|
Name |
Accession |
Description |
Interval |
E-value |
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
1-337 |
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: 645.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 1 MAIKIAINGYGRIGRNVIRALYESGrtNEIKVVAINDLGDSKTNAHLTQYDTVHGKFPFDVAVDGDYIVINGDRIRVLSE 80
Cdd:COG0057 1 MTIRVAINGFGRIGRLVLRALLERG--PDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 81 RDPSKLPWGELGIDVVHECTGLFTSKAKASAHLTAGAKKVIISAPGGNDvDATIVYGVNHNTLKASDTVISNASCTTNCL 160
Cdd:COG0057 79 RDPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGD-DPTIVYGVNHDDYDADHRIISNASCTTNCL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 161 APLVKPLHDAIGIEHGLMTTIHSYTNDQVLTDVYHSDLRRARSATQSMIPTKTGAAAAVGLVLPELKGKLDGFAMRVPTI 240
Cdd:COG0057 158 APVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 241 NVSVVDLVFKAKRPTSKEEITSVLTAASEGPLKGILAINDLPLVSSDFNHNPASSIFEAPSTYVVDGDFVKVLSWYDNEW 320
Cdd:COG0057 238 NVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEW 317
|
330
....*....|....*..
gi 522053463 321 GFSNRMLDTTVALVNAK 337
Cdd:COG0057 318 GYSNRMVDLAEYMAKLL 334
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
4-328 |
1.15e-169 |
|
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: 474.46 E-value: 1.15e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 4 KIAINGYGRIGRNVIRALYESgRTNEIKVVAINDLGDSKTNAHLTQYDTVHGKFPFDVAVDGDYIVING-DRIRVLSERD 82
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEK-PGNDLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGkEVISVFSERD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 83 PSKLPWGELGIDVVHECTGLFTSKAKASAHLTAGAKKVIISAPGGNDVdATIVYGVNHNTLKASDTVISNASCTTNCLAP 162
Cdd:TIGR01534 80 PSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDV-KTIVYGVNHDEYDGEERIISNASCTTNCLAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 163 LVKPLHDAIGIEHGLMTTIHSYTNDQVLTDVYHSDLRRARSATQSMIPTKTGAAAAVGLVLPELKGKLDGFAMRVPTINV 242
Cdd:TIGR01534 159 LAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 243 SVVDLVFKAKRPTSKEEITSVLTAASEGPLKGILAINDLPLVSSDFNHNPASSIFEAPSTYVVDGD--FVKVLSWYDNEW 320
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVTGLGdsLVKVYAWYDNEW 318
|
....*...
gi 522053463 321 GFSNRMLD 328
Cdd:TIGR01534 319 GYSNRLVD 326
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
3-337 |
7.52e-165 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 462.99 E-value: 7.52e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 3 IKIAINGYGRIGRNVIRALYESGRTNEIKVVAINDLGDSKTNAHLTQYDTVHGKFPFDVAVDGDYIVINGDRIRVLSERD 82
Cdd:PRK13535 2 IRVAINGFGRIGRNVLRALYESGRRAEITVVAINELADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 83 PSKLPWGELGIDVVHECTGLFTSKAKASAHLTAGAKKVIISAPGGNDVDATIVYGVNHNTLKASDTVISNASCTTNCLAP 162
Cdd:PRK13535 82 IASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSNDLDATVVYGVNHDQLRAEHRIVSNASCTTNCIIP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 163 LVKPLHDAIGIEHGLMTTIHSYTNDQVLTDVYHSDLRRARSATQSMIPTKTGAAAAVGLVLPELKGKLDGFAMRVPTINV 242
Cdd:PRK13535 162 VIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPTINV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 243 SVVDLVFKAKRPTSKEEITSVLTAASEGPLKGILAINDLPLVSSDFNHNPASSIFEAPSTYVVDGDFVKVLSWYDNEWGF 322
Cdd:PRK13535 242 TAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNEWGF 321
|
330
....*....|....*
gi 522053463 323 SNRMLDTTVALVNAK 337
Cdd:PRK13535 322 ANRMLDTTLAMAAAG 336
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
5-328 |
9.29e-145 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 411.25 E-value: 9.29e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 5 IAINGYGRIGRNVIRALYESGrtnEIKVVAINDL-GDSKTNAHLTQYDTVHGKFPFDVAVDGDYIVINGDRIRVLSERDP 83
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRP---GLEIVHINDLaGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 84 SKLPWGElGIDVVHECTGLFTSKAKASAHLTAGAKKVIISAPGGNDVDATIVYGVNHNTLK-ASDTVISNASCTTNCLAP 162
Cdd:NF033735 78 EDTPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLNIVYGVNDHLYDpARHRIVTAASCTTNCLAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 163 LVKPLHDAIGIEHGLMTTIHSYTNDQVLTDVYHSDLRRARSATQSMIPTKTGAAAAVGLVLPELKGKLDGFAMRVPTINV 242
Cdd:NF033735 157 VVKVIHEKIGIKHGSITTIHDITNTQTIVDAPHKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 243 SVVDLVFKAKRPTSKEEITSVLTAASEGPLKGILAINDLPLVSSDFNHNPASSIFEAPSTYVVDGDFVKVLSWYDNEWGF 322
Cdd:NF033735 237 SLTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGY 316
|
....*.
