|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
3-338 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 569.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 3 KPSVGINGFGRIGRLVLRAAVEKDSVNVVAVNDPFISIDYMVYLFQYDSTHGRFKGTVAHEGDYLLvakEGKSQhKIKVY 82
Cdd:PLN02272 85 KTKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVVDDSTL---EINGK-QIKVT 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 83 NSRDPAEIQWGASGADYVVESTGVFTTIEKANAHLKGGAKKVIISAPSADAPMFVVGVNHEKYDhANDHIISNASCTTNC 162
Cdd:PLN02272 161 SKRDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYK-PNMNIVSNASCTTNC 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 163 LAPLAKVINDNFGIIEGLMTTVHAVTATQKTVDGPSGKLWRDGRGAGQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVP 242
Cdd:PLN02272 240 LAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVP 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 243 TPDVSVVDLTARLEKPASLDDIKKVIKAAADGPMKGILAYTEDQVVSTDFVSDTNSSIFDAGASISLNPHFVKLVSWYDN 322
Cdd:PLN02272 320 TPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDN 399
|
330
....*....|....*.
gi 1845979520 323 EFGYSNRVVDLISYIA 338
Cdd:PLN02272 400 EWGYSNRVLDLIEHMA 415
|
|
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
6-340 |
0e+00 |
|
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]; Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 439827 [Multi-domain] Cd Length: 334 Bit Score: 562.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 6 VGINGFGRIGRLVLRAAVEK-DSVNVVAVNDPfISIDYMVYLFQYDSTHGRFKGTVAHEGDYLLVAkegksQHKIKVYNS 84
Cdd:COG0057 5 VAINGFGRIGRLVLRALLERgPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVN-----GKKIKVLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 85 RDPAEIQWGASGADYVVESTGVFTTIEKANAHLKGGAKKVIISAPSADA-PMFVVGVNHEKYDhANDHIISNASCTTNCL 163
Cdd:COG0057 79 RDPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYD-ADHRIISNASCTTNCL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 164 APLAKVINDNFGIIEGLMTTVHAVTATQKTVDGPSGKlWRDGRGAGQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPT 243
Cdd:COG0057 158 APVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKD-LRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 244 PDVSVVDLTARLEKPASLDDIKKVIKAAADGPMKGILAYTEDQVVSTDFVSDTNSSIFDAGASISLNPHFVKLVSWYDNE 323
Cdd:COG0057 237 PNVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNE 316
|
330
....*....|....*..
gi 1845979520 324 FGYSNRVVDLISYIATK 340
Cdd:COG0057 317 WGYSNRMVDLAEYMAKL 333
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
6-332 |
7.35e-165 |
|
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: 462.52 E-value: 7.35e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 6 VGINGFGRIGRLVLRAAVEKDS--VNVVAVNDPfISIDYMVYLFQYDSTHGRFKGTVAHEGDYLLVakegKSQHKIKVYN 83
Cdd:TIGR01534 2 VGINGFGRIGRLVLRRILEKPGndLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVV----NGKEVISVFS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 84 SRDPAEIQWGASGADYVVESTGVFTTIEKANAHLKGGAKKVIISAPSADA-PMFVVGVNHEKYDHaNDHIISNASCTTNC 162
Cdd:TIGR01534 77 ERDPSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDG-EERIISNASCTTNC 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 163 LAPLAKVINDNFGIIEGLMTTVHAVTATQKTVDGPSGKlWRDGRGAGQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVP 242
Cdd:TIGR01534 156 LAPLAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKD-LRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 243 TPDVSVVDLTARLEKPASLDDIKKVIKAAADGPMKGILAYTEDQVVSTDFVSDTNSSIFDAGASI--SLNPHFVKLVSWY 320
Cdd:TIGR01534 235 TPNVSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKvtGLGDSLVKVYAWY 314
|
330
....*....|..
gi 1845979520 321 DNEFGYSNRVVD 332
Cdd:TIGR01534 315 DNEWGYSNRLVD 326
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
158-323 |
1.38e-117 |
|
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: 336.35 E-value: 1.38e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 158 CTTNCLAPLAKVINDNFGIIEGLMTTVHAVTATQKTVDGPSgKLWRDGRGAGQNIIPASTGAAKAVGKVIPELNGKLTGM 237
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 238 AFRVPTPDVSVVDLTARLEKPASLDDIKKVIKAAADGPMKGILAYTEDQVVSTDFVSDTNSSIFDAGASISLNPHFVKLV 317
Cdd:cd18126 80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159
|
....*.
