|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
1-460 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 915.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 1 MIPLIGQLYRNNNVVTSIHGRGLINRSVIAIMKAHRFARHrmADDAELSVHETFPILKAMSELKLGAASVDLGKMVAKFK 80
Cdd:PRK08289 22 MIPLIGKLYRNKNVVVSLYGRSLINRSVIDILKAHRFARR--IVGKELSVRETFPILEALSKLDLGPARVDIGKLAVKYK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 81 AEGNGRSIEDFVKAELAEVVGKQngDAREGTDVVLYGFGRIGRLLARILIEKTGGGDGLRLRAIVVRKGAENDLVKRASL 160
Cdd:PRK08289 100 AEGDGSDVEAFVAEELADAVGGA--DDIEPRDVVLYGFGRIGRLLARLLIEKTGGGNGLRLRAIVVRKGSEGDLEKRASL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 161 LRRDSVHGPFDGTITIDEENNTLTANGNLIQVIYSNDPASIDYTQYGIKNALLVDNTGKWRDAEGLGQHLKCPGIDRVVL 240
Cdd:PRK08289 178 LRRDSVHGPFNGTITVDEENNAIIANGNYIQVIYANSPEEVDYTAYGINNALVVDNTGKWRDEEGLSQHLKSKGVAKVLL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 241 TAPGKGALKNIVHGINHTDIGADDKIISAASCTTNAIVPVLKAVNDQYGIVNGHVETVHSYTNDQNLIDNFHKGSRRGRS 320
Cdd:PRK08289 258 TAPGKGDIKNIVHGVNHSDITDEDKIVSAASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKGDRRGRS 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 321 APLNMVITETGAATAAAKALPVLKGKLTGNAIRVPTPNVSMAILNLNLEKATTREEINEYLRQMAMHSDLQKQIDFVSSQ 400
Cdd:PRK08289 338 APLNMVITETGAAKAVAKALPELAGKLTGNAIRVPTPNVSMAILNLNLEKETSREELNEYLRQMSLHSPLQNQIDYTDST 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 401 EVVSTDFVGSRHAGVVDAEATICNDNRVVLYVWYDNEFGYSCQVVRVMEDMAGVNPPAFP 460
Cdd:PRK08289 418 EVVSSDFVGSRHAGVVDSQATIVNGNRAVLYVWYDNEFGYSCQVVRVMEQMAGVRYPTYP 477
|
|
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
111-455 |
7.66e-164 |
|
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: 465.25 E-value: 7.66e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 111 TDVVLYGFGRIGRLLARILIEKtggGDGLRLRAIvvrkgaeNDLV---KRASLLRRDSVHGPFDGTITIDEenNTLTANG 187
Cdd:COG0057 3 IRVAINGFGRIGRLVLRALLER---GPDIEVVAI-------NDLGdaeTLAHLLKYDSVHGRFPGEVEVEG--DSLIVNG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 188 NLIQVIYSNDPASIDYTQYGIKnaLLVDNTGKWRDAEGLGQHLKCpGIDRVVLTAPGKGALKNIVHGINHTDIGADDKII 267
Cdd:COG0057 71 KKIKVLAERDPAELPWGELGVD--VVIECTGKFTDREKASAHLKA-GAKKVLISAPAKGDDPTIVYGVNHDDYDADHRII 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 268 SAASCTTNAIVPVLKAVNDQYGIVNGHVETVHSYTNDQNLIDNFHKGSRRGRSAPLNMVITETGAATAAAKALPVLKGKL 347
Cdd:COG0057 148 SNASCTTNCLAPVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 348 TGNAIRVPTPNVSMAILNLNLEKATTREEINEYLRQMAmHSDLQKQIDFvSSQEVVSTDFVGSRHAGVVDAEATI-CNDN 426
Cdd:COG0057 228 DGMAVRVPTPNVSLVDLTVELEKETTVEEVNAALKEAA-EGPLKGILGY-TEEPLVSSDFNGDPHSSIFDALQTIvIGGN 305
|
330 340
....*....|....*....|....*....
gi 15598197 427 RVVLYVWYDNEFGYSCQVVRVMEDMAGVN 455
Cdd:COG0057 306 LVKVLAWYDNEWGYSNRMVDLAEYMAKLL 334
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
112-446 |
7.93e-141 |
|
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: 406.66 E-value: 7.93e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 112 DVVLYGFGRIGRLLARILIEKtgggDGLRLRAIVVRKGAenDLVKRASLLRRDSVHGPFDGTITIDEenNTLTANGNL-I 190
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEK----PGNDLEVVAINDLT--DLEKLAYLLKYDSVHGRFEGEVTVDE--DGLVVNGKEvI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 191 QVIYSNDPASIDYTQYGIknALLVDNTGKWRDAEGLGQHLKcPGIDRVVLTAPGKGALKNIVHGINHTDIGADDKIISAA 270
Cdd:TIGR01534 73 SVFSERDPSDLPWKALGV--DIVIECTGKFRDKEKLEKHLE-AGAKKVLISAPSKGDVKTIVYGVNHDEYDGEERIISNA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 271 SCTTNAIVPVLKAVNDQYGIVNGHVETVHSYTNDQNLIDNFHKGSRRGRSAPLNMVITETGAATAAAKALPVLKGKLTGN 350
Cdd:TIGR01534 150 SCTTNCLAPLAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 351 AIRVPTPNVSMAILNLNLEKATTREEINEYLRQMAMHSdLQKQIDFvSSQEVVSTDFVGSRHAGVVDAEATICN---DNR 427
Cdd:TIGR01534 230 AIRVPTPNVSLVDLVVNLEKDVTVEEVNAALKEASEGE-LKGVLGY-TEDELVSSDFIGSPYSSIVDATATKVTglgDSL 307
|
330
....*....|....*....
