|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
1-310 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 581.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 1 MADKKIRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKHHELKVKDDKTLLFGEKPVTV 80
Cdd:PLN02358 1 MADKKIRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKHHELKVKDDKTLLFGEKPVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 81 FGIRNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHE----------------- 143
Cdd:PLN02358 81 FGIRNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEyksdldivsnascttnc 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 144 -----------FGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVP 212
Cdd:PLN02358 161 laplakvindrFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 213 TVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKMKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDN 292
Cdd:PLN02358 241 TVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDN 320
|
330
....*....|....*...
gi 145323882 293 EWGYSSRVVDLIVHMSKA 310
Cdd:PLN02358 321 EWGYSSRVVDLIVHMSKA 338
|
|
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
5-310 |
3.50e-179 |
|
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: 497.61 E-value: 3.50e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 5 KIRIGINGFGRIGRLVARVVLQR-DDVELVAVNDPfITTEYMTYMFKYDSVHGQWKHhELKVKDDkTLLFGEKPVTVFGI 83
Cdd:COG0057 2 TIRVAINGFGRIGRLVLRALLERgPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPG-EVEVEGD-SLIVNGKKIKVLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 84 RNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDA-PMFVVGVNEH-------------------- 142
Cdd:COG0057 79 RDPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDdydadhriisnascttncla 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 143 --------EFGIVEGLMTTVHSITATQKTVDGPsMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTV 214
Cdd:COG0057 159 pvakvlndAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 215 DVSVVDLTVRLEKAATYDEIKKAIKEESEGKMKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEW 294
Cdd:COG0057 238 NVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEW 317
|
330
....*....|....*.
gi 145323882 295 GYSSRVVDLIVHMSKA 310
Cdd:COG0057 318 GYSNRMVDLAEYMAKL 333
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
7-302 |
3.33e-148 |
|
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: 418.99 E-value: 3.33e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 7 RIGINGFGRIGRLVARVVLQRDD--VELVAVNDPfITTEYMTYMFKYDSVHGQWKHhELKVKDDKTLLFGEKPVTVFGIR 84
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKPGndLEVVAINDL-TDLEKLAYLLKYDSVHGRFEG-EVTVDEDGLVVNGKEVISVFSER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 85 NPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDA-PMFVVGVNEH--------------------- 142
Cdd:TIGR01534 79 DPSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDeydgeeriisnascttnclap 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 143 -------EFGIVEGLMTTVHSITATQKTVDGPsMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVD 215
Cdd:TIGR01534 159 lakvldeAFGIVSGLMTTVHAYTNDQNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 216 VSVVDLTVRLEKAATYDEIKKAIKEESEGKMKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIA--LSDKFVKLVSWYDNE 293
Cdd:TIGR01534 238 VSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNE 317
|
....*....
gi 145323882 294 WGYSSRVVD 302
Cdd:TIGR01534 318 WGYSNRLVD 326
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
132-293 |
3.39e-106 |
|
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: 306.30 E-value: 3.39e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 132 APMFVVgVNEhEFGIVEGLMTTVHSITATQKTVDGPSmKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRV 211
Cdd:cd18126 7 APVAKV-LND-NFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMAFRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 212 PTVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKMKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYD 291
Cdd:cd18126 84 PTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVVAWYD 163
|
..
gi 145323882 292 NE 293
Cdd:cd18126 164 NE 165
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
8-303 |
2.17e-96 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 287.60 E-value: 2.17e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 8 IGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWkHHELKVKDDkTLLFGEKPVTVFGIRNPE 87
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRW-DAEVTAEED-SIVIDGKRISFSSNKDIE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 88 DIPWGEaGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMF--VVGVNEH----------------------- 142
Cdd:NF033735 79 DTPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLniVYGVNDHlydparhrivtaascttnclapv 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 143 ------EFGIVEGLMTTVHSITATQKTVDGPSmKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDV 216
Cdd:NF033735 158 vkviheKIGIKHGSITTIHDITNTQTIVDAPH-KDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 217 SVVDLTVRLEKAATYDEIKKAIKEESEGKMKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEWGY 296
Cdd:NF033735 237 SLTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGY 316
|
....*..