gi 1845979520 318 SWYDNE 323
Cdd:cd18126 160 AWYDNE 165
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
6-333 |
2.80e-115 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 336.91 E-value: 2.80e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 6 VGINGFGRIGRLVLRAAVEKDSVNVVAVNDPFISIDYMVYLFQYDSTHGRFKGTVAHEGDYLLVAkegksQHKIKVYNSR 85
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVID-----GKRISFSSNK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 86 DPAEIQWGAsGADYVVESTGVFTTIEKANAHLKGGAKKVIISAP--SADAPMFVVGVNHEKYDHANDHIISNASCTTNCL 163
Cdd:NF033735 76 DIEDTPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARHRIVTAASCTTNCL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 164 APLAKVINDNFGIIEGLMTTVHAVTATQKTVDGPSGKLwRDGRGAGQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPT 243
Cdd:NF033735 155 APVVKVIHEKIGIKHGSITTIHDITNTQTIVDAPHKDL-RRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 244 PDVSVVDLTARLEKPASLDDIKKVIKAAADGPMKGILAYTEDQVVSTDFVSDTNSSIFDAGASISLNPHFVKLVSWYDNE 323
Cdd:NF033735 234 LNASLTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNE 313
|
330
....*....|
gi 1845979520 324 FGYSNRVVDL 333
Cdd:NF033735 314 WGYANRMVDL 323
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
163-320 |
1.74e-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: 264.84 E-value: 1.74e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 163 LAPLAKVINDNFGIIEGLMTTVHAVTATQKTVDGPSGKLWRDGRGAGQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVP 242
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1845979520 243 TPDVSVVDLTARLEKPASLDDIKKVIKAAADGPMKGILAYTEDQVVSTDFVSDTNSSIFDAGASISLNPHFVKLVSWY 320
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
6-158 |
3.98e-75 |
|
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: 228.20 E-value: 3.98e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 6 VGINGFGRIGRLVLRAAVEKDSVNVVAVNDPfISIDYMVYLFQYDSTHGRFKGTVAHEGDYLLVAKegksqHKIKVYNSR 85
Cdd:smart00846 3 VGINGFGRIGRLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNG-----KAIKVFAER 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1845979520 86 DPAEIQWGASGADYVVESTGVFTTIEKANAHLKGGAKKVIISAPSADA-PMFVVGVNHEKYDhANDHIISNASC 158
Cdd:smart00846 77 DPANLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYD-GEDHIISNASC 149
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
3-338 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 569.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 3 KPSVGINGFGRIGRLVLRAAVEKDSVNVVAVNDPFISIDYMVYLFQYDSTHGRFKGTVAHEGDYLLvakEGKSQhKIKVY 82
Cdd:PLN02272 85 KTKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVVDDSTL---EINGK-QIKVT 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 83 NSRDPAEIQWGASGADYVVESTGVFTTIEKANAHLKGGAKKVIISAPSADAPMFVVGVNHEKYDhANDHIISNASCTTNC 162
Cdd:PLN02272 161 SKRDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYK-PNMNIVSNASCTTNC 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 163 LAPLAKVINDNFGIIEGLMTTVHAVTATQKTVDGPSGKLWRDGRGAGQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVP 242
Cdd:PLN02272 240 LAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVP 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 243 TPDVSVVDLTARLEKPASLDDIKKVIKAAADGPMKGILAYTEDQVVSTDFVSDTNSSIFDAGASISLNPHFVKLVSWYDN 322
Cdd:PLN02272 320 TPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDN 399
|
330
....*....|....*.
gi 1845979520 323 EFGYSNRVVDLISYIA 338
Cdd:PLN02272 400 EWGYSNRVLDLIEHMA 415
|
|
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
6-340 |
0e+00 |
|
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]; Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 439827 [Multi-domain] Cd Length: 334 Bit Score: 562.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 6 VGINGFGRIGRLVLRAAVEK-DSVNVVAVNDPfISIDYMVYLFQYDSTHGRFKGTVAHEGDYLLVAkegksQHKIKVYNS 84
Cdd:COG0057 5 VAINGFGRIGRLVLRALLERgPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVN-----GKKIKVLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 85 RDPAEIQWGASGADYVVESTGVFTTIEKANAHLKGGAKKVIISAPSADA-PMFVVGVNHEKYDhANDHIISNASCTTNCL 163
Cdd:COG0057 79 RDPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYD-ADHRIISNASCTTNCL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 164 APLAKVINDNFGIIEGLMTTVHAVTATQKTVDGPSGKlWRDGRGAGQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPT 243
Cdd:COG0057 158 APVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKD-LRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 244 PDVSVVDLTARLEKPASLDDIKKVIKAAADGPMKGILAYTEDQVVSTDFVSDTNSSIFDAGASISLNPHFVKLVSWYDNE 323
Cdd:COG0057 237 PNVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNE 316
|
330
....*....|....*..
