|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
2-330 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 609.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 2 VKVGVNGFGRIGRLVTRAAVLSGKVQVVAINDPFIDLNYMVYMFKYDSTHGHFKGTVKA-ENGKLVINGHAITIFQERDP 80
Cdd:PLN02272 86 TKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDP 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 81 SNIKWADAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNHEKYDKSLKIVSNASCTTNCLAPLAK 160
Cdd:PLN02272 166 AEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLAK 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 161 VIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSV 240
Cdd:PLN02272 246 VVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSV 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 241 VDLTCRLEKPAKYDDIKRVVKAAADGPLKGILGYTEDQVVSCDFNGDSHSSTFDAGAGIALNDHFVKLVSWYDNEFGYSN 320
Cdd:PLN02272 326 VDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYSN 405
|
330
....*....|
gi 46048961 321 RVVDLMVHMA 330
Cdd:PLN02272 406 RVLDLIEHMA 415
|
|
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
2-333 |
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: 586.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 2 VKVGVNGFGRIGRLVTRAAVLSGK-VQVVAINDPfIDLNYMVYMFKYDSTHGHFKGTVKAENGKLVINGHAITIFQERDP 80
Cdd:COG0057 3 IRVAINGFGRIGRLVLRALLERGPdIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 81 SNIKWADAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADA-PMFVMGVNHEKYDKSLKIVSNASCTTNCLAPLA 159
Cdd:COG0057 82 AELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAPVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 160 KVIHDNFGIVEGLMTTVHAITATQKTVDGPsGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVS 239
Cdd:COG0057 162 KVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 240 VVDLTCRLEKPAKYDDIKRVVKAAADGPLKGILGYTEDQVVSCDFNGDSHSSTFDAGAGIALNDHFVKLVSWYDNEFGYS 319
Cdd:COG0057 241 LVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGYS 320
|
330
....*....|....
gi 46048961 320 NRVVDLMVHMASKE 333
Cdd:COG0057 321 NRMVDLAEYMAKLL 334
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
3-324 |
2.54e-172 |
|
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the enzyme responsible for the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. Forms exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (1.2.1.59). In some species, NAD- and NADP- utilizing forms exist, generally being responsible for reactions in the anabolic and catabolic directions respectively. Two Pfam models cover the two functional domains of this protein; pfam00044 represents the N-terminal NAD(P)-binding domain and pfam02800 represents the C-terminal catalytic domain. An additional form of gap gene is found in gamma proteobacteria and is responsible for the conversion of erythrose-4-phosphate (E4P) to 4-phospho-erythronate in the biosynthesis of pyridoxine. This pathway of pyridoxine biosynthesis appears to be limited, however, to a relatively small number of bacterial species although it is prevalent among the gamma-proteobacteria. This enzyme is described by TIGR001532. These sequences generally score between trusted and noise to this GAPDH model due to the close evolutionary relationship. There exists the possiblity that some forms of GAPDH may be bifunctional and act on E4P in species which make pyridoxine and via hydroxythreonine and lack a separate E4PDH enzyme (for instance, the GAPDH from Bacillus stearothermophilus has been shown to posess a limited E4PD activity as well as a robust GAPDH activity). There are a great number of sequences in the databases which score between trusted and noise to this model, nearly all of them due to fragmentary sequences. It seems that study of this gene has been carried out in many species utilizing PCR probes which exclude the extreme ends of the consenses used to define this model. The noise level is set relative not to E4PD, but the next closest outliers, the class II GAPDH's (found in archaea, TIGR01546) and aspartate semialdehyde dehydrogenase (ASADH, TIGR01296) both of which have highest-scoring hits around -225 to the prior model. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 273675 [Multi-domain] Cd Length: 326 Bit Score: 481.01 E-value: 2.54e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 3 KVGVNGFGRIGRLVTRAA--VLSGKVQVVAINDPfIDLNYMVYMFKYDSTHGHFKGTVKAENGKLVINGH-AITIFQERD 79
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRIleKPGNDLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKeVISVFSERD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 80 PSNIKWADAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADA-PMFVMGVNHEKYDKSLKIVSNASCTTNCLAPL 158
Cdd:TIGR01534 80 PSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLAPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 159 AKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKlWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNV 238
Cdd:TIGR01534 160 AKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKD-LRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 239 SVVDLTCRLEKPAKYDDIKRVVKAAADGPLKGILGYTEDQVVSCDFNGDSHSSTFDAGAGIA--LNDHFVKLVSWYDNEF 316
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNEW 318
|
....*...