gi 145323882 297 SSRVVDL 303
Cdd:NF033735 317 ANRMVDL 323
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
143-290 |
5.55e-83 |
|
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: 247.12 E-value: 5.55e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 143 EFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLT 222
Cdd:pfam02800 11 NFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSVVDLV 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145323882 223 VRLEKAATYDEIKKAIKEESEGKMKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWY 290
Cdd:pfam02800 91 VELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
6-144 |
1.71e-65 |
|
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: 202.40 E-value: 1.71e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 6 IRIGINGFGRIGRLVARVVLQRDDVELVAVNDPfITTEYMTYMFKYDSVHGQWkHHELKVKDDkTLLFGEKPVTVFGIRN 85
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRF-PGTVEVEGD-GLVVNGKAIKVFAERD 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 86 PEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDA-PMFVVGVNEHEF 144
Cdd:smart00846 78 PANLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEY 137
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
1-310 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 581.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 1 MADKKIRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKHHELKVKDDKTLLFGEKPVTV 80
Cdd:PLN02358 1 MADKKIRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKHHELKVKDDKTLLFGEKPVTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 81 FGIRNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHE----------------- 143
Cdd:PLN02358 81 FGIRNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEyksdldivsnascttnc 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 144 -----------FGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVP 212
Cdd:PLN02358 161 laplakvindrFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 213 TVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKMKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDN 292
Cdd:PLN02358 241 TVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDN 320
|
330
....*....|....*...
gi 145323882 293 EWGYSSRVVDLIVHMSKA 310
Cdd:PLN02358 321 EWGYSSRVVDLIVHMSKA 338
|
|
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
2-308 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 559.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 2 ADKKIRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKHHeLKVKDDKTLLFGEKPVTVF 81
Cdd:PLN02272 82 SSGKTKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGT-INVVDDSTLEINGKQIKVT 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 82 GIRNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEH------------------- 142
Cdd:PLN02272 161 SKRDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKtykpnmnivsnascttncl 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 143 ---------EFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPT 213
Cdd:PLN02272 241 aplakvvheEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPT 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 214 VDVSVVDLTVRLEKAATYDEIKKAIKEESEGKMKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNE 293
Cdd:PLN02272 321 PNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNE 400
|
330
....*....|....*
gi 145323882 294 WGYSSRVVDLIVHMS 308
Cdd:PLN02272 401 WGYSNRVLDLIEHMA 415
|
|
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
5-310 |
3.50e-179 |
|
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: 497.61 E-value: 3.50e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 5 KIRIGINGFGRIGRLVARVVLQR-DDVELVAVNDPfITTEYMTYMFKYDSVHGQWKHhELKVKDDkTLLFGEKPVTVFGI 83
Cdd:COG0057 2 TIRVAINGFGRIGRLVLRALLERgPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPG-EVEVEGD-SLIVNGKKIKVLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 84 RNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDA-PMFVVGVNEH-------------------- 142
Cdd:COG0057 79 RDPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDdydadhriisnascttncla 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 143 --------EFGIVEGLMTTVHSITATQKTVDGPsMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTV 214
Cdd:COG0057 159 pvakvlndAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 215 DVSVVDLTVRLEKAATYDEIKKAIKEESEGKMKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEW 294
Cdd:COG0057 238 NVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEW 317
|
330
....*....|....*.
gi 145323882 295 GYSSRVVDLIVHMSKA 310
Cdd:COG0057 318 GYSNRMVDLAEYMAKL 333
|
|
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
6-309 |
5.77e-154 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 434.26 E-value: 5.77e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 6 IRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKHhELKVKDDkTLLFGEKPVTVFGIRN 85
Cdd:PTZ00023 3 VKLGINGFGRIGRLVFRAALEREDVEVVAINDPFMTLDYMCYLLKYDSVHGSLPA-EVSVTDG-FLMIGSKKVHVFFEKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 86 PEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKD-APMFVVGVNEHE--------------------- 143
Cdd:PTZ00023 81 PAAIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKDdTPIYVMGVNHTQydksqrivsnascttnclapl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 144 -------FGIVEGLMTTVHSITATQKTVDGPSM--KDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTV 214
Cdd:PTZ00023 161 akvvndkFGIVEGLMTTVHASTANQLTVDGPSKggKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 215 DVSVVDLTVRLEKAATYDEIKKAIKEESEGKMKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEW 294
Cdd:PTZ00023 241 DVSVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDNEW 320
|
330
....*....|....*
gi 145323882 295 GYSSRVVDLIVHMSK 309
Cdd:PTZ00023 321 GYSNRLLDLAHYITQ 335
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
7-302 |
3.33e-148 |
|
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: 418.99 E-value: 3.33e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 7 RIGINGFGRIGRLVARVVLQRDD--VELVAVNDPfITTEYMTYMFKYDSVHGQWKHhELKVKDDKTLLFGEKPVTVFGIR 84
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKPGndLEVVAINDL-TDLEKLAYLLKYDSVHGRFEG-EVTVDEDGLVVNGKEVISVFSER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 85 NPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDA-PMFVVGVNEH--------------------- 142
Cdd:TIGR01534 79 DPSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDeydgeeriisnascttnclap 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 143 -------EFGIVEGLMTTVHSITATQKTVDGPsMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVD 215
Cdd:TIGR01534 159 lakvldeAFGIVSGLMTTVHAYTNDQNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 216 VSVVDLTVRLEKAATYDEIKKAIKEESEGKMKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIA--LSDKFVKLVSWYDNE 293
Cdd:TIGR01534 238 VSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNE 317
|
....*....