gi 15598197 428 VVLYVWYDNEFGYSCQVVR 446
Cdd:TIGR01534 308 VKVYAWYDNEWGYSNRLVD 326
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
272-437 |
7.30e-72 |
|
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: 224.26 E-value: 7.30e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 272 CTTNAIVPVLKAVNDQYGIVNGHVETVHSYTNDQNLIDNFHKGSRRGRSAPLNMVITETGAATAAAKALPVLKGKLTGNA 351
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 352 IRVPTPNVSMAILNLNLEKATTREEINEYLRQMAMHSdLQKQIDFvSSQEVVSTDFVGSRHAGVVDAEATI-CNDNRVVL 430
Cdd:cd18126 81 FRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGP-LKGILGY-TEDPLVSSDFVGDPHSSIFDATATIvLGGNLVKV 158
|
....*..
gi 15598197 431 YVWYDNE 437
Cdd:cd18126 159 VAWYDNE 165
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
111-272 |
4.73e-47 |
|
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. N-terminal domain is a Rossmann NAD(P) binding fold.
Pssm-ID: 214851 [Multi-domain] Cd Length: 149 Bit Score: 159.25 E-value: 4.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 111 TDVVLYGFGRIGRLLARILIEktgggdglRLRAIVVRKGAENDLVKRASLLRRDSVHGPFDGTITIDEENntLTANGNLI 190
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALE--------RPDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEVEGDG--LVVNGKAI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 191 QVIYSNDPASIDYTQYGIKnaLLVDNTGKWRDAEGLGQHLKCpGIDRVVLTAPGKGALKNIVHGINHTDIGADDKIISAA 270
Cdd:smart00846 71 KVFAERDPANLPWGELGVD--IVVECTGGFTTREKASAHLKA-GAKKVIISAPSKDADPTFVYGVNHDEYDGEDHIISNA 147
|
..
gi 15598197 271 SC 272
Cdd:smart00846 148 SC 149
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
277-434 |
2.59e-42 |
|
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: 146.97 E-value: 2.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 277 IVPVLKAVNDQYGIVNGHVETVHSYTNDQNLIDNFHKGS-RRGRSAPLNMVITETGAATAAAKALPVLKGKLTGNAIRVP 355
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDlRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 356 TPNVSMAILNLNLEKATTREEINEYLRQMAMHSdlQKQIDFVSSQEVVSTDFVGSRHAGVVDAEATI-CNDNRVVLYVWY 434
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGA--LKGILSYTEDPLVSSDFIGDPHSSIFDAKETIvVNGNFVKVVAWY 158
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
1-460 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 915.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 1 MIPLIGQLYRNNNVVTSIHGRGLINRSVIAIMKAHRFARHrmADDAELSVHETFPILKAMSELKLGAASVDLGKMVAKFK 80
Cdd:PRK08289 22 MIPLIGKLYRNKNVVVSLYGRSLINRSVIDILKAHRFARR--IVGKELSVRETFPILEALSKLDLGPARVDIGKLAVKYK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 81 AEGNGRSIEDFVKAELAEVVGKQngDAREGTDVVLYGFGRIGRLLARILIEKTGGGDGLRLRAIVVRKGAENDLVKRASL 160
Cdd:PRK08289 100 AEGDGSDVEAFVAEELADAVGGA--DDIEPRDVVLYGFGRIGRLLARLLIEKTGGGNGLRLRAIVVRKGSEGDLEKRASL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 161 LRRDSVHGPFDGTITIDEENNTLTANGNLIQVIYSNDPASIDYTQYGIKNALLVDNTGKWRDAEGLGQHLKCPGIDRVVL 240
Cdd:PRK08289 178 LRRDSVHGPFNGTITVDEENNAIIANGNYIQVIYANSPEEVDYTAYGINNALVVDNTGKWRDEEGLSQHLKSKGVAKVLL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 241 TAPGKGALKNIVHGINHTDIGADDKIISAASCTTNAIVPVLKAVNDQYGIVNGHVETVHSYTNDQNLIDNFHKGSRRGRS 320
Cdd:PRK08289 258 TAPGKGDIKNIVHGVNHSDITDEDKIVSAASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKGDRRGRS 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 321 APLNMVITETGAATAAAKALPVLKGKLTGNAIRVPTPNVSMAILNLNLEKATTREEINEYLRQMAMHSDLQKQIDFVSSQ 400
Cdd:PRK08289 338 APLNMVITETGAAKAVAKALPELAGKLTGNAIRVPTPNVSMAILNLNLEKETSREELNEYLRQMSLHSPLQNQIDYTDST 417
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 401 EVVSTDFVGSRHAGVVDAEATICNDNRVVLYVWYDNEFGYSCQVVRVMEDMAGVNPPAFP 460
Cdd:PRK08289 418 EVVSSDFVGSRHAGVVDSQATIVNGNRAVLYVWYDNEFGYSCQVVRVMEQMAGVRYPTYP 477
|
|
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
111-455 |
7.66e-164 |
|
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: 465.25 E-value: 7.66e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 111 TDVVLYGFGRIGRLLARILIEKtggGDGLRLRAIvvrkgaeNDLV---KRASLLRRDSVHGPFDGTITIDEenNTLTANG 187
Cdd:COG0057 3 IRVAINGFGRIGRLVLRALLER---GPDIEVVAI-------NDLGdaeTLAHLLKYDSVHGRFPGEVEVEG--DSLIVNG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 188 NLIQVIYSNDPASIDYTQYGIKnaLLVDNTGKWRDAEGLGQHLKCpGIDRVVLTAPGKGALKNIVHGINHTDIGADDKII 267
Cdd:COG0057 71 KKIKVLAERDPAELPWGELGVD--VVIECTGKFTDREKASAHLKA-GAKKVLISAPAKGDDPTIVYGVNHDDYDADHRII 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 268 SAASCTTNAIVPVLKAVNDQYGIVNGHVETVHSYTNDQNLIDNFHKGSRRGRSAPLNMVITETGAATAAAKALPVLKGKL 347
Cdd:COG0057 148 SNASCTTNCLAPVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 348 TGNAIRVPTPNVSMAILNLNLEKATTREEINEYLRQMAmHSDLQKQIDFvSSQEVVSTDFVGSRHAGVVDAEATI-CNDN 426
Cdd:COG0057 228 DGMAVRVPTPNVSLVDLTVELEKETTVEEVNAALKEAA-EGPLKGILGY-TEEPLVSSDFNGDPHSSIFDALQTIvIGGN 305
|
330 340
....*....|....*....|....*....