gi 46048961 317 GYSNRVVD 324
Cdd:TIGR01534 319 GYSNRLVD 326
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
150-315 |
1.75e-122 |
|
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: 348.68 E-value: 1.75e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 150 CTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSgKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGM 229
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 230 AFRVPTPNVSVVDLTCRLEKPAKYDDIKRVVKAAADGPLKGILGYTEDQVVSCDFNGDSHSSTFDAGAGIALNDHFVKLV 309
Cdd:cd18126 80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159
|
....*.
gi 46048961 310 SWYDNE 315
Cdd:cd18126 160 AWYDNE 165
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
4-325 |
3.06e-114 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 333.82 E-value: 3.06e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 4 VGVNGFGRIGRLVTRAAVLSGKVQVVAINDPFIDLNYMVYMFKYDSTHGHFKGTVKAENGKLVINGHAITIFQERDPSNI 83
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 84 KWADaGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAP--SADAPMFVMGVNHEKYDKSL-KIVSNASCTTNCLAPLAK 160
Cdd:NF033735 81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARhRIVTAASCTTNCLAPVVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 161 VIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLwRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSV 240
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAPHKDL-RRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 241 VDLTCRLEKPAKYDDIKRVVKAAADGPLKGILGYTEDQVVSCDFNGDSHSSTFDAGAGIALNDHFVKLVSWYDNEFGYSN 320
Cdd:NF033735 239 TDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYAN 318
|
....*
gi 46048961 321 RVVDL 325
Cdd:NF033735 319 RMVDL 323
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
155-312 |
1.42e-91 |
|
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: 269.85 E-value: 1.42e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 155 LAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVP 234
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46048961 235 TPNVSVVDLTCRLEKPAKYDDIKRVVKAAADGPLKGILGYTEDQVVSCDFNGDSHSSTFDAGAGIALNDHFVKLVSWY 312
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
2-150 |
1.15e-81 |
|
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: 244.38 E-value: 1.15e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 2 VKVGVNGFGRIGRLVTRAAVLSGKVQVVAINDPfIDLNYMVYMFKYDSTHGHFKGTVKAENGKLVINGHAITIFQERDPS 81
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 82 NIKWADAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADA-PMFVMGVNHEKYDKSLKIVSNASC 150
Cdd:smart00846 80 NLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
2-330 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 609.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 2 VKVGVNGFGRIGRLVTRAAVLSGKVQVVAINDPFIDLNYMVYMFKYDSTHGHFKGTVKA-ENGKLVINGHAITIFQERDP 80
Cdd:PLN02272 86 TKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDP 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 81 SNIKWADAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNHEKYDKSLKIVSNASCTTNCLAPLAK 160
Cdd:PLN02272 166 AEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLAK 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 161 VIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSV 240
Cdd:PLN02272 246 VVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSV 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 241 VDLTCRLEKPAKYDDIKRVVKAAADGPLKGILGYTEDQVVSCDFNGDSHSSTFDAGAGIALNDHFVKLVSWYDNEFGYSN 320
Cdd:PLN02272 326 VDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYSN 405
|
330
....*....|
gi 46048961 321 RVVDLMVHMA 330
Cdd:PLN02272 406 RVLDLIEHMA 415
|
|
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
2-333 |
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: 586.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 2 VKVGVNGFGRIGRLVTRAAVLSGK-VQVVAINDPfIDLNYMVYMFKYDSTHGHFKGTVKAENGKLVINGHAITIFQERDP 80
Cdd:COG0057 3 IRVAINGFGRIGRLVLRALLERGPdIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 81 SNIKWADAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADA-PMFVMGVNHEKYDKSLKIVSNASCTTNCLAPLA 159
Cdd:COG0057 82 AELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAPVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 160 KVIHDNFGIVEGLMTTVHAITATQKTVDGPsGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVS 239
Cdd:COG0057 162 KVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 240 VVDLTCRLEKPAKYDDIKRVVKAAADGPLKGILGYTEDQVVSCDFNGDSHSSTFDAGAGIALNDHFVKLVSWYDNEFGYS 319
Cdd:COG0057 241 LVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGYS 320
|
330
....*....|....
