|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
2-337 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 676.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 2 AVTKLGINGFGRIGRLVFRAAFGRKDIEVVAINDPFMDLNHLCYLLKYDSVHGQFPCEVTHADGFLLIGEKKVSVFAEKD 81
Cdd:PTZ00023 1 MVVKLGINGFGRIGRLVFRAALEREDVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 82 PSQIPWGKCQVDVVCESTGVFLTKELASSHLKGGAKKVIMSAPPKDDTPIYVMGINHHQYDTKQLIVSNASCTTNCLAPL 161
Cdd:PTZ00023 81 PAAIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKDDTPIYVMGVNHTQYDKSQRIVSNASCTTNCLAPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 162 AKVINDRFGIVEGLMTTVHASTANQLVVDGPSKGGKDWRAGRCALSNIIPASTGAAKAVGKVLPELNGKLTGVAFRVPIG 241
Cdd:PTZ00023 161 AKVVNDKFGIVEGLMTTVHASTANQLTVDGPSKGGKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 242 TVSVVDLVCRLQKPAKYEEVALEIKKAAEGPLKGILGYTEDEVVSQDFVHDNRSSIFDMKAGLALNDNFFKLVSWYDNEW 321
Cdd:PTZ00023 241 DVSVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDNEW 320
|
330
....*....|....*.
gi 124810131 322 GYSNRVLDLAVHITNN 337
Cdd:PTZ00023 321 GYSNRLLDLAHYITQK 336
|
|
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
1-336 |
0e+00 |
|
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]; Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 439827 [Multi-domain] Cd Length: 334 Bit Score: 580.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 1 MAVtKLGINGFGRIGRLVFRAAFGR-KDIEVVAINDPfMDLNHLCYLLKYDSVHGQFPCEVTHADGFLLIGEKKVSVFAE 79
Cdd:COG0057 1 MTI-RVAINGFGRIGRLVLRALLERgPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 80 KDPSQIPWGKCQVDVVCESTGVFLTKELASSHLKGGAKKVIMSAPPKDDTPIYVMGINHHQYDTKQLIVSNASCTTNCLA 159
Cdd:COG0057 79 RDPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDDPTIVYGVNHDDYDADHRIISNASCTTNCLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 160 PLAKVINDRFGIVEGLMTTVHASTANQLVVDGPskgGKDWRAGRCALSNIIPASTGAAKAVGKVLPELNGKLTGVAFRVP 239
Cdd:COG0057 159 PVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP---HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 240 IGTVSVVDLVCRLQKPAKYEEVALEIKKAAEGPLKGILGYTEDEVVSQDFVHDNRSSIFDMKAGLALNDNFFKLVSWYDN 319
Cdd:COG0057 236 TPNVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDN 315
|
330
....*....|....*..
gi 124810131 320 EWGYSNRVLDLAVHITN 336
Cdd:COG0057 316 EWGYSNRMVDLAEYMAK 332
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
5-329 |
3.86e-172 |
|
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: 481.01 E-value: 3.86e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 5 KLGINGFGRIGRLVFRAAFGRKD--IEVVAINDPfMDLNHLCYLLKYDSVHGQFPCEVTHADGFLLI-GEKKVSVFAEKD 81
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKPGndLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVnGKEVISVFSERD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 82 PSQIPWGKCQVDVVCESTGVFLTKELASSHLKGGAKKVIMSAPPKDDTPIYVMGINHHQYDTKQLIVSNASCTTNCLAPL 161
Cdd:TIGR01534 80 PSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDVKTIVYGVNHDEYDGEERIISNASCTTNCLAPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 162 AKVINDRFGIVEGLMTTVHASTANQLVVDGPskgGKDWRAGRCALSNIIPASTGAAKAVGKVLPELNGKLTGVAFRVPIG 241
Cdd:TIGR01534 160 AKVLDEAFGIVSGLMTTVHAYTNDQNLLDGP---HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 242 TVSVVDLVCRLQKPAKYEEVALEIKKAAEGPLKGILGYTEDEVVSQDFVHDNRSSIFDMKAGLA--LNDNFFKLVSWYDN 319
Cdd:TIGR01534 237 NVSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDN 316
|
330
....*....|
gi 124810131 320 EWGYSNRVLD 329
Cdd:TIGR01534 317 EWGYSNRLVD 326
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
7-331 |
7.93e-130 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 373.50 E-value: 7.93e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 7 GINGFGRIGRLVFRAAFGRKDIEVVAINDPFMDLNHLCYLLKYDSVHGQFPCEVTHADGFLLIGEKKVSVFAEKDPSQIP 86
Cdd:NF033735 2 GINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 87 WGKcQVDVVCESTGVFLTKELASSHLKGGAKKVIMSAPPKDDTPI-YVMGINHHQYDTKQ-LIVSNASCTTNCLAPLAKV 164
Cdd:NF033735 82 WGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLnIVYGVNDHLYDPARhRIVTAASCTTNCLAPVVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 165 INDRFGIVEGLMTTVHASTANQLVVDGPSKggkDWRAGRCALSNIIPASTGAAKAVGKVLPELNGKLTGVAFRVPIGTVS 244
Cdd:NF033735 161 IHEKIGIKHGSITTIHDITNTQTIVDAPHK---DLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNAS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 245 VVDLVCRLQKPAKYEEVALEIKKAAEGPLKGILGYTEDEVVSQDFVHDNRSSIFDMKAGLALNDNFFKLVSWYDNEWGYS 324
Cdd:NF033735 238 LTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYA 317
|
....*..
