|
Name |
Accession |
Description |
Interval |
E-value |
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
1-334 |
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: 576.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 1 MAVKVAINGFGRIGRLAFRRIQD-VEGIEVVAVNDLTDDDMLAHLLKYDTMQGRFTSEVEVVDGGFRVNGKEVKSFEEPD 79
Cdd:COG0057 1 MTIRVAINGFGRIGRLVLRALLErGPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 80 ASKLPWGDLGVDVVLECTGFYTDKEKAEAHIHAGAKKVLISAPAKGDVKTIVYNTNHSDLDGSETVVSGASCTTNSLAPV 159
Cdd:COG0057 81 PAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDDPTIVYGVNHDDYDADHRIISNASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 160 AKVISDEFGLVEGLMTTIHAYTGDQMTQDGPHRkgDKRRARAAAQNIVPNSTGAAKAIGKVIPEIDGKLDGGAQRVPVAT 239
Cdd:COG0057 161 AKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHK--DLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 240 GSLTELTVVLEKqDVTVEQVNEAMKKASNES----FGYNEDEIVSSDVVGMTYGSLFDATQTRVMsvGGRqLVKVAAWYD 315
Cdd:COG0057 239 VSLVDLTVELEK-ETTVEEVNAALKEAAEGPlkgiLGYTEEPLVSSDFNGDPHSSIFDALQTIVI--GGN-LVKVLAWYD 314
|
330
....*....|....*....
gi 1752982040 316 NEMSYTAQLVRTLEYLAQL 334
Cdd:COG0057 315 NEWGYSNRMVDLAEYMAKL 333
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
4-326 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the enzyme responsible for the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. Forms exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (1.2.1.59). In some species, NAD- and NADP- utilizing forms exist, generally being responsible for reactions in the anabolic and catabolic directions respectively. Two Pfam models cover the two functional domains of this protein; pfam00044 represents the N-terminal NAD(P)-binding domain and pfam02800 represents the C-terminal catalytic domain. An additional form of gap gene is found in gamma proteobacteria and is responsible for the conversion of erythrose-4-phosphate (E4P) to 4-phospho-erythronate in the biosynthesis of pyridoxine. This pathway of pyridoxine biosynthesis appears to be limited, however, to a relatively small number of bacterial species although it is prevalent among the gamma-proteobacteria. This enzyme is described by TIGR001532. These sequences generally score between trusted and noise to this GAPDH model due to the close evolutionary relationship. There exists the possiblity that some forms of GAPDH may be bifunctional and act on E4P in species which make pyridoxine and via hydroxythreonine and lack a separate E4PDH enzyme (for instance, the GAPDH from Bacillus stearothermophilus has been shown to posess a limited E4PD activity as well as a robust GAPDH activity). There are a great number of sequences in the databases which score between trusted and noise to this model, nearly all of them due to fragmentary sequences. It seems that study of this gene has been carried out in many species utilizing PCR probes which exclude the extreme ends of the consenses used to define this model. The noise level is set relative not to E4PD, but the next closest outliers, the class II GAPDH's (found in archaea, TIGR01546) and aspartate semialdehyde dehydrogenase (ASADH, TIGR01296) both of which have highest-scoring hits around -225 to the prior model. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 273675 [Multi-domain] Cd Length: 326 Bit Score: 511.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 4 KVAINGFGRIGRLAFRRIQDVEG--IEVVAVNDLTDDDMLAHLLKYDTMQGRFTSEVEVVDGGFRVNGKEVKS-FEEPDA 80
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKPGndLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEVISvFSERDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 81 SKLPWGDLGVDVVLECTGFYTDKEKAEAHIHAGAKKVLISAPAKGDVKTIVYNTNHSDLDGSETVVSGASCTTNSLAPVA 160
Cdd:TIGR01534 81 SDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDVKTIVYGVNHDEYDGEERIISNASCTTNCLAPLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 161 KVISDEFGLVEGLMTTIHAYTGDQMTQDGPHRkgDKRRARAAAQNIVPNSTGAAKAIGKVIPEIDGKLDGGAQRVPVATG 240
Cdd:TIGR01534 161 KVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHK--DLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 241 SLTELTVVLEKqDVTVEQVNEAMKKAS----NESFGYNEDEIVSSDVVGMTYGSLFDATQTRVMSVGGRQlVKVAAWYDN 316
Cdd:TIGR01534 239 SLVDLVVNLEK-DVTVEEVNAALKEASegelKGVLGYTEDELVSSDFIGSPYSSIVDATATKVTGLGDSL-VKVYAWYDN 316
|
330
....*....|
gi 1752982040 317 EMSYTAQLVR 326
Cdd:TIGR01534 317 EWGYSNRLVD 326
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-332 |
3.39e-130 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 375.23 E-value: 3.39e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 1 MAVKVAINGFGRIGRLAFRRIQDVEGIEVVAVNDLTDDDMLAHLLKYDTMQGRFTSEVEVVDGGFRVNGKEVKSFEEPDA 80
Cdd:PRK07729 1 MKTKVAINGFGRIGRMVFRKAIKESAFEIVAINASYPSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 81 SKLPWGDLGVDVVLECTGFYTDKEKAEAHIHAGAKKVLISAPAKGDVKTIVYNTNHSDLD-GSETVVSGASCTTNSLAPV 159
Cdd:PRK07729 81 KELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVTIVVGVNEDQLDiEKHTIISNASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 160 AKVISDEFGLVEGLMTTIHAYTGDQMTQDGPHRkgDKRRARAAAQNIVPNSTGAAKAIGKVIPEIDGKLDGGAQRVPVAT 239
Cdd:PRK07729 161 VKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHK--DLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 240 GSLTELTVVLeKQDVTVEQVNEAMKKASNES----FGYNEDEIVSSDVVGMTYGSLFDATQTRVMsvGGRQlVKVAAWYD 315
Cdd:PRK07729 239 VSLVDLVVDV-KRDVTVEEINEAFKTAANGAlkgiLEFSEEPLVSIDFNTNTHSAIIDGLSTMVM--GDRK-VKVLAWYD 314
|
330
....*....|....*..
