|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
6-331 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 574.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 6 VGINGFGRIGRLVLR-ACLQKGIKVTAINDPFIDLQYMVYMFKYDSTHGRYKGEVH-MEDGKLIVDGQAISVFQCMKPAE 83
Cdd:PLN02272 88 IGINGFGRIGRLVLRiATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINvVDDSTLEINGKQIKVTSKRDPAE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 84 IPWGDAGALYVVESTGVFLSIEKASAHIQGGAKRVVVSAPSPDAPMFVMGVNQDKYDPSsMTIVSNASCTTNCLAPLAKV 163
Cdd:PLN02272 168 IPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPN-MNIVSNASCTTNCLAPLAKV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 164 IHDNFGIEEALMTTVHAYTATQKTVDGPSAKAWRDGRGAHQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVADVSVV 243
Cdd:PLN02272 247 VHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVV 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 244 DLTCRLTRPASYANIKESVKKAAHGPMKGILGYTEDSVVSSDFVGDTHSSIFDAGAGISLNDNFVKLISWYDNEFGYSHR 323
Cdd:PLN02272 327 DLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYSNR 406
|
....*...
gi 47085833 324 VADLLMYM 331
Cdd:PLN02272 407 VLDLIEHM 414
|
|
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
6-335 |
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: 560.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 6 VGINGFGRIGRLVLRACLQKG--IKVTAINDPfIDLQYMVYMFKYDSTHGRYKGEVHMEDGKLIVDGQAISVFQCMKPAE 83
Cdd:COG0057 5 VAINGFGRIGRLVLRALLERGpdIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 84 IPWGDAGALYVVESTGVFLSIEKASAHIQGGAKRVVVSAPSPDA-PMFVMGVNQDKYDPSsMTIVSNASCTTNCLAPLAK 162
Cdd:COG0057 84 LPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDAD-HRIISNASCTTNCLAPVAK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 163 VIHDNFGIEEALMTTVHAYTATQKTVDGPsAKAWRDGRGAHQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVADVSV 242
Cdd:COG0057 163 VLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 243 VDLTCRLTRPASYANIKESVKKAAHGPMKGILGYTEDSVVSSDFVGDTHSSIFDAGAGISLNDNFVKLISWYDNEFGYSH 322
Cdd:COG0057 242 VDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGYSN 321
|
330
....*....|...
gi 47085833 323 RVADLLMYMHSKE 335
Cdd:COG0057 322 RMVDLAEYMAKLL 334
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
6-326 |
2.03e-170 |
|
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: 476.38 E-value: 2.03e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 6 VGINGFGRIGRLVLRACLQKG---IKVTAINDPfIDLQYMVYMFKYDSTHGRYKGEVHMEDGKLIVDGQ-AISVFQCMKP 81
Cdd:TIGR01534 2 VGINGFGRIGRLVLRRILEKPgndLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKeVISVFSERDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 82 AEIPWGDAGALYVVESTGVFLSIEKASAHIQGGAKRVVVSAPS-PDAPMFVMGVNQDKYDPSSmTIVSNASCTTNCLAPL 160
Cdd:TIGR01534 81 SDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSkGDVKTIVYGVNHDEYDGEE-RIISNASCTTNCLAPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 161 AKVIHDNFGIEEALMTTVHAYTATQKTVDGPSaKAWRDGRGAHQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVADV 240
Cdd:TIGR01534 160 AKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPH-KDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 241 SVVDLTCRLTRPASYANIKESVKKAAHGPMKGILGYTEDSVVSSDFVGDTHSSIFDAGAGI--SLNDNFVKLISWYDNEF 318
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKvtGLGDSLVKVYAWYDNEW 318
|
....*...
gi 47085833 319 GYSHRVAD 326
Cdd:TIGR01534 319 GYSNRLVD 326
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
152-317 |
1.78e-120 |
|
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: 343.67 E-value: 1.78e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 152 CTTNCLAPLAKVIHDNFGIEEALMTTVHAYTATQKTVDGPSaKAWRDGRGAHQNIIPASTGAAKAVGKVIPELNGKLTGM 231
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 232 AFRVPVADVSVVDLTCRLTRPASYANIKESVKKAAHGPMKGILGYTEDSVVSSDFVGDTHSSIFDAGAGISLNDNFVKLI 311
Cdd:cd18126 80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159
|
....*.