gi 124810131 325 NRVLDLA 331
Cdd:NF033735 318 NRMVDLA 324
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
153-320 |
2.31e-114 |
|
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: 328.26 E-value: 2.31e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 153 CTTNCLAPLAKVINDRFGIVEGLMTTVHASTANQLVVDGPSKggkDWRAGRCALSNIIPASTGAAKAVGKVLPELNGKLT 232
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHK---DLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 233 GVAFRVPIGTVSVVDLVCRLQKPAKYEEVALEIKKAAEGPLKGILGYTEDEVVSQDFVHDNRSSIFDMKAGLALNDNFFK 312
Cdd:cd18126 78 GMAFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVK 157
|
....*...
gi 124810131 313 LVSWYDNE 320
Cdd:cd18126 158 VVAWYDNE 165
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
158-317 |
1.50e-87 |
|
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: 259.83 E-value: 1.50e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 158 LAPLAKVINDRFGIVEGLMTTVHASTANQLVVDGPSKggKDWRAGRCALSNIIPASTGAAKAVGKVLPELNGKLTGVAFR 237
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHH--KDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 238 VPIGTVSVVDLVCRLQKPAKYEEVALEIKKAAEGPLKGILGYTEDEVVSQDFVHDNRSSIFDMKAGLALNDNFFKLVSWY 317
Cdd:pfam02800 79 VPTPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
4-153 |
1.21e-78 |
|
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: 237.06 E-value: 1.21e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 4 TKLGINGFGRIGRLVFRAAFGRKDIEVVAINDPfMDLNHLCYLLKYDSVHGQFPCEVTHADGFLLIGEKKVSVFAEKDPS 83
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 84 QIPWGKCQVDVVCESTGVFLTKELASSHLKGGAKKVIMSAPPKDDTPIYVMGINHHQYDTKQLIVSNASC 153
Cdd:smart00846 80 NLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDADPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
2-337 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 676.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 2 AVTKLGINGFGRIGRLVFRAAFGRKDIEVVAINDPFMDLNHLCYLLKYDSVHGQFPCEVTHADGFLLIGEKKVSVFAEKD 81
Cdd:PTZ00023 1 MVVKLGINGFGRIGRLVFRAALEREDVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 82 PSQIPWGKCQVDVVCESTGVFLTKELASSHLKGGAKKVIMSAPPKDDTPIYVMGINHHQYDTKQLIVSNASCTTNCLAPL 161
Cdd:PTZ00023 81 PAAIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKDDTPIYVMGVNHTQYDKSQRIVSNASCTTNCLAPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 162 AKVINDRFGIVEGLMTTVHASTANQLVVDGPSKGGKDWRAGRCALSNIIPASTGAAKAVGKVLPELNGKLTGVAFRVPIG 241
Cdd:PTZ00023 161 AKVVNDKFGIVEGLMTTVHASTANQLTVDGPSKGGKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 242 TVSVVDLVCRLQKPAKYEEVALEIKKAAEGPLKGILGYTEDEVVSQDFVHDNRSSIFDMKAGLALNDNFFKLVSWYDNEW 321
Cdd:PTZ00023 241 DVSVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDNEW 320
|
330
....*....|....*.
gi 124810131 322 GYSNRVLDLAVHITNN 337
Cdd:PTZ00023 321 GYSNRLLDLAHYITQK 336
|
|
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
1-336 |
0e+00 |
|
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]; Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 439827 [Multi-domain] Cd Length: 334 Bit Score: 580.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 1 MAVtKLGINGFGRIGRLVFRAAFGR-KDIEVVAINDPfMDLNHLCYLLKYDSVHGQFPCEVTHADGFLLIGEKKVSVFAE 79
Cdd:COG0057 1 MTI-RVAINGFGRIGRLVLRALLERgPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 80 KDPSQIPWGKCQVDVVCESTGVFLTKELASSHLKGGAKKVIMSAPPKDDTPIYVMGINHHQYDTKQLIVSNASCTTNCLA 159
Cdd:COG0057 79 RDPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDDPTIVYGVNHDDYDADHRIISNASCTTNCLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 160 PLAKVINDRFGIVEGLMTTVHASTANQLVVDGPskgGKDWRAGRCALSNIIPASTGAAKAVGKVLPELNGKLTGVAFRVP 239
Cdd:COG0057 159 PVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP---HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 240 IGTVSVVDLVCRLQKPAKYEEVALEIKKAAEGPLKGILGYTEDEVVSQDFVHDNRSSIFDMKAGLALNDNFFKLVSWYDN 319
Cdd:COG0057 236 TPNVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDN 315
|
330
....*....|....*..