gi 145323882 294 WGYSSRVVD 302
Cdd:TIGR01534 318 WGYSNRLVD 326
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
6-308 |
5.68e-132 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 379.40 E-value: 5.68e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 6 IRIGINGFGRIGRLVARVVLQRD----DVELVAVNDPFITTEYMTYMFKYDSVHGQWKHHELKVK-------DDKTLLFG 74
Cdd:PTZ00434 4 IKVGINGFGRIGRMVFQAICDQGligtEIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVETTKsspsvktDDVLVVNG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 75 EKPVTVFGIRNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAP-SKDAPMFVVGVNEHE---------- 143
Cdd:PTZ00434 84 HRIKCVKAQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPaSGGAKTIVMGVNQHEysptehhvvs 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 144 --------------------FGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGK 203
Cdd:PTZ00434 164 nascttnclapivhvltkegFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 204 LTGMSFRVPTVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKMKGILGYTEDDVVSTDFVGDNRSSIFDAKA----GIAL 279
Cdd:PTZ00434 244 LTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKAtlqnNLPG 323
|
330 340
....*....|....*....|....*....
gi 145323882 280 SDKFVKLVSWYDNEWGYSSRVVDLIVHMS 308
Cdd:PTZ00434 324 ERRFFKIVSWYDNEWGYSHRVVDLVRYMA 352
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
6-309 |
3.54e-130 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 373.69 E-value: 3.54e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 6 IRIGINGFGRIGRLVARVVLQRDDVELVAVNDpFITTEYMTYMFKYDSVHGQWKHhELKVKDDKTLLFGEKpVTVFGIRN 85
Cdd:PRK15425 3 IKVGINGFGRIGRIVFRAAQKRSDIEIVAIND-LLDADYMAYMLKYDSTHGRFDG-TVEVKDGHLIVNGKK-IRVTAERD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 86 PEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKD-APMFVVGVN------------------------ 140
Cdd:PRK15425 80 PANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDnTPMFVKGANfdkyagqdivsnascttnclapla 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 141 ---EHEFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVS 217
Cdd:PRK15425 160 kviNDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 218 VVDLTVRLEKAATYDEIKKAIKEESEGKMKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEWGYS 297
Cdd:PRK15425 240 VVDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYS 319
|
330
....*....|..
gi 145323882 298 SRVVDLIVHMSK 309
Cdd:PRK15425 320 NKVLDLIAHISK 331
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
5-309 |
3.97e-109 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 320.53 E-value: 3.97e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 5 KIRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFiTTEYMTYMFKYDSVHGQWKHhELKVKDDKTLLFGEKpVTVFGIR 84
Cdd:PRK07729 2 KTKVAINGFGRIGRMVFRKAIKESAFEIVAINASY-PSETLAHLIKYDTVHGKFDG-TVEAFEDHLLVDGKK-IRLLNNR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 85 NPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPM-FVVGVNEH--------------------- 142
Cdd:PRK07729 79 DPKELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVtIVVGVNEDqldiekhtiisnascttncla 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 143 --------EFGIVEGLMTTVHSITATQKTVDGPSmKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTV 214
Cdd:PRK07729 159 pvvkvldeQFGIENGLMTTVHAYTNDQKNIDNPH-KDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 215 DVSVVDLTVRLEKAATYDEIKKAIKEESEGKMKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEW 294
Cdd:PRK07729 238 NVSLVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEW 317
|
330
....*....|....*
gi 145323882 295 GYSSRVVDLIVHMSK 309
Cdd:PRK07729 318 GYSCRVVDLVTLVAD 332
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
132-293 |
3.39e-106 |
|
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: 306.30 E-value: 3.39e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 132 APMFVVgVNEhEFGIVEGLMTTVHSITATQKTVDGPSmKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRV 211
Cdd:cd18126 7 APVAKV-LND-NFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMAFRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 212 PTVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKMKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYD 291
Cdd:cd18126 84 PTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVVAWYD 163
|
..