gi 47085833 312 SWYDNE 317
Cdd:cd18126 160 AWYDNE 165
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
6-327 |
4.15e-116 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 338.45 E-value: 4.15e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 6 VGINGFGRIGRLVLRACLQK-GIKVTAINDPFIDLQYMVYMFKYDSTHGRYKGEVHMEDGKLIVDGQAISVFQCMKPAEI 84
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRpGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 85 PWGDaGALYVVESTGVFLSIEKASAHIQGGAKRVVVSAP--SPDAPMFVMGVNQDKYDPSSMTIVSNASCTTNCLAPLAK 162
Cdd:NF033735 81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARHRIVTAASCTTNCLAPVVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 163 VIHDNFGIEEALMTTVHAYTATQKTVDGPsAKAWRDGRGAHQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVADVSV 242
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 243 VDLTCRLTRPASYANIKESVKKAAHGPMKGILGYTEDSVVSSDFVGDTHSSIFDAGAGISLNDNFVKLISWYDNEFGYSH 322
Cdd:NF033735 239 TDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYAN 318
|
....*
gi 47085833 323 RVADL 327
Cdd:NF033735 319 RMVDL 323
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
157-314 |
1.21e-89 |
|
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: 265.23 E-value: 1.21e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 157 LAPLAKVIHDNFGIEEALMTTVHAYTATQKTVDGPSAKAWRDGRGAHQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVP 236
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47085833 237 VADVSVVDLTCRLTRPASYANIKESVKKAAHGPMKGILGYTEDSVVSSDFVGDTHSSIFDAGAGISLNDNFVKLISWY 314
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
6-152 |
2.68e-73 |
|
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: 223.20 E-value: 2.68e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 6 VGINGFGRIGRLVLRACL-QKGIKVTAINDPfIDLQYMVYMFKYDSTHGRYKGEVHMEDGKLIVDGQAISVFQCMKPAEI 84
Cdd:smart00846 3 VGINGFGRIGRLVLRAALeRPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANL 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47085833 85 PWGDAGALYVVESTGVFLSIEKASAHIQGGAKRVVVSAPSPDA-PMFVMGVNQDKYDPsSMTIVSNASC 152
Cdd:smart00846 82 PWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDG-EDHIISNASC 149
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
6-331 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 574.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 6 VGINGFGRIGRLVLR-ACLQKGIKVTAINDPFIDLQYMVYMFKYDSTHGRYKGEVH-MEDGKLIVDGQAISVFQCMKPAE 83
Cdd:PLN02272 88 IGINGFGRIGRLVLRiATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINvVDDSTLEINGKQIKVTSKRDPAE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 84 IPWGDAGALYVVESTGVFLSIEKASAHIQGGAKRVVVSAPSPDAPMFVMGVNQDKYDPSsMTIVSNASCTTNCLAPLAKV 163
Cdd:PLN02272 168 IPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPN-MNIVSNASCTTNCLAPLAKV 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 164 IHDNFGIEEALMTTVHAYTATQKTVDGPSAKAWRDGRGAHQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVADVSVV 243
Cdd:PLN02272 247 VHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVV 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 244 DLTCRLTRPASYANIKESVKKAAHGPMKGILGYTEDSVVSSDFVGDTHSSIFDAGAGISLNDNFVKLISWYDNEFGYSHR 323
Cdd:PLN02272 327 DLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYSNR 406
|
....*...
gi 47085833 324 VADLLMYM 331
Cdd:PLN02272 407 VLDLIEHM 414
|
|
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
6-335 |
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: 560.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 6 VGINGFGRIGRLVLRACLQKG--IKVTAINDPfIDLQYMVYMFKYDSTHGRYKGEVHMEDGKLIVDGQAISVFQCMKPAE 83
Cdd:COG0057 5 VAINGFGRIGRLVLRALLERGpdIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 84 IPWGDAGALYVVESTGVFLSIEKASAHIQGGAKRVVVSAPSPDA-PMFVMGVNQDKYDPSsMTIVSNASCTTNCLAPLAK 162
Cdd:COG0057 84 LPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDAD-HRIISNASCTTNCLAPVAK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 163 VIHDNFGIEEALMTTVHAYTATQKTVDGPsAKAWRDGRGAHQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVADVSV 242
Cdd:COG0057 163 VLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 243 VDLTCRLTRPASYANIKESVKKAAHGPMKGILGYTEDSVVSSDFVGDTHSSIFDAGAGISLNDNFVKLISWYDNEFGYSH 322
Cdd:COG0057 242 VDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGYSN 321
|
330
....*....|...
gi 47085833 323 RVADLLMYMHSKE 335
Cdd:COG0057 322 RMVDLAEYMAKLL 334
|
|
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
6-335 |
1.34e-175 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 490.12 E-value: 1.34e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 6 VGINGFGRIGRLVLRACLQKG-IKVTAINDPFIDLQYMVYMFKYDSTHGRYKGEVHMEDGKLIVDGQAISVFQCMKPAEI 84
Cdd:PTZ00023 5 LGINGFGRIGRLVFRAALEREdVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKDPAAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 85 PWGDAGALYVVESTGVFLSIEKASAHIQGGAKRVVVSAP-SPDAPMFVMGVNQDKYDPSSmTIVSNASCTTNCLAPLAKV 163
Cdd:PTZ00023 85 PWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPpKDDTPIYVMGVNHTQYDKSQ-RIVSNASCTTNCLAPLAKV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 164 IHDNFGIEEALMTTVHAYTATQKTVDGPS--AKAWRDGRGAHQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVADVS 241
Cdd:PTZ00023 164 VNDKFGIVEGLMTTVHASTANQLTVDGPSkgGKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVPDVS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 242 VVDLTCRLTRPASYANIKESVKKAAHGPMKGILGYTEDSVVSSDFVGDTHSSIFDAGAGISLNDNFVKLISWYDNEFGYS 321
Cdd:PTZ00023 244 VVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDNEWGYS 323
|
330
....*....|....