gi 15598197 427 RVVLYVWYDNEFGYSCQVVRVMEDMAGVN 455
Cdd:COG0057 306 LVKVLAWYDNEWGYSNRMVDLAEYMAKLL 334
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
112-446 |
7.93e-141 |
|
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: 406.66 E-value: 7.93e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 112 DVVLYGFGRIGRLLARILIEKtgggDGLRLRAIVVRKGAenDLVKRASLLRRDSVHGPFDGTITIDEenNTLTANGNL-I 190
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEK----PGNDLEVVAINDLT--DLEKLAYLLKYDSVHGRFEGEVTVDE--DGLVVNGKEvI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 191 QVIYSNDPASIDYTQYGIknALLVDNTGKWRDAEGLGQHLKcPGIDRVVLTAPGKGALKNIVHGINHTDIGADDKIISAA 270
Cdd:TIGR01534 73 SVFSERDPSDLPWKALGV--DIVIECTGKFRDKEKLEKHLE-AGAKKVLISAPSKGDVKTIVYGVNHDEYDGEERIISNA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 271 SCTTNAIVPVLKAVNDQYGIVNGHVETVHSYTNDQNLIDNFHKGSRRGRSAPLNMVITETGAATAAAKALPVLKGKLTGN 350
Cdd:TIGR01534 150 SCTTNCLAPLAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 351 AIRVPTPNVSMAILNLNLEKATTREEINEYLRQMAMHSdLQKQIDFvSSQEVVSTDFVGSRHAGVVDAEATICN---DNR 427
Cdd:TIGR01534 230 AIRVPTPNVSLVDLVVNLEKDVTVEEVNAALKEASEGE-LKGVLGY-TEDELVSSDFIGSPYSSIVDATATKVTglgDSL 307
|
330
....*....|....*....
gi 15598197 428 VVLYVWYDNEFGYSCQVVR 446
Cdd:TIGR01534 308 VKVYAWYDNEWGYSNRLVD 326
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
110-452 |
2.96e-85 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 265.06 E-value: 2.96e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 110 GTDVVLYGFGRIGRLLARILIEKtgggDGLRLRAIVVRKGAENdlvkRASLLRRDSVHGPFDGTITIDEEnnTLTANGNL 189
Cdd:PRK07729 2 KTKVAINGFGRIGRMVFRKAIKE----SAFEIVAINASYPSET----LAHLIKYDTVHGKFDGTVEAFED--HLLVDGKK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 190 IQVIYSNDPASIDYTQYGIKnaLLVDNTGKWRDAEGLGQHLKCpGIDRVVLTAPGKGALKNIVHGINHTDIGAD-DKIIS 268
Cdd:PRK07729 72 IRLLNNRDPKELPWTDLGID--IVIEATGKFNSKEKAILHVEA-GAKKVILTAPGKNEDVTIVVGVNEDQLDIEkHTIIS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 269 AASCTTNAIVPVLKAVNDQYGIVNGHVETVHSYTNDQNLIDNFHKGSRRGRSAPLNMVITETGAATAAAKALPVLKGKLT 348
Cdd:PRK07729 149 NASCTTNCLAPVVKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLH 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 349 GNAIRVPTPNVSMAILNLNLEKATTREEINEYLRQMAMHSdlQKQIDFVSSQEVVSTDFVGSRHAGVVDAEATIC-NDNR 427
Cdd:PRK07729 229 GMALRVPTPNVSLVDLVVDVKRDVTVEEINEAFKTAANGA--LKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVmGDRK 306
|
330 340
....*....|....*....|....*
gi 15598197 428 VVLYVWYDNEFGYSCQVVRVMEDMA 452
Cdd:PRK07729 307 VKVLAWYDNEWGYSCRVVDLVTLVA 331
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
113-452 |
4.62e-73 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 233.65 E-value: 4.62e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 113 VVLYGFGRIGRLLARILIEKTGggDGLRLRAIvvrkGAENDLVKRASLLRRDSVHGPFDGTITIDEenNTLTANGNLIQV 192
Cdd:PRK07403 4 VAINGFGRIGRNFLRCWLGREN--SQLELVAI----NDTSDPRTNAHLLKYDSMLGKLNADISADE--NSITVNGKTIKC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 193 IYSNDPASIDYTQYGIKnaLLVDNTGKWRDAEGLGQHLKCpGIDRVVLTAPGKGA-LKNIVHGINHTDIGADD-KIISAA 270
Cdd:PRK07403 76 VSDRNPLNLPWKEWGID--LIIESTGVFVTKEGASKHIQA-GAKKVLITAPGKGEdIGTYVVGVNHHEYDHEDhNIISNA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 271 SCTTNAIVPVLKAVNDQYGIVNGHVETVHSYTNDQNLIDNFHKGSRRGRSAPLNMVITETGAATAAAKALPVLKGKLTGN 350
Cdd:PRK07403 153 SCTTNCLAPIAKVLHDNFGIIKGTMTTTHSYTGDQRILDASHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 351 AIRVPTPNVSMAILNLNLEKATTREEINEYLRQmAMHSDLQKQIDFvSSQEVVSTDFVGSRHAGVVDAEATICNDNRVV- 429
Cdd:PRK07403 233 ALRVPTPNVSVVDLVVQVEKRTITEQVNEVLKD-ASEGPLKGILEY-SDLPLVSSDYRGTDASSIVDASLTMVMGGDMVk 310
|
330 340
....*....|....*....|...