gi 145323882 292 NE 293
Cdd:cd18126 164 NE 165
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
8-303 |
2.17e-96 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 287.60 E-value: 2.17e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 8 IGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWkHHELKVKDDkTLLFGEKPVTVFGIRNPE 87
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRW-DAEVTAEED-SIVIDGKRISFSSNKDIE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 88 DIPWGEaGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMF--VVGVNEH----------------------- 142
Cdd:NF033735 79 DTPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLniVYGVNDHlydparhrivtaascttnclapv 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 143 ------EFGIVEGLMTTVHSITATQKTVDGPSmKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDV 216
Cdd:NF033735 158 vkviheKIGIKHGSITTIHDITNTQTIVDAPH-KDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 217 SVVDLTVRLEKAATYDEIKKAIKEESEGKMKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEWGY 296
Cdd:NF033735 237 SLTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGY 316
|
....*..
gi 145323882 297 SSRVVDL 303
Cdd:NF033735 317 ANRMVDL 323
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
6-303 |
5.63e-96 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 286.80 E-value: 5.63e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 6 IRIGINGFGRIGRLVARVVLQRDD--VELVAVNDpfiTTEYMT--YMFKYDSVHGqwKHHELKVKDDKTLLFGEKPVTVF 81
Cdd:PRK07403 2 IRVAINGFGRIGRNFLRCWLGRENsqLELVAIND---TSDPRTnaHLLKYDSMLG--KLNADISADENSITVNGKTIKCV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 82 GIRNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSK--DAPMFVVGVNEHE---------------- 143
Cdd:PRK07403 77 SDRNPLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPGKgeDIGTYVVGVNHHEydhedhniisnasctt 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 144 -------------FGIVEGLMTTVHSITATQKTVDGpSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFR 210
Cdd:PRK07403 157 nclapiakvlhdnFGIIKGTMTTTHSYTGDQRILDA-SHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 211 VPTVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKMKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWY 290
Cdd:PRK07403 236 VPTPNVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWY 315
|
330
....*....|...
gi 145323882 291 DNEWGYSSRVVDL 303
Cdd:PRK07403 316 DNEWGYSQRVVDL 328
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
1-303 |
5.04e-90 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 275.24 E-value: 5.04e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 1 MADKKIRIGINGFGRIGRLVARVVLQRDD--VELVAVNDPFiTTEYMTYMFKYDSVHGQWKHhELKVKDDKTLLFGEKPV 78
Cdd:PLN02237 71 ETVAKLKVAINGFGRIGRNFLRCWHGRKDspLDVVVVNDSG-GVKNASHLLKYDSMLGTFKA-DVKIVDDETISVDGKPI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 79 TVFGIRNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSK--DAPMFVVGVNE--------------- 141
Cdd:PLN02237 149 KVVSNRDPLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAKgaDIPTYVVGVNEddydhevanivsnas 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 142 --------------HEFGIVEGLMTTVHSITATQKTVDGpSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGM 207
Cdd:PLN02237 229 cttnclapfvkvldEEFGIVKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGI 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 208 SFRVPTVDVSVVDLTVRLEKAA-TYDEIKKAIKEESEGKMKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKL 286
Cdd:PLN02237 308 ALRVPTPNVSVVDLVVNVEKKGiTAEDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKV 387
|
330
....*....|....*..