gi 47085833 322 HRVADLLMYMHSKE 335
Cdd:PTZ00023 324 NRLLDLAHYITQKY 337
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
6-326 |
2.03e-170 |
|
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: 476.38 E-value: 2.03e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 6 VGINGFGRIGRLVLRACLQKG---IKVTAINDPfIDLQYMVYMFKYDSTHGRYKGEVHMEDGKLIVDGQ-AISVFQCMKP 81
Cdd:TIGR01534 2 VGINGFGRIGRLVLRRILEKPgndLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKeVISVFSERDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 82 AEIPWGDAGALYVVESTGVFLSIEKASAHIQGGAKRVVVSAPS-PDAPMFVMGVNQDKYDPSSmTIVSNASCTTNCLAPL 160
Cdd:TIGR01534 81 SDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSkGDVKTIVYGVNHDEYDGEE-RIISNASCTTNCLAPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 161 AKVIHDNFGIEEALMTTVHAYTATQKTVDGPSaKAWRDGRGAHQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVADV 240
Cdd:TIGR01534 160 AKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPH-KDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 241 SVVDLTCRLTRPASYANIKESVKKAAHGPMKGILGYTEDSVVSSDFVGDTHSSIFDAGAGI--SLNDNFVKLISWYDNEF 318
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKvtGLGDSLVKVYAWYDNEW 318
|
....*...
gi 47085833 319 GYSHRVAD 326
Cdd:TIGR01534 319 GYSNRLVD 326
|
|
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
6-331 |
4.03e-156 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 440.70 E-value: 4.03e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 6 VGINGFGRIGRLVLRACLQKG-IKVTAINDPFIDLQYMVYMFKYDSTHGRYK-GEVHMEDGKLIVDGQA-ISVFQCMKPA 82
Cdd:PLN02358 8 IGINGFGRIGRLVARVVLQRDdVELVAVNDPFITTEYMTYMFKYDSVHGQWKhHELKVKDDKTLLFGEKpVTVFGIRNPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 83 EIPWGDAGALYVVESTGVFLSIEKASAHIQGGAKRVVVSAPSPDAPMFVMGVNQDKYDpSSMTIVSNASCTTNCLAPLAK 162
Cdd:PLN02358 88 DIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYK-SDLDIVSNASCTTNCLAPLAK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 163 VIHDNFGIEEALMTTVHAYTATQKTVDGPSAKAWRDGRGAHQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVADVSV 242
Cdd:PLN02358 167 VINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 243 VDLTCRLTRPASYANIKESVKKAAHGPMKGILGYTEDSVVSSDFVGDTHSSIFDAGAGISLNDNFVKLISWYDNEFGYSH 322
Cdd:PLN02358 247 VDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEWGYSS 326
|
....*....
gi 47085833 323 RVADLLMYM 331
Cdd:PLN02358 327 RVVDLIVHM 335
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
6-331 |
2.18e-147 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 418.37 E-value: 2.18e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 6 VGINGFGRIGRLVLRACLQKG-IKVTAINDpFIDLQYMVYMFKYDSTHGRYKGEVHMEDGKLIVDGQAISVFQCMKPAEI 84
Cdd:PRK15425 5 VGINGFGRIGRIVFRAAQKRSdIEIVAIND-LLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPANL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 85 PWGDAGALYVVESTGVFLSIEKASAHIQGGAKRVVVSAPSPD-APMFVMGVNQDKYdpSSMTIVSNASCTTNCLAPLAKV 163
Cdd:PRK15425 84 KWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDnTPMFVKGANFDKY--AGQDIVSNASCTTNCLAPLAKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 164 IHDNFGIEEALMTTVHAYTATQKTVDGPSAKAWRDGRGAHQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVADVSVV 243
Cdd:PRK15425 162 INDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 244 DLTCRLTRPASYANIKESVKKAAHGPMKGILGYTEDSVVSSDFVGDTHSSIFDAGAGISLNDNFVKLISWYDNEFGYSHR 323
Cdd:PRK15425 242 DLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYSNK 321
|
....*...
