|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
2-328 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 580.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 2 SKIGINGFGRIGRLVLRAAVDKG-ASVVAVNDPFIDVNYMVYLFKFDSTHGRFKGTVSA-EGGFLVVNGQKITVFSERDP 79
Cdd:PLN02272 86 TKIGINGFGRIGRLVLRIATSRDdIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDP 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 80 ANINWASAGAEYVVESTGVFTTTEKASTHLKGGAKKVVISAPSADAPMFVCGVNLDAYSPDMKVVSNASCTTNCLAPLAK 159
Cdd:PLN02272 166 AEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLAK 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 160 VINDNFEIVEVLMTTVHATTATQKTVDGPSGKLWRDGRGACQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNVSV 239
Cdd:PLN02272 246 VVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSV 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 240 VDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFEPKAGISLNDKFVKLISWYDNEFGYSN 319
Cdd:PLN02272 326 VDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYSN 405
|
....*....
gi 232120 320 RVIDLIKYM 328
Cdd:PLN02272 406 RVLDLIEHM 414
|
|
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
1-332 |
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: 562.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 1 MS-KIGINGFGRIGRLVLRAAVDKGAS--VVAVNDPfIDVNYMVYLFKFDSTHGRFKGTVSAEGGFLVVNGQKITVFSER 77
Cdd:COG0057 1 MTiRVAINGFGRIGRLVLRALLERGPDieVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 78 DPANINWASAGAEYVVESTGVFTTTEKASTHLKGGAKKVVISAPSADA-PMFVCGVNLDAYSPDMKVVSNASCTTNCLAP 156
Cdd:COG0057 80 DPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 157 LAKVINDNFEIVEVLMTTVHATTATQKTVDGPSGKlWRDGRGACQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPN 236
Cdd:COG0057 160 VAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKD-LRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 237 VSVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFEPKAGISLNDKFVKLISWYDNEFG 316
Cdd:COG0057 239 VSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWG 318
|
330
....*....|....*.
gi 232120 317 YSNRVIDLIKYMQSKD 332
Cdd:COG0057 319 YSNRMVDLAEYMAKLL 334
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
3-323 |
3.48e-166 |
|
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: 465.60 E-value: 3.48e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 3 KIGINGFGRIGRLVLRAAVDKGAS---VVAVNDPfIDVNYMVYLFKFDSTHGRFKGTVSAEGGFLVVNGQKIT-VFSERD 78
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKPGNdleVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEVIsVFSERD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 79 PANINWASAGAEYVVESTGVFTTTEKASTHLKGGAKKVVISAPSADA-PMFVCGVNLDAYSPDMKVVSNASCTTNCLAPL 157
Cdd:TIGR01534 80 PSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLAPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 158 AKVINDNFEIVEVLMTTVHATTATQKTVDGPSGKlWRDGRGACQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNV 237
Cdd:TIGR01534 160 AKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKD-LRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 238 SVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFEPKAGI--SLNDKFVKLISWYDNEF 315
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKvtGLGDSLVKVYAWYDNEW 318
|
....*...
gi 232120 316 GYSNRVID 323
Cdd:TIGR01534 319 GYSNRLVD 326
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
149-314 |
1.04e-112 |
|
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: 323.64 E-value: 1.04e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 149 CTTNCLAPLAKVINDNFEIVEVLMTTVHATTATQKTVDGPSgKLWRDGRGACQNIIPASTGAAKAVGKVIPALNGKLTGM 228
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 229 AFRVPTPNVSVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFEPKAGISLNDKFVKLI 308
Cdd:cd18126 80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159
|
....*.