gi 522053463 323 SNRMLD 328
Cdd:NF033735 317 ANRMVD 322
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
155-319 |
9.65e-106 |
|
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: 306.30 E-value: 9.65e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 155 CTTNCLAPLVKPLHDAIGIEHGLMTTIHSYTNDQVLTDVYHSDLRRARSATQSMIPTKTGAAAAVGLVLPELKGKLDGFA 234
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 235 MRVPTINVSVVDLVFKAKRPTSKEEITSVLTAASEGPLKGILAINDLPLVSSDFNHNPASSIFEAPSTYVVDGDFVKVLS 314
Cdd:cd18126 81 FRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVVA 160
|
....*
gi 522053463 315 WYDNE 319
Cdd:cd18126 161 WYDNE 165
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-155 |
2.29e-83 |
|
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: 249.01 E-value: 2.29e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 3 IKIAINGYGRIGRNVIRALYESgrtNEIKVVAINDLGDSKTNAHLTQYDTVHGKFPFDVAVDGDYIVINGDRIRVLSERD 82
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALER---PDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERD 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522053463 83 PSKLPWGELGIDVVHECTGLFTSKAKASAHLTAGAKKVIISAPgGNDVDATIVYGVNHNTLKASDTVISNASC 155
Cdd:smart00846 78 PANLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAP-SKDADPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
160-316 |
4.49e-80 |
|
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. C-terminal domain is a mixed alpha/antiparallel beta fold.
Pssm-ID: 460700 Cd Length: 158 Bit Score: 240.96 E-value: 4.49e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 160 LAPLVKPLHDAIGIEHGLMTTIHSYTNDQVLTD-VYHSDLRRARSATQSMIPTKTGAAAAVGLVLPELKGKLDGFAMRVP 238
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDgPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522053463 239 TINVSVVDLVFKAKRPTSKEEITSVLTAASEGPLKGILAINDLPLVSSDFNHNPASSIFEAPSTYVVDGDFVKVLSWY 316
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
1-337 |
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: 645.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 1 MAIKIAINGYGRIGRNVIRALYESGrtNEIKVVAINDLGDSKTNAHLTQYDTVHGKFPFDVAVDGDYIVINGDRIRVLSE 80
Cdd:COG0057 1 MTIRVAINGFGRIGRLVLRALLERG--PDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 81 RDPSKLPWGELGIDVVHECTGLFTSKAKASAHLTAGAKKVIISAPGGNDvDATIVYGVNHNTLKASDTVISNASCTTNCL 160
Cdd:COG0057 79 RDPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGD-DPTIVYGVNHDDYDADHRIISNASCTTNCL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 161 APLVKPLHDAIGIEHGLMTTIHSYTNDQVLTDVYHSDLRRARSATQSMIPTKTGAAAAVGLVLPELKGKLDGFAMRVPTI 240
Cdd:COG0057 158 APVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 241 NVSVVDLVFKAKRPTSKEEITSVLTAASEGPLKGILAINDLPLVSSDFNHNPASSIFEAPSTYVVDGDFVKVLSWYDNEW 320
Cdd:COG0057 238 NVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEW 317
|
330
....*....|....*..
gi 522053463 321 GFSNRMLDTTVALVNAK 337
Cdd:COG0057 318 GYSNRMVDLAEYMAKLL 334
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
4-328 |
1.15e-169 |
|
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: 474.46 E-value: 1.15e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 4 KIAINGYGRIGRNVIRALYESgRTNEIKVVAINDLGDSKTNAHLTQYDTVHGKFPFDVAVDGDYIVING-DRIRVLSERD 82
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEK-PGNDLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGkEVISVFSERD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 83 PSKLPWGELGIDVVHECTGLFTSKAKASAHLTAGAKKVIISAPGGNDVdATIVYGVNHNTLKASDTVISNASCTTNCLAP 162
Cdd:TIGR01534 80 PSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDV-KTIVYGVNHDEYDGEERIISNASCTTNCLAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 163 LVKPLHDAIGIEHGLMTTIHSYTNDQVLTDVYHSDLRRARSATQSMIPTKTGAAAAVGLVLPELKGKLDGFAMRVPTINV 242
Cdd:TIGR01534 159 LAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 243 SVVDLVFKAKRPTSKEEITSVLTAASEGPLKGILAINDLPLVSSDFNHNPASSIFEAPSTYVVDGD--FVKVLSWYDNEW 320
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVTGLGdsLVKVYAWYDNEW 318
|
....*...