gi 124810131 320 EWGYSNRVLDLAVHITN 336
Cdd:COG0057 316 EWGYSNRMVDLAEYMAK 332
|
|
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
4-334 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 537.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 4 TKLGINGFGRIGRLVFRAAFGRKDIEVVAINDPFMDLNHLCYLLKYDSVHGQFPCEVTHAD-GFLLIGEKKVSVFAEKDP 82
Cdd:PLN02272 86 TKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVVDdSTLEINGKQIKVTSKRDP 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 83 SQIPWGKCQVDVVCESTGVFLTKELASSHLKGGAKKVIMSAPPKDdTPIYVMGINHHQYDTKQLIVSNASCTTNCLAPLA 162
Cdd:PLN02272 166 AEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSAD-APMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 163 KVINDRFGIVEGLMTTVHASTANQLVVDGPSkgGKDWRAGRCALSNIIPASTGAAKAVGKVLPELNGKLTGVAFRVPIGT 242
Cdd:PLN02272 245 KVVHEEFGILEGLMTTVHATTATQKTVDGPS--MKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPN 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 243 VSVVDLVCRLQKPAKYEEVALEIKKAAEGPLKGILGYTEDEVVSQDFVHDNRSSIFDMKAGLALNDNFFKLVSWYDNEWG 322
Cdd:PLN02272 323 VSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWG 402
|
330
....*....|..
gi 124810131 323 YSNRVLDLAVHI 334
Cdd:PLN02272 403 YSNRVLDLIEHM 414
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
5-329 |
3.86e-172 |
|
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: 481.01 E-value: 3.86e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 5 KLGINGFGRIGRLVFRAAFGRKD--IEVVAINDPfMDLNHLCYLLKYDSVHGQFPCEVTHADGFLLI-GEKKVSVFAEKD 81
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKPGndLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVnGKEVISVFSERD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 82 PSQIPWGKCQVDVVCESTGVFLTKELASSHLKGGAKKVIMSAPPKDDTPIYVMGINHHQYDTKQLIVSNASCTTNCLAPL 161
Cdd:TIGR01534 80 PSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDVKTIVYGVNHDEYDGEERIISNASCTTNCLAPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 162 AKVINDRFGIVEGLMTTVHASTANQLVVDGPskgGKDWRAGRCALSNIIPASTGAAKAVGKVLPELNGKLTGVAFRVPIG 241
Cdd:TIGR01534 160 AKVLDEAFGIVSGLMTTVHAYTNDQNLLDGP---HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 242 TVSVVDLVCRLQKPAKYEEVALEIKKAAEGPLKGILGYTEDEVVSQDFVHDNRSSIFDMKAGLA--LNDNFFKLVSWYDN 319
Cdd:TIGR01534 237 NVSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDN 316
|
330
....*....|
gi 124810131 320 EWGYSNRVLD 329
Cdd:TIGR01534 317 EWGYSNRLVD 326
|
|
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
5-335 |
6.71e-155 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 437.61 E-value: 6.71e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 5 KLGINGFGRIGRLVFRAAFGRKDIEVVAINDPFMDLNHLCYLLKYDSVHGQFP-CEVTHAD-GFLLIGEKKVSVFAEKDP 82
Cdd:PLN02358 7 RIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKhHELKVKDdKTLLFGEKPVTVFGIRNP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 83 SQIPWGKCQVDVVCESTGVFLTKELASSHLKGGAKKVIMSAPPKDdTPIYVMGINHHQYDTKQLIVSNASCTTNCLAPLA 162
Cdd:PLN02358 87 EDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKD-APMFVVGVNEHEYKSDLDIVSNASCTTNCLAPLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 163 KVINDRFGIVEGLMTTVHASTANQLVVDGPSKggKDWRAGRCALSNIIPASTGAAKAVGKVLPELNGKLTGVAFRVPIGT 242
Cdd:PLN02358 166 KVINDRFGIVEGLMTTVHSITATQKTVDGPSM--KDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 243 VSVVDLVCRLQKPAKYEEVALEIKKAAEGPLKGILGYTEDEVVSQDFVHDNRSSIFDMKAGLALNDNFFKLVSWYDNEWG 322
Cdd:PLN02358 244 VSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEWG 323
|
330
....*....|...