gi 47085833 324 VADLLMYM 331
Cdd:PRK15425 322 VLDLIAHI 329
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
1-335 |
2.25e-139 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 399.04 E-value: 2.25e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 1 MSELCVGINGFGRIGRLVLRACLQKG-----IKVTAINDPFIDLQYMVYMFKYDSTHGRYKGEVHM--------EDGKLI 67
Cdd:PTZ00434 1 MAPIKVGINGFGRIGRMVFQAICDQGligteIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVETtksspsvkTDDVLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 68 VDGQAIsvfQCMK----PAEIPWGDAGALYVVESTGVFLSIEKASAHIQGGAKRVVVSAP-SPDAPMFVMGVNQDKYDPS 142
Cdd:PTZ00434 81 VNGHRI---KCVKaqrnPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPaSGGAKTIVMGVNQHEYSPT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 143 SMTIVSNASCTTNCLAPLAKVI-HDNFGIEEALMTTVHAYTATQKTVDGPSAKAWRDGRGAHQNIIPASTGAAKAVGKVI 221
Cdd:PTZ00434 158 EHHVVSNASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 222 PELNGKLTGMAFRVPVADVSVVDLTCRLTRPASYANIKESVKKAAHGPMKGILGYTEDSVVSSDFVGDTHSSIFDAGAGI 301
Cdd:PTZ00434 238 PSTKGKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKATL 317
|
330 340 350
....*....|....*....|....*....|....*...
gi 47085833 302 SLN----DNFVKLISWYDNEFGYSHRVADLLMYMHSKE 335
Cdd:PTZ00434 318 QNNlpgeRRFFKIVSWYDNEWGYSHRVVDLVRYMAAKD 355
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
6-334 |
9.39e-133 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 381.78 E-value: 9.39e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 6 VGINGFGRIGRLVLR-ACLQKGIKVTAINDPFiDLQYMVYMFKYDSTHGRYKGEVHMEDGKLIVDGQAISVFQCMKPAEI 84
Cdd:PRK07729 5 VAINGFGRIGRMVFRkAIKESAFEIVAINASY-PSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDPKEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 85 PWGDAGALYVVESTGVFLSIEKASAHIQGGAKRVVVSAPSPDAPM-FVMGVNQDKYDPSSMTIVSNASCTTNCLAPLAKV 163
Cdd:PRK07729 84 PWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVtIVVGVNEDQLDIEKHTIISNASCTTNCLAPVVKV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 164 IHDNFGIEEALMTTVHAYTATQKTVDGPSaKAWRDGRGAHQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVADVSVV 243
Cdd:PRK07729 164 LDEQFGIENGLMTTVHAYTNDQKNIDNPH-KDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNVSLV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 244 DLTCRLTRPASYANIKESVKKAAHGPMKGILGYTEDSVVSSDFVGDTHSSIFDAGAGISLNDNFVKLISWYDNEFGYSHR 323
Cdd:PRK07729 243 DLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEWGYSCR 322
|
330
....*....|.
gi 47085833 324 VADLLMYMHSK 334
Cdd:PRK07729 323 VVDLVTLVADE 333
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
152-317 |
1.78e-120 |
|
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: 343.67 E-value: 1.78e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 152 CTTNCLAPLAKVIHDNFGIEEALMTTVHAYTATQKTVDGPSaKAWRDGRGAHQNIIPASTGAAKAVGKVIPELNGKLTGM 231
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 232 AFRVPVADVSVVDLTCRLTRPASYANIKESVKKAAHGPMKGILGYTEDSVVSSDFVGDTHSSIFDAGAGISLNDNFVKLI 311
Cdd:cd18126 80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159
|
....*.
gi 47085833 312 SWYDNE 317
Cdd:cd18126 160 AWYDNE 165
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
6-327 |
4.15e-116 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 338.45 E-value: 4.15e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 6 VGINGFGRIGRLVLRACLQK-GIKVTAINDPFIDLQYMVYMFKYDSTHGRYKGEVHMEDGKLIVDGQAISVFQCMKPAEI 84
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRpGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 85 PWGDaGALYVVESTGVFLSIEKASAHIQGGAKRVVVSAP--SPDAPMFVMGVNQDKYDPSSMTIVSNASCTTNCLAPLAK 162
Cdd:NF033735 81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARHRIVTAASCTTNCLAPVVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 163 VIHDNFGIEEALMTTVHAYTATQKTVDGPsAKAWRDGRGAHQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVADVSV 242
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 243 VDLTCRLTRPASYANIKESVKKAAHGPMKGILGYTEDSVVSSDFVGDTHSSIFDAGAGISLNDNFVKLISWYDNEFGYSH 322
Cdd:NF033735 239 TDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYAN 318
|
....*
gi 47085833 323 RVADL 327
Cdd:NF033735 319 RMVDL 323
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
6-327 |
1.56e-111 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 327.63 E-value: 1.56e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 6 VGINGFGRIGRLVLRACLQK---GIKVTAINDPfIDLQYMVYMFKYDSTHGRYKGEVHMEDGKLIVDGQAISVFQCMKPA 82
Cdd:PRK07403 4 VAINGFGRIGRNFLRCWLGRensQLELVAINDT-SDPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDRNPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 83 EIPWGDAGALYVVESTGVFLSIEKASAHIQGGAKRVVVSAP--SPDAPMFVMGVNQDKYDPSSMTIVSNASCTTNCLAPL 160
Cdd:PRK07403 83 NLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPgkGEDIGTYVVGVNHHEYDHEDHNIISNASCTTNCLAPI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 161 AKVIHDNFGIEEALMTTVHAYTATQKTVDGpSAKAWRDGRGAHQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVADV 240
Cdd:PRK07403 163 AKVLHDNFGIIKGTMTTTHSYTGDQRILDA-SHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTPNV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 241 SVVDLTCRLTRPASYANIKESVKKAAHGPMKGILGYTEDSVVSSDFVGDTHSSIFDAGAGISLNDNFVKLISWYDNEFGY 320
Cdd:PRK07403 242 SVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYDNEWGY 321
|
....*..