gi 15598197 430 LYVWYDNEFGYSCQVVRVMEDMA 452
Cdd:PRK07403 311 VIAWYDNEWGYSQRVVDLAELVA 333
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
272-437 |
7.30e-72 |
|
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: 224.26 E-value: 7.30e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 272 CTTNAIVPVLKAVNDQYGIVNGHVETVHSYTNDQNLIDNFHKGSRRGRSAPLNMVITETGAATAAAKALPVLKGKLTGNA 351
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 352 IRVPTPNVSMAILNLNLEKATTREEINEYLRQMAMHSdLQKQIDFvSSQEVVSTDFVGSRHAGVVDAEATI-CNDNRVVL 430
Cdd:cd18126 81 FRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGP-LKGILGY-TEDPLVSSDFVGDPHSSIFDATATIvLGGNLVKV 158
|
....*..
gi 15598197 431 YVWYDNE 437
Cdd:cd18126 159 VAWYDNE 165
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
83-452 |
6.11e-71 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 229.82 E-value: 6.11e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 83 GNGRSIEDFVKAELAEVV---GKQNGDAREGTDVVLYGFGRIGRLLAR------------ILIEKTGGgdglrlraivvr 147
Cdd:PLN03096 30 GKRSDSLDFVVFATSAVSssgGARRAVTEAKIKVAINGFGRIGRNFLRcwhgrkdspldvVAINDTGG------------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 148 kgaendlVKRAS-LLRRDSVHGPFDGTITIdEENNTLTANGNLIQVIYSNDPASIDYTQYGIKnaLLVDNTGKWRDAEGL 226
Cdd:PLN03096 98 -------VKQAShLLKYDSTLGTFDADVKP-VGDDAISVDGKVIKVVSDRNPLNLPWGELGID--LVIEGTGVFVDREGA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 227 GQHLKCpGIDRVVLTAPGKGALKNIVHGINHTDIGADDKIISAASCTTNAIVPVLKAVNDQYGIVNGHVETVHSYTNDQN 306
Cdd:PLN03096 168 GKHIQA-GAKKVLITAPGKGDIPTYVVGVNADDYKHSDPIISNASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 307 LIDNFHKGSRRGRSAPLNMVITETGAATAAAKALPVLKGKLTGNAIRVPTPNVSMAILNLNLEKATTREEINEYLRQMAm 386
Cdd:PLN03096 247 LLDASHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQVEKKTFAEEVNAAFRDAA- 325
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598197 387 hSDLQKQIDFVSSQEVVSTDFVGSRHAGVVDAEAT-ICNDNRVVLYVWYDNEFGYSCQVVRVMEDMA 452
Cdd:PLN03096 326 -EKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTmVMGDDMVKVVAWYDNEWGYSQRVVDLADIVA 391
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
58-445 |
8.30e-65 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 215.15 E-value: 8.30e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 58 KAMSELKLGAASVDLGKMVAKFKAEGNGR--SIEDFVKAELAEVVGKQ---NGDAREGTDVVLYGFGRIGRLLARILIEK 132
Cdd:PLN02237 18 SKASHKRLEVAEFSGLRASSCVTFAKNAReaSFFDVVASQLAPKVAGStpvRGETVAKLKVAINGFGRIGRNFLRCWHGR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 133 TGGgdglRLRAIVVRKGAEndlVKRAS-LLRRDSVHGPFDGTITIdEENNTLTANGNLIQVIYSNDPASIDYTQYGIKna 211
Cdd:PLN02237 98 KDS----PLDVVVVNDSGG---VKNAShLLKYDSMLGTFKADVKI-VDDETISVDGKPIKVVSNRDPLKLPWAELGID-- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 212 LLVDNTGKWRDAEGLGQHLKCpGIDRVVLTAPGKGA-LKNIVHGINHTDIGADD-KIISAASCTTNAIVPVLKAVNDQYG 289
Cdd:PLN02237 168 IVIEGTGVFVDGPGAGKHIQA-GAKKVIITAPAKGAdIPTYVVGVNEDDYDHEVaNIVSNASCTTNCLAPFVKVLDEEFG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 290 IVNGHVETVHSYTNDQNLIDNFHKGSRRGRSAPLNMVITETGAATAAAKALPVLKGKLTGNAIRVPTPNVSMAILNLNLE 369
Cdd:PLN02237 247 IVKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTPNVSVVDLVVNVE 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598197 370 K-ATTREEINEYLRQMAmhSDLQKQIDFVSSQEVVSTDFVGSRHAGVVDAEAT-ICNDNRVVLYVWYDNEFGYSCQVV 445
