|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
2-334 |
0e+00 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 746.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 2 TVRVAINGFGRIGRNVVRALYESGRRAEITVVAINELADAAGMAHLLKYDTSHGRFAWEVRQERDQLFVGDDAIRVLHER 81
Cdd:PRK13535 1 TIRVAINGFGRIGRNVLRALYESGRRAEITVVAINELADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 82 SLQSLPWRELGVDVVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGSNDLDTTVVYGVNQDQLRAEHRIVSNASCTTNCII 161
Cdd:PRK13535 81 DIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSNDLDATVVYGVNHDQLRAEHRIVSNASCTTNCII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 162 PVIKLLDDAYGIESGTVTTIHSAMHDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVPTIN 241
Cdd:PRK13535 161 PVIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPTIN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 242 VTAIDLSVTVKKPVKANEVNLLLQKAAQGAFHGIVDYAELPLVSVDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNEWG 321
Cdd:PRK13535 241 VTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNEWG 320
|
330
....*....|...
gi 254782092 322 FANRMLDTTLAMA 334
Cdd:PRK13535 321 FANRMLDTTLAMA 333
|
|
| E4PD_g-proteo |
TIGR01532 |
erythrose-4-phosphate dehydrogenase; This model represents the small clade of dehydrogenases ... |
4-328 |
0e+00 |
|
erythrose-4-phosphate dehydrogenase; This model represents the small clade of dehydrogenases in gamma-proteobacteria 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. This enzyme activity appears to have evolved from glyceraldehyde-3-phosphate dehydrogenase, whose substrate differs only in the lack of one carbon relative to E4P. Accordingly, this model is very close to the corresponding models for GAPDH, and those sequences which hit above trusted here invariably hit between trusted and noise to the GAPDH model (TIGR01534). Similarly, it may be found that there are species outside of the gamma proteobacteria which synthesize pyridoxine and have more than one aparrent GAPDH gene of which one may have E4PD activity - this may necessitate a readjustment of these models. Alternatively, some of the GAPDH enzymes may prove to be bifunctional in certain species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
Pssm-ID: 130595 Cd Length: 325 Bit Score: 648.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 4 RVAINGFGRIGRNVVRALYESGRRAEITVVAINELADAAGMAHLLKYDTSHGRFAWEVRQERDQLFVGDDAIRVLHERSL 83
Cdd:TIGR01532 1 RVAINGFGRIGRNVLRALYESGRRAEITVVAINELADAAGMAHLLKYDTSHGRFAWEVRQDRDQLFVGDDAIRVLHERSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 84 QSLPWRELGVDVVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGSNDLDTTVVYGVNQDQLRAEHRIVSNASCTTNCIIPV 163
Cdd:TIGR01532 81 QSLPWRELGVDLVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGASDLDATIVYGVNQDQLRAEHRIVSNASCTTNCIVPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 164 IKLLDDAYGIESGTVTTIHSAMHDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVPTINVT 243
Cdd:TIGR01532 161 IKLLDDAYGIESGTITTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGIERFFPQFNDRFEAIAVRVPTVNVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 244 AIDLSVTVKKPVKANEVNLLLQKAAQGAFHGIVDYAELPLVSVDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNEWGFA 323
Cdd:TIGR01532 241 AIDLSVTVKKPVKANEVNLLLQKAAQGALRGIVDYTELPLVSVDFNHDPHSAIVDGTQTRVSGAHLVKTLVWCDNEWGFA 320
|
....*
gi 254782092 324 NRMLD 328
Cdd:TIGR01532 321 NRMLD 325
|
|
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
1-336 |
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: 550.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 1 MTVRVAINGFGRIGRNVVRALYESGrrAEITVVAINELADAAGMAHLLKYDTSHGRFAWEVRQERDQLFVGDDAIRVLHE 80
Cdd:COG0057 1 MTIRVAINGFGRIGRLVLRALLERG--PDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 81 RSLQSLPWRELGVDVVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGSNDlDTTVVYGVNQDQLRAEHRIVSNASCTTNCI 160
Cdd:COG0057 79 RDPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGD-DPTIVYGVNHDDYDADHRIISNASCTTNCL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 161 IPVIKLLDDAYGIESGTVTTIHSAMHDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVPTI 240
Cdd:COG0057 158 APVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 241 NVTAIDLSVTVKKPVKANEVNLLLQKAAQGAFHGIVDYAELPLVSVDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNEW 320
Cdd:COG0057 238 NVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEW 317
|
330
....*....|....*.
