 319
|
....*
gi 488384039 321 VVEVA 325
Cdd:NF033735 320 MVDLA 324
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
5-330 |
1.89e-132 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 380.79 E-value: 1.89e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 5 IAINGMGRIGRMVLRIAL--KNKNLNVVAINASYPSETIAHLINYDTTHGTYDKKVEATENGIKVDNHEIKLVSDRNPEN 82
Cdd:PRK07403 4 VAINGFGRIGRNFLRCWLgrENSQLELVAINDTSDPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDRNPLN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 83 LPWNELDIDIVIEATGKFNHGDKAIAHINAGAKKVLLTGPSKGGEVQMIVKGVNDDKLDINQYDIFSNASCTTNCIGPVA 162
Cdd:PRK07403 84 LPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPGKGEDIGTYVVGVNHHEYDHEDHNIISNASCTTNCLAPIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 163 KVLNDKFGIVNGLMTTVHAITNDQKNIDNPHKDLRRARSCNESIIPTSTGAAKALKEVLPEVEGKLHGMALRVPTKNVSL 242
Cdd:PRK07403 164 KVLHDNFGIIKGTMTTTHSYTGDQRILDASHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTPNVSV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 243 VDLVVDLEKNVTAEEVNEAFR---QSDLDGILDVEDAPLVSVDFNTNPNSAVLDSQSTMVMGENKVKVIAWYDNEWGYSN 319
Cdd:PRK07403 244 VDLVVQVEKRTITEQVNEVLKdasEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYDNEWGYSQ 323
|
330
....*....|.
gi 488384039 320 RVVEVAEQIGE 330
Cdd:PRK07403 324 RVVDLAELVAR 334
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
5-330 |
2.33e-129 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 375.42 E-value: 2.33e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 5 IAINGMGRIGRMVLRI--ALKNKNLNVVAINASYPSETIAHLINYDTTHGTYDKKVEAT-ENGIKVDNHEIKLVSDRNPE 81
Cdd:PLN03096 63 VAINGFGRIGRNFLRCwhGRKDSPLDVVAINDTGGVKQASHLLKYDSTLGTFDADVKPVgDDAISVDGKVIKVVSDRNPL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 82 NLPWNELDIDIVIEATGKFNHGDKAIAHINAGAKKVLLTGPSKGgEVQMIVKGVNDDKLDiNQYDIFSNASCTTNCIGPV 161
Cdd:PLN03096 143 NLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKG-DIPTYVVGVNADDYK-HSDPIISNASCTTNCLAPF 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 162 AKVLNDKFGIVNGLMTTVHAITNDQKNIDNPHKDLRRARSCNESIIPTSTGAAKALKEVLPEVEGKLHGMALRVPTKNVS 241
Cdd:PLN03096 221 VKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVS 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 242 LVDLVVDLEKNVTAEEVNEAFRQS---DLDGILDVEDAPLVSVDFNTNPNSAVLDSQSTMVMGENKVKVIAWYDNEWGYS 318
Cdd:PLN03096 301 VVDLVVQVEKKTFAEEVNAAFRDAaekELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAWYDNEWGYS 380
|
330
....*....|..
gi 488384039 319 NRVVEVAEQIGE 330
Cdd:PLN03096 381 QRVVDLADIVAN 392
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
5-325 |
1.54e-126 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 369.61 E-value: 1.54e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 5 IAINGMGRIGRMVLRI--ALKNKNLNVVAINASYPSETIAHLINYDTTHGTYDKKVEATENG-IKVDNHEIKLVSDRNPE 81
Cdd:PLN02237 78 VAINGFGRIGRNFLRCwhGRKDSPLDVVVVNDSGGVKNASHLLKYDSMLGTFKADVKIVDDEtISVDGKPIKVVSNRDPL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 82 NLPWNELDIDIVIEATGKFNHGDKAIAHINAGAKKVLLTGPSKGGEVQMIVKGVNDDKLDINQYDIFSNASCTTNCIGPV 161
Cdd:PLN02237 158 KLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAKGADIPTYVVGVNEDDYDHEVANIVSNASCTTNCLAPF 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 162 AKVLNDKFGIVNGLMTTVHAITNDQKNIDNPHKDLRRARSCNESIIPTSTGAAKALKEVLPEVEGKLHGMALRVPTKNVS 241
Cdd:PLN02237 238 VKVLDEEFGIVKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTPNVS 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 242 LVDLVVDLEKN-VTAEEVNEAFRQSD---LDGILDVEDAPLVSVDFNTNPNSAVLDSQSTMVMGENKVKVIAWYDNEWGY 317
Cdd:PLN02237 318 VVDLVVNVEKKgITAEDVNAAFRKAAdgpLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVAWYDNEWGY 397
|
....*...