gi 47085833 321 SHRVADL 327
Cdd:PRK07403 322 SQRVVDL 328
|
|
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
6-327 |
2.06e-101 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 301.65 E-value: 2.06e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 6 VGINGFGRIGRLVLRACLQ-KGIKVTAINDPFIDLQYMVYMFKYDSTHGRYKGEVHMEDGKLIVDGQAISVFQCMKPAEI 84
Cdd:PRK08955 5 VGINGFGRIGRLALRAAWDwPELEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKAIADT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 85 PWgdAGALYVVESTGVFLSIEKASAHIQGGAKRVVVSAP--SPDAPMFVMGVNQDKYDPSSMTIVSNASCTTNCLAPLAK 162
Cdd:PRK08955 85 DW--SGCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPvkEEGVLNIVMGVNDHLFDPAIHPIVTAASCTTNCLAPVVK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 163 VIHDNFGIEEALMTTVHAYTATQKTVDGPSaKAWRDGRGAHQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVADVSV 242
Cdd:PRK08955 163 VIHEKLGIKHGSMTTIHDLTNTQTILDAPH-KDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLANASL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 243 VDLTCRLTRPASYANIKESVKKAAHGPMKGILGYTEDSVVSSDFVGDTHSSIFDAGAGISLNDNFVKLISWYDNEFGYSH 322
Cdd:PRK08955 242 TDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNEWGYAN 321
|
....*
gi 47085833 323 RVADL 327
Cdd:PRK08955 322 RTAEL 326
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
2-327 |
5.68e-98 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 296.81 E-value: 5.68e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 2 SELCVGINGFGRIGRLVLRACLQKG---IKVTAINDPFiDLQYMVYMFKYDSTHGRYKGEVHMEDGKLI-VDGQAISVFQ 77
Cdd:PLN02237 74 AKLKVAINGFGRIGRNFLRCWHGRKdspLDVVVVNDSG-GVKNASHLLKYDSMLGTFKADVKIVDDETIsVDGKPIKVVS 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 78 CMKPAEIPWGDAGALYVVESTGVFLSIEKASAHIQGGAKRVVVSAPSP--DAPMFVMGVNQDKYDPSSMTIVSNASCTTN 155
Cdd:PLN02237 153 NRDPLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAKgaDIPTYVVGVNEDDYDHEVANIVSNASCTTN 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 156 CLAPLAKVIHDNFGIEEALMTTVHAYTATQKTVDGpSAKAWRDGRGAHQNIIPASTGAAKAVGKVIPELNGKLTGMAFRV 235
Cdd:PLN02237 233 CLAPFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRV 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 236 PVADVSVVDLTCRLTRPASYA-NIKESVKKAAHGPMKGILGYTEDSVVSSDFVGDTHSSIFDAGAGISLNDNFVKLISWY 314
Cdd:PLN02237 312 PTPNVSVVDLVVNVEKKGITAeDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVAWY 391
|
330
....*....|...
gi 47085833 315 DNEFGYSHRVADL 327
Cdd:PLN02237 392 DNEWGYSQRVVDL 404
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
6-327 |
5.80e-95 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 287.21 E-value: 5.80e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 6 VGINGFGRIGRLVLRACLQKG---IKVTAINDPFiDLQYMVYMFKYDSTHGRYKGEVHMEDGKLI-VDGQAISVFQCMKP 81
Cdd:PLN03096 63 VAINGFGRIGRNFLRCWHGRKdspLDVVAINDTG-GVKQASHLLKYDSTLGTFDADVKPVGDDAIsVDGKVIKVVSDRNP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 82 AEIPWGDAGALYVVESTGVFLSIEKASAHIQGGAKRVVVSAPSP-DAPMFVMGVNQDKYDPSSmTIVSNASCTTNCLAPL 160
Cdd:PLN03096 142 LNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKgDIPTYVVGVNADDYKHSD-PIISNASCTTNCLAPF 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 161 AKVIHDNFGIEEALMTTVHAYTATQKTVDGpSAKAWRDGRGAHQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVADV 240
Cdd:PLN03096 221 VKVLDQKFGIIKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNV 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 241 SVVDLTCRLTRPASYANIKESVKKAAHGPMKGILGYTEDSVVSSDFVGDTHSSIFDAGAGISLNDNFVKLISWYDNEFGY 320
Cdd:PLN03096 300 SVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAWYDNEWGY 379
|
....*..