gi 124810131 323 YSNRVLDLAVHIT 335
Cdd:PLN02358 324 YSSRVVDLIVHMS 336
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
5-335 |
3.46e-153 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 433.01 E-value: 3.46e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 5 KLGINGFGRIGRLVFRAAFGRKDIEVVAINDpFMDLNHLCYLLKYDSVHGQFPCEVTHADGFLLIGEKKVSVFAEKDPSQ 84
Cdd:PRK15425 4 KVGINGFGRIGRIVFRAAQKRSDIEIVAIND-LLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPAN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 85 IPWGKCQVDVVCESTGVFLTKELASSHLKGGAKKVIMSAPPKDDTPIYVMGINHHQYdTKQLIVSNASCTTNCLAPLAKV 164
Cdd:PRK15425 83 LKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDNTPMFVKGANFDKY-AGQDIVSNASCTTNCLAPLAKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 165 INDRFGIVEGLMTTVHASTANQLVVDGPSKggKDWRAGRCALSNIIPASTGAAKAVGKVLPELNGKLTGVAFRVPIGTVS 244
Cdd:PRK15425 162 INDNFGIIEGLMTTVHATTATQKTVDGPSH--KDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 245 VVDLVCRLQKPAKYEEVALEIKKAAEGPLKGILGYTEDEVVSQDFVHDNRSSIFDMKAGLALNDNFFKLVSWYDNEWGYS 324
Cdd:PRK15425 240 VVDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYS 319
|
330
....*....|.
gi 124810131 325 NRVLDLAVHIT 335
Cdd:PRK15425 320 NKVLDLIAHIS 330
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
4-336 |
8.41e-138 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 394.49 E-value: 8.41e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 4 TKLGINGFGRIGRLVFRAAFGRKDIEVVAIND--PFMDLNHLcylLKYDSVHGQFPCEVTHADGFLLIGEKKVSVFAEKD 81
Cdd:PRK07729 3 TKVAINGFGRIGRMVFRKAIKESAFEIVAINAsyPSETLAHL---IKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 82 PSQIPWGKCQVDVVCESTGVFLTKELASSHLKGGAKKVIMSAPPKDDTPIYVMGINHHQYD-TKQLIVSNASCTTNCLAP 160
Cdd:PRK07729 80 PKELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVTIVVGVNEDQLDiEKHTIISNASCTTNCLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 161 LAKVINDRFGIVEGLMTTVHASTANQLVVDGPSKggkDWRAGRCALSNIIPASTGAAKAVGKVLPELNGKLTGVAFRVPI 240
Cdd:PRK07729 160 VVKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHK---DLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 241 GTVSVVDLVCRLQKPAKYEEVALEIKKAAEGPLKGILGYTEDEVVSQDFVHDNRSSIFDMKAGLALNDNFFKLVSWYDNE 320
Cdd:PRK07729 237 PNVSLVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNE 316
|
330
....*....|....*.
gi 124810131 321 WGYSNRVLDLAVHITN 336
Cdd:PRK07729 317 WGYSCRVVDLVTLVAD 332
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
1-334 |
1.04e-131 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 379.79 E-value: 1.04e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 1 MAVTKLGINGFGRIGRLVFRAAFGR----KDIEVVAINDPFMDLNHLCYLLKYDSVHGQFPCEVTHA---------DGFL 67
Cdd:PTZ00434 1 MAPIKVGINGFGRIGRMVFQAICDQgligTEIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVETTksspsvktdDVLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 68 LIGEKKVSVFAEKDPSQIPWGKCQVDVVCESTGVFLTKELASSHLKGGAKKVIMSAPPKDDTPIYVMGINHHQYD-TKQL 146
Cdd:PTZ00434 81 VNGHRIKCVKAQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPASGGAKTIVMGVNQHEYSpTEHH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 147 IVSNASCTTNCLAPLAKVI-NDRFGIVEGLMTTVHASTANQLVVDGPSKggKDWRAGRCALSNIIPASTGAAKAVGKVLP 225
Cdd:PTZ00434 161 VVSNASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSV--KDWRGGRAAAVNIIPSTTGAAKAVGMVIP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 226 ELNGKLTGVAFRVPIGTVSVVDLVCRLQKPAKYEEVALEIKKAAEGPLKGILGYTEDEVVSQDFVHDNRSSIFDMKAGLA 305
Cdd:PTZ00434 239 STKGKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKATLQ 318
|
330 340 350
....*....|....*....|....*....|...