gi 232120 309 SWYDNE 314
Cdd:cd18126 160 AWYDNE 165
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
4-324 |
1.28e-108 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 319.57 E-value: 1.28e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 4 IGINGFGRIGRLVLRAAVDK-GASVVAVNDPFIDVNYMVYLFKFDSTHGRFKGTVSAEGGFLVVNGQKITVFSERDPANI 82
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRpGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 83 NWaSAGAEYVVESTGVFTTTEKASTHLKGGAKKVVISAP--SADAPMFVCGVNLDAYSPDM-KVVSNASCTTNCLAPLAK 159
Cdd:NF033735 81 PW-GDGVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARhRIVTAASCTTNCLAPVVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 160 VINDNFEIVEVLMTTVHATTATQKTVDGPSGKLwRDGRGACQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNVSV 239
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAPHKDL-RRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 240 VDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFEPKAGISLNDKFVKLISWYDNEFGYSN 319
Cdd:NF033735 239 TDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYAN 318
|
....*
gi 232120 320 RVIDL 324
Cdd:NF033735 319 RMVDL 323
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
154-311 |
4.50e-84 |
|
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: 250.97 E-value: 4.50e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 154 LAPLAKVINDNFEIVEVLMTTVHATTATQKTVDGPSGKLWRDGRGACQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVP 233
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 232120 234 TPNVSVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFEPKAGISLNDKFVKLISWY 311
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-149 |
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: 236.68 E-value: 1.21e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 3 KIGINGFGRIGRLVLRAAV-DKGASVVAVNDPfIDVNYMVYLFKFDSTHGRFKGTVSAEGGFLVVNGQKITVFSERDPAN 81
Cdd:smart00846 2 KVGINGFGRIGRLVLRAALeRPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPAN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 232120 82 INWASAGAEYVVESTGVFTTTEKASTHLKGGAKKVVISAPSADA-PMFVCGVNLDAYSPDMKVVSNASC 149
Cdd:smart00846 81 LPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
2-328 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 580.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 2 SKIGINGFGRIGRLVLRAAVDKG-ASVVAVNDPFIDVNYMVYLFKFDSTHGRFKGTVSA-EGGFLVVNGQKITVFSERDP 79
Cdd:PLN02272 86 TKIGINGFGRIGRLVLRIATSRDdIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDP 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 80 ANINWASAGAEYVVESTGVFTTTEKASTHLKGGAKKVVISAPSADAPMFVCGVNLDAYSPDMKVVSNASCTTNCLAPLAK 159
Cdd:PLN02272 166 AEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLAK 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 160 VINDNFEIVEVLMTTVHATTATQKTVDGPSGKLWRDGRGACQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNVSV 239
Cdd:PLN02272 246 VVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSV 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 240 VDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFEPKAGISLNDKFVKLISWYDNEFGYSN 319
Cdd:PLN02272 326 VDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYSN 405
|
....*....
gi 232120 320 RVIDLIKYM 328
Cdd:PLN02272 406 RVLDLIEHM 414
|
|
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
1-332 |
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: 562.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 1 MS-KIGINGFGRIGRLVLRAAVDKGAS--VVAVNDPfIDVNYMVYLFKFDSTHGRFKGTVSAEGGFLVVNGQKITVFSER 77
Cdd:COG0057 1 MTiRVAINGFGRIGRLVLRALLERGPDieVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 78 DPANINWASAGAEYVVESTGVFTTTEKASTHLKGGAKKVVISAPSADA-PMFVCGVNLDAYSPDMKVVSNASCTTNCLAP 156
Cdd:COG0057 80 DPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 157 LAKVINDNFEIVEVLMTTVHATTATQKTVDGPSGKlWRDGRGACQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPN 236
Cdd:COG0057 160 VAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKD-LRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 237 VSVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFEPKAGISLNDKFVKLISWYDNEFG 316
Cdd:COG0057 239 VSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWG 318
|
330
....*....|....*.