gi 46048961 320 NRVVDLMVHMASKE 333
Cdd:COG0057 321 NRMVDLAEYMAKLL 334
|
|
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
2-333 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 517.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 2 VKVGVNGFGRIGRLVTRAAVLSGKVQVVAINDPFIDLNYMVYMFKYDSTHGHFKGTVKAENGKLVINGHAITIFQERDPS 81
Cdd:PTZ00023 3 VKLGINGFGRIGRLVFRAALEREDVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKDPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 82 NIKWADAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAP-SADAPMFVMGVNHEKYDKSLKIVSNASCTTNCLAPLAK 160
Cdd:PTZ00023 83 AIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPpKDDTPIYVMGVNHTQYDKSQRIVSNASCTTNCLAPLAK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 161 VIHDNFGIVEGLMTTVHAITATQKTVDGPS--GKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNV 238
Cdd:PTZ00023 163 VVNDKFGIVEGLMTTVHASTANQLTVDGPSkgGKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVPDV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 239 SVVDLTCRLEKPAKYDDIKRVVKAAADGPLKGILGYTEDQVVSCDFNGDSHSSTFDAGAGIALNDHFVKLVSWYDNEFGY 318
Cdd:PTZ00023 243 SVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDNEWGY 322
|
330
....*....|....*
gi 46048961 319 SNRVVDLMVHMASKE 333
Cdd:PTZ00023 323 SNRLLDLAHYITQKY 337
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
3-324 |
2.54e-172 |
|
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the enzyme responsible for the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. Forms exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (1.2.1.59). In some species, NAD- and NADP- utilizing forms exist, generally being responsible for reactions in the anabolic and catabolic directions respectively. Two Pfam models cover the two functional domains of this protein; pfam00044 represents the N-terminal NAD(P)-binding domain and pfam02800 represents the C-terminal catalytic domain. An additional form of gap gene is found in gamma proteobacteria and is responsible for the conversion of erythrose-4-phosphate (E4P) to 4-phospho-erythronate in the biosynthesis of pyridoxine. This pathway of pyridoxine biosynthesis appears to be limited, however, to a relatively small number of bacterial species although it is prevalent among the gamma-proteobacteria. This enzyme is described by TIGR001532. These sequences generally score between trusted and noise to this GAPDH model due to the close evolutionary relationship. There exists the possiblity that some forms of GAPDH may be bifunctional and act on E4P in species which make pyridoxine and via hydroxythreonine and lack a separate E4PDH enzyme (for instance, the GAPDH from Bacillus stearothermophilus has been shown to posess a limited E4PD activity as well as a robust GAPDH activity). There are a great number of sequences in the databases which score between trusted and noise to this model, nearly all of them due to fragmentary sequences. It seems that study of this gene has been carried out in many species utilizing PCR probes which exclude the extreme ends of the consenses used to define this model. The noise level is set relative not to E4PD, but the next closest outliers, the class II GAPDH's (found in archaea, TIGR01546) and aspartate semialdehyde dehydrogenase (ASADH, TIGR01296) both of which have highest-scoring hits around -225 to the prior model. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 273675 [Multi-domain] Cd Length: 326 Bit Score: 481.01 E-value: 2.54e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 3 KVGVNGFGRIGRLVTRAA--VLSGKVQVVAINDPfIDLNYMVYMFKYDSTHGHFKGTVKAENGKLVINGH-AITIFQERD 79
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRIleKPGNDLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKeVISVFSERD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 80 PSNIKWADAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADA-PMFVMGVNHEKYDKSLKIVSNASCTTNCLAPL 158
Cdd:TIGR01534 80 PSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLAPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 159 AKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKlWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNV 238
Cdd:TIGR01534 160 AKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKD-LRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 239 SVVDLTCRLEKPAKYDDIKRVVKAAADGPLKGILGYTEDQVVSCDFNGDSHSSTFDAGAGIA--LNDHFVKLVSWYDNEF 316
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNEW 318
|
....*...