gi 1752982040 316 NEMSYTAQLVRTLEYLA 332
Cdd:PRK07729 315 NEWGYSCRVVDLVTLVA 331
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
5-325 |
5.17e-107 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 315.72 E-value: 5.17e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 5 VAINGFGRIGRLAFRRIQDVEGIEVVAVNDL-TDDDMLAHLLKYDTMQGRFTSEVEVVDGGFRVNGKEVKSFEEPDASKL 83
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLaGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 84 PWGDlGVDVVLECTGFYTDKEKAEAHIHAGAKKVLISAPAKGD-VKTIVYNTNHSDLDGSE-TVVSGASCTTNSLAPVAK 161
Cdd:NF033735 81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEgVLNIVYGVNDHLYDPARhRIVTAASCTTNCLAPVVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 162 VISDEFGLVEGLMTTIHAYTGDQMTQDGPHRkgDKRRARAAAQNIVPNSTGAAKAIGKVIPEIDGKLDGGAQRVPVATGS 241
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAPHK--DLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNAS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 242 LTELtvVLE-KQDVTVEQVNEAMKKASNES----FGYNEDEIVSSDVVGMTYGSLFDATQTrvMSVGGRQlVKVAAWYDN 316
Cdd:NF033735 238 LTDC--VFEvERPTTVEEVNALFKAAAEGPlkgiLGYEERPLVSVDYVNDPRSSIIDALST--MVVNGTQ-VKIYAWYDN 312
|
....*....
gi 1752982040 317 EMSYTAQLV 325
Cdd:NF033735 313 EWGYANRMV 321
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
151-317 |
1.13e-99 |
|
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: 290.90 E-value: 1.13e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 151 CTTNSLAPVAKVISDEFGLVEGLMTTIHAYTGDQMTQDGPHRkgDKRRARAAAQNIVPNSTGAAKAIGKVIPEIDGKLDG 230
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHK--DLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 231 GAQRVPVATGSLTELTVVLEKqDVTVEQVNEAMKKASN----ESFGYNEDEIVSSDVVGMTYGSLFDATQTRVMsvgGRQ 306
Cdd:cd18126 79 MAFRVPTPNVSVVDLTVRLEK-PVTVEEVNAALKKAAEgplkGILGYTEDPLVSSDFVGDPHSSIFDATATIVL---GGN 154
|
170
....*....|.
gi 1752982040 307 LVKVAAWYDNE 317
Cdd:cd18126 155 LVKVVAWYDNE 165
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-151 |
1.12e-77 |
|
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: 234.37 E-value: 1.12e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 3 VKVAINGFGRIGRLAFRRIQDVEGIEVVAVNDLTDDDMLAHLLKYDTMQGRFTSEVEVVDGGFRVNGKEVKSFEEPDASK 82
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPAN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752982040 83 LPWGDLGVDVVLECTGFYTDKEKAEAHIHAGAKKVLISAPAKGDVKTIVYNTNHSDLDGSETVVSGASC 151
Cdd:smart00846 81 LPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDADPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
156-314 |
1.33e-74 |
|
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: 226.71 E-value: 1.33e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 156 LAPVAKVISDEFGLVEGLMTTIHAYTGDQMTQDGPHRKgDKRRARAAAQNIVPNSTGAAKAIGKVIPEIDGKLDGGAQRV 235
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHK-DLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 236 PVATGSLTELTVVLEKqDVTVEQVNEAMKKAS----NESFGYNEDEIVSSDVVGMTYGSLFDATQTRVMsvgGRQLVKVA 311
Cdd:pfam02800 80 PTPNVSVVDLVVELEK-PVTVEEVNAALKEAAegalKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVV---NGNFVKVV 155
|
...
gi 1752982040 312 AWY 314
Cdd:pfam02800 156 AWY 158
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
1-334 |
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: 576.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 1 MAVKVAINGFGRIGRLAFRRIQD-VEGIEVVAVNDLTDDDMLAHLLKYDTMQGRFTSEVEVVDGGFRVNGKEVKSFEEPD 79
Cdd:COG0057 1 MTIRVAINGFGRIGRLVLRALLErGPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 80 ASKLPWGDLGVDVVLECTGFYTDKEKAEAHIHAGAKKVLISAPAKGDVKTIVYNTNHSDLDGSETVVSGASCTTNSLAPV 159
Cdd:COG0057 81 PAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDDPTIVYGVNHDDYDADHRIISNASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 160 AKVISDEFGLVEGLMTTIHAYTGDQMTQDGPHRkgDKRRARAAAQNIVPNSTGAAKAIGKVIPEIDGKLDGGAQRVPVAT 239
Cdd:COG0057 161 AKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHK--DLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 240 GSLTELTVVLEKqDVTVEQVNEAMKKASNES----FGYNEDEIVSSDVVGMTYGSLFDATQTRVMsvGGRqLVKVAAWYD 315
Cdd:COG0057 239 VSLVDLTVELEK-ETTVEEVNAALKEAAEGPlkgiLGYTEEPLVSSDFNGDPHSSIFDALQTIVI--GGN-LVKVLAWYD 314
|
330
....*....|....*....