gi 488384039 318 SNRVVEVA 325
Cdd:PLN02237 398 SQRVVDLA 405
|
|
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-329 |
2.62e-119 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 347.49 E-value: 2.62e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 1 MSTNIAINGMGRIGRMVLRIALKNKNLNVVAIN-ASYPSETIAHLINYDTTHGTYDKKVEATENGIKVDNHEIKLVSDRN 79
Cdd:PRK08955 1 MTIKVGINGFGRIGRLALRAAWDWPELEFVQINdPAGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 80 PENLPWNelDIDIVIEATGKfnHGDKAI--AHINAGAKKVLLTGPSKGGEVQMIVKGVNDDKLDINQYDIFSNASCTTNC 157
Cdd:PRK08955 81 IADTDWS--GCDVVIEASGV--MKTKALlqAYLDQGVKRVVVTAPVKEEGVLNIVMGVNDHLFDPAIHPIVTAASCTTNC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 158 IGPVAKVLNDKFGIVNGLMTTVHAITNDQKNIDNPHKDLRRARSCNESIIPTSTGAAKALKEVLPEVEGKLHGMALRVPT 237
Cdd:PRK08955 157 LAPVVKVIHEKLGIKHGSMTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 238 KNVSLVDLVVDLEKNVTAEEVNEAFRQ---SDLDGILDVEDAPLVSVDFNTNPNSAVLDSQSTMVMGENKVKVIAWYDNE 314
Cdd:PRK08955 237 ANASLTDCVFEVERDTTVEEVNALLKEaaeGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNE 316
|
330
....*....|....*
gi 488384039 315 WGYSNRVVEVAEQIG 329
Cdd:PRK08955 317 WGYANRTAELARKVG 331
|
|
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
3-340 |
2.90e-114 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 337.60 E-value: 2.90e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 3 TNIAINGMGRIGRMVLRIALKNKNLNVVAINASY-PSETIAHLINYDTTHGTYDKKVEAT-ENGIKVDNHEIKLVSDRNP 80
Cdd:PLN02272 86 TKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFiDAKYMAYMFKYDSTHGNFKGTINVVdDSTLEINGKQIKVTSKRDP 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 81 ENLPWNELDIDIVIEATGKFNHGDKAIAHINAGAKKVLLTGPSkgGEVQMIVKGVNDDKLDINQyDIFSNASCTTNCIGP 160
Cdd:PLN02272 166 AEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPS--ADAPMFVVGVNEKTYKPNM-NIVSNASCTTNCLAP 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 161 VAKVLNDKFGIVNGLMTTVHAITNDQKNIDNPH-KDLRRARSCNESIIPTSTGAAKALKEVLPEVEGKLHGMALRVPTKN 239
Cdd:PLN02272 243 LAKVVHEEFGILEGLMTTVHATTATQKTVDGPSmKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPN 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 240 VSLVDLVVDLEKNVTAEEVNEAFRQSD---LDGILDVEDAPLVSVDFNTNPNSAVLDSQSTMVMGENKVKVIAWYDNEWG 316
Cdd:PLN02272 323 VSVVDLTCRLEKSASYEDVKAAIKYASegpLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWG 402
|
330 340
....*....|....*....|....