gi 254782092 321 GFANRMLDTTLAMATV 336
Cdd:COG0057 318 GYSNRMVDLAEYMAKL 333
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
155-319 |
4.17e-113 |
|
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: 325.14 E-value: 4.17e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 155 CTTNCIIPVIKLLDDAYGIESGTVTTIHSAMHDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIA 234
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 235 VRVPTINVTAIDLSVTVKKPVKANEVNLLLQKAAQGAFHGIVDYAELPLVSVDFNHDPHSAIVDGTQTRVSGAHLIKTLV 314
Cdd:cd23937 81 VRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLLV 160
|
....*
gi 254782092 315 WCDNE 319
Cdd:cd23937 161 WCDNE 165
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
5-328 |
3.06e-110 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 323.81 E-value: 3.06e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 5 VAINGFGRIGRNVVRALYEsgrRAEITVVAINELA-DAAGMAHLLKYDTSHGRFAWEVRQERDQLFVGDDAIRVLHERSL 83
Cdd:NF033735 1 IGINGFGRIGRLALRALWG---RPGLEIVHINDLAgDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 84 QSLPWRElGVDVVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGSNDLDTTVVYGVNQDQLR-AEHRIVSNASCTTNCIIP 162
Cdd:NF033735 78 EDTPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLNIVYGVNDHLYDpARHRIVTAASCTTNCLAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 163 VIKLLDDAYGIESGTVTTIHSAMHDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVPTINV 242
Cdd:NF033735 157 VVKVIHEKIGIKHGSITTIHDITNTQTIVDAPHKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 243 TAIDLSVTVKKPVKANEVNLLLQKAAQGAFHGIVDYAELPLVSVDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNEWGF 322
Cdd:NF033735 237 SLTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGY 316
|
....*.
gi 254782092 323 ANRMLD 328
Cdd:NF033735 317 ANRMVD 322
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-155 |
1.46e-73 |
|
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: 223.97 E-value: 1.46e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 3 VRVAINGFGRIGRNVVRALYEsgrRAEITVVAINELADAAGMAHLLKYDTSHGRFAWEVRQERDQLFVGDDAIRVLHERS 82
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALE---RPDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERD 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254782092 83 LQSLPWRELGVDVVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGSNDlDTTVVYGVNQDQLRAEHRIVSNASC 155
Cdd:smart00846 78 PANLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDA-DPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
160-316 |
3.02e-69 |
|
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: 213.22 E-value: 3.02e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 160 IIPVIKLLDDAYGIESGTVTTIHSAMHDQQVIDAYHP-DLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVP 238
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHkDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254782092 239 TINVTAIDLSVTVKKPVKANEVNLLLQKAAQGAFHGIVDYAELPLVSVDFNHDPHSAIVDGTQTRVSGAHLIKTLVWC 316
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
2-334 |
0e+00 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 746.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 2 TVRVAINGFGRIGRNVVRALYESGRRAEITVVAINELADAAGMAHLLKYDTSHGRFAWEVRQERDQLFVGDDAIRVLHER 81
Cdd:PRK13535 1 TIRVAINGFGRIGRNVLRALYESGRRAEITVVAINELADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 82 SLQSLPWRELGVDVVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGSNDLDTTVVYGVNQDQLRAEHRIVSNASCTTNCII 161
Cdd:PRK13535 81 DIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSNDLDATVVYGVNHDQLRAEHRIVSNASCTTNCII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 162 PVIKLLDDAYGIESGTVTTIHSAMHDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVPTIN 241
Cdd:PRK13535 161 PVIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPTIN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 242 VTAIDLSVTVKKPVKANEVNLLLQKAAQGAFHGIVDYAELPLVSVDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNEWG 321
Cdd:PRK13535 241 VTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNEWG 320
|
330
....*....|...