gi 1845979520 324 FGYSNRVVDLISYIATK 340
Cdd:COG0057 317 WGYSNRMVDLAEYMAKL 333
|
|
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
6-340 |
4.91e-177 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 493.97 E-value: 4.91e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 6 VGINGFGRIGRLVLRAAVEKDSVNVVAVNDPFISIDYMVYLFQYDSTHGRFKGTVAHEGDYLLVAKEgksqhKIKVYNSR 85
Cdd:PTZ00023 5 LGINGFGRIGRLVFRAALEREDVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSK-----KVHVFFEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 86 DPAEIQWGASGADYVVESTGVFTTIEKANAHLKGGAKKVIISAP-SADAPMFVVGVNHEKYDhANDHIISNASCTTNCLA 164
Cdd:PTZ00023 80 DPAAIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPpKDDTPIYVMGVNHTQYD-KSQRIVSNASCTTNCLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 165 PLAKVINDNFGIIEGLMTTVHAVTATQKTVDGPS--GKLWRDGRGAGQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVP 242
Cdd:PTZ00023 159 PLAKVVNDKFGIVEGLMTTVHASTANQLTVDGPSkgGKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 243 TPDVSVVDLTARLEKPASLDDIKKVIKAAADGPMKGILAYTEDQVVSTDFVSDTNSSIFDAGASISLNPHFVKLVSWYDN 322
Cdd:PTZ00023 239 VPDVSVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDN 318
|
330
....*....|....*...
gi 1845979520 323 EFGYSNRVVDLISYIATK 340
Cdd:PTZ00023 319 EWGYSNRLLDLAHYITQK 336
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
6-332 |
7.35e-165 |
|
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: 462.52 E-value: 7.35e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 6 VGINGFGRIGRLVLRAAVEKDS--VNVVAVNDPfISIDYMVYLFQYDSTHGRFKGTVAHEGDYLLVakegKSQHKIKVYN 83
Cdd:TIGR01534 2 VGINGFGRIGRLVLRRILEKPGndLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVV----NGKEVISVFS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 84 SRDPAEIQWGASGADYVVESTGVFTTIEKANAHLKGGAKKVIISAPSADA-PMFVVGVNHEKYDHaNDHIISNASCTTNC 162
Cdd:TIGR01534 77 ERDPSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDG-EERIISNASCTTNC 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 163 LAPLAKVINDNFGIIEGLMTTVHAVTATQKTVDGPSGKlWRDGRGAGQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVP 242
Cdd:TIGR01534 156 LAPLAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKD-LRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 243 TPDVSVVDLTARLEKPASLDDIKKVIKAAADGPMKGILAYTEDQVVSTDFVSDTNSSIFDAGASI--SLNPHFVKLVSWY 320
Cdd:TIGR01534 235 TPNVSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKvtGLGDSLVKVYAWY 314
|
330
....*....|..
gi 1845979520 321 DNEFGYSNRVVD 332
Cdd:TIGR01534 315 DNEWGYSNRLVD 326
|
|
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
3-338 |
2.35e-153 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 434.15 E-value: 2.35e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 3 KPSVGINGFGRIGRLVLRAAVEKDSVNVVAVNDPFISIDYMVYLFQYDSTHGRFKGT---VAHEGDYLLvakegkSQHKI 79
Cdd:PLN02358 5 KIRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKHHelkVKDDKTLLF------GEKPV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 80 KVYNSRDPAEIQWGASGADYVVESTGVFTTIEKANAHLKGGAKKVIISAPSADAPMFVVGVNHEKYDHANDhIISNASCT 159
Cdd:PLN02358 79 TVFGIRNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLD-IVSNASCT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 160 TNCLAPLAKVINDNFGIIEGLMTTVHAVTATQKTVDGPSGKLWRDGRGAGQNIIPASTGAAKAVGKVIPELNGKLTGMAF 239
Cdd:PLN02358 158 TNCLAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 240 RVPTPDVSVVDLTARLEKPASLDDIKKVIKAAADGPMKGILAYTEDQVVSTDFVSDTNSSIFDAGASISLNPHFVKLVSW 319
Cdd:PLN02358 238 RVPTVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSW 317
|
330
....*....|....*....
gi 1845979520 320 YDNEFGYSNRVVDLISYIA 338
Cdd:PLN02358 318 YDNEWGYSSRVVDLIVHMS 336
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
6-338 |
1.24e-148 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 421.84 E-value: 1.24e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 6 VGINGFGRIGRLVLRAAVEKDSVNVVAVNDpFISIDYMVYLFQYDSTHGRFKGTVAHEGDYLLVakEGKsqhKIKVYNSR 85
Cdd:PRK15425 5 VGINGFGRIGRIVFRAAQKRSDIEIVAIND-LLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIV--NGK---KIRVTAER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 86 DPAEIQWGASGADYVVESTGVFTTIEKANAHLKGGAKKVIISAPSAD-APMFVVGVNHEKYdhANDHIISNASCTTNCLA 164
Cdd:PRK15425 79 DPANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDnTPMFVKGANFDKY--AGQDIVSNASCTTNCLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 165 PLAKVINDNFGIIEGLMTTVHAVTATQKTVDGPSGKLWRDGRGAGQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTP 244
Cdd:PRK15425 157 PLAKVINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 245 DVSVVDLTARLEKPASLDDIKKVIKAAADGPMKGILAYTEDQVVSTDFVSDTNSSIFDAGASISLNPHFVKLVSWYDNEF 324
Cdd:PRK15425 237 NVSVVDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNET 316
|
330
....*....|....