gi 232120 317 YSNRVIDLIKYMQSKD 332
Cdd:COG0057 319 YSNRMVDLAEYMAKLL 334
|
|
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
3-332 |
4.71e-174 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 485.88 E-value: 4.71e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 3 KIGINGFGRIGRLVLRAAVDKG-ASVVAVNDPFIDVNYMVYLFKFDSTHGRFKGTVSAEGGFLVVNGQKITVFSERDPAN 81
Cdd:PTZ00023 4 KLGINGFGRIGRLVFRAALEREdVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKDPAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 82 INWASAGAEYVVESTGVFTTTEKASTHLKGGAKKVVISAP-SADAPMFVCGVNLDAYSPDMKVVSNASCTTNCLAPLAKV 160
Cdd:PTZ00023 84 IPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPpKDDTPIYVMGVNHTQYDKSQRIVSNASCTTNCLAPLAKV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 161 INDNFEIVEVLMTTVHATTATQKTVDGPS--GKLWRDGRGACQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNVS 238
Cdd:PTZ00023 164 VNDKFGIVEGLMTTVHASTANQLTVDGPSkgGKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVPDVS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 239 VVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFEPKAGISLNDKFVKLISWYDNEFGYS 318
Cdd:PTZ00023 244 VVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDNEWGYS 323
|
330
....*....|....
gi 232120 319 NRVIDLIKYMQSKD 332
Cdd:PTZ00023 324 NRLLDLAHYITQKY 337
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
3-323 |
3.48e-166 |
|
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: 465.60 E-value: 3.48e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 3 KIGINGFGRIGRLVLRAAVDKGAS---VVAVNDPfIDVNYMVYLFKFDSTHGRFKGTVSAEGGFLVVNGQKIT-VFSERD 78
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKPGNdleVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEVIsVFSERD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 79 PANINWASAGAEYVVESTGVFTTTEKASTHLKGGAKKVVISAPSADA-PMFVCGVNLDAYSPDMKVVSNASCTTNCLAPL 157
Cdd:TIGR01534 80 PSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLAPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 158 AKVINDNFEIVEVLMTTVHATTATQKTVDGPSGKlWRDGRGACQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNV 237
Cdd:TIGR01534 160 AKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKD-LRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 238 SVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFEPKAGI--SLNDKFVKLISWYDNEF 315
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKvtGLGDSLVKVYAWYDNEW 318
|
....*...
gi 232120 316 GYSNRVID 323
Cdd:TIGR01534 319 GYSNRLVD 326
|
|
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
3-328 |
2.05e-153 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 433.76 E-value: 2.05e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 3 KIGINGFGRIGRLVLRAAVDKG-ASVVAVNDPFIDVNYMVYLFKFDSTHGRFK-GTVSAEGGFLVVNGQK-ITVFSERDP 79
Cdd:PLN02358 7 RIGINGFGRIGRLVARVVLQRDdVELVAVNDPFITTEYMTYMFKYDSVHGQWKhHELKVKDDKTLLFGEKpVTVFGIRNP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 80 ANINWASAGAEYVVESTGVFTTTEKASTHLKGGAKKVVISAPSADAPMFVCGVNLDAYSPDMKVVSNASCTTNCLAPLAK 159
Cdd:PLN02358 87 EDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCTTNCLAPLAK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 160 VINDNFEIVEVLMTTVHATTATQKTVDGPSGKLWRDGRGACQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNVSV 239
Cdd:PLN02358 167 VINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 240 VDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFEPKAGISLNDKFVKLISWYDNEFGYSN 319
Cdd:PLN02358 247 VDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEWGYSS 326
|
....*....
gi 232120 320 RVIDLIKYM 328
Cdd:PLN02358 327 RVVDLIVHM 335
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
3-328 |
6.08e-151 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 427.23 E-value: 6.08e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 3 KIGINGFGRIGRLVLRAAVDKG-ASVVAVNDpFIDVNYMVYLFKFDSTHGRFKGTVSAEGGFLVVNGQKITVFSERDPAN 81
Cdd:PRK15425 4 KVGINGFGRIGRIVFRAAQKRSdIEIVAIND-LLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPAN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 82 INWASAGAEYVVESTGVFTTTEKASTHLKGGAKKVVISAPSAD-APMFVCGVNLDAYSpDMKVVSNASCTTNCLAPLAKV 160
Cdd:PRK15425 83 LKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDnTPMFVKGANFDKYA-GQDIVSNASCTTNCLAPLAKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 161 INDNFEIVEVLMTTVHATTATQKTVDGPSGKLWRDGRGACQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNVSVV 240
Cdd:PRK15425 162 INDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 241 DLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFEPKAGISLNDKFVKLISWYDNEFGYSNR 320
Cdd:PRK15425 242 DLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYSNK 321
|
....*...