gi 254782092 322 FANRMLDTTLAMA 334
Cdd:PRK13535 321 FANRMLDTTLAMA 333
|
|
| E4PD_g-proteo |
TIGR01532 |
erythrose-4-phosphate dehydrogenase; This model represents the small clade of dehydrogenases ... |
4-328 |
0e+00 |
|
erythrose-4-phosphate dehydrogenase; This model represents the small clade of dehydrogenases in gamma-proteobacteria 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. This enzyme activity appears to have evolved from glyceraldehyde-3-phosphate dehydrogenase, whose substrate differs only in the lack of one carbon relative to E4P. Accordingly, this model is very close to the corresponding models for GAPDH, and those sequences which hit above trusted here invariably hit between trusted and noise to the GAPDH model (TIGR01534). Similarly, it may be found that there are species outside of the gamma proteobacteria which synthesize pyridoxine and have more than one aparrent GAPDH gene of which one may have E4PD activity - this may necessitate a readjustment of these models. Alternatively, some of the GAPDH enzymes may prove to be bifunctional in certain species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
Pssm-ID: 130595 Cd Length: 325 Bit Score: 648.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 4 RVAINGFGRIGRNVVRALYESGRRAEITVVAINELADAAGMAHLLKYDTSHGRFAWEVRQERDQLFVGDDAIRVLHERSL 83
Cdd:TIGR01532 1 RVAINGFGRIGRNVLRALYESGRRAEITVVAINELADAAGMAHLLKYDTSHGRFAWEVRQDRDQLFVGDDAIRVLHERSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 84 QSLPWRELGVDVVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGSNDLDTTVVYGVNQDQLRAEHRIVSNASCTTNCIIPV 163
Cdd:TIGR01532 81 QSLPWRELGVDLVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGASDLDATIVYGVNQDQLRAEHRIVSNASCTTNCIVPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 164 IKLLDDAYGIESGTVTTIHSAMHDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVPTINVT 243
Cdd:TIGR01532 161 IKLLDDAYGIESGTITTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGIERFFPQFNDRFEAIAVRVPTVNVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 244 AIDLSVTVKKPVKANEVNLLLQKAAQGAFHGIVDYAELPLVSVDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNEWGFA 323
Cdd:TIGR01532 241 AIDLSVTVKKPVKANEVNLLLQKAAQGALRGIVDYTELPLVSVDFNHDPHSAIVDGTQTRVSGAHLVKTLVWCDNEWGFA 320
|
....*
gi 254782092 324 NRMLD 328
Cdd:TIGR01532 321 NRMLD 325
|
|
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
1-336 |
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: 550.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 1 MTVRVAINGFGRIGRNVVRALYESGrrAEITVVAINELADAAGMAHLLKYDTSHGRFAWEVRQERDQLFVGDDAIRVLHE 80
Cdd:COG0057 1 MTIRVAINGFGRIGRLVLRALLERG--PDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 81 RSLQSLPWRELGVDVVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGSNDlDTTVVYGVNQDQLRAEHRIVSNASCTTNCI 160
Cdd:COG0057 79 RDPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGD-DPTIVYGVNHDDYDADHRIISNASCTTNCL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 161 IPVIKLLDDAYGIESGTVTTIHSAMHDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVPTI 240
Cdd:COG0057 158 APVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 241 NVTAIDLSVTVKKPVKANEVNLLLQKAAQGAFHGIVDYAELPLVSVDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNEW 320
Cdd:COG0057 238 NVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEW 317
|
330
....*....|....*.
gi 254782092 321 GFANRMLDTTLAMATV 336
Cdd:COG0057 318 GYSNRMVDLAEYMAKL 333
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
4-328 |
8.42e-136 |
|
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: 388.94 E-value: 8.42e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 4 RVAINGFGRIGRNVVRALYESgRRAEITVVAINELADAAGMAHLLKYDTSHGRFAWEVRQERDQLFV-GDDAIRVLHERS 82
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEK-PGNDLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVnGKEVISVFSERD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 83 LQSLPWRELGVDVVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGSNDlDTTVVYGVNQDQLRAEHRIVSNASCTTNCIIP 162
Cdd:TIGR01534 80 PSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGD-VKTIVYGVNHDEYDGEERIISNASCTTNCLAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 163 VIKLLDDAYGIESGTVTTIHSAMHDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVPTINV 242
Cdd:TIGR01534 159 LAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 243 TAIDLSVTVKKPVKANEVNLLLQKAAQGAFHGIVDYAELPLVSVDFNHDPHSAIVDGTQTRVSGAH--LIKTLVWCDNEW 320
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVTGLGdsLVKVYAWYDNEW 318
|
....*...
gi 254782092 321 GFANRMLD 328
Cdd:TIGR01534 319 GYSNRLVD 326
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-328 |
4.18e-131 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 377.54 E-value: 4.18e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 1 MTVRVAINGFGRIGRNVVRALYESGRraeITVVAINELADAAGMAHLLKYDTSHGRFAWEVRQERDQLFVGDDAIRVLHE 80
Cdd:PRK07729 1 MKTKVAINGFGRIGRMVFRKAIKESA---FEIVAINASYPSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 81 RSLQSLPWRELGVDVVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGSNDlDTTVVYGVNQDQLRAE-HRIVSNASCTTNC 159
Cdd:PRK07729 78 RDPKELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNE-DVTIVVGVNEDQLDIEkHTIISNASCTTNC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 160 IIPVIKLLDDAYGIESGTVTTIHSAMHDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVPT 239
Cdd:PRK07729 157 LAPVVKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 240 INVTAIDLSVTVKKPVKANEVNLLLQKAAQGAFHGIVDYAELPLVSVDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNE 319
Cdd:PRK07729 237 PNVSLVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNE 316
|
....*....