gi 46048961 317 GYSNRVVD 324
Cdd:TIGR01534 319 GYSNRLVD 326
|
|
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
2-330 |
4.45e-163 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 458.42 E-value: 4.45e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 2 VKVGVNGFGRIGRLVTRAAVLSGKVQVVAINDPFIDLNYMVYMFKYDSTHGHFK-GTVKAENGKLVINGHA-ITIFQERD 79
Cdd:PLN02358 6 IRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKhHELKVKDDKTLLFGEKpVTVFGIRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 80 PSNIKWADAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNHEKYDKSLKIVSNASCTTNCLAPLA 159
Cdd:PLN02358 86 PEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCTTNCLAPLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 160 KVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVS 239
Cdd:PLN02358 166 KVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 240 VVDLTCRLEKPAKYDDIKRVVKAAADGPLKGILGYTEDQVVSCDFNGDSHSSTFDAGAGIALNDHFVKLVSWYDNEFGYS 319
Cdd:PLN02358 246 VVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEWGYS 325
|
330
....*....|.
gi 46048961 320 NRVVDLMVHMA 330
Cdd:PLN02358 326 SRVVDLIVHMS 336
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
2-330 |
1.59e-159 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 449.18 E-value: 1.59e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 2 VKVGVNGFGRIGRLVTRAAVLSGKVQVVAINDpFIDLNYMVYMFKYDSTHGHFKGTVKAENGKLVINGHAITIFQERDPS 81
Cdd:PRK15425 3 IKVGINGFGRIGRIVFRAAQKRSDIEIVAIND-LLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 82 NIKWADAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSAD-APMFVMGVNHEKYdKSLKIVSNASCTTNCLAPLAK 160
Cdd:PRK15425 82 NLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDnTPMFVKGANFDKY-AGQDIVSNASCTTNCLAPLAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 161 VIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSV 240
Cdd:PRK15425 161 VINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 241 VDLTCRLEKPAKYDDIKRVVKAAADGPLKGILGYTEDQVVSCDFNGDSHSSTFDAGAGIALNDHFVKLVSWYDNEFGYSN 320
Cdd:PRK15425 241 VDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYSN 320
|
330
....*....|
gi 46048961 321 RVVDLMVHMA 330
Cdd:PRK15425 321 KVLDLIAHIS 330
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-332 |
2.95e-138 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 395.64 E-value: 2.95e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 1 MVKVGVNGFGRIGRLVTRAAVLSGKVQVVAINDPFiDLNYMVYMFKYDSTHGHFKGTVKAENGKLVINGHAITIFQERDP 80
Cdd:PRK07729 2 KTKVAINGFGRIGRMVFRKAIKESAFEIVAINASY-PSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 81 SNIKWADAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPM-FVMGVNHEKYD-KSLKIVSNASCTTNCLAPL 158
Cdd:PRK07729 81 KELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVtIVVGVNEDQLDiEKHTIISNASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 159 AKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLwRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNV 238
Cdd:PRK07729 161 VKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHKDL-RRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 239 SVVDLTCRLEKPAKYDDIKRVVKAAADGPLKGILGYTEDQVVSCDFNGDSHSSTFDAGAGIALNDHFVKLVSWYDNEFGY 318
Cdd:PRK07729 240 SLVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEWGY 319
|
330
....*....|....
gi 46048961 319 SNRVVDLMVHMASK 332
Cdd:PRK07729 320 SCRVVDLVTLVADE 333
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
2-333 |
7.23e-134 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 385.18 E-value: 7.23e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 2 VKVGVNGFGRIGRLVTRA----AVLSGKVQVVAINDPFIDLNYMVYMFKYDSTHGHFKGTVKAENGK--------LVING 69
Cdd:PTZ00434 4 IKVGINGFGRIGRMVFQAicdqGLIGTEIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVETTKSSpsvktddvLVVNG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 70 HAITIFQ-ERDPSNIKWADAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAP-SADAPMFVMGVNHEKYD-KSLKIVS 146
Cdd:PTZ00434 84 HRIKCVKaQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPaSGGAKTIVMGVNQHEYSpTEHHVVS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 147 NASCTTNCLAPLAKVI-HDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGK 225
Cdd:PTZ00434 164 NASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 226 LTGMAFRVPTPNVSVVDLTCRLEKPAKYDDIKRVVKAAADGPLKGILGYTEDQVVSCDFNGDSHSSTFDAGAGIALN--- 302
Cdd:PTZ00434 244 LTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKATLQNNlpg 323
|
330 340 350
....*....|....*....|....*....|..