gi 1752982040 316 NEMSYTAQLVRTLEYLAQL 334
Cdd:COG0057 315 NEWGYSNRMVDLAEYMAKL 333
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
4-326 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the enzyme responsible for the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. Forms exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (1.2.1.59). In some species, NAD- and NADP- utilizing forms exist, generally being responsible for reactions in the anabolic and catabolic directions respectively. Two Pfam models cover the two functional domains of this protein; pfam00044 represents the N-terminal NAD(P)-binding domain and pfam02800 represents the C-terminal catalytic domain. An additional form of gap gene is found in gamma proteobacteria and is responsible for the conversion of erythrose-4-phosphate (E4P) to 4-phospho-erythronate in the biosynthesis of pyridoxine. This pathway of pyridoxine biosynthesis appears to be limited, however, to a relatively small number of bacterial species although it is prevalent among the gamma-proteobacteria. This enzyme is described by TIGR001532. These sequences generally score between trusted and noise to this GAPDH model due to the close evolutionary relationship. There exists the possiblity that some forms of GAPDH may be bifunctional and act on E4P in species which make pyridoxine and via hydroxythreonine and lack a separate E4PDH enzyme (for instance, the GAPDH from Bacillus stearothermophilus has been shown to posess a limited E4PD activity as well as a robust GAPDH activity). There are a great number of sequences in the databases which score between trusted and noise to this model, nearly all of them due to fragmentary sequences. It seems that study of this gene has been carried out in many species utilizing PCR probes which exclude the extreme ends of the consenses used to define this model. The noise level is set relative not to E4PD, but the next closest outliers, the class II GAPDH's (found in archaea, TIGR01546) and aspartate semialdehyde dehydrogenase (ASADH, TIGR01296) both of which have highest-scoring hits around -225 to the prior model. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 273675 [Multi-domain] Cd Length: 326 Bit Score: 511.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 4 KVAINGFGRIGRLAFRRIQDVEG--IEVVAVNDLTDDDMLAHLLKYDTMQGRFTSEVEVVDGGFRVNGKEVKS-FEEPDA 80
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKPGndLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEVISvFSERDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 81 SKLPWGDLGVDVVLECTGFYTDKEKAEAHIHAGAKKVLISAPAKGDVKTIVYNTNHSDLDGSETVVSGASCTTNSLAPVA 160
Cdd:TIGR01534 81 SDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDVKTIVYGVNHDEYDGEERIISNASCTTNCLAPLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 161 KVISDEFGLVEGLMTTIHAYTGDQMTQDGPHRkgDKRRARAAAQNIVPNSTGAAKAIGKVIPEIDGKLDGGAQRVPVATG 240
Cdd:TIGR01534 161 KVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHK--DLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 241 SLTELTVVLEKqDVTVEQVNEAMKKAS----NESFGYNEDEIVSSDVVGMTYGSLFDATQTRVMSVGGRQlVKVAAWYDN 316
Cdd:TIGR01534 239 SLVDLVVNLEK-DVTVEEVNAALKEASegelKGVLGYTEDELVSSDFIGSPYSSIVDATATKVTGLGDSL-VKVYAWYDN 316
|
330
....*....|
gi 1752982040 317 EMSYTAQLVR 326
Cdd:TIGR01534 317 EWGYSNRLVD 326
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-332 |
3.39e-130 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 375.23 E-value: 3.39e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 1 MAVKVAINGFGRIGRLAFRRIQDVEGIEVVAVNDLTDDDMLAHLLKYDTMQGRFTSEVEVVDGGFRVNGKEVKSFEEPDA 80
Cdd:PRK07729 1 MKTKVAINGFGRIGRMVFRKAIKESAFEIVAINASYPSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 81 SKLPWGDLGVDVVLECTGFYTDKEKAEAHIHAGAKKVLISAPAKGDVKTIVYNTNHSDLD-GSETVVSGASCTTNSLAPV 159
Cdd:PRK07729 81 KELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVTIVVGVNEDQLDiEKHTIISNASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 160 AKVISDEFGLVEGLMTTIHAYTGDQMTQDGPHRkgDKRRARAAAQNIVPNSTGAAKAIGKVIPEIDGKLDGGAQRVPVAT 239
Cdd:PRK07729 161 VKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHK--DLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 240 GSLTELTVVLeKQDVTVEQVNEAMKKASNES----FGYNEDEIVSSDVVGMTYGSLFDATQTRVMsvGGRQlVKVAAWYD 315
Cdd:PRK07729 239 VSLVDLVVDV-KRDVTVEEINEAFKTAANGAlkgiLEFSEEPLVSIDFNTNTHSAIIDGLSTMVM--GDRK-VKVLAWYD 314
|
330
....*....|....*..
gi 1752982040 316 NEMSYTAQLVRTLEYLA 332
Cdd:PRK07729 315 NEWGYSCRVVDLVTLVA 331
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
3-333 |
1.09e-111 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 328.02 E-value: 1.09e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 3 VKVAINGFGRIGRlAFRRI---QDVEGIEVVAVNDLTDDDMLAHLLKYDTMQGRFTSEVEVVDGGFRVNGKEVKSFEEPD 79
Cdd:PRK07403 2 IRVAINGFGRIGR-NFLRCwlgRENSQLELVAINDTSDPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 80 ASKLPWGDLGVDVVLECTGFYTDKEKAEAHIHAGAKKVLISAPAKG-DVKTIVYNTNHSDLDGSE-TVVSGASCTTNSLA 157
Cdd:PRK07403 81 PLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPGKGeDIGTYVVGVNHHEYDHEDhNIISNASCTTNCLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 158 PVAKVISDEFGLVEGLMTTIHAYTGDQMTQDGPHRkgDKRRARAAAQNIVPNSTGAAKAIGKVIPEIDGKLDGGAQRVPV 237
Cdd:PRK07403 161 PIAKVLHDNFGIIKGTMTTTHSYTGDQRILDASHR--DLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 238 ATGSLTELTVVLEKQDVTvEQVNEAMKKASNESF----GYNEDEIVSSDVVGMTYGSLFDATQTRVMsvgGRQLVKVAAW 313
Cdd:PRK07403 239 PNVSVVDLVVQVEKRTIT-EQVNEVLKDASEGPLkgilEYSDLPLVSSDYRGTDASSIVDASLTMVM---GGDMVKVIAW 314
|
330 340
....*....|....*....|
gi 1752982040 314 YDNEMSYTAQLVRTLEYLAQ 333
Cdd:PRK07403 315 YDNEWGYSQRVVDLAELVAR 334
|
|
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
3-332 |
1.18e-111 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 331.05 E-value: 1.18e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 3 VKVAINGFGRIGRLAFRRIQDVEGIEVVAVND-LTDDDMLAHLLKYDTMQGRFTSEVEVVD-GGFRVNGKEVKSFEEPDA 80
Cdd:PLN02272 86 TKIGINGFGRIGRLVLRIATSRDDIEVVAVNDpFIDAKYMAYMFKYDSTHGNFKGTINVVDdSTLEINGKQIKVTSKRDP 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 81 SKLPWGDLGVDVVLECTGFYTDKEKAEAHIHAGAKKVLISAPAkGDVKTIVYNTNHSDLDGSETVVSGASCTTNSLAPVA 160
Cdd:PLN02272 166 AEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPS-ADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 161 KVISDEFGLVEGLMTTIHAYTGDQMTQDGPHRKgDKRRARAAAQNIVPNSTGAAKAIGKVIPEIDGKLDGGAQRVPVATG 240
Cdd:PLN02272 245 KVVHEEFGILEGLMTTVHATTATQKTVDGPSMK-DWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNV 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 241 SLTELTVVLEKqDVTVEQVNEAMKKASNES----FGYNEDEIVSSDVVGMTYGSLFDATQTRVMSvggRQLVKVAAWYDN 316
Cdd:PLN02272 324 SVVDLTCRLEK-SASYEDVKAAIKYASEGPlkgiLGYTDEDVVSNDFVGDSRSSIFDAKAGIGLS---ASFMKLVSWYDN 399
|
330
....*....|....*.