Cdd:PLN02237 327 KkGITAEDVNAAFRKAA--DGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTmVMGDDMVKVVAWYDNEWGYSQRVV 402
|
|
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
83-455 |
8.58e-63 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 209.33 E-value: 8.58e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 83 GNGRSIEDfVKAELAEV-VGKQNGDAREGTDVVLYGFGRIGRLLARILIEKtgggDGLRLRAIvvrkgaeND----LVKR 157
Cdd:PLN02272 58 CSARSVQP-IKATATEApPAVLKSSSSGKTKIGINGFGRIGRLVLRIATSR----DDIEVVAV-------NDpfidAKYM 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 158 ASLLRRDSVHGPFDGTITIDEENnTLTANGNLIQVIYSNDPASIDYTQYGIKnaLLVDNTGKWRDAEGLGQHLKcPGIDR 237
Cdd:PLN02272 126 AYMFKYDSTHGNFKGTINVVDDS-TLEINGKQIKVTSKRDPAEIPWGDFGAE--YVVESSGVFTTVEKASAHLK-GGAKK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 238 VVLTAPGKGALKNIVhGINHTDIGADDKIISAASCTTNAIVPVLKAVNDQYGIVNGHVETVHSYTNDQNLIDN-FHKGSR 316
Cdd:PLN02272 202 VVISAPSADAPMFVV-GVNEKTYKPNMNIVSNASCTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGpSMKDWR 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 317 RGRSAPLNMVITETGAATAAAKALPVLKGKLTGNAIRVPTPNVSMAILNLNLEKATTREEINEYLRQmAMHSDLqKQIDF 396
Cdd:PLN02272 281 GGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKY-ASEGPL-KGILG 358
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 397 VSSQEVVSTDFVGSRHAGVVDAEATI-CNDNRVVLYVWYDNEFGYSCQVVRVMEDMAGVN 455
Cdd:PLN02272 359 YTDEDVVSNDFVGDSRSSIFDAKAGIgLSASFMKLVSWYDNEWGYSNRVLDLIEHMALVA 418
|
|
| GAPDH_I_N |
cd05214 |
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
111-271 |
1.35e-57 |
|
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: 187.22 E-value: 1.35e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 111 TDVVLYGFGRIGRLLARILIEKtgggDGLRLRAIVVRKGAEndlvKRASLLRRDSVHGPFDGTITIDEenNTLTANGNLI 190
Cdd:cd05214 1 IKVGINGFGRIGRLVFRAALER----DDIEVVAINDLTDDE----TLAYLLKYDSVHGRFDGEVEVDD--DALIVNGKKI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 191 QVIYSNDPASIDYTQYGIknALLVDNTGKWRDAEGLGQHLKCpGIDRVVLTAPGKGALKNIVHGINHTDIGADDKIISAA 270
Cdd:cd05214 71 KVFAERDPAELPWGELGV--DIVIESTGVFTTKEKASAHLKA-GAKKVIISAPAKDDDPTIVMGVNHDKYDADDKIISNA 147
|
.
gi 15598197 271 S 271
Cdd:cd05214 148 S 148
|
|
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
117-445 |
5.38e-57 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 191.59 E-value: 5.38e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 117 GFGRIGRLLARILIEKtgggDGLRLRAIvvrkgaeND----LVKRASLLRRDSVHGPFDGTITIDEEnnTLTANGNLIQV 192
Cdd:PTZ00023 9 GFGRIGRLVFRAALER----EDVEVVAI-------NDpfmtLDYMCYLLKYDSVHGSLPAEVSVTDG--FLMIGSKKVHV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 193 IYSNDPASIDYTQYGIKnaLLVDNTGKWRDAEGLGQHLKcPGIDRVVLTAPGKGALKNIVHGINHTDIGADDKIISAASC 272
Cdd:PTZ00023 76 FFEKDPAAIPWGKNGVD--VVCESTGVFLTKEKAQAHLK-GGAKKVIMSAPPKDDTPIYVMGVNHTQYDKSQRIVSNASC 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 273 TTNAIVPVLKAVNDQYGIVNGHVETVHSYTNDQNLIDNFHKGS---RRGRSAPLNMVITETGAATAAAKALPVLKGKLTG 349
Cdd:PTZ00023 153 TTNCLAPLAKVVNDKFGIVEGLMTTVHASTANQLTVDGPSKGGkdwRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 350 NAIRVPTPNVSMAILNLNLEKATTREEINEYLRQMAmhSDLQKQIDFVSSQEVVSTDFVGSRHAGVVDAEATIC-NDNRV 428
Cdd:PTZ00023 233 MAFRVPVPDVSVVDLTCKLAKPAKYEEIVAAVKKAA--EGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIAlNDTFV 310
|
330
....*....|....*..