gi 232120 321 VIDLIKYM 328
Cdd:PRK15425 322 VLDLIAHI 329
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
3-332 |
2.09e-136 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 391.73 E-value: 2.09e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 3 KIGINGFGRIGRLVLRAAVDKG-----ASVVAVNDPFIDVNYMVYLFKFDSTHGRFKGTVS--------AEGGFLVVNGQ 69
Cdd:PTZ00434 5 KVGINGFGRIGRMVFQAICDQGligteIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVEttksspsvKTDDVLVVNGH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 70 KI-TVFSERDPANINWASAGAEYVVESTGVFTTTEKASTHLKGGAKKVVISAP-SADAPMFVCGVNLDAYSP-DMKVVSN 146
Cdd:PTZ00434 85 RIkCVKAQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPaSGGAKTIVMGVNQHEYSPtEHHVVSN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 147 ASCTTNCLAPLAKVI-NDNFEIVEVLMTTVHATTATQKTVDGPSGKLWRDGRGACQNIIPASTGAAKAVGKVIPALNGKL 225
Cdd:PTZ00434 165 ASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGKL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 226 TGMAFRVPTPNVSVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFEPKAGISLN---- 301
Cdd:PTZ00434 245 TGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKATLQNNlpge 324
|
330 340 350
....*....|....*....|....*....|.
gi 232120 302 DKFVKLISWYDNEFGYSNRVIDLIKYMQSKD 332
Cdd:PTZ00434 325 RRFFKIVSWYDNEWGYSHRVVDLVRYMAAKD 355
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-331 |
9.11e-129 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 371.38 E-value: 9.11e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 1 MSKIGINGFGRIGRLVLRAAVDKGAS-VVAVNDPFiDVNYMVYLFKFDSTHGRFKGTVSAEGGFLVVNGQKITVFSERDP 79
Cdd:PRK07729 2 KTKVAINGFGRIGRMVFRKAIKESAFeIVAINASY-PSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 80 ANINWASAGAEYVVESTGVFTTTEKASTHLKGGAKKVVISAPSADAPM-FVCGVNLDAYSPDMK-VVSNASCTTNCLAPL 157
Cdd:PRK07729 81 KELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVtIVVGVNEDQLDIEKHtIISNASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 158 AKVINDNFEIVEVLMTTVHATTATQKTVDGPSGKLwRDGRGACQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNV 237
Cdd:PRK07729 161 VKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHKDL-RRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 238 SVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFEPKAGISLNDKFVKLISWYDNEFGY 317
Cdd:PRK07729 240 SLVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEWGY 319
|
330
....*....|....
gi 232120 318 SNRVIDLIKYMQSK 331
Cdd:PRK07729 320 SCRVVDLVTLVADE 333
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
149-314 |
1.04e-112 |
|
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: 323.64 E-value: 1.04e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 149 CTTNCLAPLAKVINDNFEIVEVLMTTVHATTATQKTVDGPSgKLWRDGRGACQNIIPASTGAAKAVGKVIPALNGKLTGM 228
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 229 AFRVPTPNVSVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFEPKAGISLNDKFVKLI 308
Cdd:cd18126 80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159
|
....*.