gi 124810131 306 LN----DNFFKLVSWYDNEWGYSNRVLDLAVHI 334
Cdd:PTZ00434 319 NNlpgeRRFFKIVSWYDNEWGYSHRVVDLVRYM 351
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
7-331 |
7.93e-130 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 373.50 E-value: 7.93e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 7 GINGFGRIGRLVFRAAFGRKDIEVVAINDPFMDLNHLCYLLKYDSVHGQFPCEVTHADGFLLIGEKKVSVFAEKDPSQIP 86
Cdd:NF033735 2 GINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDTP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 87 WGKcQVDVVCESTGVFLTKELASSHLKGGAKKVIMSAPPKDDTPI-YVMGINHHQYDTKQ-LIVSNASCTTNCLAPLAKV 164
Cdd:NF033735 82 WGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLnIVYGVNDHLYDPARhRIVTAASCTTNCLAPVVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 165 INDRFGIVEGLMTTVHASTANQLVVDGPSKggkDWRAGRCALSNIIPASTGAAKAVGKVLPELNGKLTGVAFRVPIGTVS 244
Cdd:NF033735 161 IHEKIGIKHGSITTIHDITNTQTIVDAPHK---DLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNAS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 245 VVDLVCRLQKPAKYEEVALEIKKAAEGPLKGILGYTEDEVVSQDFVHDNRSSIFDMKAGLALNDNFFKLVSWYDNEWGYS 324
Cdd:NF033735 238 LTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYA 317
|
....*..
gi 124810131 325 NRVLDLA 331
Cdd:NF033735 318 NRMVDLA 324
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
3-331 |
3.11e-119 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 347.28 E-value: 3.11e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 3 VTKLGINGFGRIGRLVFRAAFGRKD--IEVVAINDPfMDLNHLCYLLKYDSVHGQFPCEVTHADGFLLIGEKKVSVFAEK 80
Cdd:PRK07403 1 MIRVAINGFGRIGRNFLRCWLGRENsqLELVAINDT-SDPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 81 DPSQIPWGKCQVDVVCESTGVFLTKELASSHLKGGAKKVIMSAPPK-DDTPIYVMGINHHQYD-TKQLIVSNASCTTNCL 158
Cdd:PRK07403 80 NPLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPGKgEDIGTYVVGVNHHEYDhEDHNIISNASCTTNCL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 159 APLAKVINDRFGIVEGLMTTVHASTANQLVVDGPSKggkDWRAGRCALSNIIPASTGAAKAVGKVLPELNGKLTGVAFRV 238
Cdd:PRK07403 160 APIAKVLHDNFGIIKGTMTTTHSYTGDQRILDASHR---DLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 239 PIGTVSVVDLVCRLQKPAKYEEVALEIKKAAEGPLKGILGYTEDEVVSQDFVHDNRSSIFDMKAGLALNDNFFKLVSWYD 318
Cdd:PRK07403 237 PTPNVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYD 316
|
330
....*....|...
gi 124810131 319 NEWGYSNRVLDLA 331
Cdd:PRK07403 317 NEWGYSQRVVDLA 329
|
|
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
5-331 |
9.80e-115 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 335.55 E-value: 9.80e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 5 KLGINGFGRIGRLVFRAAFGRKDIEVVAINDPFMDLNHLCYLLKYDSVHGQFPCEVTHADGFLLIGEKKVSVFAEKDPSQ 84
Cdd:PRK08955 4 KVGINGFGRIGRLALRAAWDWPELEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKAIAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 85 IPWGKCqvDVVCESTGVFLTKELASSHLKGGAKKVIMSAPPKDDTPI-YVMGINHHQYD-TKQLIVSNASCTTNCLAPLA 162
Cdd:PRK08955 84 TDWSGC--DVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLnIVMGVNDHLFDpAIHPIVTAASCTTNCLAPVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 163 KVINDRFGIVEGLMTTVHASTANQLVVDGPSKggkDWRAGR-CALSnIIPASTGAAKAVGKVLPELNGKLTGVAFRVPIG 241
Cdd:PRK08955 162 KVIHEKLGIKHGSMTTIHDLTNTQTILDAPHK---DLRRARaCGMS-LIPTTTGSATAITEIFPELKGKLNGHAVRVPLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 242 TVSVVDLVCRLQKPAKYEEVALEIKKAAEGPLKGILGYTEDEVVSQDFVHDNRSSIFDMKAGLALNDNFFKLVSWYDNEW 321
Cdd:PRK08955 238 NASLTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNEW 317
|
330
....*....|
gi 124810131 322 GYSNRVLDLA 331
Cdd:PRK08955 318 GYANRTAELA 327
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
153-320 |
2.31e-114 |
|
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: 328.26 E-value: 2.31e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 153 CTTNCLAPLAKVINDRFGIVEGLMTTVHASTANQLVVDGPSKggkDWRAGRCALSNIIPASTGAAKAVGKVLPELNGKLT 232
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHK---DLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 233 GVAFRVPIGTVSVVDLVCRLQKPAKYEEVALEIKKAAEGPLKGILGYTEDEVVSQDFVHDNRSSIFDMKAGLALNDNFFK 312
Cdd:cd18126 78 GMAFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVK 157
|
....*...