gi 46048961 303 -DHFVKLVSWYDNEFGYSNRVVDLMVHMASKE 333
Cdd:PTZ00434 324 eRRFFKIVSWYDNEWGYSHRVVDLVRYMAAKD 355
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
150-315 |
1.75e-122 |
|
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: 348.68 E-value: 1.75e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 150 CTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSgKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGM 229
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 230 AFRVPTPNVSVVDLTCRLEKPAKYDDIKRVVKAAADGPLKGILGYTEDQVVSCDFNGDSHSSTFDAGAGIALNDHFVKLV 309
Cdd:cd18126 80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159
|
....*.
gi 46048961 310 SWYDNE 315
Cdd:cd18126 160 AWYDNE 165
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
1-332 |
2.28e-118 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 344.97 E-value: 2.28e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 1 MVKVGVNGFGRIGRLVTRAAV--LSGKVQVVAINDPfIDLNYMVYMFKYDSTHGHFKGTVKAENGKLVINGHAITIFQER 78
Cdd:PRK07403 1 MIRVAINGFGRIGRNFLRCWLgrENSQLELVAINDT-SDPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 79 DPSNIKWADAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAP--SADAPMFVMGVNHEKYDKSL-KIVSNASCTTNCL 155
Cdd:PRK07403 80 NPLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPgkGEDIGTYVVGVNHHEYDHEDhNIISNASCTTNCL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 156 APLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLwRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPT 235
Cdd:PRK07403 160 APIAKVLHDNFGIIKGTMTTTHSYTGDQRILDASHRDL-RRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 236 PNVSVVDLTCRLEKPAKYDDIKRVVKAAADGPLKGILGYTEDQVVSCDFNGDSHSSTFDAGAGIALNDHFVKLVSWYDNE 315
Cdd:PRK07403 239 PNVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYDNE 318
|
330
....*....|....*..
gi 46048961 316 FGYSNRVVDLMVHMASK 332
Cdd:PRK07403 319 WGYSQRVVDLAELVARK 335
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
4-325 |
3.06e-114 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 333.82 E-value: 3.06e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 4 VGVNGFGRIGRLVTRAAVLSGKVQVVAINDPFIDLNYMVYMFKYDSTHGHFKGTVKAENGKLVINGHAITIFQERDPSNI 83
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 84 KWADaGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAP--SADAPMFVMGVNHEKYDKSL-KIVSNASCTTNCLAPLAK 160
Cdd:NF033735 81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARhRIVTAASCTTNCLAPVVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 161 VIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLwRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSV 240
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAPHKDL-RRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 241 VDLTCRLEKPAKYDDIKRVVKAAADGPLKGILGYTEDQVVSCDFNGDSHSSTFDAGAGIALNDHFVKLVSWYDNEFGYSN 320
Cdd:NF033735 239 TDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYAN 318
|
....*
gi 46048961 321 RVVDL 325
Cdd:NF033735 319 RMVDL 323
|
|
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
2-326 |
4.36e-106 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 313.59 E-value: 4.36e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 2 VKVGVNGFGRIGRLVTRAAVLSGKVQVVAINDPFIDLNYMVYMFKYDSTHGHFKGTVKAENGKLVINGHAITIFQERDPS 81
Cdd:PRK08955 3 IKVGINGFGRIGRLALRAAWDWPELEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKAIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 82 NIKWAdaGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMF--VMGVNHEKYDKSL-KIVSNASCTTNCLAPL 158
Cdd:PRK08955 83 DTDWS--GCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLniVMGVNDHLFDPAIhPIVTAASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 159 AKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLwRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNV 238
Cdd:PRK08955 161 VKVIHEKLGIKHGSMTTIHDLTNTQTILDAPHKDL-RRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLANA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 239 SVVDLTCRLEKPAKYDDIKRVVKAAADGPLKGILGYTEDQVVSCDFNGDSHSSTFDAGAGIALNDHFVKLVSWYDNEFGY 318
Cdd:PRK08955 240 SLTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNEWGY 319
|
....*...