gi 15598197 429 VLYVWYDNEFGYSCQVV 445
Cdd:PTZ00023 311 KLVSWYDNEWGYSNRLL 327
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
113-452 |
1.06e-56 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 190.72 E-value: 1.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 113 VVLYGFGRIGRLLARILIEKTGggdgLRLRAIvvrkgaeNDLVK---RASLLRRDSVHGPFDGTITIdeENNTLTANGNL 189
Cdd:PRK15425 5 VGINGFGRIGRIVFRAAQKRSD----IEIVAI-------NDLLDadyMAYMLKYDSTHGRFDGTVEV--KDGHLIVNGKK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 190 IQVIYSNDPASIDYTQYGIKnaLLVDNTGKWRDAEGLGQHLKCpGIDRVVLTAPGKGALKNIVHGINHTDIGADDkIISA 269
Cdd:PRK15425 72 IRVTAERDPANLKWDEVGVD--VVAEATGLFLTDETARKHITA-GAKKVVMTGPSKDNTPMFVKGANFDKYAGQD-IVSN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 270 ASCTTNAIVPVLKAVNDQYGIVNGHVETVHSYTNDQNLIDN-FHKGSRRGRSAPLNMVITETGAATAAAKALPVLKGKLT 348
Cdd:PRK15425 148 ASCTTNCLAPLAKVINDNFGIIEGLMTTVHATTATQKTVDGpSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 349 GNAIRVPTPNVSMAILNLNLEKATTREEINEYLRqmAMHSDLQKQIDFVSSQEVVSTDFVGSRHAGVVDAEATIC-NDNR 427
Cdd:PRK15425 228 GMAFRVPTPNVSVVDLTVRLEKAATYEQIKAAVK--AAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIAlNDNF 305
|
330 340
....*....|....*....|....*
gi 15598197 428 VVLYVWYDNEFGYSCQVVRVMEDMA 452
Cdd:PRK15425 306 VKLVSWYDNETGYSNKVLDLIAHIS 330
|
|
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
117-441 |
1.09e-56 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 190.71 E-value: 1.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 117 GFGRIGRLLARILIEktggGDGLRLRAIVVRKGaenDLVKRASLLRRDSVHGPFDGTITIDeeNNTLTANGNLIQVIYSN 196
Cdd:PRK08955 9 GFGRIGRLALRAAWD----WPELEFVQINDPAG---DAATLAHLLEFDSVHGRWHHEVTAE--GDAIVINGKRIRTTQNK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 197 DPASIDYTQYGiknaLLVDNTGKWRDAEGLGQHLKcPGIDRVVLTAPGK--GALkNIVHGIN-HTDIGADDKIISAASCT 273
Cdd:PRK08955 80 AIADTDWSGCD----VVIEASGVMKTKALLQAYLD-QGVKRVVVTAPVKeeGVL-NIVMGVNdHLFDPAIHPIVTAASCT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 274 TNAIVPVLKAVNDQYGIVNGHVETVHSYTNDQNLIDNFHKGSRRGRSAPLNMVITETGAATAAAKALPVLKGKLTGNAIR 353
Cdd:PRK08955 154 TNCLAPVVKVIHEKLGIKHGSMTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 354 VPTPNVSMAILNLNLEKATTREEINEYLRQmAMHSDLqKQIDFVSSQEVVSTDFVGSRHAGVVDAEAT-ICNDNRVVLYV 432
Cdd:PRK08955 234 VPLANASLTDCVFEVERDTTVEEVNALLKE-AAEGEL-KGILGYEERPLVSIDYKTDPRSSIVDALSTmVVNGTQVKLYA 311
|
....*....
gi 15598197 433 WYDNEFGYS 441
Cdd:PRK08955 312 WYDNEWGYA 320
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
113-452 |
1.57e-53 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 183.33 E-value: 1.57e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 113 VVLYGFGRIGRLLARILIEKTGGGDGLRLRAIVvrkGAENDLVKRASLLRRDSVHGPFDGTITIDE------ENNTLTAN 186
Cdd:PTZ00434 6 VGINGFGRIGRMVFQAICDQGLIGTEIDVVAVV---DMSTNAEYFAYQMKYDTVHGRPKYTVETTKsspsvkTDDVLVVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 187 GNLIQVIYSN-DPASIDYTQYGIKnaLLVDNTGKWRDAEGLGQHLKcPGIDRVVLTAPGKGALKNIVHGINHTDIG-ADD 264
Cdd:PTZ00434 83 GHRIKCVKAQrNPADLPWGKLGVD--YVIESTGLFTDKLAAEGHLK-GGAKKVVISAPASGGAKTIVMGVNQHEYSpTEH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 265 KIISAASCTTNAIVPVLKA-VNDQYGIVNGHVETVHSYTNDQNLIDNFH-KGSRRGRSAPLNMVITETGAATAAAKALPV 342
Cdd:PTZ00434 160 HVVSNASCTTNCLAPIVHVlTKEGFGIETGLMTTIHSYTATQKTVDGVSvKDWRGGRAAAVNIIPSTTGAAKAVGMVIPS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 343 LKGKLTGNAIRVPTPNVSMAILNLNLEKATTREEINEYLRQMAmhSDLQKQIDFVSSQEVVSTDFVGSRHAGVVDAEATI 422
Cdd:PTZ00434 240 TKGKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRAS--QTYMKGILGFTDDELVSADFINDNRSSIYDSKATL 317
|
330 340 350
....*....|....*....|....*....|....*
gi 15598197 423 CN----DNRVVLYV-WYDNEFGYSCQVVRVMEDMA 452
Cdd:PTZ00434 318 QNnlpgERRFFKIVsWYDNEWGYSHRVVDLVRYMA 352
|
|
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
117-452 |
1.58e-53 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 182.61 E-value: 1.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 117 GFGRIGRLLARILIEKtgggDGLRLRAIvvrkgaeNDLVKRAS----LLRRDSVHGPFDGTITIDEENNTLTANGNLIQV 192
Cdd:PLN02358 12 GFGRIGRLVARVVLQR----DDVELVAV-------NDPFITTEymtyMFKYDSVHGQWKHHELKVKDDKTLLFGEKPVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 193 IYSNDPASIDYTQYGIKnaLLVDNTGKWRDAEGLGQHLKcPGIDRVVLTAPGKGALKNIVhGINHTDIGADDKIISAASC 272
Cdd:PLN02358 81 FGIRNPEDIPWGEAGAD--FVVESTGVFTDKDKAAAHLK-GGAKKVVISAPSKDAPMFVV-GVNEHEYKSDLDIVSNASC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 273 TTNAIVPVLKAVNDQYGIVNGHVETVHSYTNDQNLIDN-FHKGSRRGRSAPLNMVITETGAATAAAKALPVLKGKLTGNA 351
Cdd:PLN02358 157 TTNCLAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGpSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 352 IRVPTPNVSMAILNLNLEKATTREEINEYLRQMAmhSDLQKQIDFVSSQEVVSTDFVGSRHAGVVDAEATIC-NDNRVVL 430
Cdd:PLN02358 237 FRVPTVDVSVVDLTVRLEKAATYDEIKKAIKEES--EGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIAlSDKFVKL 314
|
330 340
....*....|....*....|..