gi 124810131 313 LVSWYDNE 320
Cdd:cd18126 158 VVAWYDNE 165
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
2-337 |
2.20e-111 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 329.20 E-value: 2.20e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 2 AVTKLGINGFGRIGRLVFRAAFGRKD--IEVVAINDPfMDLNHLCYLLKYDSVHGQFPCEVT-HADGFLLIGEKKVSVFA 78
Cdd:PLN03096 59 AKIKVAINGFGRIGRNFLRCWHGRKDspLDVVAINDT-GGVKQASHLLKYDSTLGTFDADVKpVGDDAISVDGKVIKVVS 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 79 EKDPSQIPWGKCQVDVVCESTGVFLTKELASSHLKGGAKKVIMSAPPKDDTPIYVMGINHHQYDTKQLIVSNASCTTNCL 158
Cdd:PLN03096 138 DRNPLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKGDIPTYVVGVNADDYKHSDPIISNASCTTNCL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 159 APLAKVINDRFGIVEGLMTTVHASTANQLVVDGPSkggKDWRAGRCALSNIIPASTGAAKAVGKVLPELNGKLTGVAFRV 238
Cdd:PLN03096 218 APFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASH---RDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 239 PIGTVSVVDLVCRLQKPAKYEEVALEIKKAAEGPLKGILGYTEDEVVSQDFVHDNRSSIFDMKAGLALNDNFFKLVSWYD 318
Cdd:PLN03096 295 PTPNVSVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAWYD 374
|
330
....*....|....*....
gi 124810131 319 NEWGYSNRVLDLAVHITNN 337
Cdd:PLN03096 375 NEWGYSQRVVDLADIVANK 393
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
2-337 |
5.04e-105 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 314.92 E-value: 5.04e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 2 AVTKLGINGFGRIGRLVFRAAFGRKD--IEVVAINDPfMDLNHLCYLLKYDSVHGQFPCEVTHADGFLL-IGEKKVSVFA 78
Cdd:PLN02237 74 AKLKVAINGFGRIGRNFLRCWHGRKDspLDVVVVNDS-GGVKNASHLLKYDSMLGTFKADVKIVDDETIsVDGKPIKVVS 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 79 EKDPSQIPWGKCQVDVVCESTGVFLTKELASSHLKGGAKKVIMSAPPK-DDTPIYVMGINHHQYDTKQL-IVSNASCTTN 156
Cdd:PLN02237 153 NRDPLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAKgADIPTYVVGVNEDDYDHEVAnIVSNASCTTN 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 157 CLAPLAKVINDRFGIVEGLMTTVHASTANQLVVDGPSKggkDWRAGRCALSNIIPASTGAAKAVGKVLPELNGKLTGVAF 236
Cdd:PLN02237 233 CLAPFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDASHR---DLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIAL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 237 RVPIGTVSVVDLVCRLQKPA-KYEEVALEIKKAAEGPLKGILGYTEDEVVSQDFVHDNRSSIFDMKAGLALNDNFFKLVS 315
Cdd:PLN02237 310 RVPTPNVSVVDLVVNVEKKGiTAEDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVA 389
|
330 340
....*....|....*....|..
gi 124810131 316 WYDNEWGYSNRVLDLAvHITNN 337
Cdd:PLN02237 390 WYDNEWGYSQRVVDLA-HLVAA 410
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
5-329 |
3.85e-100 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 298.51 E-value: 3.85e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 5 KLGINGFGRIGRLVFRAAF--GRKD-IEVVAINDpFMDLNHLCYLLKYDSVHGQFPCEVTHADGFLLIGEKKVSVFAEKD 81
Cdd:PRK13535 3 RVAINGFGRIGRNVLRALYesGRRAeITVVAINE-LADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 82 PSQIPWGKCQVDVVCESTGVFLTKELASSHLKGGAKKVIMSAPPKDD---TPIYvmGINHHQYDTKQLIVSNASCTTNCL 158
Cdd:PRK13535 82 IASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSNDldaTVVY--GVNHDQLRAEHRIVSNASCTTNCI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 159 APLAKVINDRFGIVEGLMTTVHASTANQLVVDGPSKggkDWRAGRCALSNIIPASTGAAKAVGKVLPELNGKLTGVAFRV 238
Cdd:PRK13535 160 IPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHP---DLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 239 PIGTVSVVDLVCRLQKPAKYEEVALEIKKAAEGPLKGILGYTEDEVVSQDFVHDNRSSIFDMKAGLALNDNFFKLVSWYD 318
Cdd:PRK13535 237 PTINVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCD 316
|
330
....*....|.
