|
Name |
Accession |
Description |
Interval |
E-value |
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
3-336 |
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: 508.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 3 RIAINGFGRIGRNVLRAWFESPKQFhfEIVAINDIADVHTLVHLFKYDSTHGRFNGkvDITIENEKIYLNIQsnqrllKV 82
Cdd:COG0057 4 RVAINGFGRIGRLVLRALLERGPDI--EVVAINDLGDAETLAHLLKYDSVHGRFPG--EVEVEGDSLIVNGK------KI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 83 EVLQQKQPELLPWASLKIDVVLECTGLFRSHADATRHLEAGAKRVIIgAAPFDHVDAAIVYGVNHADVKATDQIISSVSC 162
Cdd:COG0057 74 KVLAERDPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLI-SAPAKGDDPTIVYGVNHDDYDADHRIISNASC 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 163 TTQALVPLVKIIDDAFGIETALMTEIHAVTADQSVLDHAHRDLRRARASGQNIIPTTSSALGALKRVMPKMEDRIDGYSI 242
Cdd:COG0057 153 TTNCLAPVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 243 RVPTINVAAIDLTFIAQSPITVHHINELLIKASQTDYAEIMAVTDEPLVSSDFNHSPYSLIVDSTQTMVV-GHQAKVFAW 321
Cdd:COG0057 233 RVPTPNVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIgGNLVKVLAW 312
|
330
....*....|....*
gi 447111569 322 YDNEWGYANRLLDLC 336
Cdd:COG0057 313 YDNEWGYSNRMVDLA 327
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
3-334 |
6.54e-140 |
|
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: 399.34 E-value: 6.54e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 3 RIAINGFGRIGRNVLRAWFESPkQFHFEIVAINDIADVHTLVHLFKYDSTHGRFNGKVdiTIENEKIYLNIQSNQRLLKV 82
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKP-GNDLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEV--TVDEDGLVVNGKEVISVFSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 83 evlqqKQPELLPWASLKIDVVLECTGLFRSHADATRHLEAGAKRVIIgAAPFDHVDAAIVYGVNHADVKATDQIISSVSC 162
Cdd:TIGR01534 78 -----RDPSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLI-SAPSKGDVKTIVYGVNHDEYDGEERIISNASC 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 163 TTQALVPLVKIIDDAFGIETALMTEIHAVTADQSVLDHAHRDLRRARASGQNIIPTTSSALGALKRVMPKMEDRIDGYSI 242
Cdd:TIGR01534 152 TTNCLAPLAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 243 RVPTINVAAIDLTFIAQSPITVHHINELLIKASQTDYAEIMAVTDEPLVSSDFNHSPYSLIVDSTQTMVVG---HQAKVF 319
Cdd:TIGR01534 232 RVPTPNVSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVTGlgdSLVKVY 311
|
330
....*....|....*
gi 447111569 320 AWYDNEWGYANRLLD 334
Cdd:TIGR01534 312 AWYDNEWGYSNRLVD 326
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
1-334 |
8.66e-134 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 384.02 E-value: 8.66e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 1 MQRIAINGFGRIGRNVLRAWFESPKQFHFEIVAINDIADVHTLVHLFKYDSTHGRFngKVDITIENEKIYLNIQSnqrll 80
Cdd:PRK13535 1 TIRVAINGFGRIGRNVLRALYESGRRAEITVVAINELADAEGMAHLLKYDTSHGRF--AWDVRQERDQLFVGDDA----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 81 kVEVLQQKQPELLPWASLKIDVVLECTGLFRSHADATRHLEAGAKRVIIGAAPFDHVDAAIVYGVNHADVKATDQIISSV 160
Cdd:PRK13535 74 -IRLLHERDIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSNDLDATVVYGVNHDQLRAEHRIVSNA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 161 SCTTQALVPLVKIIDDAFGIETALMTEIHAVTADQSVLDHAHRDLRRARASGQNIIPTTSSALGALKRVMPKMEDRIDGY 240
Cdd:PRK13535 153 SCTTNCIIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 241 SIRVPTINVAAIDLTFIAQSPITVHHINELLIKASQTDYAEIMAVTDEPLVSSDFNHSPYSLIVDSTQTMVVG-HQAKVF 319
Cdd:PRK13535 233 SVRVPTINVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGaHLIKTL 312
|
330
....*....|....*
gi 447111569 320 AWYDNEWGYANRLLD 334
Cdd:PRK13535 313 VWCDNEWGFANRMLD 327
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
4-335 |
1.09e-105 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 312.25 E-value: 1.09e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 4 IAINGFGRIGRNVLRAWFESPKqfhFEIVAINDIA-DVHTLVHLFKYDSTHGRFNgkVDITIENEKIYLNIQsnqrllKV 82
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPG---LEIVHINDLAgDAATLAHLLEFDSVHGRWD--AEVTAEEDSIVIDGK------RI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 83 EVLQQKQPELLPWaSLKIDVVLECTGLFRSHADATRHLEAGAKRVIIgAAPFDHVDAA-IVYGVNHAD-VKATDQIISSV 160
Cdd:NF033735 70 SFSSNKDIEDTPW-GDGVDVVIECTGKFKTPEKLQPYFDQGVKKVVV-SAPVKEEGVLnIVYGVNDHLyDPARHRIVTAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 161 SCTTQALVPLVKIIDDAFGIETALMTEIHAVTADQSVLDHAHRDLRRARASGQNIIPTTSSALGALKRVMPKMEDRIDGY 240
Cdd:NF033735 148 SCTTNCLAPVVKVIHEKIGIKHGSITTIHDITNTQTIVDAPHKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGH 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 241 SIRVPTINVAAIDLTFIAQSPITVHHINELLIKASQTDYAEIMAVTDEPLVSSDFNHSPYSLIVDSTQTMVV-GHQAKVF 319
Cdd:NF033735 228 AVRVPLLNASLTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVnGTQVKIY 307
|
330
....*....|....*.