gi 1845979520 325 GYSNRVVDLISYIA 338
Cdd:PRK15425 317 GYSNKVLDLIAHIS 330
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
6-340 |
4.48e-137 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 393.65 E-value: 4.48e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 6 VGINGFGRIGRLVLRAAVEKD----SVNVVAVNDPFISIDYMVYLFQYDSTHGRFKGTVAHEGDYLLVAKEGK---SQHK 78
Cdd:PTZ00434 6 VGINGFGRIGRMVFQAICDQGligtEIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVETTKSSPSVKTDDVlvvNGHR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 79 IK-VYNSRDPAEIQWGASGADYVVESTGVFTTIEKANAHLKGGAKKVIISAP-SADAPMFVVGVNHEKYDHANDHIISNA 156
Cdd:PTZ00434 86 IKcVKAQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPaSGGAKTIVMGVNQHEYSPTEHHVVSNA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 157 SCTTNCLAPLAKVI-NDNFGIIEGLMTTVHAVTATQKTVDGPSGKLWRDGRGAGQNIIPASTGAAKAVGKVIPELNGKLT 235
Cdd:PTZ00434 166 SCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGKLT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 236 GMAFRVPTPDVSVVDLTARLEKPASLDDIKKVIKAAADGPMKGILAYTEDQVVSTDFVSDTNSSIFDAGASISLN----P 311
Cdd:PTZ00434 246 GMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKATLQNNlpgeR 325
|
330 340
....*....|....*....|....*....
gi 1845979520 312 HFVKLVSWYDNEFGYSNRVVDLISYIATK 340
Cdd:PTZ00434 326 RFFKIVSWYDNEWGYSHRVVDLVRYMAAK 354
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
3-340 |
4.06e-135 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 387.94 E-value: 4.06e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 3 KPSVGINGFGRIGRLVLRAAVEKDSVNVVAVNDPFiSIDYMVYLFQYDSTHGRFKGTVAHEGDYLLVakEGKsqhKIKVY 82
Cdd:PRK07729 2 KTKVAINGFGRIGRMVFRKAIKESAFEIVAINASY-PSETLAHLIKYDTVHGKFDGTVEAFEDHLLV--DGK---KIRLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 83 NSRDPAEIQWGASGADYVVESTGVFTTIEKANAHLKGGAKKVIISAPSADAPM-FVVGVNHEKYDHANDHIISNASCTTN 161
Cdd:PRK07729 76 NNRDPKELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVtIVVGVNEDQLDIEKHTIISNASCTTN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 162 CLAPLAKVINDNFGIIEGLMTTVHAVTATQKTVDGPSGKLwRDGRGAGQNIIPASTGAAKAVGKVIPELNGKLTGMAFRV 241
Cdd:PRK07729 156 CLAPVVKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHKDL-RRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 242 PTPDVSVVDLTARLEKPASLDDIKKVIKAAADGPMKGILAYTEDQVVSTDFVSDTNSSIFDAGASISLNPHFVKLVSWYD 321
Cdd:PRK07729 235 PTPNVSLVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYD 314
|
330
....*....|....*....
gi 1845979520 322 NEFGYSNRVVDLISYIATK 340
Cdd:PRK07729 315 NEWGYSCRVVDLVTLVADE 333
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
158-323 |
1.38e-117 |
|
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: 336.35 E-value: 1.38e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 158 CTTNCLAPLAKVINDNFGIIEGLMTTVHAVTATQKTVDGPSgKLWRDGRGAGQNIIPASTGAAKAVGKVIPELNGKLTGM 237
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 238 AFRVPTPDVSVVDLTARLEKPASLDDIKKVIKAAADGPMKGILAYTEDQVVSTDFVSDTNSSIFDAGASISLNPHFVKLV 317
Cdd:cd18126 80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159
|
....*.