gi 1752982040 317 EMSYTAQLVRTLEYLA 332
Cdd:PLN02272 400 EWGYSNRVLDLIEHMA 415
|
|
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-333 |
3.36e-110 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 324.10 E-value: 3.36e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 1 MAVKVAINGFGRIGRLAFRRIQDVEGIEVVAVND-LTDDDMLAHLLKYDTMQGRFTSEVEVVDGGFRVNGKEVKSFEEPD 79
Cdd:PTZ00023 1 MVVKLGINGFGRIGRLVFRAALEREDVEVVAINDpFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 80 ASKLPWGDLGVDVVLECTGFYTDKEKAEAHIHAGAKKVLISAPAKGDVKTIVYNTNHSDLDGSETVVSGASCTTNSLAPV 159
Cdd:PTZ00023 81 PAAIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKDDTPIYVMGVNHTQYDKSQRIVSNASCTTNCLAPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 160 AKVISDEFGLVEGLMTTIHAYTGDQMTQDGPHRKG-DKRRARAAAQNIVPNSTGAAKAIGKVIPEIDGKLDGGAQRVPVA 238
Cdd:PTZ00023 161 AKVVNDKFGIVEGLMTTVHASTANQLTVDGPSKGGkDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 239 TGSLTELTVVLEKQdVTVEQVNEAMKKASNES----FGYNEDEIVSSDVVGMTYGSLFDATQTRVMSvggRQLVKVAAWY 314
Cdd:PTZ00023 241 DVSVVDLTCKLAKP-AKYEEIVAAVKKAAEGPlkgiLGYTDDEVVSSDFVHDKRSSIFDVKAGIALN---DTFVKLVSWY 316
|
330
....*....|....*....
gi 1752982040 315 DNEMSYTAQLVRTLEYLAQ 333
Cdd:PTZ00023 317 DNEWGYSNRLLDLAHYITQ 335
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
5-325 |
5.17e-107 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 315.72 E-value: 5.17e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 5 VAINGFGRIGRLAFRRIQDVEGIEVVAVNDL-TDDDMLAHLLKYDTMQGRFTSEVEVVDGGFRVNGKEVKSFEEPDASKL 83
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLaGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 84 PWGDlGVDVVLECTGFYTDKEKAEAHIHAGAKKVLISAPAKGD-VKTIVYNTNHSDLDGSE-TVVSGASCTTNSLAPVAK 161
Cdd:NF033735 81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEgVLNIVYGVNDHLYDPARhRIVTAASCTTNCLAPVVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 162 VISDEFGLVEGLMTTIHAYTGDQMTQDGPHRkgDKRRARAAAQNIVPNSTGAAKAIGKVIPEIDGKLDGGAQRVPVATGS 241
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAPHK--DLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNAS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 242 LTELtvVLE-KQDVTVEQVNEAMKKASNES----FGYNEDEIVSSDVVGMTYGSLFDATQTrvMSVGGRQlVKVAAWYDN 316
Cdd:NF033735 238 LTDC--VFEvERPTTVEEVNALFKAAAEGPlkgiLGYEERPLVSVDYVNDPRSSIIDALST--MVVNGTQ-VKIYAWYDN 312
|
....*....
gi 1752982040 317 EMSYTAQLV 325
Cdd:NF033735 313 EWGYANRMV 321
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
3-317 |
2.40e-100 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 298.89 E-value: 2.40e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 3 VKVAINGFGRIGRLAFR-------RIQdvegIEVVAVNDLTDDDMLAHLLKYDTMQGRFTSEVEVVDGGFRVNGKEVKSF 75
Cdd:PRK13535 2 IRVAINGFGRIGRNVLRalyesgrRAE----ITVVAINELADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 76 EEPDASKLPWGDLGVDVVLECTGFYTDKEKAEAHIHAGAKKVLISAPAKGDV-KTIVYNTNHSDLDGSETVVSGASCTTN 154
Cdd:PRK13535 78 HERDIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSNDLdATVVYGVNHDQLRAEHRIVSNASCTTN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 155 SLAPVAKVISDEFGLVEGLMTTIHAYTGDQMTQDGPHRkgDKRRARAAAQNIVPNSTGAAKAIGKVIPEIDGKLDGGAQR 234
Cdd:PRK13535 158 CIIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHP--DLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 235 VPVATGSLTELTVVLEKQdVTVEQVNEAMKKASNESF----GYNEDEIVSSDVVGMTYGSLFDATQTRvmsVGGRQLVKV 310
Cdd:PRK13535 236 VPTINVTAIDLSVTVKKP-VKVNEVNQLLQKAAQGAFhgivDYTELPLVSIDFNHDPHSAIVDGTQTR---VSGAHLIKT 311
|
....*..