gi 46048961 319 SNRVVDLM 326
Cdd:PRK08955 320 ANRTAELA 327
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
2-332 |
3.28e-104 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 312.61 E-value: 3.28e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 2 VKVGVNGFGRIGRLVTRA--AVLSGKVQVVAINDPFIDLNyMVYMFKYDSTHGHFKGTVK-AENGKLVINGHAITIFQER 78
Cdd:PLN02237 76 LKVAINGFGRIGRNFLRCwhGRKDSPLDVVVVNDSGGVKN-ASHLLKYDSMLGTFKADVKiVDDETISVDGKPIKVVSNR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 79 DPSNIKWADAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPS--ADAPMFVMGVNHEKYDKSL-KIVSNASCTTNCL 155
Cdd:PLN02237 155 DPLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAkgADIPTYVVGVNEDDYDHEVaNIVSNASCTTNCL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 156 APLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLwRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPT 235
Cdd:PLN02237 235 APFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDASHRDL-RRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPT 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 236 PNVSVVDLTCRLEKPA-KYDDIKRVVKAAADGPLKGILGYTEDQVVSCDFNGDSHSSTFDAGAGIALNDHFVKLVSWYDN 314
Cdd:PLN02237 314 PNVSVVDLVVNVEKKGiTAEDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVAWYDN 393
|
330
....*....|....*...
gi 46048961 315 EFGYSNRVVDLMVHMASK 332
Cdd:PLN02237 394 EWGYSQRVVDLAHLVAAK 411
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
2-332 |
7.94e-104 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 309.94 E-value: 7.94e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 2 VKVGVNGFGRIGRLVTRA--AVLSGKVQVVAINDPFiDLNYMVYMFKYDSTHGHFKGTVKAE-NGKLVINGHAITIFQER 78
Cdd:PLN03096 61 IKVAINGFGRIGRNFLRCwhGRKDSPLDVVAINDTG-GVKQASHLLKYDSTLGTFDADVKPVgDDAISVDGKVIKVVSDR 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 79 DPSNIKWADAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPS-ADAPMFVMGVNHEKYDKSLKIVSNASCTTNCLAP 157
Cdd:PLN03096 140 NPLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGkGDIPTYVVGVNADDYKHSDPIISNASCTTNCLAP 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 158 LAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLwRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPN 237
Cdd:PLN03096 220 FVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDL-RRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPN 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 238 VSVVDLTCRLEKPAKYDDIKRVVKAAADGPLKGILGYTEDQVVSCDFNGDSHSSTFDAGAGIALNDHFVKLVSWYDNEFG 317
Cdd:PLN03096 299 VSVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAWYDNEWG 378
|
330
....*....|....*
gi 46048961 318 YSNRVVDLMVHMASK 332
Cdd:PLN03096 379 YSQRVVDLADIVANK 393
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
1-330 |
2.63e-100 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 298.89 E-value: 2.63e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 1 MVKVGVNGFGRIGRLVTRAAVLSGK---VQVVAINDpFIDLNYMVYMFKYDSTHGHFKGTVKAENGKLVINGHAITIFQE 77
Cdd:PRK13535 1 TIRVAINGFGRIGRNVLRALYESGRraeITVVAINE-LADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 78 RDPSNIKWADAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSA---DAPMfVMGVNHEKYDKSLKIVSNASCTTNC 154
Cdd:PRK13535 80 RDIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSndlDATV-VYGVNHDQLRAEHRIVSNASCTTNC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 155 LAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLwRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVP 234
Cdd:PRK13535 159 IIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHPDL-RRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 235 TPNVSVVDLTCRLEKPAKYDDIKRVVKAAADGPLKGILGYTEDQVVSCDFNGDSHSSTFDAGAGIALNDHFVKLVSWYDN 314
Cdd:PRK13535 238 TINVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDN 317
|
330
....*....|....*.