gi 1845979520 318 SWYDNE 323
Cdd:cd18126 160 AWYDNE 165
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
6-333 |
2.80e-115 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 336.91 E-value: 2.80e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 6 VGINGFGRIGRLVLRAAVEKDSVNVVAVNDPFISIDYMVYLFQYDSTHGRFKGTVAHEGDYLLVAkegksQHKIKVYNSR 85
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVID-----GKRISFSSNK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 86 DPAEIQWGAsGADYVVESTGVFTTIEKANAHLKGGAKKVIISAP--SADAPMFVVGVNHEKYDHANDHIISNASCTTNCL 163
Cdd:NF033735 76 DIEDTPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARHRIVTAASCTTNCL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 164 APLAKVINDNFGIIEGLMTTVHAVTATQKTVDGPSGKLwRDGRGAGQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPT 243
Cdd:NF033735 155 APVVKVIHEKIGIKHGSITTIHDITNTQTIVDAPHKDL-RRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 244 PDVSVVDLTARLEKPASLDDIKKVIKAAADGPMKGILAYTEDQVVSTDFVSDTNSSIFDAGASISLNPHFVKLVSWYDNE 323
Cdd:NF033735 234 LNASLTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNE 313
|
330
....*....|
gi 1845979520 324 FGYSNRVVDL 333
Cdd:NF033735 314 WGYANRMVDL 323
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
6-340 |
7.07e-114 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 333.80 E-value: 7.07e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 6 VGINGFGRIGRLVLRAAV--EKDSVNVVAVN---DPFISidymVYLFQYDSTHGRFKGTVAHEGDYLLVakEGKSqhkIK 80
Cdd:PRK07403 4 VAINGFGRIGRNFLRCWLgrENSQLELVAINdtsDPRTN----AHLLKYDSMLGKLNADISADENSITV--NGKT---IK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 81 VYNSRDPAEIQWGASGADYVVESTGVFTTIEKANAHLKGGAKKVIISAP--SADAPMFVVGVNHEKYDHANDHIISNASC 158
Cdd:PRK07403 75 CVSDRNPLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPgkGEDIGTYVVGVNHHEYDHEDHNIISNASC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 159 TTNCLAPLAKVINDNFGIIEGLMTTVHAVTATQKTVDGPSGKLwRDGRGAGQNIIPASTGAAKAVGKVIPELNGKLTGMA 238
Cdd:PRK07403 155 TTNCLAPIAKVLHDNFGIIKGTMTTTHSYTGDQRILDASHRDL-RRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 239 FRVPTPDVSVVDLTARLEKPASLDDIKKVIKAAADGPMKGILAYTEDQVVSTDFVSDTNSSIFDAGASISLNPHFVKLVS 318
Cdd:PRK07403 234 LRVPTPNVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIA 313
|
330 340
....*....|....*....|..
gi 1845979520 319 WYDNEFGYSNRVVDLISYIATK 340
Cdd:PRK07403 314 WYDNEWGYSQRVVDLAELVARK 335
|
|
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
6-334 |
3.32e-105 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 311.66 E-value: 3.32e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 6 VGINGFGRIGRLVLRAAVEKDSVNVVAVNDPFISIDYMVYLFQYDSTHGRFKGTVAHEGDYLLVAKegksqHKIKVYNSR 85
Cdd:PRK08955 5 VGINGFGRIGRLALRAAWDWPELEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVING-----KRIRTTQNK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 86 DPAEIQWgaSGADYVVESTGVFTTIEKANAHLKGGAKKVIISAPSADAPMF--VVGVNHEKYDHANDHIISNASCTTNCL 163
Cdd:PRK08955 80 AIADTDW--SGCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLniVMGVNDHLFDPAIHPIVTAASCTTNCL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 164 APLAKVINDNFGIIEGLMTTVHAVTATQKTVDGPSGKLwRDGRGAGQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPT 243
Cdd:PRK08955 158 APVVKVIHEKLGIKHGSMTTIHDLTNTQTILDAPHKDL-RRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 244 PDVSVVDLTARLEKPASLDDIKKVIKAAADGPMKGILAYTEDQVVSTDFVSDTNSSIFDAGASISLNPHFVKLVSWYDNE 323
Cdd:PRK08955 237 ANASLTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNE 316
|
330
....*....|.
gi 1845979520 324 FGYSNRVVDLI 334
Cdd:PRK08955 317 WGYANRTAELA 327
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
3-340 |
1.31e-101 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 304.55 E-value: 1.31e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 3 KPSVGINGFGRIGRLVLRA-AVEKDS-VNVVAVNDPFiSIDYMVYLFQYDSTHGRFKGTVAHEGDYLlVAKEGKSqhkIK 80
Cdd:PLN03096 60 KIKVAINGFGRIGRNFLRCwHGRKDSpLDVVAINDTG-GVKQASHLLKYDSTLGTFDADVKPVGDDA-ISVDGKV---IK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 81 VYNSRDPAEIQWGASGADYVVESTGVFTTIEKANAHLKGGAKKVIISAPS-ADAPMFVVGVNHEKYDHAnDHIISNASCT 159
Cdd:PLN03096 135 VVSDRNPLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGkGDIPTYVVGVNADDYKHS-DPIISNASCT 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 160 TNCLAPLAKVINDNFGIIEGLMTTVHAVTATQKTVDGPSGKLwRDGRGAGQNIIPASTGAAKAVGKVIPELNGKLTGMAF 239
Cdd:PLN03096 214 TNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDL-RRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIAL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 240 RVPTPDVSVVDLTARLEKPASLDDIKKVIKAAADGPMKGILAYTEDQVVSTDFVSDTNSSIFDAGASISLNPHFVKLVSW 319
Cdd:PLN03096 293 RVPTPNVSVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAW 372
|
330 340
....*....|....*....|.