gi 254782092 320 WGFANRMLD 328
Cdd:PRK07729 317 WGYSCRVVD 325
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
155-319 |
4.17e-113 |
|
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: 325.14 E-value: 4.17e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 155 CTTNCIIPVIKLLDDAYGIESGTVTTIHSAMHDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIA 234
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 235 VRVPTINVTAIDLSVTVKKPVKANEVNLLLQKAAQGAFHGIVDYAELPLVSVDFNHDPHSAIVDGTQTRVSGAHLIKTLV 314
Cdd:cd23937 81 VRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLLV 160
|
....*
gi 254782092 315 WCDNE 319
Cdd:cd23937 161 WCDNE 165
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
5-328 |
3.06e-110 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 323.81 E-value: 3.06e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 5 VAINGFGRIGRNVVRALYEsgrRAEITVVAINELA-DAAGMAHLLKYDTSHGRFAWEVRQERDQLFVGDDAIRVLHERSL 83
Cdd:NF033735 1 IGINGFGRIGRLALRALWG---RPGLEIVHINDLAgDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 84 QSLPWRElGVDVVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGSNDLDTTVVYGVNQDQLR-AEHRIVSNASCTTNCIIP 162
Cdd:NF033735 78 EDTPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLNIVYGVNDHLYDpARHRIVTAASCTTNCLAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 163 VIKLLDDAYGIESGTVTTIHSAMHDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVPTINV 242
Cdd:NF033735 157 VVKVIHEKIGIKHGSITTIHDITNTQTIVDAPHKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 243 TAIDLSVTVKKPVKANEVNLLLQKAAQGAFHGIVDYAELPLVSVDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNEWGF 322
Cdd:NF033735 237 SLTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGY 316
|
....*.
gi 254782092 323 ANRMLD 328
Cdd:NF033735 317 ANRMVD 322
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
2-328 |
2.39e-106 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 314.54 E-value: 2.39e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 2 TVRVAINGFGRIGRNVVRALYesGRR-AEITVVAINELADAAGMAHLLKYDTSHGRFAWEVRQERDQLFVGDDAIRVLHE 80
Cdd:PRK07403 1 MIRVAINGFGRIGRNFLRCWL--GREnSQLELVAINDTSDPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 81 RSLQSLPWRELGVDVVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGSNDLDTTVVYGVNQDQLRAE-HRIVSNASCTTNC 159
Cdd:PRK07403 79 RNPLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPGKGEDIGTYVVGVNHHEYDHEdHNIISNASCTTNC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 160 IIPVIKLLDDAYGIESGTVTTIHSAMHDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVPT 239
Cdd:PRK07403 159 LAPIAKVLHDNFGIIKGTMTTTHSYTGDQRILDASHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 240 INVTAIDLSVTVKKPVKANEVNLLLQKAAQGAFHGIVDYAELPLVSVDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNE 319
Cdd:PRK07403 239 PNVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYDNE 318
|
....*....
gi 254782092 320 WGFANRMLD 328
Cdd:PRK07403 319 WGYSQRVVD 327
|
|
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-325 |
1.20e-100 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 299.72 E-value: 1.20e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 1 MTVRVAINGFGRIGRNVVRALYESgrrAEITVVAINELA-DAAGMAHLLKYDTSHGRFAWEVRQERDQLFVGDDAIRVLH 79
Cdd:PRK08955 1 MTIKVGINGFGRIGRLALRAAWDW---PELEFVQINDPAgDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 80 ERSLQSLPWRelGVDVVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGSNDLDTTVVYGVNqDQL--RAEHRIVSNASCTT 157
Cdd:PRK08955 78 NKAIADTDWS--GCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLNIVMGVN-DHLfdPAIHPIVTAASCTT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 158 NCIIPVIKLLDDAYGIESGTVTTIHSAMHDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRV 237
Cdd:PRK08955 155 NCLAPVVKVIHEKLGIKHGSMTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 238 PTINVTAIDLSVTVKKPVKANEVNLLLQKAAQGAFHGIVDYAELPLVSVDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCD 317
Cdd:PRK08955 235 PLANASLTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYD 314
|
....*...
gi 254782092 318 NEWGFANR 325
Cdd:PRK08955 315 NEWGYANR 322
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
3-328 |
1.13e-96 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 291.83 E-value: 1.13e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 3 VRVAINGFGRIGRNVVRALYesGRR-AEITVVAINELADAAGMAHLLKYDTSHGRFAWEVRQERDQ-LFVGDDAIRVLHE 80
Cdd:PLN03096 61 IKVAINGFGRIGRNFLRCWH--GRKdSPLDVVAINDTGGVKQASHLLKYDSTLGTFDADVKPVGDDaISVDGKVIKVVSD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 81 RSLQSLPWRELGVDVVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGSNDLDTTVVyGVNQDQLRAEHRIVSNASCTTNCI 160
Cdd:PLN03096 139 RNPLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKGDIPTYVV-GVNADDYKHSDPIISNASCTTNCL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 161 IPVIKLLDDAYGIESGTVTTIHSAMHDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVPTI 240
Cdd:PLN03096 218 APFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTP 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 241 NVTAIDLSVTVKKPVKANEVNLLLQKAAQGAFHGIVDYAELPLVSVDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNEW 320
Cdd:PLN03096 298 NVSVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAWYDNEW 377
|
....*...