gi 46048961 315 EFGYSNRVVDLMVHMA 330
Cdd:PRK13535 318 EWGFANRMLDTTLAMA 333
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
150-315 |
5.53e-92 |
|
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: 271.41 E-value: 5.53e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 150 CTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGM 229
Cdd:cd18123 1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 230 AFRVPTPNVSVVDLTCRLEKPAKYDDIKRVVKAAADGplKGILGYTEDQVVSCDFNGDSHSSTFDAGAGIALNDHFVKLV 309
Cdd:cd18123 81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLM 158
|
....*.
gi 46048961 310 SWYDNE 315
Cdd:cd18123 159 QWYDNE 164
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
155-312 |
1.42e-91 |
|
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: 269.85 E-value: 1.42e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 155 LAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVP 234
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46048961 235 TPNVSVVDLTCRLEKPAKYDDIKRVVKAAADGPLKGILGYTEDQVVSCDFNGDSHSSTFDAGAGIALNDHFVKLVSWY 312
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| GAPDH_I_N |
cd05214 |
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
2-149 |
2.46e-90 |
|
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: 266.95 E-value: 2.46e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 2 VKVGVNGFGRIGRLVTRAAVLSGKVQVVAINDPFIDlNYMVYMFKYDSTHGHFKGTVKAENGKLVINGHAITIFQERDPS 81
Cdd:cd05214 1 IKVGINGFGRIGRLVFRAALERDDIEVVAINDLTDD-ETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPA 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46048961 82 NIKWADAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSAD-APMFVMGVNHEKYDKSLKIVSNAS 149
Cdd:cd05214 80 ELPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDADDKIISNAS 148
|
|
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
8-330 |
2.06e-85 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 265.25 E-value: 2.06e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 8 GFGRIGRLVTRAAV----LSGKVQVVAI---NDPFIDLNYMVYMFKYDSTHGHFKGTVKA--ENGKLVINGHAITIFQER 78
Cdd:PRK08289 134 GFGRIGRLLARLLIektgGGNGLRLRAIvvrKGSEGDLEKRASLLRRDSVHGPFNGTITVdeENNAIIANGNYIQVIYAN 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 79 DPSNIKWADAGAE--YVVESTGVFTTMEKAGAHLKG-GAKRVIISAPS-ADAPMFVMGVNHEKYDKSLKIVSNASCTTNC 154
Cdd:PRK08289 214 SPEEVDYTAYGINnaLVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGkGDIKNIVHGVNHSDITDEDKIVSAASCTTNA 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 155 LAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSgKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVP 234
Cdd:PRK08289 294 ITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYH-KGDRRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNAIRVP 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 235 TPNVSVVDLTCRLEKPAKYDDIKRVVKAAA-DGPLKGILGYTEDQ-VVSCDFNGDSHSSTFDAGAGIALNDHFVkLVSWY 312
Cdd:PRK08289 373 TPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQIDYTDSTeVVSSDFVGSRHAGVVDSQATIVNGNRAV-LYVWY 451
|
330
....*....|....*...
gi 46048961 313 DNEFGYSNRVVDLMVHMA 330
Cdd:PRK08289 452 DNEFGYSCQVVRVMEQMA 469
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
2-150 |
1.15e-81 |
|
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: 244.38 E-value: 1.15e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 2 VKVGVNGFGRIGRLVTRAAVLSGKVQVVAINDPfIDLNYMVYMFKYDSTHGHFKGTVKAENGKLVINGHAITIFQERDPS 81
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 82 NIKWADAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADA-PMFVMGVNHEKYDKSLKIVSNASC 150
Cdd:smart00846 80 NLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
2-329 |
4.27e-60 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 195.86 E-value: 4.27e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 2 VKVGVNGFGRIGRLVTRAAVLSGKVQVVAINDPFIDLNYMVYMFKYDSTHGHFKGT-VKAENGKLVING-HAITIFQERD 79
Cdd:PTZ00353 3 ITVGINGFGPVGKAVLFASLTDPLVTVVAVNDASVSIAYIAYVLEQESPLSAPDGAsIRVVGEQIVLNGtQKIRVSAKHD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 80 PSNIKWADAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNHEKYDKSLKIVSNASCTTNCLAPLA 159
Cdd:PTZ00353 83 LVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDERLSASLPVCCAGAPIAVALAPVI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 160 KVIHDNFGIVEGLMTTVHAITATQKT-VDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNV 238
Cdd:PTZ00353 163 RALHEVYGVEECSYTAIHGMQPQEPIaARSKNSQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVKKG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 239 SVVDLTCRLEKPAKYDDIKRVVKAAADGPLKGILGYTEDQVVSCDFNGDShSSTFDAGAGIALNDHFV-KLVSWYDNEFG 317
Cdd:PTZ00353 243 CAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCIPNG-KLCYDATSSSSSREGEVhKMVLWFDVECY 321
|
330
....*....|..