gi 447111569 320 AWYDNEWGYANRLLDL 335
Cdd:NF033735 308 AWYDNEWGYANRMVDL 323
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
162-325 |
6.85e-79 |
|
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: 238.12 E-value: 6.85e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 162 CTTQALVPLVKIIDDAFGIETALMTEIHAVTADQSVLDHAHRDLRRARASGQNIIPTTSSALGALKRVMPKMEDRIDGYS 241
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 242 IRVPTINVAAIDLTFIAQSPITVHHINELLIKASQTDYAEIMAVTDEPLVSSDFNHSPYSLIVDSTQTMVV-GHQAKVFA 320
Cdd:cd18126 81 FRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLgGNLVKVVA 160
|
....*
gi 447111569 321 WYDNE 325
Cdd:cd18126 161 WYDNE 165
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-162 |
1.46e-67 |
|
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: 208.56 E-value: 1.46e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 3 RIAINGFGRIGRNVLRAWFESPKqfhFEIVAINDIADVHTLVHLFKYDSTHGRFNGKVdiTIENEKIYLNIQsnqrllKV 82
Cdd:smart00846 2 KVGINGFGRIGRLVLRAALERPD---VEVVAINDLTDPEYLAYLLKYDSVHGRFPGTV--EVEGDGLVVNGK------AI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 83 EVLQQKQPELLPWASLKIDVVLECTGLFRSHADATRHLEAGAKRVIIGaAPFDHVDAAIVYGVNHADVKATDQIISSVSC 162
Cdd:smart00846 71 KVFAERDPANLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIIS-APSKDADPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
167-322 |
5.89e-62 |
|
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: 194.73 E-value: 5.89e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 167 LVPLVKIIDDAFGIETALMTEIHAVTADQSVLDHAH-RDLRRARASGQNIIPTTSSALGALKRVMPKMEDRIDGYSIRVP 245
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHhKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447111569 246 TINVAAIDLTFIAQSPITVHHINELLIKASQTDYAEIMAVTDEPLVSSDFNHSPYSLIVDSTQTMVV-GHQAKVFAWY 322
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVnGNFVKVVAWY 158
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
3-336 |
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: 508.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 3 RIAINGFGRIGRNVLRAWFESPKQFhfEIVAINDIADVHTLVHLFKYDSTHGRFNGkvDITIENEKIYLNIQsnqrllKV 82
Cdd:COG0057 4 RVAINGFGRIGRLVLRALLERGPDI--EVVAINDLGDAETLAHLLKYDSVHGRFPG--EVEVEGDSLIVNGK------KI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 83 EVLQQKQPELLPWASLKIDVVLECTGLFRSHADATRHLEAGAKRVIIgAAPFDHVDAAIVYGVNHADVKATDQIISSVSC 162
Cdd:COG0057 74 KVLAERDPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLI-SAPAKGDDPTIVYGVNHDDYDADHRIISNASC 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 163 TTQALVPLVKIIDDAFGIETALMTEIHAVTADQSVLDHAHRDLRRARASGQNIIPTTSSALGALKRVMPKMEDRIDGYSI 242
Cdd:COG0057 153 TTNCLAPVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 243 RVPTINVAAIDLTFIAQSPITVHHINELLIKASQTDYAEIMAVTDEPLVSSDFNHSPYSLIVDSTQTMVV-GHQAKVFAW 321
Cdd:COG0057 233 RVPTPNVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIgGNLVKVLAW 312
|
330
....*....|....*
gi 447111569 322 YDNEWGYANRLLDLC 336
Cdd:COG0057 313 YDNEWGYSNRMVDLA 327
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
3-334 |
6.54e-140 |
|
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: 399.34 E-value: 6.54e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 3 RIAINGFGRIGRNVLRAWFESPkQFHFEIVAINDIADVHTLVHLFKYDSTHGRFNGKVdiTIENEKIYLNIQSNQRLLKV 82
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKP-GNDLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEV--TVDEDGLVVNGKEVISVFSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 83 evlqqKQPELLPWASLKIDVVLECTGLFRSHADATRHLEAGAKRVIIgAAPFDHVDAAIVYGVNHADVKATDQIISSVSC 162
Cdd:TIGR01534 78 -----RDPSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLI-SAPSKGDVKTIVYGVNHDEYDGEERIISNASC 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 163 TTQALVPLVKIIDDAFGIETALMTEIHAVTADQSVLDHAHRDLRRARASGQNIIPTTSSALGALKRVMPKMEDRIDGYSI 242