gi 15598197 431 YVWYDNEFGYSCQVVRVMEDMA 452
Cdd:PLN02358 315 VSWYDNEWGYSSRVVDLIVHMS 336
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
113-441 |
1.97e-48 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 169.08 E-value: 1.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 113 VVLYGFGRIGRLLARILIEKtgggdGLRLRAIVVrkgAENDLVKR---ASLLRRDSVHGPFDGTITIDeeNNTLTANGNL 189
Cdd:PRK13535 4 VAINGFGRIGRNVLRALYES-----GRRAEITVV---AINELADAegmAHLLKYDTSHGRFAWDVRQE--RDQLFVGDDA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 190 IQVIYSNDPASIDYTQYGIKnaLLVDNTGKWRDAEGLGQHLKCpGIDRVVLTAPGKGALKN-IVHGINHTDIGADDKIIS 268
Cdd:PRK13535 74 IRLLHERDIASLPWRELGVD--VVLDCTGVYGSREDGEAHIAA-GAKKVLFSHPGSNDLDAtVVYGVNHDQLRAEHRIVS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 269 AASCTTNAIVPVLKAVNDQYGIVNGHVETVHSYTNDQNLIDNFHKGSRRGRSAPLNMVITETGAATAAAKALPVLKGKLT 348
Cdd:PRK13535 151 NASCTTNCIIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 349 GNAIRVPTPNVSMAILNLNLEKATTREEINEYLrQMAMHSDLQKQIDFvSSQEVVSTDFVGSRHAGVVDAEAT-ICNDNR 427
Cdd:PRK13535 231 AISVRVPTINVTAIDLSVTVKKPVKVNEVNQLL-QKAAQGAFHGIVDY-TELPLVSIDFNHDPHSAIVDGTQTrVSGAHL 308
|
330
....*....|....
gi 15598197 428 VVLYVWYDNEFGYS 441
Cdd:PRK13535 309 IKTLVWCDNEWGFA 322
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
111-272 |
4.73e-47 |
|
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. N-terminal domain is a Rossmann NAD(P) binding fold.
Pssm-ID: 214851 [Multi-domain] Cd Length: 149 Bit Score: 159.25 E-value: 4.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 111 TDVVLYGFGRIGRLLARILIEktgggdglRLRAIVVRKGAENDLVKRASLLRRDSVHGPFDGTITIDEENntLTANGNLI 190
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALE--------RPDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEVEGDG--LVVNGKAI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 191 QVIYSNDPASIDYTQYGIKnaLLVDNTGKWRDAEGLGQHLKCpGIDRVVLTAPGKGALKNIVHGINHTDIGADDKIISAA 270
Cdd:smart00846 71 KVFAERDPANLPWGELGVD--IVVECTGGFTTREKASAHLKA-GAKKVIISAPSKDADPTFVYGVNHDEYDGEDHIISNA 147
|
..
gi 15598197 271 SC 272
Cdd:smart00846 148 SC 149
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
277-434 |
2.59e-42 |
|
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: 146.97 E-value: 2.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 277 IVPVLKAVNDQYGIVNGHVETVHSYTNDQNLIDNFHKGS-RRGRSAPLNMVITETGAATAAAKALPVLKGKLTGNAIRVP 355
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDlRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 356 TPNVSMAILNLNLEKATTREEINEYLRQMAMHSdlQKQIDFVSSQEVVSTDFVGSRHAGVVDAEATI-CNDNRVVLYVWY 434
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGA--LKGILSYTEDPLVSSDFIGDPHSSIFDAKETIvVNGNFVKVVAWY 158
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
272-437 |
3.34e-35 |
|
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: 128.69 E-value: 3.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 272 CTTNAIVPVLKAVNDQYGIVNGHVETVHSYTNDQNLIDNFHKGSRRGRSAPLNMVITETGAATAAAKALPVLKGKLTGNA 351
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 352 IRVPTPNVSMAILNLNLEKATTREEINEYLRQmAMHSDLQKQIDFvSSQEVVSTDFVGSRHAGVVDAEATICNDNRVV-L 430
Cdd:cd23937 81 VRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQ-ASQGRLKGILGY-TEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVkL 158
|
....*..