gi 47085833 321 SHRVADL 327
Cdd:PLN03096 380 SQRVVDL 386
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
157-314 |
1.21e-89 |
|
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: 265.23 E-value: 1.21e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 157 LAPLAKVIHDNFGIEEALMTTVHAYTATQKTVDGPSAKAWRDGRGAHQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVP 236
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47085833 237 VADVSVVDLTCRLTRPASYANIKESVKKAAHGPMKGILGYTEDSVVSSDFVGDTHSSIFDAGAGISLNDNFVKLISWY 314
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| E4PD_g-proteo |
TIGR01532 |
erythrose-4-phosphate dehydrogenase; This model represents the small clade of dehydrogenases ... |
6-326 |
9.82e-89 |
|
erythrose-4-phosphate dehydrogenase; This model represents the small clade of dehydrogenases in gamma-proteobacteria which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose. This enzyme activity appears to have evolved from glyceraldehyde-3-phosphate dehydrogenase, whose substrate differs only in the lack of one carbon relative to E4P. Accordingly, this model is very close to the corresponding models for GAPDH, and those sequences which hit above trusted here invariably hit between trusted and noise to the GAPDH model (TIGR01534). Similarly, it may be found that there are species outside of the gamma proteobacteria which synthesize pyridoxine and have more than one aparrent GAPDH gene of which one may have E4PD activity - this may necessitate a readjustment of these models. Alternatively, some of the GAPDH enzymes may prove to be bifunctional in certain species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
Pssm-ID: 130595 Cd Length: 325 Bit Score: 269.07 E-value: 9.82e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 6 VGINGFGRIGRLVLRACLQKG----IKVTAINDpFIDLQYMVYMFKYDSTHGRYKGEVHMEDGKLIVDGQAISVFQCMKP 81
Cdd:TIGR01532 2 VAINGFGRIGRNVLRALYESGrraeITVVAINE-LADAAGMAHLLKYDTSHGRFAWEVRQDRDQLFVGDDAIRVLHERSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 82 AEIPWGDAGALYVVESTGVFLSIEKASAHIQGGAKRVVVSAPSP---DAPMfVMGVNQDKYDpSSMTIVSNASCTTNCLA 158
Cdd:TIGR01532 81 QSLPWRELGVDLVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGAsdlDATI-VYGVNQDQLR-AEHRIVSNASCTTNCIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 159 PLAKVIHDNFGIEEALMTTVHAYTATQKTVDGPSAKAwRDGRGAHQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVA 238
Cdd:TIGR01532 159 PVIKLLDDAYGIESGTITTIHSAMNDQQVIDAYHPDL-RRTRAASQSIIPVDTKLAAGIERFFPQFNDRFEAIAVRVPTV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 239 DVSVVDLTCRLTRPASYANIKESVKKAAHGPMKGILGYTEDSVVSSDFVGDTHSSIFDAGAGISLNDNFVKLISWYDNEF 318
Cdd:TIGR01532 238 NVTAIDLSVTVKKPVKANEVNLLLQKAAQGALRGIVDYTELPLVSVDFNHDPHSAIVDGTQTRVSGAHLVKTLVWCDNEW 317
|
....*...
gi 47085833 319 GYSHRVAD 326
Cdd:TIGR01532 318 GFANRMLD 325
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
152-317 |
4.02e-87 |
|
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: 259.09 E-value: 4.02e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 152 CTTNCLAPLAKVIHDNFGIEEALMTTVHAYTATQKTVDGPSAKAWRDGRGAHQNIIPASTGAAKAVGKVIPELNGKLTGM 231
Cdd:cd18123 1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 232 AFRVPVADVSVVDLTCRLTRPASYANIKESVKKAAHGpmKGILGYTEDSVVSSDFVGDTHSSIFDAGAGISLNDNFVKLI 311
Cdd:cd18123 81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLM 158
|
....*.