Cdd:TIGR01534 152 TTNCLAPLAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 243 RVPTINVAAIDLTFIAQSPITVHHINELLIKASQTDYAEIMAVTDEPLVSSDFNHSPYSLIVDSTQTMVVG---HQAKVF 319
Cdd:TIGR01534 232 RVPTPNVSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVTGlgdSLVKVY 311
|
330
....*....|....*
gi 447111569 320 AWYDNEWGYANRLLD 334
Cdd:TIGR01534 312 AWYDNEWGYSNRLVD 326
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
1-334 |
8.66e-134 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 384.02 E-value: 8.66e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 1 MQRIAINGFGRIGRNVLRAWFESPKQFHFEIVAINDIADVHTLVHLFKYDSTHGRFngKVDITIENEKIYLNIQSnqrll 80
Cdd:PRK13535 1 TIRVAINGFGRIGRNVLRALYESGRRAEITVVAINELADAEGMAHLLKYDTSHGRF--AWDVRQERDQLFVGDDA----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 81 kVEVLQQKQPELLPWASLKIDVVLECTGLFRSHADATRHLEAGAKRVIIGAAPFDHVDAAIVYGVNHADVKATDQIISSV 160
Cdd:PRK13535 74 -IRLLHERDIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSNDLDATVVYGVNHDQLRAEHRIVSNA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 161 SCTTQALVPLVKIIDDAFGIETALMTEIHAVTADQSVLDHAHRDLRRARASGQNIIPTTSSALGALKRVMPKMEDRIDGY 240
Cdd:PRK13535 153 SCTTNCIIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 241 SIRVPTINVAAIDLTFIAQSPITVHHINELLIKASQTDYAEIMAVTDEPLVSSDFNHSPYSLIVDSTQTMVVG-HQAKVF 319
Cdd:PRK13535 233 SVRVPTINVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGaHLIKTL 312
|
330
....*....|....*
gi 447111569 320 AWYDNEWGYANRLLD 334
Cdd:PRK13535 313 VWCDNEWGFANRMLD 327
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-335 |
7.16e-125 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 361.75 E-value: 7.16e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 1 MQRIAINGFGRIGRNVLRAWFESPKqfhFEIVAINDIADVHTLVHLFKYDSTHGRFNGKVDItiENEKIYLNIQsnqrll 80
Cdd:PRK07729 2 KTKVAINGFGRIGRMVFRKAIKESA---FEIVAINASYPSETLAHLIKYDTVHGKFDGTVEA--FEDHLLVDGK------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 81 KVEVLQQKQPELLPWASLKIDVVLECTGLFRSHADATRHLEAGAKRVIIgAAPFDHVDAAIVYGVNHADVKAT-DQIISS 159
Cdd:PRK07729 71 KIRLLNNRDPKELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVIL-TAPGKNEDVTIVVGVNEDQLDIEkHTIISN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 160 VSCTTQALVPLVKIIDDAFGIETALMTEIHAVTADQSVLDHAHRDLRRARASGQNIIPTTSSALGALKRVMPKMEDRIDG 239
Cdd:PRK07729 150 ASCTTNCLAPVVKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 240 YSIRVPTINVAAIDLTFIAQSPITVHHINELLIKASQTDYAEIMAVTDEPLVSSDFNHSPYSLIVDSTQTMVV-GHQAKV 318
Cdd:PRK07729 230 MALRVPTPNVSLVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMgDRKVKV 309
|
330
....*....|....*..
gi 447111569 319 FAWYDNEWGYANRLLDL 335
Cdd:PRK07729 310 LAWYDNEWGYSCRVVDL 326
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
4-335 |
1.09e-105 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 312.25 E-value: 1.09e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 4 IAINGFGRIGRNVLRAWFESPKqfhFEIVAINDIA-DVHTLVHLFKYDSTHGRFNgkVDITIENEKIYLNIQsnqrllKV 82
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPG---LEIVHINDLAgDAATLAHLLEFDSVHGRWD--AEVTAEEDSIVIDGK------RI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 83 EVLQQKQPELLPWaSLKIDVVLECTGLFRSHADATRHLEAGAKRVIIgAAPFDHVDAA-IVYGVNHAD-VKATDQIISSV 160
Cdd:NF033735 70 SFSSNKDIEDTPW-GDGVDVVIECTGKFKTPEKLQPYFDQGVKKVVV-SAPVKEEGVLnIVYGVNDHLyDPARHRIVTAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 161 SCTTQALVPLVKIIDDAFGIETALMTEIHAVTADQSVLDHAHRDLRRARASGQNIIPTTSSALGALKRVMPKMEDRIDGY 240
Cdd:NF033735 148 SCTTNCLAPVVKVIHEKIGIKHGSITTIHDITNTQTIVDAPHKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGH 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 241 SIRVPTINVAAIDLTFIAQSPITVHHINELLIKASQTDYAEIMAVTDEPLVSSDFNHSPYSLIVDSTQTMVV-GHQAKVF 319
Cdd:NF033735 228 AVRVPLLNASLTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVnGTQVKIY 307
|
330
....*....|....*.