gi 522053463 321 GFSNRMLD 328
Cdd:TIGR01534 319 GYSNRLVD 326
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
3-337 |
7.52e-165 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 462.99 E-value: 7.52e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 3 IKIAINGYGRIGRNVIRALYESGRTNEIKVVAINDLGDSKTNAHLTQYDTVHGKFPFDVAVDGDYIVINGDRIRVLSERD 82
Cdd:PRK13535 2 IRVAINGFGRIGRNVLRALYESGRRAEITVVAINELADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 83 PSKLPWGELGIDVVHECTGLFTSKAKASAHLTAGAKKVIISAPGGNDVDATIVYGVNHNTLKASDTVISNASCTTNCLAP 162
Cdd:PRK13535 82 IASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSNDLDATVVYGVNHDQLRAEHRIVSNASCTTNCIIP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 163 LVKPLHDAIGIEHGLMTTIHSYTNDQVLTDVYHSDLRRARSATQSMIPTKTGAAAAVGLVLPELKGKLDGFAMRVPTINV 242
Cdd:PRK13535 162 VIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPTINV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 243 SVVDLVFKAKRPTSKEEITSVLTAASEGPLKGILAINDLPLVSSDFNHNPASSIFEAPSTYVVDGDFVKVLSWYDNEWGF 322
Cdd:PRK13535 242 TAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNEWGF 321
|
330
....*....|....*
gi 522053463 323 SNRMLDTTVALVNAK 337
Cdd:PRK13535 322 ANRMLDTTLAMAAAG 336
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-328 |
2.49e-153 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 433.78 E-value: 2.49e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 1 MAIKIAINGYGRIGRNVIRALYESGRtneIKVVAINDLGDSKTNAHLTQYDTVHGKFPFDVAVDGDYIVINGDRIRVLSE 80
Cdd:PRK07729 1 MKTKVAINGFGRIGRMVFRKAIKESA---FEIVAINASYPSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 81 RDPSKLPWGELGIDVVHECTGLFTSKAKASAHLTAGAKKVIISAPGGNDvDATIVYGVNHNTLKA-SDTVISNASCTTNC 159
Cdd:PRK07729 78 RDPKELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNE-DVTIVVGVNEDQLDIeKHTIISNASCTTNC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 160 LAPLVKPLHDAIGIEHGLMTTIHSYTNDQVLTDVYHSDLRRARSATQSMIPTKTGAAAAVGLVLPELKGKLDGFAMRVPT 239
Cdd:PRK07729 157 LAPVVKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 240 INVSVVDLVFKAKRPTSKEEITSVLTAASEGPLKGILAINDLPLVSSDFNHNPASSIFEAPSTYVVDGDFVKVLSWYDNE 319
Cdd:PRK07729 237 PNVSLVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNE 316
|
....*....
gi 522053463 320 WGFSNRMLD 328
Cdd:PRK07729 317 WGYSCRVVD 325
|
|
| E4PD_g-proteo |
TIGR01532 |
erythrose-4-phosphate dehydrogenase; This model represents the small clade of dehydrogenases ... |
4-328 |
5.44e-152 |
|
erythrose-4-phosphate dehydrogenase; This model represents the small clade of dehydrogenases in gamma-proteobacteria which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose. This enzyme activity appears to have evolved from glyceraldehyde-3-phosphate dehydrogenase, whose substrate differs only in the lack of one carbon relative to E4P. Accordingly, this model is very close to the corresponding models for GAPDH, and those sequences which hit above trusted here invariably hit between trusted and noise to the GAPDH model (TIGR01534). Similarly, it may be found that there are species outside of the gamma proteobacteria which synthesize pyridoxine and have more than one aparrent GAPDH gene of which one may have E4PD activity - this may necessitate a readjustment of these models. Alternatively, some of the GAPDH enzymes may prove to be bifunctional in certain species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
Pssm-ID: 130595 Cd Length: 325 Bit Score: 429.70 E-value: 5.44e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 4 KIAINGYGRIGRNVIRALYESGRTNEIKVVAINDLGDSKTNAHLTQYDTVHGKFPFDVAVDGDYIVINGDRIRVLSERDP 83
Cdd:TIGR01532 1 RVAINGFGRIGRNVLRALYESGRRAEITVVAINELADAAGMAHLLKYDTSHGRFAWEVRQDRDQLFVGDDAIRVLHERSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 84 SKLPWGELGIDVVHECTGLFTSKAKASAHLTAGAKKVIISAPGGNDVDATIVYGVNHNTLKASDTVISNASCTTNCLAPL 163
Cdd:TIGR01532 81 QSLPWRELGVDLVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGASDLDATIVYGVNQDQLRAEHRIVSNASCTTNCIVPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 164 VKPLHDAIGIEHGLMTTIHSYTNDQVLTDVYHSDLRRARSATQSMIPTKTGAAAAVGLVLPELKGKLDGFAMRVPTINVS 243
Cdd:TIGR01532 161 IKLLDDAYGIESGTITTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGIERFFPQFNDRFEAIAVRVPTVNVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 244 VVDLVFKAKRPTSKEEITSVLTAASEGPLKGILAINDLPLVSSDFNHNPASSIFEAPSTYVVDGDFVKVLSWYDNEWGFS 323
Cdd:TIGR01532 241 AIDLSVTVKKPVKANEVNLLLQKAAQGALRGIVDYTELPLVSVDFNHDPHSAIVDGTQTRVSGAHLVKTLVWCDNEWGFA 320
|
....*
gi 522053463 324 NRMLD 328
Cdd:TIGR01532 321 NRMLD 325
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
5-328 |
9.29e-145 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 411.25 E-value: 9.29e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 5 IAINGYGRIGRNVIRALYESGrtnEIKVVAINDL-GDSKTNAHLTQYDTVHGKFPFDVAVDGDYIVINGDRIRVLSERDP 83
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRP---GLEIVHINDLaGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 84 SKLPWGElGIDVVHECTGLFTSKAKASAHLTAGAKKVIISAPGGNDVDATIVYGVNHNTLK-ASDTVISNASCTTNCLAP 162
Cdd:NF033735 78 EDTPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLNIVYGVNDHLYDpARHRIVTAASCTTNCLAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 163 LVKPLHDAIGIEHGLMTTIHSYTNDQVLTDVYHSDLRRARSATQSMIPTKTGAAAAVGLVLPELKGKLDGFAMRVPTINV 242
Cdd:NF033735 157 VVKVIHEKIGIKHGSITTIHDITNTQTIVDAPHKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 243 SVVDLVFKAKRPTSKEEITSVLTAASEGPLKGILAINDLPLVSSDFNHNPASSIFEAPSTYVVDGDFVKVLSWYDNEWGF 322
Cdd:NF033735 237 SLTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGY 316
|
....*.