gi 145323882 287 VSWYDNEWGYSSRVVDL 303
Cdd:PLN02237 388 VAWYDNEWGYSQRVVDL 404
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
1-303 |
5.66e-90 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 273.73 E-value: 5.66e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 1 MADKKIRIGINGFGRIGRLVARVVLQRDD--VELVAVNDPFiTTEYMTYMFKYDSVHGQWKHhELKVKDDKTLLFGEKPV 78
Cdd:PLN03096 56 VTEAKIKVAINGFGRIGRNFLRCWHGRKDspLDVVAINDTG-GVKQASHLLKYDSTLGTFDA-DVKPVGDDAISVDGKVI 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 79 TVFGIRNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSK-DAPMFVVGVNEHE-------------- 143
Cdd:PLN03096 134 KVVSDRNPLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKgDIPTYVVGVNADDykhsdpiisnasct 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 144 --------------FGIVEGLMTTVHSITATQKTVDGpSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSF 209
Cdd:PLN03096 214 tnclapfvkvldqkFGIIKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIAL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 210 RVPTVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKMKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSW 289
Cdd:PLN03096 293 RVPTPNVSVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAW 372
|
330
....*....|....
gi 145323882 290 YDNEWGYSSRVVDL 303
Cdd:PLN03096 373 YDNEWGYSQRVVDL 386
|
|
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
5-304 |
3.51e-86 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 261.97 E-value: 3.51e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 5 KIRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWkHHELKVKDDkTLLFGEKPVTVFGIR 84
Cdd:PRK08955 2 TIKVGINGFGRIGRLALRAAWDWPELEFVQINDPAGDAATLAHLLEFDSVHGRW-HHEVTAEGD-AIVINGKRIRTTQNK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 85 NPEDIPWgeAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMF--VVGVNEH-------------------- 142
Cdd:PRK08955 80 AIADTDW--SGCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLniVMGVNDHlfdpaihpivtaascttncl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 143 ---------EFGIVEGLMTTVHSITATQKTVDGPSmKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPT 213
Cdd:PRK08955 158 apvvkviheKLGIKHGSMTTIHDLTNTQTILDAPH-KDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 214 VDVSVVDLTVRLEKAATYDEIKKAIKEESEGKMKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNE 293
Cdd:PRK08955 237 ANASLTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNE 316
|
330
....*....|.
gi 145323882 294 WGYSSRVVDLI 304
Cdd:PRK08955 317 WGYANRTAELA 327
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
143-290 |
5.55e-83 |
|
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: 247.12 E-value: 5.55e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 143 EFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLT 222
Cdd:pfam02800 11 NFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSVVDLV 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145323882 223 VRLEKAATYDEIKKAIKEESEGKMKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWY 290
Cdd:pfam02800 91 VELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
6-310 |
1.14e-74 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 232.25 E-value: 1.14e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 6 IRIGINGFGRIGRLVARVVLQ---RDDVELVAVNDpFITTEYMTYMFKYDSVHGQWKHhelKVKDDKTLLF-GEKPVTVF 81
Cdd:PRK13535 2 IRVAINGFGRIGRNVLRALYEsgrRAEITVVAINE-LADAEGMAHLLKYDTSHGRFAW---DVRQERDQLFvGDDAIRLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 82 GIRNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSK---DAPMfVVGVNEHE--------------- 143
Cdd:PRK13535 78 HERDIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSndlDATV-VYGVNHDQlraehrivsnasctt 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 144 -------------FGIVEGLMTTVHSITATQKTVDGpSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFR 210
Cdd:PRK13535 157 nciipvikllddaFGIESGTVTTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 211 VPTVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKMKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWY 290
Cdd:PRK13535 236 VPTINVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWC 315
|
330 340
....*....|....*....|
gi 145323882 291 DNEWGYSSRVVDLIVHMSKA 310
Cdd:PRK13535 316 DNEWGFANRMLDTTLAMAAA 335
|
|
| GAPDH_I_N |
cd05214 |
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
6-144 |
1.20e-74 |
|
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: 226.12 E-value: 1.20e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 6 IRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITtEYMTYMFKYDSVHGQWKHhELKVKDDKtLLFGEKPVTVFGIRN 85