gi 232120 309 SWYDNE 314
Cdd:cd18126 160 AWYDNE 165
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
4-324 |
1.28e-108 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 319.57 E-value: 1.28e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 4 IGINGFGRIGRLVLRAAVDK-GASVVAVNDPFIDVNYMVYLFKFDSTHGRFKGTVSAEGGFLVVNGQKITVFSERDPANI 82
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRpGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 83 NWaSAGAEYVVESTGVFTTTEKASTHLKGGAKKVVISAP--SADAPMFVCGVNLDAYSPDM-KVVSNASCTTNCLAPLAK 159
Cdd:NF033735 81 PW-GDGVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARhRIVTAASCTTNCLAPVVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 160 VINDNFEIVEVLMTTVHATTATQKTVDGPSGKLwRDGRGACQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNVSV 239
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAPHKDL-RRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 240 VDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFEPKAGISLNDKFVKLISWYDNEFGYSN 319
Cdd:NF033735 239 TDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYAN 318
|
....*
gi 232120 320 RVIDL 324
Cdd:NF033735 319 RMVDL 323
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
1-331 |
2.27e-107 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 316.85 E-value: 2.27e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 1 MSKIGINGFGRIGRLVLRAAV---DKGASVVAVNDPfIDVNYMVYLFKFDSTHGRFKGTVSAEGGFLVVNGQKITVFSER 77
Cdd:PRK07403 1 MIRVAINGFGRIGRNFLRCWLgreNSQLELVAINDT-SDPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 78 DPANINWASAGAEYVVESTGVFTTTEKASTHLKGGAKKVVISAP--SADAPMFVCGVNLDAYSPDM-KVVSNASCTTNCL 154
Cdd:PRK07403 80 NPLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPgkGEDIGTYVVGVNHHEYDHEDhNIISNASCTTNCL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 155 APLAKVINDNFEIVEVLMTTVHATTATQKTVDGPSGKLwRDGRGACQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPT 234
Cdd:PRK07403 160 APIAKVLHDNFGIIKGTMTTTHSYTGDQRILDASHRDL-RRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 235 PNVSVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFEPKAGISLNDKFVKLISWYDNE 314
Cdd:PRK07403 239 PNVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYDNE 318
|
330
....*....|....*..
gi 232120 315 FGYSNRVIDLIKYMQSK 331
Cdd:PRK07403 319 WGYSQRVVDLAELVARK 335
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
3-324 |
5.90e-101 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 302.62 E-value: 5.90e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 3 KIGINGFGRIGRLVLRAAVDKGAS---VVAVNDPFiDVNYMVYLFKFDSTHGRFKGTVSAEG-GFLVVNGQKITVFSERD 78
Cdd:PLN03096 62 KVAINGFGRIGRNFLRCWHGRKDSpldVVAINDTG-GVKQASHLLKYDSTLGTFDADVKPVGdDAISVDGKVIKVVSDRN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 79 PANINWASAGAEYVVESTGVFTTTEKASTHLKGGAKKVVISAPS-ADAPMFVCGVNLDAYSPDMKVVSNASCTTNCLAPL 157
Cdd:PLN03096 141 PLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGkGDIPTYVVGVNADDYKHSDPIISNASCTTNCLAPF 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 158 AKVINDNFEIVEVLMTTVHATTATQKTVDGPSGKLwRDGRGACQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNV 237
Cdd:PLN03096 221 VKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDL-RRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNV 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 238 SVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFEPKAGISLNDKFVKLISWYDNEFGY 317
Cdd:PLN03096 300 SVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAWYDNEWGY 379
|
....*..
gi 232120 318 SNRVIDL 324
Cdd:PLN03096 380 SQRVVDL 386
|
|
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
3-326 |
2.80e-97 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 290.86 E-value: 2.80e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 3 KIGINGFGRIGRLVLRAAVD-KGASVVAVNDPFIDVNYMVYLFKFDSTHGRFKGTVSAEGGFLVVNGQKITVFSERDPAN 81
Cdd:PRK08955 4 KVGINGFGRIGRLALRAAWDwPELEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKAIAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 82 INWAsaGAEYVVESTGVFTTTEKASTHLKGGAKKVVISAPSADAPMF--VCGVNLDAYSPDM-KVVSNASCTTNCLAPLA 158
Cdd:PRK08955 84 TDWS--GCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLniVMGVNDHLFDPAIhPIVTAASCTTNCLAPVV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 159 KVINDNFEIVEVLMTTVHATTATQKTVDGPSGKLwRDGRGACQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNVS 238
Cdd:PRK08955 162 KVIHEKLGIKHGSMTTIHDLTNTQTILDAPHKDL-RRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLANAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 239 VVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFEPKAGISLNDKFVKLISWYDNEFGYS 318
Cdd:PRK08955 241 LTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNEWGYA 320
|
....*...