gi 47085833 312 SWYDNE 317
Cdd:cd18123 159 QWYDNE 164
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
6-332 |
1.30e-85 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 261.53 E-value: 1.30e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 6 VGINGFGRIGRLVLRACLQKG----IKVTAINDpFIDLQYMVYMFKYDSTHGRYKGEVHMEDGKLIVDGQAISVFQCMKP 81
Cdd:PRK13535 4 VAINGFGRIGRNVLRALYESGrraeITVVAINE-LADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHERDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 82 AEIPWGDAGALYVVESTGVFLSIEKASAHIQGGAKRVVVSAPSP---DAPMfVMGVNQDKYDPSSmTIVSNASCTTNCLA 158
Cdd:PRK13535 83 ASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSndlDATV-VYGVNHDQLRAEH-RIVSNASCTTNCII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 159 PLAKVIHDNFGIEEALMTTVHAYTATQKTVDGpSAKAWRDGRGAHQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVA 238
Cdd:PRK13535 161 PVIKLLDDAFGIESGTVTTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPTI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 239 DVSVVDLTCRLTRPASYANIKESVKKAAHGPMKGILGYTEDSVVSSDFVGDTHSSIFDAGAGISLNDNFVKLISWYDNEF 318
Cdd:PRK13535 240 NVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNEW 319
|
330
....*....|....
gi 47085833 319 GYSHRVADLLMYMH 332
Cdd:PRK13535 320 GFANRMLDTTLAMA 333
|
|
| GAPDH_I_N |
cd05214 |
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
6-151 |
5.45e-84 |
|
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; GAPDH plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (EC 1.2.1.59). The family corresponds to the ubiquitous NAD+ or NADP+ utilizing type I GAPDH and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose.
Pssm-ID: 467614 [Multi-domain] Cd Length: 164 Bit Score: 250.77 E-value: 5.45e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 6 VGINGFGRIGRLVLRACLQK-GIKVTAINDPFIDlQYMVYMFKYDSTHGRYKGEVHMEDGKLIVDGQAISVFQCMKPAEI 84
Cdd:cd05214 3 VGINGFGRIGRLVFRAALERdDIEVVAINDLTDD-ETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAEL 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47085833 85 PWGDAGALYVVESTGVFLSIEKASAHIQGGAKRVVVSAPSPD-APMFVMGVNQDKYDPsSMTIVSNAS 151
Cdd:cd05214 82 PWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDA-DDKIISNAS 148
|
|
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
10-331 |
1.11e-79 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 250.61 E-value: 1.11e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 10 GFGRIGRLVLRACLQK-----GIKVTAI-----NDPfiDLQYMVYMFKYDSTHGRYKG--EVHMEDGKLIVDGQAISVFQ 77
Cdd:PRK08289 134 GFGRIGRLLARLLIEKtgggnGLRLRAIvvrkgSEG--DLEKRASLLRRDSVHGPFNGtiTVDEENNAIIANGNYIQVIY 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 78 CMKPAEIPWGDAG---ALyVVESTGVFLSIEKASAHIQG-GAKRVVVSAPSP-DAPMFVMGVNQDKYDPSSmTIVSNASC 152
Cdd:PRK08289 212 ANSPEEVDYTAYGinnAL-VVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGKgDIKNIVHGVNHSDITDED-KIVSAASC 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 153 TTNCLAPLAKVIHDNFGIEEALMTTVHAYTATQKTVDGpSAKAWRDGRGAHQNIIPASTGAAKAVGKVIPELNGKLTGMA 232
Cdd:PRK08289 290 TTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDN-YHKGDRRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNA 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 233 FRVPVADVSVVDLTCRLTRPASYANIKESVKKAA-HGPMKGILGYTEDS-VVSSDFVGDTHSSIFDAGAGISLNDNFVkL 310
Cdd:PRK08289 369 IRVPTPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQIDYTDSTeVVSSDFVGSRHAGVVDSQATIVNGNRAV-L 447
|
330 340
....*....|....*....|.
gi 47085833 311 ISWYDNEFGYSHRVADLLMYM 331
Cdd:PRK08289 448 YVWYDNEFGYSCQVVRVMEQM 468
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
6-152 |
2.68e-73 |
|
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: 223.20 E-value: 2.68e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 6 VGINGFGRIGRLVLRACL-QKGIKVTAINDPfIDLQYMVYMFKYDSTHGRYKGEVHMEDGKLIVDGQAISVFQCMKPAEI 84
Cdd:smart00846 3 VGINGFGRIGRLVLRAALeRPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANL 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47085833 85 PWGDAGALYVVESTGVFLSIEKASAHIQGGAKRVVVSAPSPDA-PMFVMGVNQDKYDPsSMTIVSNASC 152
Cdd:smart00846 82 PWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDG-EDHIISNASC 149
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
4-333 |
1.44e-55 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 184.31 E-value: 1.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 4 LCVGINGFGRIGRLVLRACL-QKGIKVTAINDPFIDLQYMVYMFKYDSTHGRYKGEVHMEDGKLIV--DGQAISVFQCMK 80
Cdd:PTZ00353 3 ITVGINGFGPVGKAVLFASLtDPLVTVVAVNDASVSIAYIAYVLEQESPLSAPDGASIRVVGEQIVlnGTQKIRVSAKHD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 81 PAEIPWGDAGALYVVESTGVFLSIEKASAHIQGGAKRVVVSAPSPDAPMFVMGVNQDKYDpSSMTIVSNASCTTNCLAPL 160
Cdd:PTZ00353 83 LVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDERLS-ASLPVCCAGAPIAVALAPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 161 AKVIHDNFGIEEALMTTVHAyTATQKTVDGPSAKA--WRDGRGAHQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVA 238
Cdd:PTZ00353 162 IRALHEVYGVEECSYTAIHG-MQPQEPIAARSKNSqdWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 239 DVSVVDLTCRLTRPASYANIKESVKKAAHGPMKGILGYTEDSVVSSDFVGDThSSIFDAGAGISLNDNFV-KLISWYDNE 317
Cdd:PTZ00353 241 KGCAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCIPNG-KLCYDATSSSSSREGEVhKMVLWFDVE 319
|
330
....*....|....*.