gi 447111569 320 AWYDNEWGYANRLLDL 335
Cdd:NF033735 308 AWYDNEWGYANRMVDL 323
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
1-337 |
6.88e-103 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 305.68 E-value: 6.88e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 1 MQRIAINGFGRIGRNVLRAWFeSPKQFHFEIVAINDIADVHTLVHLFKYDSTHGRFNgkVDITIENEKIYLNIQSnqrll 80
Cdd:PRK07403 1 MIRVAINGFGRIGRNFLRCWL-GRENSQLELVAINDTSDPRTNAHLLKYDSMLGKLN--ADISADENSITVNGKT----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 81 kVEVLQQKQPELLPWASLKIDVVLECTGLFRSHADATRHLEAGAKRVIIGAAPFDHVDAAIVYGVNHADVKATD-QIISS 159
Cdd:PRK07403 73 -IKCVSDRNPLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPGKGEDIGTYVVGVNHHEYDHEDhNIISN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 160 VSCTTQALVPLVKIIDDAFGIETALMTEIHAVTADQSVLDHAHRDLRRARASGQNIIPTTSSALGALKRVMPKMEDRIDG 239
Cdd:PRK07403 152 ASCTTNCLAPIAKVLHDNFGIIKGTMTTTHSYTGDQRILDASHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 240 YSIRVPTINVAAIDLTFIAQSPITVHHINELLIKASQTDYAEIMAVTDEPLVSSDFNHSPYSLIVDSTQTMVVGHQ-AKV 318
Cdd:PRK07403 232 IALRVPTPNVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDmVKV 311
|
330
....*....|....*....
gi 447111569 319 FAWYDNEWGYANRLLDLCD 337
Cdd:PRK07403 312 IAWYDNEWGYSQRVVDLAE 330
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
3-337 |
4.50e-97 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 292.99 E-value: 4.50e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 3 RIAINGFGRIGRNVLRAWfESPKQFHFEIVAINDIADVHTLVHLFKYDSTHGRFNGKVDItIENEKIYLNIQSnqrllkV 82
Cdd:PLN03096 62 KVAINGFGRIGRNFLRCW-HGRKDSPLDVVAINDTGGVKQASHLLKYDSTLGTFDADVKP-VGDDAISVDGKV------I 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 83 EVLQQKQPELLPWASLKIDVVLECTGLFRSHADATRHLEAGAKRVIIGAAPFDHVDAAIVyGVNHADVKATDQIISSVSC 162
Cdd:PLN03096 134 KVVSDRNPLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKGDIPTYVV-GVNADDYKHSDPIISNASC 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 163 TTQALVPLVKIIDDAFGIETALMTEIHAVTADQSVLDHAHRDLRRARASGQNIIPTTSSALGALKRVMPKMEDRIDGYSI 242
Cdd:PLN03096 213 TTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIAL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 243 RVPTINVAAIDLTFIAQSPITVHHINELLIKASQTDYAEIMAVTDEPLVSSDFNHSPYSLIVDSTQTMVVGHQ-AKVFAW 321
Cdd:PLN03096 293 RVPTPNVSVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDmVKVVAW 372
|
330
....*....|....*.
gi 447111569 322 YDNEWGYANRLLDLCD 337
Cdd:PLN03096 373 YDNEWGYSQRVVDLAD 388
|
|
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
3-335 |
1.28e-94 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 284.32 E-value: 1.28e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 3 RIAINGFGRIGRNVLRAWFESPKqfhFEIVAINDIA-DVHTLVHLFKYDSTHGRFNGKVdiTIENEKIYLNIQsnqrllK 81
Cdd:PRK08955 4 KVGINGFGRIGRLALRAAWDWPE---LEFVQINDPAgDAATLAHLLEFDSVHGRWHHEV--TAEGDAIVINGK------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 82 VEVLQQKQPELLPWAslKIDVVLECTGLFRSHADATRHLEAGAKRVIIGAAPFDHVDAAIVYGVN-HADVKATDQIISSV 160
Cdd:PRK08955 73 IRTTQNKAIADTDWS--GCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLNIVMGVNdHLFDPAIHPIVTAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 161 SCTTQALVPLVKIIDDAFGIETALMTEIHAVTADQSVLDHAHRDLRRARASGQNIIPTTSSALGALKRVMPKMEDRIDGY 240
Cdd:PRK08955 151 SCTTNCLAPVVKVIHEKLGIKHGSMTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 241 SIRVPTINVAAIDLTFIAQSPITVHHINELLIKASQTDYAEIMAVTDEPLVSSDFNHSPYSLIVDSTQTMVVGH-QAKVF 319
Cdd:PRK08955 231 AVRVPLANASLTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGtQVKLY 310
|
330
....*....|....*.