gi 488384039 317 YSNRVVevaeqigELIEKEATVKA 340
Cdd:PLN02272 403 YSNRVL-------DLIEHMALVAA 419
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
5-325 |
2.69e-112 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 329.71 E-value: 2.69e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 5 IAINGMGRIGRMVLRiAL----KNKNLNVVAINASYPSETIAHLINYDTTHGTYDKKVEATENGIKVDNHEIKLVSDRNP 80
Cdd:PRK13535 4 VAINGFGRIGRNVLR-ALyesgRRAEITVVAINELADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHERDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 81 ENLPWNELDIDIVIEATGKFNHGDKAIAHINAGAKKVLLTGPSKGGEVQMIVKGVNDDKLdINQYDIFSNASCTTNCIGP 160
Cdd:PRK13535 83 ASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSNDLDATVVYGVNHDQL-RAEHRIVSNASCTTNCIIP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 161 VAKVLNDKFGIVNGLMTTVHAITNDQKNIDNPHKDLRRARSCNESIIPTSTGAAKALKEVLPEVEGKLHGMALRVPTKNV 240
Cdd:PRK13535 162 VIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPTINV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 241 SLVDLVVDLEKNVTAEEVNEAFRQS---DLDGILDVEDAPLVSVDFNTNPNSAVLDSQSTMVMGENKVKVIAWYDNEWGY 317
Cdd:PRK13535 242 TAIDLSVTVKKPVKVNEVNQLLQKAaqgAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNEWGF 321
|
....*...
gi 488384039 318 SNRVVEVA 325
Cdd:PRK13535 322 ANRMLDTT 329
|
|
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-328 |
1.52e-102 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 304.84 E-value: 1.52e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 1 MSTNIAINGMGRIGRMVLRIALKNKNLNVVAINASYPS-ETIAHLINYDTTHGTYDKKVEATENGIKVDNHEIKLVSDRN 79
Cdd:PTZ00023 1 MVVKLGINGFGRIGRLVFRAALEREDVEVVAINDPFMTlDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 80 PENLPWNELDIDIVIEATGKFNHGDKAIAHINAGAKKVLLTGPSKGgEVQMIVKGVNDDKLDINQYdIFSNASCTTNCIG 159
Cdd:PTZ00023 81 PAAIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKD-DTPIYVMGVNHTQYDKSQR-IVSNASCTTNCLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 160 PVAKVLNDKFGIVNGLMTTVHAITNDQKNIDNPH---KDLRRARSCNESIIPTSTGAAKALKEVLPEVEGKLHGMALRVP 236
Cdd:PTZ00023 159 PLAKVVNDKFGIVEGLMTTVHASTANQLTVDGPSkggKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 237 TKNVSLVDLVVDLEKNVTAEEVNEAFRQS---DLDGILDVEDAPLVSVDFNTNPNSAVLDSQSTMVMGENKVKVIAWYDN 313
Cdd:PTZ00023 239 VPDVSVVDLTCKLAKPAKYEEIVAAVKKAaegPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDN 318
|
330
....*....|....*
gi 488384039 314 EWGYSNRVVEVAEQI 328
Cdd:PTZ00023 319 EWGYSNRLLDLAHYI 333
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
1-330 |
1.90e-101 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 302.04 E-value: 1.90e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 1 MSTNIAINGMGRIGRMVLRIALKNKNLNVVAINASYPSETIAHLINYDTTHGTYDKKVEATENGIKVDNHEIKLVSDRNP 80
Cdd:PRK15425 1 MTIKVGINGFGRIGRIVFRAAQKRSDIEIVAINDLLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 81 ENLPWNELDIDIVIEATGKFNHGDKAIAHINAGAKKVLLTGPSKgGEVQMIVKGVNDDKLdiNQYDIFSNASCTTNCIGP 160
Cdd:PRK15425 81 ANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSK-DNTPMFVKGANFDKY--AGQDIVSNASCTTNCLAP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 161 VAKVLNDKFGIVNGLMTTVHAITNDQKNIDNP-HKDLRRARSCNESIIPTSTGAAKALKEVLPEVEGKLHGMALRVPTKN 239
Cdd:PRK15425 158 LAKVINDNFGIIEGLMTTVHATTATQKTVDGPsHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 240 VSLVDLVVDLEKNVTAEEVNEAFRQSD---LDGILDVEDAPLVSVDFNTNPNSAVLDSQSTMVMGENKVKVIAWYDNEWG 316
Cdd:PRK15425 238 VSVVDLTVRLEKAATYEQIKAAVKAAAegeMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETG 317
|
330
....*....|....