gi 522053463 323 SNRMLD 328
Cdd:NF033735 317 ANRMVD 322
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
3-328 |
2.70e-139 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 398.13 E-value: 2.70e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 3 IKIAINGYGRIGRNVIRALYesGRTN-EIKVVAINDLGDSKTNAHLTQYDTVHGKFPFDVAVDGDYIVINGDRIRVLSER 81
Cdd:PRK07403 2 IRVAINGFGRIGRNFLRCWL--GRENsQLELVAINDTSDPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 82 DPSKLPWGELGIDVVHECTGLFTSKAKASAHLTAGAKKVIISAPGGNDVDATIVYGVNHNTLKASD-TVISNASCTTNCL 160
Cdd:PRK07403 80 NPLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPGKGEDIGTYVVGVNHHEYDHEDhNIISNASCTTNCL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 161 APLVKPLHDAIGIEHGLMTTIHSYTNDQVLTDVYHSDLRRARSATQSMIPTKTGAAAAVGLVLPELKGKLDGFAMRVPTI 240
Cdd:PRK07403 160 APIAKVLHDNFGIIKGTMTTTHSYTGDQRILDASHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 241 NVSVVDLVFKAKRPTSKEEITSVLTAASEGPLKGILAINDLPLVSSDFNHNPASSIFEAPSTYVVDGDFVKVLSWYDNEW 320
Cdd:PRK07403 240 NVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYDNEW 319
|
....*...
gi 522053463 321 GFSNRMLD 328
Cdd:PRK07403 320 GYSQRVVD 327
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
3-328 |
6.88e-125 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 363.87 E-value: 6.88e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 3 IKIAINGYGRIGRNVIRALYesGRTNE-IKVVAINDLGDSKTNAHLTQYDTVHGKFPFDVAVDGD-YIVINGDRIRVLSE 80
Cdd:PLN03096 61 IKVAINGFGRIGRNFLRCWH--GRKDSpLDVVAINDTGGVKQASHLLKYDSTLGTFDADVKPVGDdAISVDGKVIKVVSD 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 81 RDPSKLPWGELGIDVVHECTGLFTSKAKASAHLTAGAKKVIISAPGGNDVdATIVYGVNHNTLKASDTVISNASCTTNCL 160
Cdd:PLN03096 139 RNPLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKGDI-PTYVVGVNADDYKHSDPIISNASCTTNCL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 161 APLVKPLHDAIGIEHGLMTTIHSYTNDQVLTDVYHSDLRRARSATQSMIPTKTGAAAAVGLVLPELKGKLDGFAMRVPTI 240
Cdd:PLN03096 218 APFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTP 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 241 NVSVVDLVFKAKRPTSKEEITSVLTAASEGPLKGILAINDLPLVSSDFNHNPASSIFEAPSTYVVDGDFVKVLSWYDNEW 320
Cdd:PLN03096 298 NVSVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAWYDNEW 377
|
....*...
gi 522053463 321 GFSNRMLD 328
Cdd:PLN03096 378 GYSQRVVD 385
|
|
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-334 |
6.12e-124 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 359.04 E-value: 6.12e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 1 MAIKIAINGYGRIGRNVIRALYEsgrTNEIKVVAINDL-GDSKTNAHLTQYDTVHGKFPFDVAVDGDYIVINGDRIRVLS 79
Cdd:PRK08955 1 MTIKVGINGFGRIGRLALRAAWD---WPELEFVQINDPaGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 80 ERDPSKLPWGelGIDVVHECTGLFTSKAKASAHLTAGAKKVIISAPGGNDVDATIVYGVNHNTL-KASDTVISNASCTTN 158
Cdd:PRK08955 78 NKAIADTDWS--GCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLNIVMGVNDHLFdPAIHPIVTAASCTTN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 159 CLAPLVKPLHDAIGIEHGLMTTIHSYTNDQVLTDVYHSDLRRARSATQSMIPTKTGAAAAVGLVLPELKGKLDGFAMRVP 238
Cdd:PRK08955 156 CLAPVVKVIHEKLGIKHGSMTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 239 TINVSVVDLVFKAKRPTSKEEITSVLTAASEGPLKGILAINDLPLVSSDFNHNPASSIFEAPSTYVVDGDFVKVLSWYDN 318
Cdd:PRK08955 236 LANASLTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDN 315
|
330
....*....|....*.