gi 447111569 320 AWYDNEWGYANRLLDL 335
Cdd:PRK08955 311 AWYDNEWGYANRTAEL 326
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
3-335 |
3.16e-91 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 279.48 E-value: 3.16e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 3 RIAINGFGRIGRNVLRAWfESPKQFHFEIVAINDIADVHTLVHLFKYDSTHGRFNGKVDItIENEKIYLNIQSnqrllkV 82
Cdd:PLN02237 77 KVAINGFGRIGRNFLRCW-HGRKDSPLDVVVVNDSGGVKNASHLLKYDSMLGTFKADVKI-VDDETISVDGKP------I 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 83 EVLQQKQPELLPWASLKIDVVLECTGLFRSHADATRHLEAGAKRVIIgAAPFDHVD-AAIVYGVNHADVK-ATDQIISSV 160
Cdd:PLN02237 149 KVVSNRDPLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVII-TAPAKGADiPTYVVGVNEDDYDhEVANIVSNA 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 161 SCTTQALVPLVKIIDDAFGIETALMTEIHAVTADQSVLDHAHRDLRRARASGQNIIPTTSSALGALKRVMPKMEDRIDGY 240
Cdd:PLN02237 228 SCTTNCLAPFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGI 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 241 SIRVPTINVAAIDLTF-IAQSPITVHHINELLIKASQTDYAEIMAVTDEPLVSSDFNHSPYSLIVDSTQTMVVGHQ-AKV 318
Cdd:PLN02237 308 ALRVPTPNVSVVDLVVnVEKKGITAEDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDmVKV 387
|
330
....*....|....*..
gi 447111569 319 FAWYDNEWGYANRLLDL 335
Cdd:PLN02237 388 VAWYDNEWGYSQRVVDL 404
|
|
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
3-335 |
3.40e-84 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 257.84 E-value: 3.40e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 3 RIAINGFGRIGRNVLRAWFESPkqfHFEIVAIND-IADVHTLVHLFKYDSTHGRFNGKVDITIEnekiYLNIQSNqrllK 81
Cdd:PTZ00023 4 KLGINGFGRIGRLVFRAALERE---DVEVVAINDpFMTLDYMCYLLKYDSVHGSLPAEVSVTDG----FLMIGSK----K 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 82 VEVLQQKQPELLPWASLKIDVVLECTGLFRSHADATRHLEAGAKRVIIGAAPFDhvDAAI-VYGVNHADVKATDQIISSV 160
Cdd:PTZ00023 73 VHVFFEKDPAAIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKD--DTPIyVMGVNHTQYDKSQRIVSNA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 161 SCTTQALVPLVKIIDDAFGIETALMTEIHAVTADQSVLDHAHR---DLRRARASGQNIIPTTSSALGALKRVMPKMEDRI 237
Cdd:PTZ00023 151 SCTTNCLAPLAKVVNDKFGIVEGLMTTVHASTANQLTVDGPSKggkDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 238 DGYSIRVPTINVAAIDLTFIAQSPITVHHINELLIKASQTDYAEIMAVTDEPLVSSDFNHSPYSLIVDSTQTMVVGHQ-A 316
Cdd:PTZ00023 231 TGMAFRVPVPDVSVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTfV 310
|
330
....*....|....*....
gi 447111569 317 KVFAWYDNEWGYANRLLDL 335
Cdd:PTZ00023 311 KLVSWYDNEWGYSNRLLDL 329
|
|
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
3-335 |
2.99e-81 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 253.24 E-value: 2.99e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 3 RIAINGFGRIGRNVLR-AWFESpkqfHFEIVAIND-IADVHTLVHLFKYDSTHGRFNGKVDITIENEkiyLNIQSNQrll 80
Cdd:PLN02272 87 KIGINGFGRIGRLVLRiATSRD----DIEVVAVNDpFIDAKYMAYMFKYDSTHGNFKGTINVVDDST---LEINGKQ--- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 81 kVEVLQQKQPELLPWASLKIDVVLECTGLFRSHADATRHLEAGAKRVIIgAAPfdHVDAAI-VYGVNHADVKATDQIISS 159
Cdd:PLN02272 157 -IKVTSKRDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVI-SAP--SADAPMfVVGVNEKTYKPNMNIVSN 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 160 VSCTTQALVPLVKIIDDAFGIETALMTEIHAVTADQSVLDH-AHRDLRRARASGQNIIPTTSSALGALKRVMPKMEDRID 238
Cdd:PLN02272 233 ASCTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGpSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLT 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 239 GYSIRVPTINVAAIDLTFIAQSPITVHHINELLIKASQTDYAEIMAVTDEPLVSSDFNHSPYSLIVDSTQTMVVGHQ-AK 317
Cdd:PLN02272 313 GMAFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASfMK 392
|
330
....*....|....*...