gi 254782092 321 GFANRMLD 328
Cdd:PLN03096 378 GYSQRVVD 385
|
|
| GAPDH_N_E4PDH |
cd17892 |
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
3-154 |
3.82e-96 |
|
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: 282.23 E-value: 3.82e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 3 VRVAINGFGRIGRNVVRALYESGRRAEITVVAINELADAAGMAHLLKYDTSHGRFAWEVRQERDQLFVGDDAIRVLHERS 82
Cdd:cd17892 1 YRVAINGYGRIGRNVLRALYESGRRAEFQVVAINELADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254782092 83 LQSLPWRELGVDVVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGSNDLDTTVVYGVNQDQLRAEHRIVSNAS 154
Cdd:cd17892 81 PENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASNDVDATIVYGINQDLLRAEHRIVSNAS 152
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
3-334 |
1.47e-92 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 282.94 E-value: 1.47e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 3 VRVAINGFGRIGRNVVRAlYESGRRAEITVVAINELADAAGMAHLLKYDTSHGRFAWEVRQERDQ-LFVGDDAIRVLHER 81
Cdd:PLN02237 76 LKVAINGFGRIGRNFLRC-WHGRKDSPLDVVVVNDSGGVKNASHLLKYDSMLGTFKADVKIVDDEtISVDGKPIKVVSNR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 82 SLQSLPWRELGVDVVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGS-NDLDTTVVyGVNQDQLRAEH-RIVSNASCTTNC 159
Cdd:PLN02237 155 DPLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAKgADIPTYVV-GVNEDDYDHEVaNIVSNASCTTNC 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 160 IIPVIKLLDDAYGIESGTVTTIHSAMHDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVPT 239
Cdd:PLN02237 234 LAPFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPT 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 240 INVTAIDLSVTV-KKPVKANEVNLLLQKAAQGAFHGIVDYAELPLVSVDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDN 318
Cdd:PLN02237 314 PNVSVVDLVVNVeKKGITAEDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVAWYDN 393
|
330
....*....|....*.
gi 254782092 319 EWGFANRMLDTTLAMA 334
Cdd:PLN02237 394 EWGYSQRVVDLAHLVA 409
|
|
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-333 |
3.47e-89 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 270.55 E-value: 3.47e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 1 MTVRVAINGFGRIGRNVVRALYEsgrRAEITVVAINE-LADAAGMAHLLKYDTSHGRFAWEVRQERDQLFVGDDAIRVLH 79
Cdd:PTZ00023 1 MVVKLGINGFGRIGRLVFRAALE---REDVEVVAINDpFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 80 ERSLQSLPWRELGVDVVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGSNDlDTTVVYGVNQDQLRAEHRIVSNASCTTNC 159
Cdd:PTZ00023 78 EKDPAAIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKDD-TPIYVMGVNHTQYDKSQRIVSNASCTTNC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 160 IIPVIKLLDDAYGIESGTVTTIHSAMHDQQVIDAYH---PDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVR 236
Cdd:PTZ00023 157 LAPLAKVVNDKFGIVEGLMTTVHASTANQLTVDGPSkggKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 237 VPTINVTAIDLSVTVKKPVKANEVNLLLQKAAQGAFHGIVDYAELPLVSVDFNHDPHSAIVDGTQTRVSGAHLIKTLVWC 316
Cdd:PTZ00023 237 VPVPDVSVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWY 316
|
330
....*....|....*..