gi 522053463 319 EWGFSNRmldtTVALV 334
Cdd:PRK08955 316 EWGYANR----TAELA 327
|
|
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
3-337 |
9.11e-121 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 354.16 E-value: 9.11e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 3 IKIAINGYGRIGRNVIRALyeSGRtNEIKVVAIND-LGDSKTNAHLTQYDTVHGKFPFDV-AVDGDYIVINGDRIRVLSE 80
Cdd:PLN02272 86 TKIGINGFGRIGRLVLRIA--TSR-DDIEVVAVNDpFIDAKYMAYMFKYDSTHGNFKGTInVVDDSTLEINGKQIKVTSK 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 81 RDPSKLPWGELGIDVVHECTGLFTSKAKASAHLTAGAKKVIISAPGGndvDATI-VYGVNHNTLKASDTVISNASCTTNC 159
Cdd:PLN02272 163 RDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSA---DAPMfVVGVNEKTYKPNMNIVSNASCTTNC 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 160 LAPLVKPLHDAIGIEHGLMTTIHSYTNDQVLTD-VYHSDLRRARSATQSMIPTKTGAAAAVGLVLPELKGKLDGFAMRVP 238
Cdd:PLN02272 240 LAPLAKVVHEEFGILEGLMTTVHATTATQKTVDgPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVP 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 239 TINVSVVDLVFKAKRPTSKEEITSVLTAASEGPLKGILAINDLPLVSSDFNHNPASSIFEAPSTYVVDGDFVKVLSWYDN 318
Cdd:PLN02272 320 TPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDN 399
|
330 340
....*....|....*....|.
gi 522053463 319 EWGFSNRMLDTT--VALVNAK 337
Cdd:PLN02272 400 EWGYSNRVLDLIehMALVAAS 420
|
|
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-328 |
1.37e-120 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 350.67 E-value: 1.37e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 1 MAIKIAINGYGRIGRNVIRALYESgrtNEIKVVAIND-LGDSKTNAHLTQYDTVHGKFPFDVAVDGDYIVINGDRIRVLS 79
Cdd:PTZ00023 1 MVVKLGINGFGRIGRLVFRAALER---EDVEVVAINDpFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 80 ERDPSKLPWGELGIDVVHECTGLFTSKAKASAHLTAGAKKVIISAPGGNDVdATIVYGVNHNTLKASDTVISNASCTTNC 159
Cdd:PTZ00023 78 EKDPAAIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKDDT-PIYVMGVNHTQYDKSQRIVSNASCTTNC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 160 LAPLVKPLHDAIGIEHGLMTTIHSYTNDQVLTDVYH---SDLRRARSATQSMIPTKTGAAAAVGLVLPELKGKLDGFAMR 236
Cdd:PTZ00023 157 LAPLAKVVNDKFGIVEGLMTTVHASTANQLTVDGPSkggKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 237 VPTINVSVVDLVFKAKRPTSKEEITSVLTAASEGPLKGILAINDLPLVSSDFNHNPASSIFEAPSTYVVDGDFVKVLSWY 316
Cdd:PTZ00023 237 VPVPDVSVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWY 316
|
330
....*....|..
gi 522053463 317 DNEWGFSNRMLD 328
Cdd:PTZ00023 317 DNEWGYSNRLLD 328
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
3-330 |
4.03e-117 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 345.73 E-value: 4.03e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 3 IKIAINGYGRIGRNVIRAlYESGRTNEIKVVAINDLGDSKTNAHLTQYDTVHGKFPFDVA-VDGDYIVINGDRIRVLSER 81
Cdd:PLN02237 76 LKVAINGFGRIGRNFLRC-WHGRKDSPLDVVVVNDSGGVKNASHLLKYDSMLGTFKADVKiVDDETISVDGKPIKVVSNR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 82 DPSKLPWGELGIDVVHECTGLFTSKAKASAHLTAGAKKVIISAPG-GNDVdATIVYGVNHNTLKASDT-VISNASCTTNC 159
Cdd:PLN02237 155 DPLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAkGADI-PTYVVGVNEDDYDHEVAnIVSNASCTTNC 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 160 LAPLVKPLHDAIGIEHGLMTTIHSYTNDQVLTDVYHSDLRRARSATQSMIPTKTGAAAAVGLVLPELKGKLDGFAMRVPT 239
Cdd:PLN02237 234 LAPFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPT 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 240 INVSVVDLVFKA-KRPTSKEEITSVLTAASEGPLKGILAINDLPLVSSDFNHNPASSIFEAPSTYVVDGDFVKVLSWYDN 318
Cdd:PLN02237 314 PNVSVVDLVVNVeKKGITAEDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVAWYDN 393
|
330
....*....|..