gi 447111569 318 VFAWYDNEWGYANRLLDL 335
Cdd:PLN02272 393 LVSWYDNEWGYSNRVLDL 410
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
162-325 |
6.85e-79 |
|
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: 238.12 E-value: 6.85e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 162 CTTQALVPLVKIIDDAFGIETALMTEIHAVTADQSVLDHAHRDLRRARASGQNIIPTTSSALGALKRVMPKMEDRIDGYS 241
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 242 IRVPTINVAAIDLTFIAQSPITVHHINELLIKASQTDYAEIMAVTDEPLVSSDFNHSPYSLIVDSTQTMVV-GHQAKVFA 320
Cdd:cd18126 81 FRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLgGNLVKVVA 160
|
....*
gi 447111569 321 WYDNE 325
Cdd:cd18126 161 WYDNE 165
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
3-335 |
5.76e-78 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 243.04 E-value: 5.76e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 3 RIAINGFGRIGRNVLRAWFESPK-QFHFEIVAINDIA-DVHTLVHLFKYDSTHGRFNGKVDITIENEKIYLN---IQSNQ 77
Cdd:PTZ00434 5 KVGINGFGRIGRMVFQAICDQGLiGTEIDVVAVVDMStNAEYFAYQMKYDTVHGRPKYTVETTKSSPSVKTDdvlVVNGH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 78 RLLKVEVlqQKQPELLPWASLKIDVVLECTGLFRSHADATRHLEAGAKRVIIgAAPFDHVDAAIVYGVNHADVKATDQ-I 156
Cdd:PTZ00434 85 RIKCVKA--QRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVI-SAPASGGAKTIVMGVNQHEYSPTEHhV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 157 ISSVSCTTQALVPLVKII-DDAFGIETALMTEIHAVTADQSVLDHAH-RDLRRARASGQNIIPTTSSALGALKRVMPKME 234
Cdd:PTZ00434 162 VSNASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSvKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 235 DRIDGYSIRVPTINVAAIDLTFIAQSPITVHHINELLIKASQTDYAEIMAVTDEPLVSSDFNHSPYSLIVDSTQTM---V 311
Cdd:PTZ00434 242 GKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKATLqnnL 321
|
330 340
....*....|....*....|....*.
gi 447111569 312 VGHQA--KVFAWYDNEWGYANRLLDL 335
Cdd:PTZ00434 322 PGERRffKIVSWYDNEWGYSHRVVDL 347
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
3-335 |
7.89e-75 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 233.86 E-value: 7.89e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 3 RIAINGFGRIGRNVLRAwfeSPKQFHFEIVAINDIADVHTLVHLFKYDSTHGRFNGKVDItiENEKIYLNIQsnqrllKV 82
Cdd:PRK15425 4 KVGINGFGRIGRIVFRA---AQKRSDIEIVAINDLLDADYMAYMLKYDSTHGRFDGTVEV--KDGHLIVNGK------KI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 83 EVLQQKQPELLPWASLKIDVVLECTGLFRSHADATRHLEAGAKRVIIGAAPFDHVdAAIVYGVNHADVKATDqIISSVSC 162
Cdd:PRK15425 73 RVTAERDPANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDNT-PMFVKGANFDKYAGQD-IVSNASC 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 163 TTQALVPLVKIIDDAFGIETALMTEIHAVTADQSVLDH-AHRDLRRARASGQNIIPTTSSALGALKRVMPKMEDRIDGYS 241
Cdd:PRK15425 151 TTNCLAPLAKVINDNFGIIEGLMTTVHATTATQKTVDGpSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 242 IRVPTINVAAIDLTFIAQSPITVHHINELLIKASQTDYAEIMAVTDEPLVSSDFNHSPYSLIVDSTQTMVVGHQ-AKVFA 320
Cdd:PRK15425 231 FRVPTPNVSVVDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNfVKLVS 310
|
330
....*....|....*
gi 447111569 321 WYDNEWGYANRLLDL 335
Cdd:PRK15425 311 WYDNETGYSNKVLDL 325
|
|
| GAPDH_N_E4PDH |
cd17892 |
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
2-161 |
2.24e-73 |
|
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: 224.45 E-value: 2.24e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 2 QRIAINGFGRIGRNVLRAWFESPKQFHFEIVAINDIADVHTLVHLFKYDSTHGRFNGKVDItiENEKiyLNIQSNqrllK 81
Cdd:cd17892 1 YRVAINGYGRIGRNVLRALYESGRRAEFQVVAINELADAETIAHLTKYDTTHGRFPGEVRV--ENDQ--LFVNGD----K 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 82 VEVLQQKQPELLPWASLKIDVVLECTGLFRSHADATRHLEAGAKRVIIGAAPFDHVDAAIVYGVNHADVKATDQIISSVS 161
Cdd:cd17892 73 IRVLHEPDPENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASNDVDATIVYGINQDLLRAEHRIVSNAS 152
|
|
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
3-335 |
4.06e-69 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 219.59 E-value: 4.06e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 3 RIAINGFGRIGRNVLRAWFESPKqfhFEIVAIND-IADVHTLVHLFKYDSTHGRFNGKvDITIENEKIYLNIQSnqrllK 81
Cdd:PLN02358 7 RIGINGFGRIGRLVARVVLQRDD---VELVAVNDpFITTEYMTYMFKYDSVHGQWKHH-ELKVKDDKTLLFGEK-----P 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 82 VEVLQQKQPELLPWASLKIDVVLECTGLFRSHADATRHLEAGAKRVIIGAAPFDHvdAAIVYGVNHADVKATDQIISSVS 161
Cdd:PLN02358 78 VTVFGIRNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDA--PMFVVGVNEHEYKSDLDIVSNAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 162 CTTQALVPLVKIIDDAFGIETALMTEIHAVTADQSVLDH-AHRDLRRARASGQNIIPTTSSALGALKRVMPKMEDRIDGY 240
Cdd:PLN02358 156 CTTNCLAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGpSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 241 SIRVPTINVAAIDLTFIAQSPITVHHINELLIKASQTDYAEIMAVTDEPLVSSDFNHSPYSLIVDSTQTMVVGHQ-AKVF 319
Cdd:PLN02358 236 SFRVPTVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKfVKLV 315
|
330
....*....|....*.