gi 1752982040 311 AAWYDNE 317
Cdd:PRK13535 312 LVWCDNE 318
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
151-317 |
1.13e-99 |
|
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: 290.90 E-value: 1.13e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 151 CTTNSLAPVAKVISDEFGLVEGLMTTIHAYTGDQMTQDGPHRkgDKRRARAAAQNIVPNSTGAAKAIGKVIPEIDGKLDG 230
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHK--DLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 231 GAQRVPVATGSLTELTVVLEKqDVTVEQVNEAMKKASN----ESFGYNEDEIVSSDVVGMTYGSLFDATQTRVMsvgGRQ 306
Cdd:cd18126 79 MAFRVPTPNVSVVDLTVRLEK-PVTVEEVNAALKKAAEgplkGILGYTEDPLVSSDFVGDPHSSIFDATATIVL---GGN 154
|
170
....*....|.
gi 1752982040 307 LVKVAAWYDNE 317
Cdd:cd18126 155 LVKVVAWYDNE 165
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
1-336 |
1.06e-97 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 292.02 E-value: 1.06e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 1 MAVKVAINGFGRIGRLAFRRIQDVEGIEVVAVNDLTDDDMLAHLLKYDTMQGRFTSEVEVVDGGFRVNGKEVKSFEEPDA 80
Cdd:PRK15425 1 MTIKVGINGFGRIGRIVFRAAQKRSDIEIVAINDLLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 81 SKLPWGDLGVDVVLECTGFYTDKEKAEAHIHAGAKKVLISAPAKGDVKTIVYNTNHSDLDGSEtVVSGASCTTNSLAPVA 160
Cdd:PRK15425 81 ANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDNTPMFVKGANFDKYAGQD-IVSNASCTTNCLAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 161 KVISDEFGLVEGLMTTIHAYTGDQMTQDGPHRKgDKRRARAAAQNIVPNSTGAAKAIGKVIPEIDGKLDGGAQRVPVATG 240
Cdd:PRK15425 160 KVINDNFGIIEGLMTTVHATTATQKTVDGPSHK-DWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 241 SLTELTVVLEKQdVTVEQVNEAMKKASNES----FGYNEDEIVSSDVVGMTYGSLFDATQTRVMSvggRQLVKVAAWYDN 316
Cdd:PRK15425 239 SVVDLTVRLEKA-ATYEQIKAAVKAAAEGEmkgvLGYTEDDVVSTDFNGEVCTSVFDAKAGIALN---DNFVKLVSWYDN 314
|
330 340
....*....|....*....|
gi 1752982040 317 EMSYTAQLvrtLEYLAQLSK 336
Cdd:PRK15425 315 ETGYSNKV---LDLIAHISK 331
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
1-332 |
3.17e-97 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 291.96 E-value: 3.17e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 1 MAVKVAINGFGRIGRLAFRRI--QDVEG--IEVVAVNDL-TDDDMLAHLLKYDTMQGRFTSEVEVV--------DGGFRV 67
Cdd:PTZ00434 2 APIKVGINGFGRIGRMVFQAIcdQGLIGteIDVVAVVDMsTNAEYFAYQMKYDTVHGRPKYTVETTksspsvktDDVLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 68 NGKEVKSFE-EPDASKLPWGDLGVDVVLECTGFYTDKEKAEAHIHAGAKKVLISAPAKGDVKTIVYNTNHSDLDGSE-TV 145
Cdd:PTZ00434 82 NGHRIKCVKaQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPASGGAKTIVMGVNQHEYSPTEhHV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 146 VSGASCTTNSLAPVAKVISDE-FGLVEGLMTTIHAYTGDQMTQDGPHRKgDKRRARAAAQNIVPNSTGAAKAIGKVIPEI 224
Cdd:PTZ00434 162 VSNASCTTNCLAPIVHVLTKEgFGIETGLMTTIHSYTATQKTVDGVSVK-DWRGGRAAAVNIIPSTTGAAKAVGMVIPST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 225 DGKLDGGAQRVPVATGSLTELTVVlEKQDVTVEQVNEAMKKASN----ESFGYNEDEIVSSDVVGMTYGSLFDATQTRVM 300
Cdd:PTZ00434 241 KGKLTGMSFRVPTPDVSVVDLTFR-ATRDTSIQEIDAAIKRASQtymkGILGFTDDELVSADFINDNRSSIYDSKATLQN 319
|
330 340 350
....*....|....*....|....*....|...
gi 1752982040 301 SV-GGRQLVKVAAWYDNEMSYTAQLVRTLEYLA 332
Cdd:PTZ00434 320 NLpGERRFFKIVSWYDNEWGYSHRVVDLVRYMA 352
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
3-325 |
1.76e-96 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 292.96 E-value: 1.76e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 3 VKVAINGFGRIGRLAFRRIQDVEG--IEVVAVNDLTDDDMLAHLLKYDTMQGRFTSEVEVVDGG-FRVNGKEVKSFEEPD 79
Cdd:PLN02237 76 LKVAINGFGRIGRNFLRCWHGRKDspLDVVVVNDSGGVKNASHLLKYDSMLGTFKADVKIVDDEtISVDGKPIKVVSNRD 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 80 ASKLPWGDLGVDVVLECTGFYTDKEKAEAHIHAGAKKVLISAPAKG-DVKTIVYNTNHSDLDGSET-VVSGASCTTNSLA 157
Cdd:PLN02237 156 PLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAKGaDIPTYVVGVNEDDYDHEVAnIVSNASCTTNCLA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 158 PVAKVISDEFGLVEGLMTTIHAYTGDQMTQDGPHRkgDKRRARAAAQNIVPNSTGAAKAIGKVIPEIDGKLDGGAQRVPV 237
Cdd:PLN02237 236 PFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDASHR--DLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPT 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 238 ATGSLTELTVVLEKQDVTVEQVNEAMKKASNES----FGYNEDEIVSSDVVGMTYGSLFDATQTRVMsvgGRQLVKVAAW 313
Cdd:PLN02237 314 PNVSVVDLVVNVEKKGITAEDVNAAFRKAADGPlkgiLAVCDVPLVSVDFRCSDVSSTIDASLTMVM---GDDMVKVVAW 390
|
330
....*....|..