gi 254782092 317 DNEWGFANRMLDTTLAM 333
Cdd:PTZ00023 317 DNEWGYSNRLLDLAHYI 333
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
155-319 |
6.00e-85 |
|
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: 253.53 E-value: 6.00e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 155 CTTNCIIPVIKLLDDAYGIESGTVTTIHSAMHDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIA 234
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 235 VRVPTINVTAIDLSVTVKKPVKANEVNLLLQKAAQGAFHGIVDYAELPLVSVDFNHDPHSAIVDGTQTRVSGAHLIKTLV 314
Cdd:cd18126 81 FRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVVA 160
|
....*
gi 254782092 315 WCDNE 319
Cdd:cd18126 161 WYDNE 165
|
|
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
3-337 |
1.20e-82 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 256.71 E-value: 1.20e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 3 VRVAINGFGRIGRNVVRAlyeSGRRAEITVVAINE-LADAAGMAHLLKYDTSHGRFAWEVRQERDQ-LFVGDDAIRVLHE 80
Cdd:PLN02272 86 TKIGINGFGRIGRLVLRI---ATSRDDIEVVAVNDpFIDAKYMAYMFKYDSTHGNFKGTINVVDDStLEINGKQIKVTSK 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 81 RSLQSLPWRELGVDVVLDCTGVYGSREHGEAHIAAGAKKVLFSHPgSNDLDTTVVyGVNQDQLRAEHRIVSNASCTTNCI 160
Cdd:PLN02272 163 RDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAP-SADAPMFVV-GVNEKTYKPNMNIVSNASCTTNCL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 161 IPVIKLLDDAYGIESGTVTTIHSAMHDQQVIDAyhP---DLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRV 237
Cdd:PLN02272 241 APLAKVVHEEFGILEGLMTTVHATTATQKTVDG--PsmkDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRV 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 238 PTINVTAIDLSVTVKKPVKANEVNLLLQKAAQGAFHGIVDYAELPLVSVDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCD 317
Cdd:PLN02272 319 PTPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYD 398
|
330 340
....*....|....*....|
gi 254782092 318 NEWGFANRMLDTTLAMATVA 337
Cdd:PLN02272 399 NEWGYSNRVLDLIEHMALVA 418
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
1-328 |
1.99e-82 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 253.50 E-value: 1.99e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 1 MTVRVAINGFGRIGRNVVRAlyeSGRRAEITVVAINELADAAGMAHLLKYDTSHGRFAWEVRQERDQLFVGDDAIRVLHE 80
Cdd:PRK15425 1 MTIKVGINGFGRIGRIVFRA---AQKRSDIEIVAINDLLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 81 RSLQSLPWRELGVDVVLDCTGVYGSREHGEAHIAAGAKKVLFSHPgSNDLDTTVVYGVNQDQLrAEHRIVSNASCTTNCI 160
Cdd:PRK15425 78 RDPANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGP-SKDNTPMFVKGANFDKY-AGQDIVSNASCTTNCL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 161 IPVIKLLDDAYGIESGTVTTIHSAMHDQQVIDA-YHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVPT 239
Cdd:PRK15425 156 APLAKVINDNFGIIEGLMTTVHATTATQKTVDGpSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 240 INVTAIDLSVTVKKPVKANEVNLLLQKAAQGAFHGIVDYAELPLVSVDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNE 319
Cdd:PRK15425 236 PNVSVVDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNE 315
|
....*....
gi 254782092 320 WGFANRMLD 328
Cdd:PRK15425 316 TGYSNKVLD 324
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
1-335 |
3.61e-77 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 240.73 E-value: 3.61e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 1 MTVRVAINGFGRIGRNVVRALYESGRRA-EITVVAINELA-DAAGMAHLLKYDTSHGRFAWEVRQERDQLFVGDDAIRVL 78
Cdd:PTZ00434 2 APIKVGINGFGRIGRMVFQAICDQGLIGtEIDVVAVVDMStNAEYFAYQMKYDTVHGRPKYTVETTKSSPSVKTDDVLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 79 H---------ERSLQSLPWRELGVDVVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGSNDLdTTVVYGVNQDQLR-AEHR 148
Cdd:PTZ00434 82 NghrikcvkaQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPASGGA-KTIVMGVNQHEYSpTEHH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 149 IVSNASCTTNCIIPVIKLL-DDAYGIESGTVTTIHSAMHDQQVIDAYH-PDLRRTRAASQSIIPVDTKLAAGITRFFPQF 226
Cdd:PTZ00434 161 VVSNASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSvKDWRGGRAAAVNIIPSTTGAAKAVGMVIPST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 227 NDRFEAIAVRVPTINVTAIDLSVTVKKPVKANEVNLLLQKAAQGAFHGIVDYAELPLVSVDFNHDPHSAIVDGTQTRVSG 306
Cdd:PTZ00434 241 KGKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKATLQNN 320
|
330 340 350
....*....|....*....|....*....|...