gi 488384039 317 YSNRVVEVAEQIGE 330
Cdd:PRK15425 318 YSNKVLDLIAHISK 331
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
153-314 |
1.46e-100 |
|
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: 293.21 E-value: 1.46e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 153 CTTNCIGPVAKVLNDKFGIVNGLMTTVHAITNDQKNIDNPHKDLRRARSCNESIIPTSTGAAKALKEVLPEVEGKLHGMA 232
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 233 LRVPTKNVSLVDLVVDLEKNVTAEEVNEAFR---QSDLDGILDVEDAPLVSVDFNTNPNSAVLDSQSTMVMGENKVKVIA 309
Cdd:cd18126 81 FRVPTPNVSVVDLTVRLEKPVTVEEVNAALKkaaEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVVA 160
|
....*
gi 488384039 310 WYDNE 314
Cdd:cd18126 161 WYDNE 165
|
|
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
5-324 |
3.80e-92 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 278.53 E-value: 3.80e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 5 IAINGMGRIGRMVLRIALKNKNLNVVAINASY-PSETIAHLINYDTTHGTYdkkveaTENGIKVDNHEIKLVSD------ 77
Cdd:PLN02358 8 IGINGFGRIGRLVARVVLQRDDVELVAVNDPFiTTEYMTYMFKYDSVHGQW------KHHELKVKDDKTLLFGEkpvtvf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 78 --RNPENLPWNELDIDIVIEATGKFNHGDKAIAHINAGAKKVLLTGPSKggEVQMIVKGVNDDKLDiNQYDIFSNASCTT 155
Cdd:PLN02358 82 giRNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSK--DAPMFVVGVNEHEYK-SDLDIVSNASCTT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 156 NCIGPVAKVLNDKFGIVNGLMTTVHAITNDQKNIDNPH-KDLRRARSCNESIIPTSTGAAKALKEVLPEVEGKLHGMALR 234
Cdd:PLN02358 159 NCLAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSmKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 235 VPTKNVSLVDLVVDLEKNVTAEEVNEAFRQSD---LDGILDVEDAPLVSVDFNTNPNSAVLDSQSTMVMGENKVKVIAWY 311
Cdd:PLN02358 239 VPTVDVSVVDLTVRLEKAATYDEIKKAIKEESegkLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWY 318
|
330
....*....|...
gi 488384039 312 DNEWGYSNRVVEV 324
Cdd:PLN02358 319 DNEWGYSSRVVDL 331
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
1-324 |
4.98e-90 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 273.86 E-value: 4.98e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 1 MSTNIAINGMGRIGRMVLRI----ALKNKNLNVVAI-NASYPSETIAHLINYDTTHGTYDKKVEATENG--------IKV 67
Cdd:PTZ00434 2 APIKVGINGFGRIGRMVFQAicdqGLIGTEIDVVAVvDMSTNAEYFAYQMKYDTVHGRPKYTVETTKSSpsvktddvLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 68 DNHEIKLV-SDRNPENLPWNELDIDIVIEATGKFNHGDKAIAHINAGAKKVLLTGPSKGGeVQMIVKGVNDDKLDINQYD 146
Cdd:PTZ00434 82 NGHRIKCVkAQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPASGG-AKTIVMGVNQHEYSPTEHH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 147 IFSNASCTTNCIGPVAKVL-NDKFGIVNGLMTTVHAITNDQKNIDNPH-KDLRRARSCNESIIPTSTGAAKALKEVLPEV 224
Cdd:PTZ00434 161 VVSNASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSvKDWRGGRAAAVNIIPSTTGAAKAVGMVIPST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 225 EGKLHGMALRVPTKNVSLVDLVVDLEKNVTAEEVNEAFR---QSDLDGILDVEDAPLVSVDFNTNPNSAVLDSQSTM--- 298
Cdd:PTZ00434 241 KGKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKrasQTYMKGILGFTDDELVSADFINDNRSSIYDSKATLqnn 320
|
330 340
....*....|....*....|....*..