gi 1752982040 314 YDNEMSYTAQLV 325
Cdd:PLN02237 391 YDNEWGYSQRVV 402
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
3-333 |
5.63e-95 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 287.60 E-value: 5.63e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 3 VKVAINGFGRIGRLAFR--RIQDVEGIEVVAVNDLTDDDMLAHLLKYDTMQGRFTSEVEVV-DGGFRVNGKEVKSFEEPD 79
Cdd:PLN03096 61 IKVAINGFGRIGRNFLRcwHGRKDSPLDVVAINDTGGVKQASHLLKYDSTLGTFDADVKPVgDDAISVDGKVIKVVSDRN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 80 ASKLPWGDLGVDVVLECTGFYTDKEKAEAHIHAGAKKVLISAPAKGDVKTIVYNTNHSDLDGSETVVSGASCTTNSLAPV 159
Cdd:PLN03096 141 PLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKGDIPTYVVGVNADDYKHSDPIISNASCTTNCLAPF 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 160 AKVISDEFGLVEGLMTTIHAYTGDQMTQDGPHRkgDKRRARAAAQNIVPNSTGAAKAIGKVIPEIDGKLDGGAQRVPVAT 239
Cdd:PLN03096 221 VKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHR--DLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPN 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 240 GSLTELTVVLEKQdVTVEQVNEAMKKASNES----FGYNEDEIVSSDVVGMTYGSLFDATQTRVMsvgGRQLVKVAAWYD 315
Cdd:PLN03096 299 VSVVDLVVQVEKK-TFAEEVNAAFRDAAEKElkgiLAVCDEPLVSVDFRCSDVSSTIDSSLTMVM---GDDMVKVVAWYD 374
|
330
....*....|....*...
gi 1752982040 316 NEMSYTAQLVRTLEYLAQ 333
Cdd:PLN03096 375 NEWGYSQRVVDLADIVAN 392
|
|
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-327 |
5.77e-92 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 277.77 E-value: 5.77e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 1 MAVKVAINGFGRIGRLAFRRIQDVEGIEVVAVNDLTDD-DMLAHLLKYDTMQGRFTSEVEVVDGGFRVNGKEVKSFEEPD 79
Cdd:PRK08955 1 MTIKVGINGFGRIGRLALRAAWDWPELEFVQINDPAGDaATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 80 ASKLPWGdlGVDVVLECTGFYTDKEKAEAHIHAGAKKVLISAPAKGD-VKTIVYNTNHSDLDGSE-TVVSGASCTTNSLA 157
Cdd:PRK08955 81 IADTDWS--GCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEgVLNIVMGVNDHLFDPAIhPIVTAASCTTNCLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 158 PVAKVISDEFGLVEGLMTTIHAYTGDQMTQDGPHRkgDKRRARAAAQNIVPNSTGAAKAIGKVIPEIDGKLDGGAQRVPV 237
Cdd:PRK08955 159 PVVKVIHEKLGIKHGSMTTIHDLTNTQTILDAPHK--DLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 238 ATGSLTELTVVLEKqDVTVEQVNEAMKKASNES----FGYNEDEIVSSDVVGMTYGSLFDATQTrvMSVGGRQlVKVAAW 313
Cdd:PRK08955 237 ANASLTDCVFEVER-DTTVEEVNALLKEAAEGElkgiLGYEERPLVSIDYKTDPRSSIVDALST--MVVNGTQ-VKLYAW 312
|
330
....*....|....*..
gi 1752982040 314 YDNEMSY---TAQLVRT 327
Cdd:PRK08955 313 YDNEWGYanrTAELARK 329
|
|
| GAPDH_I_N |
cd05214 |
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
3-150 |
6.35e-84 |
|
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: 250.77 E-value: 6.35e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 3 VKVAINGFGRIGRLAFRRIQDVEGIEVVAVNDLTDDDMLAHLLKYDTMQGRFTSEVEVVDGGFRVNGKEVKSFEEPDASK 82
Cdd:cd05214 1 IKVGINGFGRIGRLVFRAALERDDIEVVAINDLTDDETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1752982040 83 LPWGDLGVDVVLECTGFYTDKEKAEAHIHAGAKKVLISAPAKGDVKTIVYNTNHSDLDGSETVVSGAS 150
Cdd:cd05214 81 LPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDDDPTIVMGVNHDKYDADDKIISNAS 148
|
|
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
3-333 |
3.01e-83 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 255.42 E-value: 3.01e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 3 VKVAINGFGRIGRLAFRRIQDVEGIEVVAVND-LTDDDMLAHLLKYDTMQGRFT-SEVEVVDGGFRVNG-KEVKSFEEPD 79
Cdd:PLN02358 6 IRIGINGFGRIGRLVARVVLQRDDVELVAVNDpFITTEYMTYMFKYDSVHGQWKhHELKVKDDKTLLFGeKPVTVFGIRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 80 ASKLPWGDLGVDVVLECTGFYTDKEKAEAHIHAGAKKVLISAPAKgDVKTIVYNTNHSDLDGSETVVSGASCTTNSLAPV 159
Cdd:PLN02358 86 PEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSK-DAPMFVVGVNEHEYKSDLDIVSNASCTTNCLAPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 160 AKVISDEFGLVEGLMTTIHAYTGDQMTQDGPHRKgDKRRARAAAQNIVPNSTGAAKAIGKVIPEIDGKLDGGAQRVPVAT 239
Cdd:PLN02358 165 AKVINDRFGIVEGLMTTVHSITATQKTVDGPSMK-DWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 240 GSLTELTVVLEKQdVTVEQVNEAMKKASNES----FGYNEDEIVSSDVVGMTYGSLFDATQTRVMSvggRQLVKVAAWYD 315
Cdd:PLN02358 244 VSVVDLTVRLEKA-ATYDEIKKAIKEESEGKlkgiLGYTEDDVVSTDFVGDNRSSIFDAKAGIALS---DKFVKLVSWYD 319
|
330
....*....|....*...