gi 522053463 319 EWGFSNRMLDTT 330
Cdd:PLN02237 394 EWGYSQRVVDLA 405
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
1-328 |
2.75e-110 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 325.47 E-value: 2.75e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 1 MAIKIAINGYGRIGRNVIRALYESGRT-NEIKVVAINDLG-DSKTNAHLTQYDTVHGKFPFDVAV--------DGDYIVI 70
Cdd:PTZ00434 2 APIKVGINGFGRIGRMVFQAICDQGLIgTEIDVVAVVDMStNAEYFAYQMKYDTVHGRPKYTVETtksspsvkTDDVLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 71 NGDRIR-VLSERDPSKLPWGELGIDVVHECTGLFTSKAKASAHLTAGAKKVIISAPGGNDVDaTIVYGVNHNTLKASDT- 148
Cdd:PTZ00434 82 NGHRIKcVKAQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPASGGAK-TIVMGVNQHEYSPTEHh 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 149 VISNASCTTNCLAPLVKPL-HDAIGIEHGLMTTIHSYTNDQVLTD-VYHSDLRRARSATQSMIPTKTGAAAAVGLVLPEL 226
Cdd:PTZ00434 161 VVSNASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDgVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 227 KGKLDGFAMRVPTINVSVVDLVFKAKRPTSKEEITSVLTAASEGPLKGILAINDLPLVSSDFNHNPASSIFEAPSTYV-- 304
Cdd:PTZ00434 241 KGKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKATLQnn 320
|
330 340
....*....|....*....|....*.
gi 522053463 305 --VDGDFVKVLSWYDNEWGFSNRMLD 328
Cdd:PTZ00434 321 lpGERRFFKIVSWYDNEWGYSHRVVD 346
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
155-319 |
9.65e-106 |
|
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: 306.30 E-value: 9.65e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 155 CTTNCLAPLVKPLHDAIGIEHGLMTTIHSYTNDQVLTDVYHSDLRRARSATQSMIPTKTGAAAAVGLVLPELKGKLDGFA 234
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 235 MRVPTINVSVVDLVFKAKRPTSKEEITSVLTAASEGPLKGILAINDLPLVSSDFNHNPASSIFEAPSTYVVDGDFVKVLS 314
Cdd:cd18126 81 FRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVVA 160
|
....*
gi 522053463 315 WYDNE 319
Cdd:cd18126 161 WYDNE 165
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
1-328 |
1.30e-103 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 307.43 E-value: 1.30e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 1 MAIKIAINGYGRIGRNVIRAlyeSGRTNEIKVVAINDLGDSKTNAHLTQYDTVHGKFPFDVAVDGDYIVINGDRIRVLSE 80
Cdd:PRK15425 1 MTIKVGINGFGRIGRIVFRA---AQKRSDIEIVAINDLLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 81 RDPSKLPWGELGIDVVHECTGLFTSKAKASAHLTAGAKKVIISAPGgNDVDATIVYGVNHNTLKASDtVISNASCTTNCL 160
Cdd:PRK15425 78 RDPANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPS-KDNTPMFVKGANFDKYAGQD-IVSNASCTTNCL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 161 APLVKPLHDAIGIEHGLMTTIHSYTNDQVLTD-VYHSDLRRARSATQSMIPTKTGAAAAVGLVLPELKGKLDGFAMRVPT 239
Cdd:PRK15425 156 APLAKVINDNFGIIEGLMTTVHATTATQKTVDgPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 240 INVSVVDLVFKAKRPTSKEEITSVLTAASEGPLKGILAINDLPLVSSDFNHNPASSIFEAPSTYVVDGDFVKVLSWYDNE 319
Cdd:PRK15425 236 PNVSVVDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNE 315
|
....*....
gi 522053463 320 WGFSNRMLD 328
Cdd:PRK15425 316 TGYSNKVLD 324
|
|
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
3-336 |
1.32e-87 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 266.59 E-value: 1.32e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 3 IKIAINGYGRIGRNVIRALYESgrtNEIKVVAIND-LGDSKTNAHLTQYDTVHGKFPF-DVAVDGDYIVINGDR-IRVLS 79
Cdd:PLN02358 6 IRIGINGFGRIGRLVARVVLQR---DDVELVAVNDpFITTEYMTYMFKYDSVHGQWKHhELKVKDDKTLLFGEKpVTVFG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 80 ERDPSKLPWGELGIDVVHECTGLFTSKAKASAHLTAGAKKVIISAPGGNDvdATIVYGVNHNTLKASDTVISNASCTTNC 159
Cdd:PLN02358 83 IRNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDA--PMFVVGVNEHEYKSDLDIVSNASCTTNC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 160 LAPLVKPLHDAIGIEHGLMTTIHSYTNDQVLTD-VYHSDLRRARSATQSMIPTKTGAAAAVGLVLPELKGKLDGFAMRVP 238
Cdd:PLN02358 161 LAPLAKVINDRFGIVEGLMTTVHSITATQKTVDgPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 239 TINVSVVDLVFKAKRPTSKEEITSVLTAASEGPLKGILAINDLPLVSSDFNHNPASSIFEAPSTYVVDGDFVKVLSWYDN 318
Cdd:PLN02358 241 TVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDN 320
|
330
....*....|....*...