gi 47085833 318 FGYSHRVADLLMYMHS 333
Cdd:PTZ00353 320 CYYAARLLSLVKQLHQ 335
|
|
| Gp_dh_N |
pfam00044 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
6-103 |
1.74e-47 |
|
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: 155.34 E-value: 1.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 6 VGINGFGRIGRLVLRACL-QKGIKVTAINDpFIDLQYMVYMFKYDSTHGRYKGEVHMEDGKLIVDGQAISVFQCMKPAEI 84
Cdd:pfam00044 3 VGINGFGRIGRLVLRAALeRPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAEL 81
|
90
....*....|....*....
gi 47085833 85 PWGDAGALYVVESTGVFLS 103
Cdd:pfam00044 82 PWGDLGVDVVIESTGVFTT 100
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
152-317 |
1.48e-46 |
|
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: 155.37 E-value: 1.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 152 CTTNCLAPLAKVIHDNFGIEEALMTTVHAYTATQKTVDGPSAKAWrdGRGAHQNIIPASTGAAKAVGKVIPELN--GKLT 229
Cdd:cd18122 1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIGkpIKVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 230 GMAFRVPVADVSVVDLTCRLTRPASYANIKESVKKAAHGPMKGILGYTEDSVVSSDFVGDTHSSIFDAGAGISLNDNFVK 309
Cdd:cd18122 79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLK 158
|
....*...
gi 47085833 310 LISWYDNE 317
Cdd:cd18122 159 VFSAVDNE 166
|
|
| GAPDH_N_E4PDH |
cd17892 |
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
6-151 |
3.79e-46 |
|
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: 154.35 E-value: 3.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 6 VGINGFGRIGRLVLRACL----QKGIKVTAINDPfIDLQYMVYMFKYDSTHGRYKGEVHMEDGKLIVDGQAISVFQCMKP 81
Cdd:cd17892 3 VAINGYGRIGRNVLRALYesgrRAEFQVVAINEL-ADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPDP 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47085833 82 AEIPWGDAGALYVVESTGVFLSIEKASAHIQGGAKRVVVSAPSP---DAPMfVMGVNQDKYDPsSMTIVSNAS 151
Cdd:cd17892 82 ENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASndvDATI-VYGINQDLLRA-EHRIVSNAS 152
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| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
152-317 |
2.09e-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: 147.18 E-value: 2.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 152 CTTNCLAPLAKVIHDNFGIEEALMTTVHAYTATQKTVDGpSAKAWRDGRGAHQNIIPASTGAAKAVGKVIPELNGKLTGM 231
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAI 79
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 232 AFRVPVADVSVVDLTCRLTRPASYANIKESVKKAAHGPMKGILGYTEDSVVSSDFVGDTHSSIFDAGAGISLNDNFVKLI 311
Cdd:cd23937 80 AVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLL 159
|
....*.
gi 47085833 312 SWYDNE 317
Cdd:cd23937 160 VWCDNE 165
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| GAPDH-like_N |
cd05192 |
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ... |
6-156 |
2.53e-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: 54.28 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47085833 6 VGINGFGRIGRLVLRACLQK-GIKVTAINDpfidlqymvymfkydsthgrykgevhMEDgklivdgqaisvfqcmkpaei 84
Cdd:cd05192 3 VAINGFGRIGRIVFRAIADQdDLDVVAIND--------------------------RRD--------------------- 35
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47085833 85 pwgdagalYVVESTGVFLSIEKASAHIQGGAKRVVVSAPSPDAPMFVMGVNQDKYDPSSMTIVSNASCTTNC 156
Cdd:cd05192 36 --------VVIECTGSFTDDDNAEKHIKAGGKKAVITAPEKGDIPTIVVVLNELAKSAGATVVSNANETSYS 99
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