gi 124810131 319 NEWGYSNRVLD 329
Cdd:PRK13535 317 NEWGFANRMLD 327
|
|
| GAPDH_I_N |
cd05214 |
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
4-152 |
2.42e-89 |
|
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: 264.64 E-value: 2.42e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 4 TKLGINGFGRIGRLVFRAAFGRKDIEVVAINDPFMDlNHLCYLLKYDSVHGQFPCEVTHADGFLLIGEKKVSVFAEKDPS 83
Cdd:cd05214 1 IKVGINGFGRIGRLVFRAALERDDIEVVAINDLTDD-ETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPA 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124810131 84 QIPWGKCQVDVVCESTGVFLTKELASSHLKGGAKKVIMSAPPKDDTPIYVMGINHHQYDTKQLIVSNAS 152
Cdd:cd05214 80 ELPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDDDPTIVMGVNHDKYDADDKIISNAS 148
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
158-317 |
1.50e-87 |
|
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: 259.83 E-value: 1.50e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 158 LAPLAKVINDRFGIVEGLMTTVHASTANQLVVDGPSKggKDWRAGRCALSNIIPASTGAAKAVGKVLPELNGKLTGVAFR 237
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHH--KDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 238 VPIGTVSVVDLVCRLQKPAKYEEVALEIKKAAEGPLKGILGYTEDEVVSQDFVHDNRSSIFDMKAGLALNDNFFKLVSWY 317
Cdd:pfam02800 79 VPTPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
4-153 |
1.21e-78 |
|
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: 237.06 E-value: 1.21e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 4 TKLGINGFGRIGRLVFRAAFGRKDIEVVAINDPfMDLNHLCYLLKYDSVHGQFPCEVTHADGFLLIGEKKVSVFAEKDPS 83
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 84 QIPWGKCQVDVVCESTGVFLTKELASSHLKGGAKKVIMSAPPKDDTPIYVMGINHHQYDTKQLIVSNASC 153
Cdd:smart00846 80 NLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDADPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
153-320 |
3.38e-76 |
|
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: 231.35 E-value: 3.38e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 153 CTTNCLAPLAKVINDRFGIVEGLMTTVHASTANQLVVDGPSkgGKDWRAGRCALSNIIPASTGAAKAVGKVLPELNGKLT 232
Cdd:cd18123 1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPS--GKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 233 GVAFRVPIGTVSVVDLVCRLQKPAKYEEVALEIKKAAEGplKGILGYTEDEVVSQDFVHDNRSSIFDMKAGLALNDNFFK 312
Cdd:cd18123 79 GMAVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVK 156
|
....*...
gi 124810131 313 LVSWYDNE 320
Cdd:cd18123 157 LMQWYDNE 164
|
|
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
10-334 |
7.29e-73 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 232.89 E-value: 7.29e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 10 GFGRIGRLV---------------FRAAFGRKDIEvvaindpfMDLNHLCYLLKYDSVHGQF--PCEVTHADGFLLIGEK 72
Cdd:PRK08289 134 GFGRIGRLLarlliektgggnglrLRAIVVRKGSE--------GDLEKRASLLRRDSVHGPFngTITVDEENNAIIANGN 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 73 KVSVFAEKDPSQIPWGKCQVD--VVCESTGVFLTKELASSHLKG-GAKKVIMSAPPKDDTPIYVMGINHHQYDTKQLIVS 149
Cdd:PRK08289 206 YIQVIYANSPEEVDYTAYGINnaLVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGKGDIKNIVHGVNHSDITDEDKIVS 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 150 NASCTTNCLAPLAKVINDRFGIVEGLMTTVHASTANQLVVDGPSKGGkdwRAGRCALSNIIPASTGAAKAVGKVLPELNG 229
Cdd:PRK08289 286 AASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKGD---RRGRSAPLNMVITETGAAKAVAKALPELAG 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 230 KLTGVAFRVPIGTVSVVDLVCRLQKPAKYEEVALEIKKAA-EGPLKGILGYTED-EVVSQDFVHDNRSSIFDMKAGLAlN 307
Cdd:PRK08289 363 KLTGNAIRVPTPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQIDYTDStEVVSSDFVGSRHAGVVDSQATIV-N 441
|
330 340
....*....|....*....|....*..
gi 124810131 308 DNFFKLVSWYDNEWGYSNRVLDLAVHI 334
Cdd:PRK08289 442 GNRAVLYVWYDNEFGYSCQVVRVMEQM 468
|
|
| Gp_dh_N |
pfam00044 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
4-105 |
4.97e-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: 174.98 E-value: 4.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 4 TKLGINGFGRIGRLVFRAAFGRKDIEVVAINDpFMDLNHLCYLLKYDSVHGQFPCEVTHADGFLLIGEKKVSVFAEKDPS 83
Cdd:pfam00044 1 VKVGINGFGRIGRLVLRAALERPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPA 79
|
90 100
....*....|....*....|..