gi 522053463 319 EWGFSNRMLDTTVALVNA 336
Cdd:PLN02358 321 EWGYSSRVVDLIVHMSKA 338
|
|
| GAPDH_I_N |
cd05214 |
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
3-154 |
2.65e-86 |
|
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: 256.94 E-value: 2.65e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 3 IKIAINGYGRIGRNVIRALYESgrtNEIKVVAINDLGDSKTNAHLTQYDTVHGKFPFDVAVDGDYIVINGDRIRVLSERD 82
Cdd:cd05214 1 IKVGINGFGRIGRLVFRAALER---DDIEVVAINDLTDDETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERD 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522053463 83 PSKLPWGELGIDVVHECTGLFTSKAKASAHLTAGAKKVIISAPGGNDvDATIVYGVNHNTLKASDTVISNAS 154
Cdd:cd05214 78 PAELPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDD-DPTIVMGVNHDKYDADDKIISNAS 148
|
|
| GAPDH_N_E4PDH |
cd17892 |
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
3-154 |
3.71e-86 |
|
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: 256.81 E-value: 3.71e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 3 IKIAINGYGRIGRNVIRALYESGRTNEIKVVAINDLGDSKTNAHLTQYDTVHGKFPFDVAVDGDYIVINGDRIRVLSERD 82
Cdd:cd17892 1 YRVAINGYGRIGRNVLRALYESGRRAEFQVVAINELADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 522053463 83 PSKLPWGELGIDVVHECTGLFTSKAKASAHLTAGAKKVIISAPGGNDVDATIVYGVNHNTLKASDTVISNAS 154
Cdd:cd17892 81 PENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASNDVDATIVYGINQDLLRAEHRIVSNAS 152
|
|
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
9-324 |
3.16e-84 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 262.55 E-value: 3.16e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 9 GYGRIGRNVIRALYE-SGRTNEIKVVAI----NDLGDSKTNAHLTQYDTVHGKFPFDVAVDGD--YIVINGDRIRVLSER 81
Cdd:PRK08289 134 GFGRIGRLLARLLIEkTGGGNGLRLRAIvvrkGSEGDLEKRASLLRRDSVHGPFNGTITVDEEnnAIIANGNYIQVIYAN 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 82 DPSKLPWGELGID--VVHECTGLFTSKAKASAHLTA-GAKKVIISAPGGNDVdATIVYGVNHNTLKASDTVISNASCTTN 158
Cdd:PRK08289 214 SPEEVDYTAYGINnaLVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGKGDI-KNIVHGVNHSDITDEDKIVSAASCTTN 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 159 CLAPLVKPLHDAIGIEHGLMTTIHSYTNDQVLTDVYHSDLRRARSATQSMIPTKTGAAAAVGLVLPELKGKLDGFAMRVP 238
Cdd:PRK08289 293 AITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKGDRRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNAIRVP 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 239 TINVSVVDLVFKAKRPTSKEEITSVLTAAS-EGPLKG-ILAINDLPLVSSDFNHNPASSIFEAPSTyVVDGDFVKVLSWY 316
Cdd:PRK08289 373 TPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNqIDYTDSTEVVSSDFVGSRHAGVVDSQAT-IVNGNRAVLYVWY 451
|
....*...
gi 522053463 317 DNEWGFSN 324
Cdd:PRK08289 452 DNEFGYSC 459
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-155 |
2.29e-83 |
|
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: 249.01 E-value: 2.29e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 3 IKIAINGYGRIGRNVIRALYESgrtNEIKVVAINDLGDSKTNAHLTQYDTVHGKFPFDVAVDGDYIVINGDRIRVLSERD 82
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALER---PDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERD 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 522053463 83 PSKLPWGELGIDVVHECTGLFTSKAKASAHLTAGAKKVIISAPgGNDVDATIVYGVNHNTLKASDTVISNASC 155
Cdd:smart00846 78 PANLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAP-SKDADPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
160-316 |
4.49e-80 |
|
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. C-terminal domain is a mixed alpha/antiparallel beta fold.
Pssm-ID: 460700 Cd Length: 158 Bit Score: 240.96 E-value: 4.49e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 160 LAPLVKPLHDAIGIEHGLMTTIHSYTNDQVLTD-VYHSDLRRARSATQSMIPTKTGAAAAVGLVLPELKGKLDGFAMRVP 238
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDgPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 522053463 239 TINVSVVDLVFKAKRPTSKEEITSVLTAASEGPLKGILAINDLPLVSSDFNHNPASSIFEAPSTYVVDGDFVKVLSWY 316
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
155-319 |
5.89e-66 |
|
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: 205.34 E-value: 5.89e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 155 CTTNCLAPLVKPLHDAIGIEHGLMTTIHSYTNDQVLTDVYHSDLRRARSATQSMIPTKTGAAAAVGLVLPELKGKLDGFA 234
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 235 MRVPTINVSVVDLVFKAKRPTSKEEITSVLTAASEGPLKGILAINDLPLVSSDFNHNPASSIFEAPSTYVVDGDFVKVLS 314
Cdd:cd23937 81 VRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLLV 160
|
....*
gi 522053463 315 WYDNE 319
Cdd:cd23937 161 WCDNE 165
|
|
| Gp_dh_N |
pfam00044 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-106 |
8.62e-55 |
|
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: 174.21 E-value: 8.62e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 3 IKIAINGYGRIGRNVIRALYESgrtNEIKVVAINDLGDSKTNAHLTQYDTVHGKFPFDVAVDGDYIVINGDRIRVLSERD 82
Cdd:pfam00044 1 VKVGINGFGRIGRLVLRAALER---PDIEVVAINDLTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERD 77
|
90 100
....*....|....*....|....