Cdd:cd05214 1 IKVGINGFGRIGRLVFRAALERDDIEVVAINDLTDD-ETLAYLLKYDSVHGRFDG-EVEVDDDA-LIVNGKKIKVFAERD 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 86 PEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKD-APMFVVGVNEHEF 144
Cdd:cd05214 78 PAELPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKY 137
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
144-293 |
1.22e-69 |
|
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: 213.63 E-value: 1.22e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 144 FGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTV 223
Cdd:cd18123 17 FGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGMAVRVPTTLMSVHDLMV 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 224 RLEKAATYDEIKKAIKEESEGkmKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNE 293
Cdd:cd18123 97 ELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLMQWYDNE 164
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
6-144 |
1.71e-65 |
|
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: 202.40 E-value: 1.71e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 6 IRIGINGFGRIGRLVARVVLQRDDVELVAVNDPfITTEYMTYMFKYDSVHGQWkHHELKVKDDkTLLFGEKPVTVFGIRN 85
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRF-PGTVEVEGD-GLVVNGKAIKVFAERD 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 86 PEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDA-PMFVVGVNEHEF 144
Cdd:smart00846 78 PANLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEY 137
|
|
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
12-310 |
4.89e-65 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 211.70 E-value: 4.89e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 12 GFGRIGRLVARVVLQR----DDVELVAV-------NDpfitTEYMTYMFKYDSVHGQWKHHELKVKDDKTLLFGEKPVTV 80
Cdd:PRK08289 134 GFGRIGRLLARLLIEKtgggNGLRLRAIvvrkgseGD----LEKRASLLRRDSVHGPFNGTITVDEENNAIIANGNYIQV 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 81 FGIRNPEDIPWGEAGAD--FVVESTGVFTDKDKAAAHLKG-GAKKVVISAPSK-DAPMFVVGVNEH-------------- 142
Cdd:PRK08289 210 IYANSPEEVDYTAYGINnaLVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGKgDIKNIVHGVNHSditdedkivsaasc 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 143 --------------EFGIVEGLMTTVHSITATQKTVDGPSMKDwRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMS 208
Cdd:PRK08289 290 ttnaitpvlkavndKYGIVNGHVETVHSYTNDQNLIDNYHKGD-RRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNA 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 209 FRVPTVDVSVVDLTVRLEKAATYDEIKKAIKEES-EGKMKGILGYTED-DVVSTDFVGDNRSSIFDAKAGIAlSDKFVKL 286
Cdd:PRK08289 369 IRVPTPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQIDYTDStEVVSSDFVGSRHAGVVDSQATIV-NGNRAVL 447
|
330 340
....*....|....*....|....
gi 145323882 287 VSWYDNEWGYSSRVVDLIVHMSKA 310
Cdd:PRK08289 448 YVWYDNEFGYSCQVVRVMEQMAGV 471
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
6-310 |
3.40e-52 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 174.68 E-value: 3.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 6 IRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKHHELKVKDDKTLLFGEKPVTVFGIRN 85
Cdd:PTZ00353 3 ITVGINGFGPVGKAVLFASLTDPLVTVVAVNDASVSIAYIAYVLEQESPLSAPDGASIRVVGEQIVLNGTQKIRVSAKHD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 86 PEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHE---------------------- 143
Cdd:PTZ00353 83 LVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDERlsaslpvccagapiavalapvi 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 144 ------FGIVEGLMTTVHSITAtQKTVDGPSM--KDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVD 215
Cdd:PTZ00353 163 ralhevYGVEECSYTAIHGMQP-QEPIAARSKnsQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 216 VSVVDLTVRLEKAATYDEIKKAIKEESEGKMKGILGYTEDDVVSTDFVGDNRsSIFDAKAGIALSD-KFVKLVSWYDNEW 294
Cdd:PTZ00353 242 GCAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCIPNGK-LCYDATSSSSSREgEVHKMVLWFDVEC 320
|
330
....*....|....*.
gi 145323882 295 GYSSRVVDLIVHMSKA 310
Cdd:PTZ00353 321 YYAARLLSLVKQLHQI 336
|
|
| Gp_dh_N |
pfam00044 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
6-109 |
1.20e-43 |
|
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: 144.94 E-value: 1.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 6 IRIGINGFGRIGRLVARVVLQRDDVELVAVNDpFITTEYMTYMFKYDSVHGQWKhHELKVKDDKtLLFGEKPVTVFGIRN 85
Cdd:pfam00044 1 VKVGINGFGRIGRLVLRAALERPDIEVVAIND-LTDPETLAYLLKYDSVHGRFP-GEVEAEEDG-LVVNGKKIKVFAERD 77
|
90 100
....*....|....*....|....