gi 254782092 307 ----AHLIKTLVWCDNEWGFANRMLDTTLAMAT 335
Cdd:PTZ00434 321 lpgeRRFFKIVSWYDNEWGYSHRVVDLVRYMAA 353
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-155 |
1.46e-73 |
|
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: 223.97 E-value: 1.46e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 3 VRVAINGFGRIGRNVVRALYEsgrRAEITVVAINELADAAGMAHLLKYDTSHGRFAWEVRQERDQLFVGDDAIRVLHERS 82
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALE---RPDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERD 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254782092 83 LQSLPWRELGVDVVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGSNDlDTTVVYGVNQDQLRAEHRIVSNASC 155
Cdd:smart00846 78 PANLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDA-DPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| GAPDH_I_N |
cd05214 |
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
3-154 |
1.85e-72 |
|
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: 221.88 E-value: 1.85e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 3 VRVAINGFGRIGRNVVRALYEsgrRAEITVVAINELADAAGMAHLLKYDTSHGRFAWEVRQERDQLFVGDDAIRVLHERS 82
Cdd:cd05214 1 IKVGINGFGRIGRLVFRAALE---RDDIEVVAINDLTDDETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERD 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254782092 83 LQSLPWRELGVDVVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGSNDlDTTVVYGVNQDQLRAEHRIVSNAS 154
Cdd:cd05214 78 PAELPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDD-DPTIVMGVNHDKYDADDKIISNAS 148
|
|
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
3-334 |
2.93e-72 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 227.30 E-value: 2.93e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 3 VRVAINGFGRIGRNVVRALYEsgrRAEITVVAINE-LADAAGMAHLLKYDTSHGRFA---WEVRQERDQLFvGDDAIRVL 78
Cdd:PLN02358 6 IRIGINGFGRIGRLVARVVLQ---RDDVELVAVNDpFITTEYMTYMFKYDSVHGQWKhheLKVKDDKTLLF-GEKPVTVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 79 HERSLQSLPWRELGVDVVLDCTGVYGSREHGEAHIAAGAKKVLFSHPgSNDLDTTVVyGVNQDQLRAEHRIVSNASCTTN 158
Cdd:PLN02358 82 GIRNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAP-SKDAPMFVV-GVNEHEYKSDLDIVSNASCTTN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 159 CIIPVIKLLDDAYGIESGTVTTIHSAMHDQQVIDA-YHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRV 237
Cdd:PLN02358 160 CLAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGpSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 238 PTINVTAIDLSVTVKKPVKANEVNLLLQKAAQGAFHGIVDYAELPLVSVDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCD 317
Cdd:PLN02358 240 PTVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYD 319
|
330
....*....|....*..
gi 254782092 318 NEWGFANRMLDTTLAMA 334
Cdd:PLN02358 320 NEWGYSSRVVDLIVHMS 336
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
160-316 |
3.02e-69 |
|
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: 213.22 E-value: 3.02e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 160 IIPVIKLLDDAYGIESGTVTTIHSAMHDQQVIDAYHP-DLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVP 238
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHkDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254782092 239 TINVTAIDLSVTVKKPVKANEVNLLLQKAAQGAFHGIVDYAELPLVSVDFNHDPHSAIVDGTQTRVSGAHLIKTLVWC 316
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
5-338 |
7.69e-63 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 207.08 E-value: 7.69e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 5 VAINGFGRIGRNVVRALYE-----SGRRAEITVVAINELADAAGMAHLLKYDTSHGRFAW--EVRQERDQLFVGDDAIRV 77
Cdd:PRK08289 130 VVLYGFGRIGRLLARLLIEktgggNGLRLRAIVVRKGSEGDLEKRASLLRRDSVHGPFNGtiTVDEENNAIIANGNYIQV 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 78 LHERSLQSLPWRELGVD--VVLDCTGVYGSREHGEAHIAA-GAKKVLFSHPGSNDLdTTVVYGVNQDQLRAEHRIVSNAS 154
Cdd:PRK08289 210 IYANSPEEVDYTAYGINnaLVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGKGDI-KNIVHGVNHSDITDEDKIVSAAS 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 155 CTTNCIIPVIKLLDDAYGIESGTVTTIHSAMHDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIA 234
Cdd:PRK08289 289 CTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKGDRRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNA 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 235 VRVPTINVTAIDLSVTVKKPVKANEVNLLLQKAA-QGAFHGIVDYAELP-LVSVDFNHDPHSAIVDGTQTRVSGAHLIkT 312
Cdd:PRK08289 369 IRVPTPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQIDYTDSTeVVSSDFVGSRHAGVVDSQATIVNGNRAV-L 447
|
330 340
....*....|....*....|....*.
gi 254782092 313 LVWCDNEWGFANRMLDTTLAMATVAF 338
Cdd:PRK08289 448 YVWYDNEFGYSCQVVRVMEQMAGVRY 473
|
|
| Gp_dh_N |
pfam00044 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-106 |
2.15e-48 |
|
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: 158.03 E-value: 2.15e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 3 VRVAINGFGRIGRNVVRALYEsgrRAEITVVAINELADAAGMAHLLKYDTSHGRFAWEVRQERDQLFVGDDAIRVLHERS 82
Cdd:pfam00044 1 VKVGINGFGRIGRLVLRAALE---RPDIEVVAINDLTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERD 77
|
90 100
....*....|....*....|....