gi 447111569 320 AWYDNEWGYANRLLDL 335
Cdd:PLN02358 316 SWYDNEWGYSSRVVDL 331
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-162 |
1.46e-67 |
|
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: 208.56 E-value: 1.46e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 3 RIAINGFGRIGRNVLRAWFESPKqfhFEIVAINDIADVHTLVHLFKYDSTHGRFNGKVdiTIENEKIYLNIQsnqrllKV 82
Cdd:smart00846 2 KVGINGFGRIGRLVLRAALERPD---VEVVAINDLTDPEYLAYLLKYDSVHGRFPGTV--EVEGDGLVVNGK------AI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 83 EVLQQKQPELLPWASLKIDVVLECTGLFRSHADATRHLEAGAKRVIIGaAPFDHVDAAIVYGVNHADVKATDQIISSVSC 162
Cdd:smart00846 71 KVFAERDPANLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIIS-APSKDADPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| GAPDH_I_N |
cd05214 |
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
3-161 |
5.45e-64 |
|
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: 199.93 E-value: 5.45e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 3 RIAINGFGRIGRNVLRAWFESPKqfhFEIVAINDIADVHTLVHLFKYDSTHGRFNGKVdiTIENEKIYLNIQsnqrllKV 82
Cdd:cd05214 2 KVGINGFGRIGRLVFRAALERDD---IEVVAINDLTDDETLAYLLKYDSVHGRFDGEV--EVDDDALIVNGK------KI 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447111569 83 EVLQQKQPELLPWASLKIDVVLECTGLFRSHADATRHLEAGAKRVIIgAAPFDHVDAAIVYGVNHADVKATDQIISSVS 161
Cdd:cd05214 71 KVFAERDPAELPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVII-SAPAKDDDPTIVMGVNHDKYDADDKIISNAS 148
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
167-322 |
5.89e-62 |
|
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: 194.73 E-value: 5.89e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 167 LVPLVKIIDDAFGIETALMTEIHAVTADQSVLDHAH-RDLRRARASGQNIIPTTSSALGALKRVMPKMEDRIDGYSIRVP 245
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHhKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447111569 246 TINVAAIDLTFIAQSPITVHHINELLIKASQTDYAEIMAVTDEPLVSSDFNHSPYSLIVDSTQTMVV-GHQAKVFAWY 322
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVnGNFVKVVAWY 158
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
162-325 |
1.94e-58 |
|
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: 186.08 E-value: 1.94e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 162 CTTQALVPLVKIIDDAFGIETALMTEIHAVTADQSVLDHAHRDLRRARASGQNIIPTTSSALGALKRVMPKMEDRIDGYS 241
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 242 IRVPTINVAAIDLTFIAQSPITVHHINELLIKASQTDYAEIMAVTDEPLVSSDFNHSPYSLIVDSTQTMVV-GHQAKVFA 320
Cdd:cd23937 81 VRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSgKRLVKLLV 160
|
....*
gi 447111569 321 WYDNE 325
Cdd:cd23937 161 WCDNE 165
|
|
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
8-330 |
1.43e-57 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 193.22 E-value: 1.43e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 8 GFGRIGRNVLRAWFE-SPKQFHFEIVAI----NDIADVHTLVHLFKYDSTHGRFNGKVDITIENEKIYLNIQsnqrllKV 82
Cdd:PRK08289 134 GFGRIGRLLARLLIEkTGGGNGLRLRAIvvrkGSEGDLEKRASLLRRDSVHGPFNGTITVDEENNAIIANGN------YI 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 83 EVLQQKQPELLPWASLKID--VVLECTGLFRSHADATRHLEA-GAKRVIIgAAPFDHVDAAIVYGVNHADVKATDQIISS 159
Cdd:PRK08289 208 QVIYANSPEEVDYTAYGINnaLVVDNTGKWRDEEGLSQHLKSkGVAKVLL-TAPGKGDIKNIVHGVNHSDITDEDKIVSA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 160 VSCTTQALVPLVKIIDDAFGIETALMTEIHAVTADQSVLDHAHRDLRRARASGQNIIPTTSSALGALKRVMPKMEDRIDG 239
Cdd:PRK08289 287 ASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKGDRRGRSAPLNMVITETGAAKAVAKALPELAGKLTG 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 240 YSIRVPTINV--AAIDLTFiaQSPITVHHINELLIKAS-------QTDYaeimavTDEP-LVSSDFNHSPYSLIVDSTQT 309
Cdd:PRK08289 367 NAIRVPTPNVsmAILNLNL--EKETSREELNEYLRQMSlhsplqnQIDY------TDSTeVVSSDFVGSRHAGVVDSQAT 438
|
330 340
....*....|....*....|.