gi 46048961 318 YSNRVVDLMVHM 329
Cdd:PTZ00353 322 YAARLLSLVKQL 333
|
|
| Gp_dh_N |
pfam00044 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
2-102 |
1.64e-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: 168.43 E-value: 1.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 2 VKVGVNGFGRIGRLVTRAAVLSGKVQVVAINDpFIDLNYMVYMFKYDSTHGHFKGTVKAENGKLVINGHAITIFQERDPS 81
Cdd:pfam00044 1 VKVGINGFGRIGRLVLRAALERPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPA 79
|
90 100
....*....|....*....|.
gi 46048961 82 NIKWADAGAEYVVESTGVFTT 102
Cdd:pfam00044 80 ELPWGDLGVDVVIESTGVFTT 100
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
150-315 |
9.03e-51 |
|
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: 166.05 E-value: 9.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 150 CTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLwRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGM 229
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDAYHPDL-RRTRAASQSIIPVDTKLARGIERILPHLAGRFEAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 230 AFRVPTPNVSVVDLTCRLEKPAKYDDIKRVVKAAADGPLKGILGYTEDQVVSCDFNGDSHSSTFDAGAGIALNDHFVKLV 309
Cdd:cd23937 80 AVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLL 159
|
....*.
gi 46048961 310 SWYDNE 315
Cdd:cd23937 160 VWCDNE 165
|
|
| GAPDH_N_E4PDH |
cd17892 |
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
2-149 |
2.89e-50 |
|
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: 164.75 E-value: 2.89e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 2 VKVGVNGFGRIGRLVTRAAVLSGK---VQVVAINDPfIDLNYMVYMFKYDSTHGHFKGTVKAENGKLVINGHAITIFQER 78
Cdd:cd17892 1 YRVAINGYGRIGRNVLRALYESGRraeFQVVAINEL-ADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEP 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46048961 79 DPSNIKWADAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSA---DAPMfVMGVNHEKYDKSLKIVSNAS 149
Cdd:cd17892 80 DPENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASndvDATI-VYGINQDLLRAEHRIVSNAS 152
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
150-315 |
9.71e-47 |
|
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: 155.76 E-value: 9.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 150 CTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWrdGRGAAQNIIPASTGAAKAVGKVIPELN--GKLT 227
Cdd:cd18122 1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIGkpIKVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46048961 228 GMAFRVPTPNVSVVDLTCRLEKPAKYDDIKRVVKAAADGPLKGILGYTEDQVVSCDFNGDSHSSTFDAGAGIALNDHFVK 307
Cdd:cd18122 79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLK 158
|
....*...
gi 46048961 308 LVSWYDNE 315
Cdd:cd18122 159 VFSAVDNE 166
|
|
| GAPDH-like_N |
cd05192 |
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ... |
2-154 |
2.79e-11 |
|
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: 59.67 E-value: 2.79e-11
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gi 46048961 2 VKVGVNGFGRIGRLVTRAAVLSGKVQVVAINDPfidlnymvymfkydsthghfkgtvkaengklvinghaitifqerdps 81
Cdd:cd05192 1 IRVAINGFGRIGRIVFRAIADQDDLDVVAINDR----------------------------------------------- 33
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gi 46048961 82 nikwadagAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPS-ADAPMFVMGVNHEKYDKSLKIVSNASCTTNC 154
Cdd:cd05192 34 --------RDVVIECTGSFTDDDNAEKHIKAGGKKAVITAPEkGDIPTIVVVLNELAKSAGATVVSNANETSYS 99
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