gi 232120 319 NRVIDLIK 326
Cdd:PRK08955 321 NRTAELAR 328
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
3-331 |
1.67e-96 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 292.57 E-value: 1.67e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 3 KIGINGFGRIGRLVLR---AAVDKGASVVAVNDPFiDVNYMVYLFKFDSTHGRFKGTVS-AEGGFLVVNGQKITVFSERD 78
Cdd:PLN02237 77 KVAINGFGRIGRNFLRcwhGRKDSPLDVVVVNDSG-GVKNASHLLKYDSMLGTFKADVKiVDDETISVDGKPIKVVSNRD 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 79 PANINWASAGAEYVVESTGVFTTTEKASTHLKGGAKKVVISAPS--ADAPMFVCGVNLDAYSPDM-KVVSNASCTTNCLA 155
Cdd:PLN02237 156 PLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAkgADIPTYVVGVNEDDYDHEVaNIVSNASCTTNCLA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 156 PLAKVINDNFEIVEVLMTTVHATTATQKTVDGPSGKLwRDGRGACQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTP 235
Cdd:PLN02237 236 PFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDASHRDL-RRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 236 NVSVVDLTVRL-GKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFEPKAGISLNDKFVKLISWYDNE 314
Cdd:PLN02237 315 NVSVVDLVVNVeKKGITAEDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVAWYDNE 394
|
330
....*....|....*..
gi 232120 315 FGYSNRVIDLIKYMQSK 331
Cdd:PLN02237 395 WGYSQRVVDLAHLVAAK 411
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
1-329 |
6.00e-90 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 272.32 E-value: 6.00e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 1 MSKIGINGFGRIGRLVLRAAVDKGA----SVVAVNDpFIDVNYMVYLFKFDSTHGRFKGTVSAEGGFLVVNGQKITVFSE 76
Cdd:PRK13535 1 TIRVAINGFGRIGRNVLRALYESGRraeiTVVAINE-LADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 77 RDPANINWASAGAEYVVESTGVFTTTEKASTHLKGGAKKVVISAPSA---DAPMfVCGVNLDAYSPDMKVVSNASCTTNC 153
Cdd:PRK13535 80 RDIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSndlDATV-VYGVNHDQLRAEHRIVSNASCTTNC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 154 LAPLAKVINDNFEIVEVLMTTVHATTATQKTVDGPSGKLwRDGRGACQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVP 233
Cdd:PRK13535 159 IIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHPDL-RRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 234 TPNVSVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFEPKAGISLNDKFVKLISWYDN 313
Cdd:PRK13535 238 TINVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDN 317
|
330
....*....|....*.
gi 232120 314 EFGYSNRVIDLIKYMQ 329
Cdd:PRK13535 318 EWGFANRMLDTTLAMA 333
|
|
| GAPDH_I_N |
cd05214 |
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
3-148 |
3.43e-87 |
|
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: 258.86 E-value: 3.43e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 3 KIGINGFGRIGRLVLRAAVDK-GASVVAVNDPFIDvNYMVYLFKFDSTHGRFKGTVSAEGGFLVVNGQKITVFSERDPAN 81
Cdd:cd05214 2 KVGINGFGRIGRLVFRAALERdDIEVVAINDLTDD-ETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 232120 82 INWASAGAEYVVESTGVFTTTEKASTHLKGGAKKVVISAPSAD-APMFVCGVNLDAYSPDMKVVSNAS 148
Cdd:cd05214 81 LPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDADDKIISNAS 148
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
154-311 |
4.50e-84 |
|
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: 250.97 E-value: 4.50e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 154 LAPLAKVINDNFEIVEVLMTTVHATTATQKTVDGPSGKLWRDGRGACQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVP 233
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 232120 234 TPNVSVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFEPKAGISLNDKFVKLISWY 311
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
149-314 |
5.31e-83 |
|
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: 248.30 E-value: 5.31e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 149 CTTNCLAPLAKVINDNFEIVEVLMTTVHATTATQKTVDGPSGKLWRDGRGACQNIIPASTGAAKAVGKVIPALNGKLTGM 228
Cdd:cd18123 1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 229 AFRVPTPNVSVVDLTVRLGKGASYDEIKAKVQEAANGplKGILGYTDEEVVSTDFLSDTHSSVFEPKAGISLNDKFVKLI 308
Cdd:cd18123 81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLM 158
|
....*.