gi 145323882 86 PEDIPWGEAGADFVVESTGVFTDK 109
Cdd:pfam00044 78 PAELPWGDLGVDVVIESTGVFTTK 101
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
136-293 |
3.52e-40 |
|
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: 137.93 E-value: 3.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 136 VVGVNEHEFGIVEGLMTTVHSITATQKTVDGpSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVD 215
Cdd:cd23937 9 VIKVLDEAFGIESGTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAIAVRVPTIN 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145323882 216 VSVVDLTVRLEKAATYDEIKKAIKEESEGKMKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNE 293
Cdd:cd23937 88 VTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLLVWCDNE 165
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
134-293 |
1.46e-39 |
|
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: 136.50 E-value: 1.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 134 MFVVGVNEHeFGIVEGLMTTVHSITATQKTVDGPSMKDWrgGRAASFNIIPSSTGAAKAVGKVLPSLN--GKLTGMSFRV 211
Cdd:cd18122 8 PAAKALNDK-FGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIGkpIKVDGIAVRV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 212 PTVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKMKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYD 291
Cdd:cd18122 85 PATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLKVFSAVD 164
|
..
gi 145323882 292 NE 293
Cdd:cd18122 165 NE 166
|
|
| GAPDH_N_E4PDH |
cd17892 |
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
6-143 |
3.73e-35 |
|
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: 125.07 E-value: 3.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 6 IRIGINGFGRIGRLVARVVL---QRDDVELVAVNDPfITTEYMTYMFKYDSVHGQWkHHELKVKDDKTLLFGEKpVTVFG 82
Cdd:cd17892 1 YRVAINGYGRIGRNVLRALYesgRRAEFQVVAINEL-ADAETIAHLTKYDTTHGRF-PGEVRVENDQLFVNGDK-IRVLH 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145323882 83 IRNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSK---DAPMfVVGVNEHE 143
Cdd:cd17892 78 EPDPENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASndvDATI-VYGINQDL 140
|
|
| GAPDH-like_N |
cd05192 |
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ... |
6-143 |
2.32e-14 |
|
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: 68.15 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 6 IRIGINGFGRIGRLVARVVLQRDDVELVAVNDPfitteymtymfkydsvhgqwkhhelkvkddktllfgekpvtvfgirn 85
Cdd:cd05192 1 IRVAINGFGRIGRIVFRAIADQDDLDVVAINDR----------------------------------------------- 33
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 145323882 86 pedipwgeagADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHE 143
Cdd:cd05192 34 ----------RDVVIECTGSFTDDDNAEKHIKAGGKKAVITAPEKGDIPTIVVVLNEL 81
|
|
| meso-DAPDH_N |
cd02270 |
N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and ... |
6-35 |
4.47e-05 |
|
N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and similar proteins; Meso-DAPDH (EC 1.4.1.16), also called diaminopimelate dehydrogenase, or meso-DAP dehydrogenase, probably plays a role in lysine biosynthesis. It catalyzes the reversible NADP(H)-dependent reductive amination of L-2-amino-6-oxopimelate, the acyclic form of L-tetrahydrodipicolinate, to generate the meso compound, D,L-2,6-diaminopimelate. DAPDH is a homodimer which is highly specific for meso-DAP and NADP(+) as substrates. Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.
Pssm-ID: 467610 [Multi-domain] Cd Length: 151 Bit Score: 42.94 E-value: 4.47e-05
10 20 30
....*....|....*....|....*....|
gi 145323882 6 IRIGINGFGRIGRLVARVVLQRDDVELVAV 35
Cdd:cd02270 1 IRVAIVGYGNLGRGVEEAIQANPDMELVGV 30
|
|
| MviM |
COG0673 |
Predicted dehydrogenase [General function prediction only]; |
4-38 |
6.69e-05 |
|
Predicted dehydrogenase [General function prediction only];
Pssm-ID: 440437 [Multi-domain] Cd Length: 295 Bit Score: 43.76 E-value: 6.69e-05
10 20 30
....*....|....*....|....*....|....*
gi 145323882 4 KKIRIGINGFGRIGRLVARVVLQRDDVELVAVNDP 38
Cdd:COG0673 2 DKLRVGIIGAGGIGRAHAPALAALPGVELVAVADR 36
|
|
| DapB_N |
pfam01113 |
Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the ... |
6-35 |
9.32e-05 |
|
Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the alpha,beta-unsaturated cyclic imine, dihydro-dipicolinate. This reaction is the second committed step in the biosynthesis of L-lysine and its precursor meso-diaminopimelate, which are critical for both protein and cell wall biosynthesis. The N-terminal domain of DapB binds the dinucleotide NADPH.