gi 124810131 84 QIPWGKCQVDVVCESTGVFLTK 105
Cdd:pfam00044 80 ELPWGDLGVDVVIESTGVFTTK 101
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-332 |
2.32e-51 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 173.52 E-value: 2.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 1 MAVTkLGINGFGRIGRLVFRAAFGRKDIEVVAINDPFMDLNHLCYLLKYDSVH---GQFPCEVThADGFLLIGEKKVSVF 77
Cdd:PTZ00353 1 LPIT-VGINGFGPVGKAVLFASLTDPLVTVVAVNDASVSIAYIAYVLEQESPLsapDGASIRVV-GEQIVLNGTQKIRVS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 78 AEKDPSQIPWGKCQVDVVCESTGVFLTKELASSHLKGGAKKVIMSAPPKDdTPIYVMGINHHQYDTKQLIVSNASCTTNC 157
Cdd:PTZ00353 79 AKHDLVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSAD-APTVMAGSNDERLSASLPVCCAGAPIAVA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 158 LAPLAKVINDRFGIVEGLMTTVHAsTANQLVVDGPSKGGKDWRAGRCALSNIIPASTGAAKAVGKVLPELNGKLTGVAFR 237
Cdd:PTZ00353 158 LAPVIRALHEVYGVEECSYTAIHG-MQPQEPIAARSKNSQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 238 VPIGTVSVVDLVCRLQKPAKYEEVALEIKKAAEGPLKGILGYTEDEVVSQDFVHDNRsSIFDMKAGLALND-NFFKLVSW 316
Cdd:PTZ00353 237 VPVKKGCAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCIPNGK-LCYDATSSSSSREgEVHKMVLW 315
|
330
....*....|....*.
gi 124810131 317 YDNEWGYSNRVLDLAV 332
Cdd:PTZ00353 316 FDVECYYAARLLSLVK 331
|
|
| GAPDH_N_E4PDH |
cd17892 |
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
5-152 |
1.13e-47 |
|
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: 158.20 E-value: 1.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 5 KLGINGFGRIGRLVFRAAF---GRKDIEVVAINDPfMDLNHLCYLLKYDSVHGQFPCEVTHADGFLLIGEKKVSVFAEKD 81
Cdd:cd17892 2 RVAINGYGRIGRNVLRALYesgRRAEFQVVAINEL-ADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124810131 82 PSQIPWGKCQVDVVCESTGVFLTKELASSHLKGGAKKVIMSAPPKDD---TPIYvmGINHHQYDTKQLIVSNAS 152
Cdd:cd17892 81 PENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASNDvdaTIVY--GINQDLLRAEHRIVSNAS 152
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
153-320 |
1.32e-47 |
|
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: 157.96 E-value: 1.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 153 CTTNCLAPLAKVINDRFGIVEGLMTTVHASTANQLVVDGPSKggkDWRAGRCALSNIIPASTGAAKAVGKVLPELNGKLT 232
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDAYHP---DLRRTRAASQSIIPVDTKLARGIERILPHLAGRFE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 233 GVAFRVPIGTVSVVDLVCRLQKPAKYEEVALEIKKAAEGPLKGILGYTEDEVVSQDFVHDNRSSIFDMKAGLALNDNFFK 312
Cdd:cd23937 78 AIAVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVK 157
|
....*...
gi 124810131 313 LVSWYDNE 320
Cdd:cd23937 158 LLVWCDNE 165
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
153-320 |
3.54e-38 |
|
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: 133.80 E-value: 3.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 153 CTTNCLAPLAKVINDRFGIVEGLMTTVHASTANQLVVDGPSKggKDWraGRCALSNIIPASTGAAKAVGKVLPELN--GK 230
Cdd:cd18122 1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPIL--KSE--VRAIIPNIPKNETKHAPETGKVLGEIGkpIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124810131 231 LTGVAFRVPIGTVSVVDLVCRLQKPAKYEEVALEIKKAAEGPLKGILGYTEDEVVSQDFVHDNRSSIFDMKAGLALNDNF 310
Cdd:cd18122 77 VDGIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNK 156
|
170
....*....|
gi 124810131 311 FKLVSWYDNE 320
Cdd:cd18122 157 LKVFSAVDNE 166
|
|
| GAPDH-like_N |
cd05192 |
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ... |
5-157 |
9.77e-16 |
|
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: 72.00 E-value: 9.77e-16
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gi 124810131 5 KLGINGFGRIGRLVFRAAFGRKDIEVVAINDpfmdlnhlcyllkydsvhgqfpcevthadgflligekkvsvfaekdpsq 84
Cdd:cd05192 2 RVAINGFGRIGRIVFRAIADQDDLDVVAIND------------------------------------------------- 32
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gi 124810131 85 ipwgkcQVDVVCESTGVFLTKELASSHLKGGAKKVIMSAPPKDDTPIYVMGINHHQYDTKQLIVSNASCTTNC 157
Cdd:cd05192 33 ------RRDVVIECTGSFTDDDNAEKHIKAGGKKAVITAPEKGDIPTIVVVLNELAKSAGATVVSNANETSYS 99
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