|
Name |
Accession |
Description |
Interval |
E-value |
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
1-352 |
8.36e-162 |
|
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: 456.01 E-value: 8.36e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 1 MVVRIAINGFGRIGRLVFRAVRKlYPTECQVVAIHDLFAIDVNIHLLKYDSAHGTWPEPITkIDNEHFQVGEGptawkve 80
Cdd:COG0057 1 MTIRVAINGFGRIGRLVLRALLE-RGPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVE-VEGDSLIVNGK------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 81 nmvgRIH------PKDLKWGEKKVDVVLESTGVYKT--KAQKgpdgkvtrdgydgHIAAGAKKVVLSVPAGDEIeCTLVL 152
Cdd:COG0057 72 ----KIKvlaerdPAELPWGELGVDVVIECTGKFTDreKASA-------------HLKAGAKKVLISAPAKGDD-PTIVY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 153 GVNDEDVKPTTTMISNASCTTNCLAPITKIINSKWKIITGFMTTVHAYTNDQQVADLAHQDMRRARAAAQNIIPTSTGAA 232
Cdd:COG0057 134 GVNHDDYDADHRIISNASCTTNCLAPVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 233 KALPIVVHDLRPKsLDGISIRVPVITGSLVDTSFNVEGTPTRDEINAALKAATlEGPLKGILGYTEDAIVSSDIINCTLS 312
Cdd:COG0057 214 KAVGLVLPELKGK-LDGMAVRVPTPNVSLVDLTVELEKETTVEEVNAALKEAA-EGPLKGILGYTEEPLVSSDFNGDPHS 291
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 128168587 313 SIVDSLETKVIpnpDGKsaLVKVLSWYDNEAGYSARCADI 352
Cdd:COG0057 292 SIFDALQTIVI---GGN--LVKVLAWYDNEWGYSNRMVDL 326
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
4-351 |
1.01e-147 |
|
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: 419.76 E-value: 1.01e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 4 RIAINGFGRIGRLVFRAVRKLYPTECQVVAIHDLFAIDVNIHLLKYDSAHGTWPEPITKIDNEHFQVGEGPTAWKVENmv 83
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKPGNDLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEVISVFSER-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 84 griHPKDLKWGEKKVDVVLESTGVYktkaqkgpdgkVTRDGYDGHIAAGAKKVVLSVPAGDEIeCTLVLGVNDEDVKPTT 163
Cdd:TIGR01534 79 ---DPSDLPWKALGVDIVIECTGKF-----------RDKEKLEKHLEAGAKKVLISAPSKGDV-KTIVYGVNHDEYDGEE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 164 TMISNASCTTNCLAPITKIINSKWKIITGFMTTVHAYTNDQQVADLAHQDMRRARAAAQNIIPTSTGAAKALPIVVHDLR 243
Cdd:TIGR01534 144 RIISNASCTTNCLAPLAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKDLRRARAAALNIIPTSTGAAKAIGKVLPELA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 244 PKsLDGISIRVPVITGSLVDTSFNVEGTPTRDEINAALKAATlEGPLKGILGYTEDAIVSSDIINCTLSSIVDSLETKVI 323
Cdd:TIGR01534 224 GK-LTGMAIRVPTPNVSLVDLVVNLEKDVTVEEVNAALKEAS-EGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVT 301
|
330 340
....*....|....*....|....*...
gi 128168587 324 PNPDGksaLVKVLSWYDNEAGYSARCAD 351
Cdd:TIGR01534 302 GLGDS---LVKVYAWYDNEWGYSNRLVD 326
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-357 |
7.11e-110 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 324.38 E-value: 7.11e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 1 MVVRIAINGFGRIGRLVFRavRKLYPTECQVVAIHDLFAIDVNIHLLKYDSAHGTWPEPITKIDNEHFQVGEgptawKVE 80
Cdd:PRK07729 1 MKTKVAINGFGRIGRMVFR--KAIKESAFEIVAINASYPSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGK-----KIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 81 nMVGRIHPKDLKWGEKKVDVVLESTGVYKTKAQKGpdgkvtrdgydGHIAAGAKKVVLSVPAGDEiECTLVLGVNDEDVK 160
Cdd:PRK07729 74 -LLNNRDPKELPWTDLGIDIVIEATGKFNSKEKAI-----------LHVEAGAKKVILTAPGKNE-DVTIVVGVNEDQLD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 161 PTT-TMISNASCTTNCLAPITKIINSKWKIITGFMTTVHAYTNDQQVADLAHQDMRRARAAAQNIIPTSTGAAKALPIVV 239
Cdd:PRK07729 141 IEKhTIISNASCTTNCLAPVVKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHKDLRRARACGQSIIPTTTGAAKALAKVL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 240 HDLRPKsLDGISIRVPVITGSLVDTSFNVEGTPTRDEINAALKAATlEGPLKGILGYTEDAIVSSDIINCTLSSIVDSLE 319
Cdd:PRK07729 221 PHLNGK-LHGMALRVPTPNVSLVDLVVDVKRDVTVEEINEAFKTAA-NGALKGILEFSEEPLVSIDFNTNTHSAIIDGLS 298
|
330 340 350
....*....|....*....|....*....|....*...