gi 1845979520 320 YDNEFGYSNRVVDLISYIATK 340
Cdd:PLN03096 373 YDNEWGYSQRVVDLADIVANK 393
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
3-340 |
2.28e-100 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 302.98 E-value: 2.28e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 3 KPSVGINGFGRIGRLVLRAAVE-KDS-VNVVAVNDPFiSIDYMVYLFQYDSTHGRFKGTVAHEGDYLlVAKEGKSqhkIK 80
Cdd:PLN02237 75 KLKVAINGFGRIGRNFLRCWHGrKDSpLDVVVVNDSG-GVKNASHLLKYDSMLGTFKADVKIVDDET-ISVDGKP---IK 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 81 VYNSRDPAEIQWGASGADYVVESTGVFTTIEKANAHLKGGAKKVIISAPS--ADAPMFVVGVNHEKYDHANDHIISNASC 158
Cdd:PLN02237 150 VVSNRDPLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAkgADIPTYVVGVNEDDYDHEVANIVSNASC 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 159 TTNCLAPLAKVINDNFGIIEGLMTTVHAVTATQKTVDGPSGKLwRDGRGAGQNIIPASTGAAKAVGKVIPELNGKLTGMA 238
Cdd:PLN02237 230 TTNCLAPFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDASHRDL-RRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 239 FRVPTPDVSVVDLTARLEKPA-SLDDIKKVIKAAADGPMKGILAYTEDQVVSTDFVSDTNSSIFDAGASISLNPHFVKLV 317
Cdd:PLN02237 309 LRVPTPNVSVVDLVVNVEKKGiTAEDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVV 388
|
330 340
....*....|....*....|...
gi 1845979520 318 SWYDNEFGYSNRVVDLISYIATK 340
Cdd:PLN02237 389 AWYDNEWGYSQRVVDLAHLVAAK 411
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
6-332 |
3.88e-94 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 283.49 E-value: 3.88e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 6 VGINGFGRIGRLVLRAAVE---KDSVNVVAVNDpFISIDYMVYLFQYDSTHGRFKGTVAHEGDYLLVAKEgksqhKIKVY 82
Cdd:PRK13535 4 VAINGFGRIGRNVLRALYEsgrRAEITVVAINE-LADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDD-----AIRLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 83 NSRDPAEIQWGASGADYVVESTGVFTTIEKANAHLKGGAKKVIISAPSA---DAPMfVVGVNHEKYdHANDHIISNASCT 159
Cdd:PRK13535 78 HERDIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSndlDATV-VYGVNHDQL-RAEHRIVSNASCT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 160 TNCLAPLAKVINDNFGIIEGLMTTVHAVTATQKTVDGPSGKLwRDGRGAGQNIIPASTGAAKAVGKVIPELNGKLTGMAF 239
Cdd:PRK13535 156 TNCIIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHPDL-RRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 240 RVPTPDVSVVDLTARLEKPASLDDIKKVIKAAADGPMKGILAYTEDQVVSTDFVSDTNSSIFDAGASISLNPHFVKLVSW 319
Cdd:PRK13535 235 RVPTINVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVW 314
|
330
....*....|...
gi 1845979520 320 YDNEFGYSNRVVD 332
Cdd:PRK13535 315 CDNEWGFANRMLD 327
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
163-320 |
1.74e-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: 264.84 E-value: 1.74e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 163 LAPLAKVINDNFGIIEGLMTTVHAVTATQKTVDGPSGKLWRDGRGAGQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVP 242
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1845979520 243 TPDVSVVDLTARLEKPASLDDIKKVIKAAADGPMKGILAYTEDQVVSTDFVSDTNSSIFDAGASISLNPHFVKLVSWY 320
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| GAPDH_I_N |
cd05214 |
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
6-157 |
9.68e-85 |
|
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: 253.08 E-value: 9.68e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 6 VGINGFGRIGRLVLRAAVEKDSVNVVAVNDPFIsIDYMVYLFQYDSTHGRFKGTVAHEGDYLLVakEGKsqhKIKVYNSR 85
Cdd:cd05214 3 VGINGFGRIGRLVFRAALERDDIEVVAINDLTD-DETLAYLLKYDSVHGRFDGEVEVDDDALIV--NGK---KIKVFAER 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1845979520 86 DPAEIQWGASGADYVVESTGVFTTIEKANAHLKGGAKKVIISAPSAD-APMFVVGVNHEKYDhANDHIISNAS 157
Cdd:cd05214 77 DPAELPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYD-ADDKIISNAS 148
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
158-323 |
7.69e-84 |
|
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: 251.00 E-value: 7.69e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 158 CTTNCLAPLAKVINDNFGIIEGLMTTVHAVTATQKTVDGPSGKLWRDGRGAGQNIIPASTGAAKAVGKVIPELNGKLTGM 237
Cdd:cd18123 1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 238 AFRVPTPDVSVVDLTARLEKPASLDDIKKVIKAAADGpmKGILAYTEDQVVSTDFVSDTNSSIFDAGASISLNPHFVKLV 317
Cdd:cd18123 81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLM 158
|
....*.