gi 15598197 431 YVWYDNE 437
Cdd:cd23937 159 LVWCDNE 165
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
272-437 |
4.08e-34 |
|
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: 125.42 E-value: 4.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 272 CTTNAIVPVLKAVNDQYGIVNGHVETVHSYTNDQNLIDNFHKGSRRGRSAPLNMVI-TETGAATAAAKALPVLKGKLTGN 350
Cdd:cd18123 1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIpNPTGAAKAVGKVLPELNGKLTGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 351 AIRVPTPNVSMAILNLNLEKATTREEINEYLRQMAMhsdlQKQIDFVSSQEVVSTDFVGSRHAGVVDAEATIC-NDNRVV 429
Cdd:cd18123 81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPE----GKGRLGYTEAEDVSSDFRGDIFESVFDAESIIAvNDNEVK 156
|
....*...
gi 15598197 430 LYVWYDNE 437
Cdd:cd18123 157 LMQWYDNE 164
|
|
| Gp_dh_N |
pfam00044 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
111-223 |
2.12e-23 |
|
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: 94.09 E-value: 2.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 111 TDVVLYGFGRIGRLLARILIEKtgggDGLRLRAIvvrkgaeNDLV---KRASLLRRDSVHGPFDGTITidEENNTLTANG 187
Cdd:pfam00044 1 VKVGINGFGRIGRLVLRAALER----PDIEVVAI-------NDLTdpeTLAYLLKYDSVHGRFPGEVE--AEEDGLVVNG 67
|
90 100 110
....*....|....*....|....*....|....*.
gi 15598197 188 NLIQVIYSNDPASIDYTQYGIKnaLLVDNTGKWRDA 223
Cdd:pfam00044 68 KKIKVFAERDPAELPWGDLGVD--VVIESTGVFTTK 101
|
|
| GAPDH_N_E4PDH |
cd17892 |
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
113-271 |
5.14e-23 |
|
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: 95.41 E-value: 5.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 113 VVLYGFGRIGRLLARILIEkTGGGDGLRLRAIvvrkgaeNDLVKRAS---LLRRDSVHGPFDGTITIdeENNTLTANGNL 189
Cdd:cd17892 3 VAINGYGRIGRNVLRALYE-SGRRAEFQVVAI-------NELADAETiahLTKYDTTHGRFPGEVRV--ENDQLFVNGDK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 190 IQVIYSNDPASIDYTQYGIKnaLLVDNTGKWRDAEGLGQHLKCpGIDRVVLTAPGKGALKN-IVHGINHTDIGADDKIIS 268
Cdd:cd17892 73 IRVLHEPDPENLPWRELGID--LVLECTGVFGSREDAERHLAA-GAKKVLFSHPASNDVDAtIVYGINQDLLRAEHRIVS 149
|
...
gi 15598197 269 AAS 271
Cdd:cd17892 150 NAS 152
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
272-437 |
1.89e-16 |
|
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: 76.79 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 272 CTTNAIVPVLKAVNDQYGIVNGHVETVHSYTNDQNLIDNFHKGSRRGRSAPlNMVITETGAATAAAKALPVL--KGKLTG 349
Cdd:cd18122 1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSEVRAIIP-NIPKNETKHAPETGKVLGEIgkPIKVDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 350 NAIRVPTPNVSMAILNLNLEKATTREEINEYLRQMAmhSDLQKQIDFVSSQEVVSTDFVGSRHAGVVDAEATIC-NDNRV 428
Cdd:cd18122 80 IAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAV--EEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAfDDNKL 157
|
....*....
gi 15598197 429 VLYVWYDNE 437
Cdd:cd18122 158 KVFSAVDNE 166
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
158-457 |
3.70e-11 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 64.13 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 158 ASLLRRDSVHGPFDGT-ITIDEENNTLTaNGNLIQVIYSNDPASIDYTQYGIKnaLLVDNTGKWRDAEGLGQHLKcpGID 236
Cdd:PTZ00353 43 AYVLEQESPLSAPDGAsIRVVGEQIVLN-GTQKIRVSAKHDLVEIAWRDYGVQ--YVVECTGLYSTRSRCWGHVT--GGA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 237 RVVLTAPGKGALKNIVHGINHTDIGADDKIISAASCTTNAIVPVLKAVNDQYGIVNGHVETVHSyTNDQNLIDNFHKGSR 316
Cdd:PTZ00353 118 KGVFVAGQSADAPTVMAGSNDERLSASLPVCCAGAPIAVALAPVIRALHEVYGVEECSYTAIHG-MQPQEPIAARSKNSQ 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598197 317 RGRSAPL---NMVITETGAATAAAKALPVLKGKLTGNAIRVPTPNVSMAILNLNLEKATTREEINEYLRQMAmhSDLQKQ 393
Cdd:PTZ00353 197 DWRQTRVaidAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVKKGCAIDMLVRTKQPVSKEVVDSALAEAA--SDRLNG 274
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598197 394 IDFVSSQEVVSTDFVGSRHAgVVDAEATICNDN----RVVLyvWYDNEFGYSCQVVRVMEDMAGVNPP 457
Cdd:PTZ00353 275 VLCISKRDMISVDCIPNGKL-CYDATSSSSSREgevhKMVL--WFDVECYYAARLLSLVKQLHQIHAP 339
|
|
| |