gi 488384039 299 VMGENK-VKVIAWYDNEWGYSNRVVEV 324
Cdd:PTZ00434 321 LPGERRfFKIVSWYDNEWGYSHRVVDL 347
|
|
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
2-328 |
2.18e-83 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 260.24 E-value: 2.18e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 2 STNIAINGMGRIGRMVLRIAL----KNKNLNVVAI----NASYPSETIAHLINYDTTHGTYDKKVEATE--NGIKVDNHE 71
Cdd:PRK08289 127 PRDVVLYGFGRIGRLLARLLIektgGGNGLRLRAIvvrkGSEGDLEKRASLLRRDSVHGPFNGTITVDEenNAIIANGNY 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 72 IKLVSDRNPENLPWNELDID--IVIEATGKFNHGDKAIAHINA-GAKKVLLTGPSKGgEVQMIVKGVNDDklDINQYD-I 147
Cdd:PRK08289 207 IQVIYANSPEEVDYTAYGINnaLVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGKG-DIKNIVHGVNHS--DITDEDkI 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 148 FSNASCTTNCIGPVAKVLNDKFGIVNGLMTTVHAITNDQKNIDNPHKDLRRARSCNESIIPTSTGAAKALKEVLPEVEGK 227
Cdd:PRK08289 284 VSAASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKGDRRGRSAPLNMVITETGAAKAVAKALPELAGK 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 228 LHGMALRVPTKNVSLVDLVVDLEKNVTAEEVNEAFRQ----SDLDGILDVEDAP-LVSVDFNTNPNSAVLDSQSTMVMGE 302
Cdd:PRK08289 364 LTGNAIRVPTPNVSMAILNLNLEKETSREELNEYLRQmslhSPLQNQIDYTDSTeVVSSDFVGSRHAGVVDSQATIVNGN 443
|
330 340
....*....|....*....|....*.
gi 488384039 303 NKVkVIAWYDNEWGYSNRVVEVAEQI 328
Cdd:PRK08289 444 RAV-LYVWYDNEFGYSCQVVRVMEQM 468
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
160-311 |
6.18e-77 |
|
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: 232.87 E-value: 6.18e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 160 PVAKVLNDKFGIVNGLMTTVHAITNDQKNIDNPH-KDLRRARSCNESIIPTSTGAAKALKEVLPEVEGKLHGMALRVPTK 238
Cdd:pfam02800 3 PLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHhKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTP 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488384039 239 NVSLVDLVVDLEKNVTAEEVNEAFR---QSDLDGILDVEDAPLVSVDFNTNPNSAVLDSQSTMVMGENKVKVIAWY 311
Cdd:pfam02800 83 NVSVVDLVVELEKPVTVEEVNAALKeaaEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| GAPDH_I_N |
cd05214 |
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
3-152 |
2.01e-68 |
|
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: 211.48 E-value: 2.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 3 TNIAINGMGRIGRMVLRIALKNKNLNVVAINASYPSETIAHLINYDTTHGTYDKKVEATENGIKVDNHEIKLVSDRNPEN 82
Cdd:cd05214 1 IKVGINGFGRIGRLVFRAALERDDIEVVAINDLTDDETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAE 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 83 LPWNELDIDIVIEATGKFNHGDKAIAHINAGAKKVLLTGPSKgGEVQMIVKGVNDDKLDINQyDIFSNAS 152
Cdd:cd05214 81 LPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAK-DDDPTIVMGVNHDKYDADD-KIISNAS 148
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
5-153 |
1.17e-63 |
|
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: 198.93 E-value: 1.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 5 IAINGMGRIGRMVLRIALKNKNLNVVAINASYPSETIAHLINYDTTHGTYDKKVEATENGIKVDNHEIKLVSDRNPENLP 84
Cdd:smart00846 3 VGINGFGRIGRLVLRAALERPDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANLP 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488384039 85 WNELDIDIVIEATGKFNHGDKAIAHINAGAKKVLLTGPSKgGEVQMIVKGVNDDKLDINQyDIFSNASC 153
Cdd:smart00846 83 WGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSK-DADPTFVYGVNHDEYDGED-HIISNASC 149
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
153-314 |
4.94e-59 |
|