gi 232120 309 SWYDNE 314
Cdd:cd18123 159 QWYDNE 164
|
|
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
8-328 |
5.63e-81 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 253.69 E-value: 5.63e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 8 GFGRIGRLVLRAAVDKGAS--------VVAVNDPFIDVNYMVYLFKFDSTHGRFKGTVSA--EGGFLVVNGQKITVFSER 77
Cdd:PRK08289 134 GFGRIGRLLARLLIEKTGGgnglrlraIVVRKGSEGDLEKRASLLRRDSVHGPFNGTITVdeENNAIIANGNYIQVIYAN 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 78 DPANINWASAGAE--YVVESTGVFTTTEKASTHLKG-GAKKVVISAPS-ADAPMFVCGVNLDAYSPDMKVVSNASCTTNC 153
Cdd:PRK08289 214 SPEEVDYTAYGINnaLVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGkGDIKNIVHGVNHSDITDEDKIVSAASCTTNA 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 154 LAPLAKVINDNFEIVEVLMTTVHATTATQKTVDGpSGKLWRDGRGACQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVP 233
Cdd:PRK08289 294 ITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDN-YHKGDRRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNAIRVP 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 234 TPNVSVVDLTVRLGKGASYDEIKAKVQEAA-NGPLKGILGYTDE-EVVSTDFLSDTHSSVFEPKAGISlNDKFVKLISWY 311
Cdd:PRK08289 373 TPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQIDYTDStEVVSSDFVGSRHAGVVDSQATIV-NGNRAVLYVWY 451
|
330
....*....|....*..
gi 232120 312 DNEFGYSNRVIDLIKYM 328
Cdd:PRK08289 452 DNEFGYSCQVVRVMEQM 468
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-149 |
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: 236.68 E-value: 1.21e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 3 KIGINGFGRIGRLVLRAAV-DKGASVVAVNDPfIDVNYMVYLFKFDSTHGRFKGTVSAEGGFLVVNGQKITVFSERDPAN 81
Cdd:smart00846 2 KVGINGFGRIGRLVLRAALeRPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPAN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 232120 82 INWASAGAEYVVESTGVFTTTEKASTHLKGGAKKVVISAPSADA-PMFVCGVNLDAYSPDMKVVSNASC 149
Cdd:smart00846 81 LPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
4-332 |
8.93e-61 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 197.79 E-value: 8.93e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 4 IGINGFGRIGRLVLRAAV-DKGASVVAVNDPFIDVNYMVYLFKFDSTHGRFKGT-VSAEGGFLVVNG-QKITVFSERDPA 80
Cdd:PTZ00353 5 VGINGFGPVGKAVLFASLtDPLVTVVAVNDASVSIAYIAYVLEQESPLSAPDGAsIRVVGEQIVLNGtQKIRVSAKHDLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 81 NINWASAGAEYVVESTGVFTTTEKASTHLKGGAKKVVISAPSADAPMFVCGVNLDAYSPDMKVVSNASCTTNCLAPLAKV 160
Cdd:PTZ00353 85 EIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDERLSASLPVCCAGAPIAVALAPVIRA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 161 INDNFEIVEVLMTTVHATTATQKT-VDGPSGKLWRDGRGACQNIIPASTGAAKAVGKVIPALNGKLTGMAFRVPTPNVSV 239
Cdd:PTZ00353 165 LHEVYGVEECSYTAIHGMQPQEPIaARSKNSQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVKKGCA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 240 VDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDThSSVFEPKAGISLND-KFVKLISWYDNEFGYS 318
Cdd:PTZ00353 245 IDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCIPNG-KLCYDATSSSSSREgEVHKMVLWFDVECYYA 323
|
330
....*....|....
gi 232120 319 NRVIDLIKYMQSKD 332
Cdd:PTZ00353 324 ARLLSLVKQLHQIH 337
|
|
| Gp_dh_N |
pfam00044 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-101 |
7.88e-52 |
|
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. N-terminal domain is a Rossmann NAD(P) binding fold.