gi 128168587 320 TKVIPNPDgksalVKVLSWYDNEAGYSARCADIFHRIG 357
Cdd:PRK07729 299 TMVMGDRK-----VKVLAWYDNEWGYSCRVVDLVTLVA 331
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
5-352 |
5.33e-99 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 296.07 E-value: 5.33e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 5 IAINGFGRIGRLVFRAVrkLYPTECQVVAIHDLfAIDVN--IHLLKYDSAHGTWPEPITkIDNEHFQVGEGPTAWKVENm 82
Cdd:NF033735 1 IGINGFGRIGRLALRAL--WGRPGLEIVHINDL-AGDAAtlAHLLEFDSVHGRWDAEVT-AEEDSIVIDGKRISFSSNK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 83 vgriHPKDLKWGEKkVDVVLESTGVYKTKAQKGPdgkvtrdgydgHIAAGAKKVVLSVPAGDEIECTLVLGVNDEDVKPT 162
Cdd:NF033735 76 ----DIEDTPWGDG-VDVVIECTGKFKTPEKLQP-----------YFDQGVKKVVVSAPVKEEGVLNIVYGVNDHLYDPA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 163 T-TMISNASCTTNCLAPITKIINSKWKIITGFMTTVHAYTNDQQVADLAHQDMRRARAAAQNIIPTSTGAAKALPIVVHD 241
Cdd:NF033735 140 RhRIVTAASCTTNCLAPVVKVIHEKIGIKHGSITTIHDITNTQTIVDAPHKDLRRARSCGMSLIPTTTGSATAITLIFPE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 242 LRPKsLDGISIRVPVITGSLVDTSFNVEGTPTRDEINAALKAATlEGPLKGILGYTEDAIVSSDIINCTLSSIVDSLETK 321
Cdd:NF033735 220 LKGK-LNGHAVRVPLLNASLTDCVFEVERPTTVEEVNALFKAAA-EGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTM 297
|
330 340 350
....*....|....*....|....*....|.
gi 128168587 322 VIpnpDGksALVKVLSWYDNEAGYSARCADI 352
Cdd:NF033735 298 VV---NG--TQVKIYAWYDNEWGYANRMVDL 323
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
171-342 |
4.69e-88 |
|
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: 262.39 E-value: 4.69e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 171 CTTNCLAPITKIINSKWKIITGFMTTVHAYTNDQQVADLAHQDMRRARAAAQNIIPTSTGAAKALPIVVHDLRPKsLDGI 250
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGK-LTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 251 SIRVPVITGSLVDTSFNVEGTPTRDEINAALKAATlEGPLKGILGYTEDAIVSSDIINCTLSSIVDSLETKVIpnpDGKs 330
Cdd:cd18126 80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAA-EGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVL---GGN- 154
|
170
....*....|..
gi 128168587 331 aLVKVLSWYDNE 342
Cdd:cd18126 155 -LVKVVAWYDNE 165
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
176-339 |
7.46e-63 |
|
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: 197.82 E-value: 7.46e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 176 LAPITKIINSKWKIITGFMTTVHAYTNDQQVADLAHQ-DMRRARAAAQNIIPTSTGAAKALPIVVHDLRPKsLDGISIRV 254
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHkDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGK-LDGMAVRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 255 PVITGSLVDTSFNVEGTPTRDEINAALKAATlEGPLKGILGYTEDAIVSSDIINCTLSSIVDSLETKVIPNPdgksaLVK 334
Cdd:pfam02800 80 PTPNVSVVDLVVELEKPVTVEEVNAALKEAA-EGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGN-----FVK 153
|
....*
gi 128168587 335 VLSWY 339
Cdd:pfam02800 154 VVAWY 158
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-171 |
3.78e-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: 156.94 E-value: 3.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 3 VRIAINGFGRIGRLVFRAVRKlyPTECQVVAIHDLFAIDVNIHLLKYDSAHGTWPEPITkIDNEHFQVGEgptawKVENM 82
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALE--RPDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVE-VEGDGLVVNG-----KAIKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 83 VGRIHPKDLKWGEKKVDVVLESTGVYKTKAQKGPdgkvtrdgydgHIAAGAKKVVLSVPAGDEIEcTLVLGVNDEDVKPT 162
Cdd:smart00846 73 FAERDPANLPWGELGVDIVVECTGGFTTREKASA-----------HLKAGAKKVIISAPSKDADP-TFVYGVNHDEYDGE 140
|
....*....