gi 1752982040 316 NEMSYTAQLVRTLEYLAQ 333
Cdd:PLN02358 320 NEWGYSSRVVDLIVHMSK 337
|
|
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
5-335 |
3.83e-80 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 251.77 E-value: 3.83e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 5 VAINGFGRIGRLAFRRIQDVEG------IEVVAVNDLTDDDML--AHLLKYDTMQGRFTSEVEVVD--GGFRVNGKEVKS 74
Cdd:PRK08289 130 VVLYGFGRIGRLLARLLIEKTGggnglrLRAIVVRKGSEGDLEkrASLLRRDSVHGPFNGTITVDEenNAIIANGNYIQV 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 75 FEEPDASKLPWGDLGVD--VVLECTGFYTDKEKAEAHIHA-GAKKVLISAPAKGDVKTIVYNTNHSDLDGSETVVSGASC 151
Cdd:PRK08289 210 IYANSPEEVDYTAYGINnaLVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGKGDIKNIVHGVNHSDITDEDKIVSAASC 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 152 TTNSLAPVAKVISDEFGLVEGLMTTIHAYTGDQMTQDGPHrKGDkRRARAAAQNIVPNSTGAAKAIGKVIPEIDGKLDGG 231
Cdd:PRK08289 290 TTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYH-KGD-RRGRSAPLNMVITETGAAKAVAKALPELAGKLTGN 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 232 AQRVPVATGSLTELTVVLEKqDVTVEQVNEAMKKASNES-----FGY-NEDEIVSSDVVGMTYGSLFDATQTrvmSVGGR 305
Cdd:PRK08289 368 AIRVPTPNVSMAILNLNLEK-ETSREELNEYLRQMSLHSplqnqIDYtDSTEVVSSDFVGSRHAGVVDSQAT---IVNGN 443
|
330 340 350
....*....|....*....|....*....|
gi 1752982040 306 QLVkVAAWYDNEMSYTAQLVRTLEYLAQLS 335
Cdd:PRK08289 444 RAV-LYVWYDNEFGYSCQVVRVMEQMAGVR 472
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-151 |
1.12e-77 |
|
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: 234.37 E-value: 1.12e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 3 VKVAINGFGRIGRLAFRRIQDVEGIEVVAVNDLTDDDMLAHLLKYDTMQGRFTSEVEVVDGGFRVNGKEVKSFEEPDASK 82
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPAN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1752982040 83 LPWGDLGVDVVLECTGFYTDKEKAEAHIHAGAKKVLISAPAKGDVKTIVYNTNHSDLDGSETVVSGASC 151
Cdd:smart00846 81 LPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDADPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
156-314 |
1.33e-74 |
|
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: 226.71 E-value: 1.33e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 156 LAPVAKVISDEFGLVEGLMTTIHAYTGDQMTQDGPHRKgDKRRARAAAQNIVPNSTGAAKAIGKVIPEIDGKLDGGAQRV 235
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHK-DLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 236 PVATGSLTELTVVLEKqDVTVEQVNEAMKKAS----NESFGYNEDEIVSSDVVGMTYGSLFDATQTRVMsvgGRQLVKVA 311
Cdd:pfam02800 80 PTPNVSVVDLVVELEK-PVTVEEVNAALKEAAegalKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVV---NGNFVKVV 155
|
...
gi 1752982040 312 AWY 314
Cdd:pfam02800 156 AWY 158
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
151-317 |
4.55e-59 |
|
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: 187.44 E-value: 4.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 151 CTTNSLAPVAKVISDEFGLVEGLMTTIHAYTGDQMTQDGPHRKgDKRRARAAAQNIVPNSTGAAKAIGKVIPEIDGKLDG 230
Cdd:cd18123 1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGK-DWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 231 GAQRVPVATGSLTELTVVLEKqDVTVEQVNEAMKKAS--NESFGYNEDEIVSSDVVGMTYGSLFDATQTrvmSVGGRQLV 308
Cdd:cd18123 80 MAVRVPTTLMSVHDLMVELEK-DVTYDDIKEAVKQAPegKGRLGYTEAEDVSSDFRGDIFESVFDAESI---IAVNDNEV 155
|
....*....
gi 1752982040 309 KVAAWYDNE 317
Cdd:cd18123 156 KLMQWYDNE 164
|
|
| GAPDH_N_E4PDH |
cd17892 |
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
3-150 |
2.57e-58 |
|
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: 185.55 E-value: 2.57e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 3 VKVAINGFGRIGRLAFRRIQDVE---GIEVVAVNDLTDDDMLAHLLKYDTMQGRFTSEVEVVDGGFRVNGKEVKSFEEPD 79
Cdd:cd17892 1 YRVAINGYGRIGRNVLRALYESGrraEFQVVAINELADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1752982040 80 ASKLPWGDLGVDVVLECTGFYTDKEKAEAHIHAGAKKVLISAPAKGDVK-TIVYNTNHSDLDGSETVVSGAS 150
Cdd:cd17892 81 PENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASNDVDaTIVYGINQDLLRAEHRIVSNAS 152
|
|
| Gp_dh_N |
pfam00044 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-103 |
1.12e-51 |
|
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: 166.12 E-value: 1.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 3 VKVAINGFGRIGRLAFRRIQDVEGIEVVAVNDLTDDDMLAHLLKYDTMQGRFTSEVEVVDGGFRVNGKEVKSFEEPDASK 82
Cdd:pfam00044 1 VKVGINGFGRIGRLVLRAALERPDIEVVAINDLTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAE 80
|
90 100
....*....|....*....|.
gi 1752982040 83 LPWGDLGVDVVLECTGFYTDK 103
Cdd:pfam00044 81 LPWGDLGVDVVIESTGVFTTK 101
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
151-317 |
3.67e-47 |
|
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) superfamily of proteins; GAPDH-like C-terminal catalytic domains are typically associated with a classic N-terminal Rossmann fold NAD(P)-binding domain. This superfamily includes the C-terminal domains of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), aspartate beta-semialdehyde dehydrogenase (ASADH), acetaldehyde dehydrogenase (ALDH) and USG-1 homolog proteins.