Pssm-ID: 459648 [Multi-domain] Cd Length: 101 Bit Score: 166.51 E-value: 7.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 3 KIGINGFGRIGRLVLRAAVD-KGASVVAVNDpFIDVNYMVYLFKFDSTHGRFKGTVSAEGGFLVVNGQKITVFSERDPAN 81
Cdd:pfam00044 2 KVGINGFGRIGRLVLRAALErPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAE 80
|
90 100
....*....|....*....|
gi 232120 82 INWASAGAEYVVESTGVFTT 101
Cdd:pfam00044 81 LPWGDLGVDVVIESTGVFTT 100
|
|
| GAPDH_N_E4PDH |
cd17892 |
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
3-148 |
6.31e-49 |
|
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: 161.28 E-value: 6.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 3 KIGINGFGRIGRLVLRAAVDKGAS----VVAVNDPfIDVNYMVYLFKFDSTHGRFKGTVSAEGGFLVVNGQKITVFSERD 78
Cdd:cd17892 2 RVAINGYGRIGRNVLRALYESGRRaefqVVAINEL-ADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 232120 79 PANINWASAGAEYVVESTGVFTTTEKASTHLKGGAKKVVISAPSA---DAPMfVCGVNLDAYSPDMKVVSNAS 148
Cdd:cd17892 81 PENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASndvDATI-VYGINQDLLRAEHRIVSNAS 152
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
149-314 |
1.20e-43 |
|
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: 147.56 E-value: 1.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 149 CTTNCLAPLAKVINDNFEIVEVLMTTVHATTATQKTVDGPSGKLwRDGRGACQNIIPASTGAAKAVGKVIPALNGKLTGM 228
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDAYHPDL-RRTRAASQSIIPVDTKLARGIERILPHLAGRFEAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 229 AFRVPTPNVSVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFEPKAGISLNDKFVKLI 308
Cdd:cd23937 80 AVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLL 159
|
....*.
gi 232120 309 SWYDNE 314
Cdd:cd23937 160 VWCDNE 165
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
149-314 |
1.65e-42 |
|
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: 144.97 E-value: 1.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 149 CTTNCLAPLAKVINDNFEIVEVLMTTVHATTATQKTVDGPSGKLWrdGRGACQNIIPASTGAAKAVGKVIPALN--GKLT 226
Cdd:cd18122 1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIGkpIKVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 227 GMAFRVPTPNVSVVDLTVRLGKGASYDEIKAKVQEAANGPLKGILGYTDEEVVSTDFLSDTHSSVFEPKAGISLNDKFVK 306
Cdd:cd18122 79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLK 158
|
....*...
gi 232120 307 LISWYDNE 314
Cdd:cd18122 159 VFSAVDNE 166
|
|
| GAPDH-like_N |
cd05192 |
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ... |
3-153 |
3.80e-09 |
|
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: 53.51 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 232120 3 KIGINGFGRIGRLVLRAAVDK-GASVVAVNDPfidvnymvylfkfdsthgrfkgtvsaeggflvvngqkitvfserdpan 81
Cdd:cd05192 2 RVAINGFGRIGRIVFRAIADQdDLDVVAINDR------------------------------------------------ 33
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 232120 82 inwasagAEYVVESTGVFTTTEKASTHLKGGAKKVVISAPS-ADAPMFVCGVNLDAYSPDMKVVSNASCTTNC 153
Cdd:cd05192 34 -------RDVVIECTGSFTDDDNAEKHIKAGGKKAVITAPEkGDIPTIVVVLNELAKSAGATVVSNANETSYS 99
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|
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