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: 187.62 E-value: 4.94e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 153 CTTNCIGPVAKVLNDKFGIVNGLMTTVHAITNDQKNIDNPHKDLRRARSCNESIIPTSTGAAKALKEVLPEVEGKLHGMA 232
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 233 LRVPTKNVSLVDLVVDLEKNVTAEEVNEAFRQ---SDLDGILDVEDAPLVSVDFNTNPNSAVLDSQSTMVMGENKVKVIA 309
Cdd:cd23937 81 VRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQasqGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLLV 160
|
....*
gi 488384039 310 WYDNE 314
Cdd:cd23937 161 WCDNE 165
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
153-314 |
1.03e-52 |
|
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: 171.26 E-value: 1.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 153 CTTNCIGPVAKVLNDKFGIVNGLMTTVHAITNDQKNIDNP-HKDLRRARSCNESIIPTSTGAAKALKEVLPEVEGKLHGM 231
Cdd:cd18123 1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPsGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 232 ALRVPTKNVSLVDLVVDLEKNVTAEEVNEAFRQ-SDLDGILDVEDAPLVSVDFNTNPNSAVLDSQSTMVMGENKVKVIAW 310
Cdd:cd18123 81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQaPEGKGRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLMQW 160
|
....
gi 488384039 311 YDNE 314
Cdd:cd18123 161 YDNE 164
|
|
| Gp_dh_N |
pfam00044 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-101 |
1.19e-46 |
|
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: 153.41 E-value: 1.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 3 TNIAINGMGRIGRMVLRIALKNKNLNVVAINASYPSETIAHLINYDTTHGTYDKKVEATENGIKVDNHEIKLVSDRNPEN 82
Cdd:pfam00044 1 VKVGINGFGRIGRLVLRAALERPDIEVVAINDLTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAE 80
|
90
....*....|....*....
gi 488384039 83 LPWNELDIDIVIEATGKFN 101
Cdd:pfam00044 81 LPWGDLGVDVVIESTGVFT 99
|
|
| GAPDH_N_E4PDH |
cd17892 |
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
4-152 |
1.33e-45 |
|
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: 153.19 E-value: 1.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 4 NIAINGMGRIGRMVLRiAL----KNKNLNVVAINASYPSETIAHLINYDTTHGTYDKKVEATENGIKVDNHEIKLVSDRN 79
Cdd:cd17892 2 RVAINGYGRIGRNVLR-ALyesgRRAEFQVVAINELADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488384039 80 PENLPWNELDIDIVIEATGKFNHGDKAIAHINAGAKKVLLTGPSKGGEVQMIVKGVNDDKLDINQyDIFSNAS 152
Cdd:cd17892 81 PENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASNDVDATIVYGINQDLLRAEH-RIVSNAS 152
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-328 |
3.20e-36 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 133.85 E-value: 3.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 1 MSTNIAINGMGRIGRMVLRIALKNKNLNVVAIN-ASYPSETIAHLINYDTTHGTYDK-KVEATENGIKVDN-HEIKLVSD 77
Cdd:PTZ00353 1 LPITVGINGFGPVGKAVLFASLTDPLVTVVAVNdASVSIAYIAYVLEQESPLSAPDGaSIRVVGEQIVLNGtQKIRVSAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 78 RNPENLPWNELDIDIVIEATGKFNHGDKAIAHINAGAKKVLLTGPSkgGEVQMIVKGVNDDKLdinqydifsNASCTTNC 157
Cdd:PTZ00353 81 HDLVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQS--ADAPTVMAGSNDERL---------SASLPVCC 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 158 IG--------PVAKVLNDKFGIVNGLMTTVHAITNDQKNI---DNPhKDLRRARSCNESIIPTSTGAAKALKEVLPEVEG 226
Cdd:PTZ00353 150 AGapiavalaPVIRALHEVYGVEECSYTAIHGMQPQEPIAarsKNS-QDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 227 KLHGMALRVPTKNVSLVDLVVDLEKNVTAEEVNEAFRQSDLD---GILDVEDAPLVSVDfnTNPNSAV-LDSQSTMVMGE 302
Cdd:PTZ00353 229 RISGSAFQVPVKKGCAIDMLVRTKQPVSKEVVDSALAEAASDrlnGVLCISKRDMISVD--CIPNGKLcYDATSSSSSRE 306
|
330 340
....*....|....*....|....*..