gi 522053463 83 PSKLPWGELGIDVVHECTGLFTSK 106
Cdd:pfam00044 78 PAELPWGDLGVDVVIESTGVFTTK 101
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
155-319 |
4.69e-48 |
|
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: 159.32 E-value: 4.69e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 155 CTTNCLAPLVKPLHDAIGIEHGLMTTIHSYTNDQVLTD-VYHSDLRRARSATQSMIPTKTGAAAAVGLVLPELKGKLDGF 233
Cdd:cd18123 1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDgPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 234 AMRVPTINVSVVDLVFKAKRPTSKEEITSVLTAASEGplKGILAINDLPLVSSDFNHNPASSIFEAPSTYVVDGDFVKVL 313
Cdd:cd18123 81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLM 158
|
....*.
gi 522053463 314 SWYDNE 319
Cdd:cd18123 159 QWYDNE 164
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-336 |
2.03e-47 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 163.12 E-value: 2.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 1 MAIKIAINGYGRIGRNViraLYESGRTNEIKVVAINDLGDSKTN-AHLTQYDTVH---GKFPfdVAVDGDYIVING-DRI 75
Cdd:PTZ00353 1 LPITVGINGFGPVGKAV---LFASLTDPLVTVVAVNDASVSIAYiAYVLEQESPLsapDGAS--IRVVGEQIVLNGtQKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 76 RVLSERDPSKLPWGELGIDVVHECTGLFTSKAKASAHLTAGAKKVIISAPGGndvDA-TIVYGVNHNTLKASDTVISNAS 154
Cdd:PTZ00353 76 RVSAKHDLVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSA---DApTVMAGSNDERLSASLPVCCAGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 155 CTTNCLAPLVKPLHDAIGIEHGLMTTIHSyTNDQVLTDVYHS---DLRRARSATQSMIPTKTGAAAAVGLVLPELKGKLD 231
Cdd:PTZ00353 153 PIAVALAPVIRALHEVYGVEECSYTAIHG-MQPQEPIAARSKnsqDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRIS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 232 GFAMRVPTINVSVVDLVFKAKRPTSKEEITSVLTAASEGPLKGILAINDLPLVSSDFNHNpASSIFEAPSTY-VVDGDFV 310
Cdd:PTZ00353 232 GSAFQVPVKKGCAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCIPN-GKLCYDATSSSsSREGEVH 310
|
330 340
....*....|....*....|....*.
gi 522053463 311 KVLSWYDNEWGFSNRMLdTTVALVNA 336
Cdd:PTZ00353 311 KMVLWFDVECYYAARLL-SLVKQLHQ 335
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
155-319 |
4.20e-25 |
|
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: 99.13 E-value: 4.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 155 CTTNCLAPLVKPLHDAIGIEHGLMTTIHSYTNDQVLTDVYHsDLRRARSATQSMIPTKTGAAAAVGLVLPEL--KGKLDG 232
Cdd:cd18122 1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPI-LKSEVRAIIPNIPKNETKHAPETGKVLGEIgkPIKVDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 233 FAMRVPTINVSVVDLVFKAKRPTSKEEITSVLTAASEGPLKGILAINDLPLVSSDFNHNPASSIFEAPSTYVVDGDFVKV 312
Cdd:cd18122 80 IAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLKV 159
|
....*..
gi 522053463 313 LSWYDNE 319
Cdd:cd18122 160 FSAVDNE 166
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| GAPDH-like_N |
cd05192 |
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ... |
3-159 |
3.39e-14 |
|
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: 67.76 E-value: 3.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 522053463 3 IKIAINGYGRIGRNVIRALYESgrtNEIKVVAINDLGDsktnahltqydtvhgkfpfdvavdgdyivingdrirvlserd 82
Cdd:cd05192 1 IRVAINGFGRIGRIVFRAIADQ---DDLDVVAINDRRD------------------------------------------ 35
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 522053463 83 psklpwgelgidVVHECTGLFTSKAKASAHLTAGAKKVIISAPGGNDvDATIVYGVNHNTLKASDTVISNASCTTNC 159
Cdd:cd05192 36 ------------VVIECTGSFTDDDNAEKHIKAGGKKAVITAPEKGD-IPTIVVVLNELAKSAGATVVSNANETSYS 99
|
|
| Asd |
COG0136 |
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ... |
134-175 |
8.65e-03 |
|
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; Aspartate-semialdehyde dehydrogenase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439906 [Multi-domain] Cd Length: 333 Bit Score: 37.70 E-value: 8.65e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 522053463 134 IVYGVNHNTLKA--SDTVISNASCTTNCLAPLVKPLHDAIGIEH 175
Cdd:COG0136 105 VVPEVNPEALADhlPKGIIANPNCSTIQMLVALKPLHDAAGIKR 148
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