Pssm-ID: 467672 [Multi-domain] Cd Length: 166 Bit Score: 156.91 E-value: 3.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 151 CTTNSLAPVAKVISDEFGLVEGLMTTIHAYTGDQMTQDGPHRKGDKrraRAAAQNIVPNSTGAAKAIGKVIPEID--GKL 228
Cdd:cd18122 1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSEV---RAIIPNIPKNETKHAPETGKVLGEIGkpIKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 229 DGGAQRVPVATGSLTELTVVLEKqDVTVEQVNEAMKKASNESFGYNEDE----IVSSDVVGMTYGSLFDATQTRVMsvgG 304
Cdd:cd18122 78 DGIAVRVPATLGHLVTVTVKLEK-TATLEQIAEAVAEAVEEVQISAEDGltyaKVSTRSVGGVYGVPVGRQREFAF---D 153
|
170
....*....|...
gi 1752982040 305 RQLVKVAAWYDNE 317
Cdd:cd18122 154 DNKLKVFSAVDNE 166
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
151-317 |
5.18e-41 |
|
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar proteins; D-erythrose-4-phosphate dehydrogenase (E4PDH; EC 1.2.1.72), also called E4P dehydrogenase, catalyzes the NAD-dependent conversion of D-erythrose 4-phosphate (E4P) to 4-phosphoerythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose. This enzyme activity appears to have evolved from glyceraldehyde-3-phosphate dehydrogenase (GADPH), whose substrate differs only in the lack of one carbon relative to E4P. E4PDH proteins contain an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal GADPH-like catalytic domain and are members of the GAPDH superfamily of proteins.
Pssm-ID: 467686 Cd Length: 165 Bit Score: 141.01 E-value: 5.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 151 CTTNSLAPVAKVISDEFGLVEGLMTTIHAYTGDQMTQDGPHRkgDKRRARAAAQNIVPNSTGAAKAIGKVIPEIDGKLDG 230
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDAYHP--DLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 231 GAQRVPVATGSLTELTVVLeKQDVTVEQVNEAMKKASNESF----GYNEDEIVSSDVVGMTYGSLFDATQTRvmsVGGRQ 306
Cdd:cd23937 79 IAVRVPTINVTAMDLSVTL-KKDVTAEEVNRVLRQASQGRLkgilGYTEEPLVSVDFNHDPHSCIVDGTQTR---VSGKR 154
|
170
....*....|.
gi 1752982040 307 LVKVAAWYDNE 317
Cdd:cd23937 155 LVKLLVWCDNE 165
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-325 |
1.07e-38 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 140.01 E-value: 1.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 1 MAVKVAINGFGRIGRLA-FRRIQDVEgIEVVAVNDLT-DDDMLAHLLKYDT-MQGRFTSEVEVVDGGFRVNGKEV-KSFE 76
Cdd:PTZ00353 1 LPITVGINGFGPVGKAVlFASLTDPL-VTVVAVNDASvSIAYIAYVLEQESpLSAPDGASIRVVGEQIVLNGTQKiRVSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 77 EPDASKLPWGDLGVDVVLECTGFYTDKEKAEAHIHAGAKKVLISApAKGDVKTIVYNTNHSDLDGSETVVSGASCTTNSL 156
Cdd:PTZ00353 80 KHDLVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAG-QSADAPTVMAGSNDERLSASLPVCCAGAPIAVAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 157 APVAKVISDEFGLVEGLMTTIHAYTGDQMTQDGPHRKGDKRRARAAAQNIVPNSTGAAKAIGKVIPEIDGKLDGGAQRVP 236
Cdd:PTZ00353 159 APVIRALHEVYGVEECSYTAIHGMQPQEPIAARSKNSQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 237 VATGSLTELtVVLEKQDVTVEQVNEAMKKASNESFG----YNEDEIVSSDVVGMtyGSL-FDATQTRVMSVGgrQLVKVA 311
Cdd:PTZ00353 239 VKKGCAIDM-LVRTKQPVSKEVVDSALAEAASDRLNgvlcISKRDMISVDCIPN--GKLcYDATSSSSSREG--EVHKMV 313
|
330
....*....|....
gi 1752982040 312 AWYDNEMSYTAQLV 325
Cdd:PTZ00353 314 LWFDVECYYAARLL 327
|
|
| GAPDH-like_N |
cd05192 |
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ... |
3-155 |
2.79e-22 |
|
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: 89.72 E-value: 2.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1752982040 3 VKVAINGFGRIGRLAFRRIQDVEGIEVVAVNDLTDddmlahllkydtmqgrftsevevvdggfrvngkevksfeepdask 82
Cdd:cd05192 1 IRVAINGFGRIGRIVFRAIADQDDLDVVAINDRRD--------------------------------------------- 35
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90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1752982040 83 lpwgdlgvdVVLECTGFYTDKEKAEAHIHAGAKKVLISAPAKGDVKTIVYNTNHSDLDGSETVVSGASCTTNS 155
Cdd:cd05192 36 ---------VVIECTGSFTDDDNAEKHIKAGGKKAVITAPEKGDIPTIVVVLNELAKSAGATVVSNANETSYS 99
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| MviM |
COG0673 |
Predicted dehydrogenase [General function prediction only]; |
1-38 |
6.84e-03 |
|
Predicted dehydrogenase [General function prediction only];
Pssm-ID: 440437 [Multi-domain] Cd Length: 295 Bit Score: 37.60 E-value: 6.84e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1752982040 1 MAVKVAINGFGRIGRLAFRRIQDVEGIEVVAVNDLTDD 38
Cdd:COG0673 2 DKLRVGIIGAGGIGRAHAPALAALPGVELVAVADRDPE 39
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