gi 488384039 303 NKV-KVIAWYDNEWGYSNRVVEVAEQI 328
Cdd:PTZ00353 307 GEVhKMVLWFDVECYYAARLLSLVKQL 333
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
153-314 |
9.17e-30 |
|
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: 111.84 E-value: 9.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 153 CTTNCIGPVAKVLNDKFGIVNGLMTTVHAITNDQKNIDNPHkDLRRARSCNESIIPTSTGAAKALKEVLPEVE--GKLHG 230
Cdd:cd18122 1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPI-LKSEVRAIIPNIPKNETKHAPETGKVLGEIGkpIKVDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 231 MALRVPTKNVSLVDLVVDLEKNVTAEEVNEAFR---QSDLDGILDVEDAPLVSVDFNTNPNSAVLDSQSTMVMGENKVKV 307
Cdd:cd18122 80 IAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAeavEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLKV 159
|
....*..
gi 488384039 308 IAWYDNE 314
Cdd:cd18122 160 FSAVDNE 166
|
|
| GAPDH-like_N |
cd05192 |
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ... |
5-164 |
1.05e-05 |
|
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like family; The GAPDH-like family includes glyceraldehyde-3-phosphate dehydrogenase (GAPDH), native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs), 2,4-diaminopentanoate dehydrogenase (DAPDH), meso-diaminopimelate D-dehydrogenase (meso-DAPDH), and dihydrodipicolinate reductase (DHDPR). GAPDH plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. nat-AmDHs catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. They play important roles in the efficient asymmetric synthesis of alpha-chiral amines. DAPDH is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). DHDPR catalyzes the NAD(P)H-dependent reduction of 2,3-dihydrodipicolinate (DHDP) to 2,3,4,5-tetrahydrodipicolinate (THDP). It could also function as a dehydratase in addition to the role of a nucleotide dependent reductase. The model corresponds to the N-terminal NAD(P)-binding domain of GAPDH-like family proteins. It contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft.
Pssm-ID: 467613 [Multi-domain] Cd Length: 109 Bit Score: 43.88 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 5 IAINGMGRIGRMVLRIALKNKNLNVVAINasypsetiahlinyDTThgtydkkveatengikvdnheiklvsdrnpenlp 84
Cdd:cd05192 3 VAINGFGRIGRIVFRAIADQDDLDVVAIN--------------DRR---------------------------------- 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488384039 85 wneldiDIVIEATGKFNHGDKAIAHINAGAKKVLLTGPSKGGEVQmIVKGVNDDKLDINQyDIFSNASCTTNCIGPVAKV 164
Cdd:cd05192 35 ------DVVIECTGSFTDDDNAEKHIKAGGKKAVITAPEKGDIPT-IVVVLNELAKSAGA-TVVSNANETSYSPQVVDLV 106
|
|
| |