gi 1845979520 318 SWYDNE 323
Cdd:cd18123 159 QWYDNE 164
|
|
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
10-338 |
3.49e-78 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 247.14 E-value: 3.49e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 10 GFGRIGRLVLRAAVEKDSVN--------VV---AVNDpfisIDYMVYLFQYDSTHGRFKGTVA--HEGDYLLVakegkSQ 76
Cdd:PRK08289 134 GFGRIGRLLARLLIEKTGGGnglrlraiVVrkgSEGD----LEKRASLLRRDSVHGPFNGTITvdEENNAIIA-----NG 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 77 HKIKVYNSRDPAEIQWGASGAD--YVVESTGVFTTIEKANAHLKG-GAKKVIISAPS-ADAPMFVVGVNHEKYDhANDHI 152
Cdd:PRK08289 205 NYIQVIYANSPEEVDYTAYGINnaLVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGkGDIKNIVHGVNHSDIT-DEDKI 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 153 ISNASCTTNCLAPLAKVINDNFGIIEGLMTTVHAVTATQKTVDGPSgKLWRDGRGAGQNIIPASTGAAKAVGKVIPELNG 232
Cdd:PRK08289 284 VSAASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYH-KGDRRGRSAPLNMVITETGAAKAVAKALPELAG 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 233 KLTGMAFRVPTPDVSVVDLTARLEKPASLDDIKKVIKAAA-DGPMKGILAYTEDQ-VVSTDFVSDTNSSIFDAGASISLN 310
Cdd:PRK08289 363 KLTGNAIRVPTPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQIDYTDSTeVVSSDFVGSRHAGVVDSQATIVNG 442
|
330 340
....*....|....*....|....*...
gi 1845979520 311 PHFVkLVSWYDNEFGYSNRVVDLISYIA 338
Cdd:PRK08289 443 NRAV-LYVWYDNEFGYSCQVVRVMEQMA 469
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
6-158 |
3.98e-75 |
|
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: 228.20 E-value: 3.98e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 6 VGINGFGRIGRLVLRAAVEKDSVNVVAVNDPfISIDYMVYLFQYDSTHGRFKGTVAHEGDYLLVAKegksqHKIKVYNSR 85
Cdd:smart00846 3 VGINGFGRIGRLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNG-----KAIKVFAER 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1845979520 86 DPAEIQWGASGADYVVESTGVFTTIEKANAHLKGGAKKVIISAPSADA-PMFVVGVNHEKYDhANDHIISNASC 158
Cdd:smart00846 77 DPANLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYD-GEDHIISNASC 149
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-334 |
5.58e-57 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 188.16 E-value: 5.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 1 MPKPsVGINGFGRIGRLVLRAAVEKDSVNVVAVNDPFISIDYMVYLFQYDSTHGRFKGT-VAHEGDYLLVakegKSQHKI 79
Cdd:PTZ00353 1 LPIT-VGINGFGPVGKAVLFASLTDPLVTVVAVNDASVSIAYIAYVLEQESPLSAPDGAsIRVVGEQIVL----NGTQKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 80 KVYNSRDPAEIQWGASGADYVVESTGVFTTIEKANAHLKGGAKKVIISAPSADAPMFVVGVNHEKYDhANDHIISNASCT 159
Cdd:PTZ00353 76 RVSAKHDLVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDERLS-ASLPVCCAGAPI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 160 TNCLAPLAKVINDNFGIIEGLMTTVHAvTATQKTVDGPS--GKLWRDGRGAGQNIIPASTGAAKAVGKVIPELNGKLTGM 237
Cdd:PTZ00353 155 AVALAPVIRALHEVYGVEECSYTAIHG-MQPQEPIAARSknSQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 238 AFRVPTPDVSVVDLTARLEKPASLDDIKKVIKAAADGPMKGILAYTEDQVVSTDFVSDTnSSIFDAGASISLNPHFV-KL 316
Cdd:PTZ00353 234 AFQVPVKKGCAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCIPNG-KLCYDATSSSSSREGEVhKM 312
|
330
....*....|....*...
gi 1845979520 317 VSWYDNEFGYSNRVVDLI 334
Cdd:PTZ00353 313 VLWFDVECYYAARLLSLV 330
|
|
| Gp_dh_N |
pfam00044 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
5-109 |
1.12e-48 |
|
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: 158.80 E-value: 1.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 5 SVGINGFGRIGRLVLRAAVEKDSVNVVAVNDpFISIDYMVYLFQYDSTHGRFKGTVAHEGDYLLVakEGKsqhKIKVYNS 84
Cdd:pfam00044 2 KVGINGFGRIGRLVLRAALERPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVV--NGK---KIKVFAE 75
|
90 100
....*....|....*....|....*
gi 1845979520 85 RDPAEIQWGASGADYVVESTGVFTT 109
Cdd:pfam00044 76 RDPAELPWGDLGVDVVIESTGVFTT 100
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
158-323 |
3.65e-47 |
|
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar proteins; D-erythrose-4-phosphate dehydrogenase (E4PDH; EC 1.2.1.72), also called E4P dehydrogenase, catalyzes the NAD-dependent conversion of D-erythrose 4-phosphate (E4P) to 4-phosphoerythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose. This enzyme activity appears to have evolved from glyceraldehyde-3-phosphate dehydrogenase (GADPH), whose substrate differs only in the lack of one carbon relative to E4P. E4PDH proteins contain an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal GADPH-like catalytic domain and are members of the GAPDH superfamily of proteins.