gi 447111569 310 MVVGHQAKVFAWYDNEWGYAN 330
Cdd:PRK08289 439 IVNGNRAVLYVWYDNEFGYSC 459
|
|
| Gp_dh_N |
pfam00044 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-112 |
2.29e-45 |
|
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: 149.94 E-value: 2.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 3 RIAINGFGRIGRNVLRAWFESPkqfHFEIVAINDIADVHTLVHLFKYDSTHGRFNGKVdiTIENEKIYLNIQsnqrllKV 82
Cdd:pfam00044 2 KVGINGFGRIGRLVLRAALERP---DIEVVAINDLTDPETLAYLLKYDSVHGRFPGEV--EAEEDGLVVNGK------KI 70
|
90 100 110
....*....|....*....|....*....|
gi 447111569 83 EVLQQKQPELLPWASLKIDVVLECTGLFRS 112
Cdd:pfam00044 71 KVFAERDPAELPWGDLGVDVVIESTGVFTT 100
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
4-335 |
6.36e-37 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 135.39 E-value: 6.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 4 IAINGFGRIGRNVLRAWFESPKqfhFEIVAINDIA-DVHTLVHLFKYDSTHgRFNGKVDITIENEKIYLNiqSNQRllkV 82
Cdd:PTZ00353 5 VGINGFGPVGKAVLFASLTDPL---VTVVAVNDASvSIAYIAYVLEQESPL-SAPDGASIRVVGEQIVLN--GTQK---I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 83 EVLQQKQPELLPWASLKIDVVLECTGLFRSHADATRHLEAGAKRVIIGAAPFDhvDAAIVYGVNHADVKATDQIISSVSC 162
Cdd:PTZ00353 76 RVSAKHDLVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSAD--APTVMAGSNDERLSASLPVCCAGAP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 163 TTQALVPLVKIIDDAFGIETALMTEIHAV-----TADQSvldHAHRDLRRARASGQNIIPTTSSALGALKRVMPKMEDRI 237
Cdd:PTZ00353 154 IAVALAPVIRALHEVYGVEECSYTAIHGMqpqepIAARS---KNSQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 238 DGYSIRVPTINVAAIDLTFIAQSPITVHHINELLIKASQTDYAEIMAVTDEPLVSSD-FNHSPYSLIVDSTQTMVVGHQA 316
Cdd:PTZ00353 231 SGSAFQVPVKKGCAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDcIPNGKLCYDATSSSSSREGEVH 310
|
330
....*....|....*....
gi 447111569 317 KVFAWYDNEWGYANRLLDL 335
Cdd:PTZ00353 311 KMVLWFDVECYYAARLLSL 329
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
162-325 |
1.24e-35 |
|
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: 126.96 E-value: 1.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 162 CTTQALVPLVKIIDDAFGIETALMTEIHAVTADQSVLDH-AHRDLRRARASGQNIIPTTSSALGALKRVMPKMEDRIDGY 240
Cdd:cd18123 1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGpSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 241 SIRVPTINVAAIDLTFIAQSPITVHHINELLIKASQTDyaEIMAVTDEPLVSSDFNHSPYSLIVDSTQTMVVG-HQAKVF 319
Cdd:cd18123 81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEGK--GRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNdNEVKLM 158
|
....*.
gi 447111569 320 AWYDNE 325
Cdd:cd18123 159 QWYDNE 164
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
162-325 |
6.07e-16 |
|
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: 74.48 E-value: 6.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 162 CTTQALVPLVKIIDDAFGIETALMTEIHAVTADQSVLDHAHrDLRRARASGQNIIPTTSSALGALKRVMPKMED--RIDG 239
Cdd:cd18122 1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPI-LKSEVRAIIPNIPKNETKHAPETGKVLGEIGKpiKVDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447111569 240 YSIRVPTINVAAIDLTFIAQSPITVHHINELLIKASQTDYAEIMAVTDEPLVSSDFNHSPYSLIVDSTQTMVVGHQ-AKV 318
Cdd:cd18122 80 IAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNkLKV 159
|
....*..
gi 447111569 319 FAWYDNE 325
Cdd:cd18122 160 FSAVDNE 166
|
|
| GAPDH-like_N |
cd05192 |
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ... |
3-174 |
4.89e-07 |
|
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: 47.73 E-value: 4.89e-07
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gi 447111569 3 RIAINGFGRIGRNVLRAWfesPKQFHFEIVAINDIAdvhtlvhlfkydsthgrfngkvditienekiylniqsnqrllkv 82
Cdd:cd05192 2 RVAINGFGRIGRIVFRAI---ADQDDLDVVAINDRR-------------------------------------------- 34
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90 100 110 120 130 140 150 160
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gi 447111569 83 evlqqkqpellpwaslkiDVVLECTGLFRSHADATRHLEAGAKRVIIGaAPFDHVDAAIVYGVNHADVKATDQIISSV-- 160
Cdd:cd05192 35 ------------------DVVIECTGSFTDDDNAEKHIKAGGKKAVIT-APEKGDIPTIVVVLNELAKSAGATVVSNAne 95
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170
....*....|....
gi 447111569 161 SCTTQALVPLVKII 174
Cdd:cd05192 96 TSYSPQVVDLVRAI 109
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