gi 254782092 83 LQSLPWRELGVDVVLDCTGVYGSR 106
Cdd:pfam00044 78 PAELPWGDLGVDVVIESTGVFTTK 101
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-327 |
7.86e-41 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 145.79 E-value: 7.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 1 MTVRVAINGFGRIGRNVvraLYESGRRAEITVVAINELA-DAAGMAHLLKYDTSHGRFAW-EVRQERDQLFV-GDDAIRV 77
Cdd:PTZ00353 1 LPITVGINGFGPVGKAV---LFASLTDPLVTVVAVNDASvSIAYIAYVLEQESPLSAPDGaSIRVVGEQIVLnGTQKIRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 78 LHERSLQSLPWRELGVDVVLDCTGVYGSREHGEAHIAAGAKKVLFShPGSNDLDTtVVYGVNQDQLRAEHRIVSNASCTT 157
Cdd:PTZ00353 78 SAKHDLVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVA-GQSADAPT-VMAGSNDERLSASLPVCCAGAPIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 158 NCIIPVIKLLDDAYGIESGTVTTIHsAMHDQQVIDAYHP---DLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIA 234
Cdd:PTZ00353 156 VALAPVIRALHEVYGVEECSYTAIH-GMQPQEPIAARSKnsqDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 235 VRVPTINVTAIDLSVTVKKPVKANEVNLLLQKAAQGAFHGIVDYAELPLVSVDFNHDpHSAIVDGTQTR-VSGAHLIKTL 313
Cdd:PTZ00353 235 FQVPVKKGCAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCIPN-GKLCYDATSSSsSREGEVHKMV 313
|
330
....*....|....
gi 254782092 314 VWCDNEWGFANRML 327
Cdd:PTZ00353 314 LWFDVECYYAARLL 327
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
155-319 |
3.26e-34 |
|
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: 123.50 E-value: 3.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 155 CTTNCIIPVIKLLDDAYGIESGTVTTIHSAMHDQQVIDA-YHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAI 233
Cdd:cd18123 1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGpSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 234 AVRVPTINVTAIDLSVTVKKPVKANEVNLLLQKAAQGafHGIVDYAELPLVSVDFNHDPHSAIVDGTQTRVSGAHLIKTL 313
Cdd:cd18123 81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLM 158
|
....*.
gi 254782092 314 VWCDNE 319
Cdd:cd18123 159 QWYDNE 164
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
155-319 |
5.56e-17 |
|
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: 77.17 E-value: 5.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 155 CTTNCIIPVIKLLDDAYGIESGTVTTIHSAMHDQQVIDAYHpDLRRTRAASQSIIPVDTKLAAGITRFFPQFND--RFEA 232
Cdd:cd18122 1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPI-LKSEVRAIIPNIPKNETKHAPETGKVLGEIGKpiKVDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 233 IAVRVPTINVTAIDLSVTVKKPVKANEVNLLLQKAAQGAFHGIVDYAELPLVSVDFNHDPHSAIVDGTQTRVSGAHLIKT 312
Cdd:cd18122 80 IAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLKV 159
|
....*..
gi 254782092 313 LVWCDNE 319
Cdd:cd18122 160 FSAVDNE 166
|
|
| GAPDH-like_N |
cd05192 |
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ... |
3-159 |
4.04e-10 |
|
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: 56.59 E-value: 4.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 3 VRVAINGFGRIGRNVVRALYEsgrRAEITVVAINELADaagmahllkydtshgrfawevrqerdqlfvgddairvlhers 82
Cdd:cd05192 1 IRVAINGFGRIGRIVFRAIAD---QDDLDVVAINDRRD------------------------------------------ 35
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254782092 83 lqslpwrelgvdVVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGSNDLDTTVVyGVNQDQLRAEHRIVSNASCTTNC 159
Cdd:cd05192 36 ------------VVIECTGSFTDDDNAEKHIKAGGKKAVITAPEKGDIPTIVV-VLNELAKSAGATVVSNANETSYS 99
|
|
| Asd |
COG0136 |
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ... |
92-184 |
1.24e-04 |
|
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; Aspartate-semialdehyde dehydrogenase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439906 [Multi-domain] Cd Length: 333 Bit Score: 43.10 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254782092 92 GVDVVLDCTGVYGSREHGEAHIAAGAKKVlfshpgsndlDTT-----------VVYGVNQDQLRA--EHRIVSNASCTTN 158
Cdd:COG0136 62 GVDIALFSAGGSVSKEYAPKAAAAGAVVI----------DNSsafrmdpdvplVVPEVNPEALADhlPKGIIANPNCSTI 131
|
90 100
....*....|....*....|....*.
gi 254782092 159 CIIPVIKLLDDAYGIESGTVTTIHSA 184
Cdd:COG0136 132 QMLVALKPLHDAAGIKRVVVSTYQAV 157
|
|
| |