Pssm-ID: 467686 Cd Length: 165 Bit Score: 157.19 E-value: 3.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 158 CTTNCLAPLAKVINDNFGIIEGLMTTVHAVTATQKTVDGPSGKLwRDGRGAGQNIIPASTGAAKAVGKVIPELNGKLTGM 237
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDAYHPDL-RRTRAASQSIIPVDTKLARGIERILPHLAGRFEAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 238 AFRVPTPDVSVVDLTARLEKPASLDDIKKVIKAAADGPMKGILAYTEDQVVSTDFVSDTNSSIFDAGASISLNPHFVKLV 317
Cdd:cd23937 80 AVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLL 159
|
....*.
gi 1845979520 318 SWYDNE 323
Cdd:cd23937 160 VWCDNE 165
|
|
| GAPDH_N_E4PDH |
cd17892 |
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
6-157 |
3.25e-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: 154.73 E-value: 3.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 6 VGINGFGRIGRLVLRAAVE---KDSVNVVAVNDPfISIDYMVYLFQYDSTHGRFKGTVAHEGDYLLVAkegksQHKIKVY 82
Cdd:cd17892 3 VAINGYGRIGRNVLRALYEsgrRAEFQVVAINEL-ADAETIAHLTKYDTTHGRFPGEVRVENDQLFVN-----GDKIRVL 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1845979520 83 NSRDPAEIQWGASGADYVVESTGVFTTIEKANAHLKGGAKKVIISAPSA---DAPMfVVGVNHEKYDhANDHIISNAS 157
Cdd:cd17892 77 HEPDPENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASndvDATI-VYGINQDLLR-AEHRIVSNAS 152
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
158-323 |
2.13e-45 |
|
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: 152.67 E-value: 2.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 158 CTTNCLAPLAKVINDNFGIIEGLMTTVHAVTATQKTVDGPSGKLWrdGRGAGQNIIPASTGAAKAVGKVIPELN--GKLT 235
Cdd:cd18122 1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIGkpIKVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 236 GMAFRVPTPDVSVVDLTARLEKPASLDDIKKVIKAAADGPMKGILAYTEDQVVSTDFVSDTNSSIFDAGASISLNPHFVK 315
Cdd:cd18122 79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLK 158
|
....*...
gi 1845979520 316 LVSWYDNE 323
Cdd:cd18122 159 VFSAVDNE 166
|
|
| GAPDH-like_N |
cd05192 |
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ... |
6-162 |
6.89e-13 |
|
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: 64.30 E-value: 6.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 6 VGINGFGRIGRLVLRAAVEKDSVNVVAVNDPfisidymvylfqydsthgrfkgtvahegdyllvakegksqhkikvynsr 85
Cdd:cd05192 3 VAINGFGRIGRIVFRAIADQDDLDVVAINDR------------------------------------------------- 33
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1845979520 86 dpaeiqwgasgADYVVESTGVFTTIEKANAHLKGGAKKVIISAPS-ADAPMFVVGVNHEKYDHaNDHIISNASCTTNC 162
Cdd:cd05192 34 -----------RDVVIECTGSFTDDDNAEKHIKAGGKKAVITAPEkGDIPTIVVVLNELAKSA-GATVVSNANETSYS 99
|
|
| GAPDH_II_C |
cd18127 |
C-terminal catalytic domain of type II glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
157-271 |
2.61e-03 |
|
C-terminal catalytic domain of type II 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 type II NADP+ utilizing GAPDHs, mainly from archaea.
Pssm-ID: 467677 Cd Length: 162 Bit Score: 37.95 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845979520 157 SCTTNCLAPLAKVINDNFGIIEGlmttvhAVTATQKTVDgpsgkLWRDGRGAGQNIIP---ASTGAAKAVGKVIPELNgk 233
Cdd:cd18127 1 SCNTTGLSRVLKALDRAFGLKRV------RATIVRRAAD-----PGKHKKGVINAIVPepkDPSHHAPDVKTVFPDLD-- 67
|
90 100 110
....*....|....*....|....*....|....*...
gi 1845979520 234 LTGMAFRVPTPDVSVVDLTARLEKPASLDDIKKVIKAA 271
Cdd:cd18127 68 ITTSAVKVPTTLMHLHTINVELKRKVSREEVLEALASN 105
|
|
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