Pssm-ID: 460069 [Multi-domain] Cd Length: 121 Bit Score: 41.45 E-value: 9.32e-05
10 20 30
....*....|....*....|....*....|.
gi 145323882 6 IRIGINGF-GRIGRLVARVVLQRDDVELVAV 35
Cdd:pfam01113 1 IKIAVAGAsGRMGRELIKAVLEAPDLELVAA 31
|
|
| DHDPR_N |
cd02274 |
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; ... |
6-37 |
2.38e-04 |
|
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; DHDPR (EC 1.17.1.8), also called 4-hydroxy-tetrahydrodipicolinate reductase, or HTPA reductase, is a product of an essential gene referred to as dapB. It catalyzes the NAD(P)H-dependent reduction of 2,3-dihydrodipicolinate (DHDP) to 2,3,4,5-tetrahydrodipicolinate (THDP). DHDPR could also function as a dehydratase in addition to the role of a nucleotide dependent reductase. DHDPR is a component of the biosynthetic pathway that generates meso-diaminopimelate, a component of bacterial cell walls, and the amino acid L-lysine in various bacteria, archaea, cyanobacteria and higher plants. The enzyme is a homotetramer where each monomer is composed of two domains, an N-terminal NAD(P)-binding domain which forms a Rossmann fold, and a C-terminal substrate-binding domain that forms an open, mixed alpha-beta sandwich.
Pssm-ID: 467611 [Multi-domain] Cd Length: 139 Bit Score: 40.62 E-value: 2.38e-04
10 20 30
....*....|....*....|....*....|...
gi 145323882 6 IRIGINGF-GRIGRLVARVVLQRDDVELVAVND 37
Cdd:cd02274 1 IKVAVAGAtGRMGRELVKAILEAPDLELVGAVD 33
|
|
| PRK04207 |
PRK04207 |
type II glyceraldehyde-3-phosphate dehydrogenase; |
5-35 |
4.50e-04 |
|
type II glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 179786 [Multi-domain] Cd Length: 341 Bit Score: 41.35 E-value: 4.50e-04
10 20 30
....*....|....*....|....*....|.
gi 145323882 5 KIRIGINGFGRIGRLVARVVLQRDDVELVAV 35
Cdd:PRK04207 1 MIKVGVNGYGTIGKRVADAVAAQPDMELVGV 31
|
|
| COG3804 |
COG3804 |
Uncharacterized conserved protein [Function unknown]; |
5-35 |
3.94e-03 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443017 [Multi-domain] Cd Length: 338 Bit Score: 38.24 E-value: 3.94e-03
10 20 30
....*....|....*....|....*....|.
gi 145323882 5 KIRIGINGFGRIGRLVARVVLQRDDVELVAV 35
Cdd:COG3804 1 KIRVVQWGTGNMGRGAIRAILAHPGLELVGA 31
|
|
| nat-AmDH_N_like |
cd24146 |
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ... |
6-126 |
5.04e-03 |
|
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) and similar proteins; The family corresponds to a group of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) that catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. nat-AmDHs can naturally catalyze the amination of 'neutral' carbonyl compounds using ammonia. They possess tremendous potential for the efficient asymmetric synthesis of alpha-chiral amines. The family also contains 2,4-diaminopentanoate dehydrogenase (DAPDH) and similar proteins. DAPDH, also known as ORD, 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). Although DAPDH is more efficient with (2R,4S)-DAP, the diastereoisomer (2R,4R)-DAP can also be metabolized. Different forms of DAPDH exist which utilize NAD(+) (EC 1.4.1.26) or NAD(+)/NADP(+) (EC 1.4.1.12). Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.
Pssm-ID: 467616 [Multi-domain] Cd Length: 157 Bit Score: 36.75 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145323882 6 IRIGINGFGRIGRLVARVVLQRDDVELVAVNDpfitteymtymfkydsvhgqwkHHELKVKDDKTLLFGEKP--VTVFGi 83
Cdd:cd24146 1 IRVVVWGLGAMGRGIARYLLEKPGLEIVGAVD----------------------RDPAKVGKDLGELGGGAPlgVKVTD- 57
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 145323882 84 rNPEDIpWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVIS 126
Cdd:cd24146 58 -DLDAV-LAATKPDVVVHATTSFLADVAPQIERLLEAGLNVIT 98
|
|
| |