gi 128168587 163 TTMISNASC 171
Cdd:smart00846 141 DHIISNASC 149
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
1-352 |
8.36e-162 |
|
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: 456.01 E-value: 8.36e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 1 MVVRIAINGFGRIGRLVFRAVRKlYPTECQVVAIHDLFAIDVNIHLLKYDSAHGTWPEPITkIDNEHFQVGEGptawkve 80
Cdd:COG0057 1 MTIRVAINGFGRIGRLVLRALLE-RGPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVE-VEGDSLIVNGK------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 81 nmvgRIH------PKDLKWGEKKVDVVLESTGVYKT--KAQKgpdgkvtrdgydgHIAAGAKKVVLSVPAGDEIeCTLVL 152
Cdd:COG0057 72 ----KIKvlaerdPAELPWGELGVDVVIECTGKFTDreKASA-------------HLKAGAKKVLISAPAKGDD-PTIVY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 153 GVNDEDVKPTTTMISNASCTTNCLAPITKIINSKWKIITGFMTTVHAYTNDQQVADLAHQDMRRARAAAQNIIPTSTGAA 232
Cdd:COG0057 134 GVNHDDYDADHRIISNASCTTNCLAPVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 233 KALPIVVHDLRPKsLDGISIRVPVITGSLVDTSFNVEGTPTRDEINAALKAATlEGPLKGILGYTEDAIVSSDIINCTLS 312
Cdd:COG0057 214 KAVGLVLPELKGK-LDGMAVRVPTPNVSLVDLTVELEKETTVEEVNAALKEAA-EGPLKGILGYTEEPLVSSDFNGDPHS 291
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 128168587 313 SIVDSLETKVIpnpDGKsaLVKVLSWYDNEAGYSARCADI 352
Cdd:COG0057 292 SIFDALQTIVI---GGN--LVKVLAWYDNEWGYSNRMVDL 326
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
4-351 |
1.01e-147 |
|
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: 419.76 E-value: 1.01e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 4 RIAINGFGRIGRLVFRAVRKLYPTECQVVAIHDLFAIDVNIHLLKYDSAHGTWPEPITKIDNEHFQVGEGPTAWKVENmv 83
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKPGNDLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEVISVFSER-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 84 griHPKDLKWGEKKVDVVLESTGVYktkaqkgpdgkVTRDGYDGHIAAGAKKVVLSVPAGDEIeCTLVLGVNDEDVKPTT 163
Cdd:TIGR01534 79 ---DPSDLPWKALGVDIVIECTGKF-----------RDKEKLEKHLEAGAKKVLISAPSKGDV-KTIVYGVNHDEYDGEE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 164 TMISNASCTTNCLAPITKIINSKWKIITGFMTTVHAYTNDQQVADLAHQDMRRARAAAQNIIPTSTGAAKALPIVVHDLR 243
Cdd:TIGR01534 144 RIISNASCTTNCLAPLAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKDLRRARAAALNIIPTSTGAAKAIGKVLPELA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 244 PKsLDGISIRVPVITGSLVDTSFNVEGTPTRDEINAALKAATlEGPLKGILGYTEDAIVSSDIINCTLSSIVDSLETKVI 323
Cdd:TIGR01534 224 GK-LTGMAIRVPTPNVSLVDLVVNLEKDVTVEEVNAALKEAS-EGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVT 301
|
330 340
....*....|....*....|....*...
gi 128168587 324 PNPDGksaLVKVLSWYDNEAGYSARCAD 351
Cdd:TIGR01534 302 GLGDS---LVKVYAWYDNEWGYSNRLVD 326
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-357 |
7.11e-110 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 324.38 E-value: 7.11e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 1 MVVRIAINGFGRIGRLVFRavRKLYPTECQVVAIHDLFAIDVNIHLLKYDSAHGTWPEPITKIDNEHFQVGEgptawKVE 80
Cdd:PRK07729 1 MKTKVAINGFGRIGRMVFR--KAIKESAFEIVAINASYPSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGK-----KIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 81 nMVGRIHPKDLKWGEKKVDVVLESTGVYKTKAQKGpdgkvtrdgydGHIAAGAKKVVLSVPAGDEiECTLVLGVNDEDVK 160
Cdd:PRK07729 74 -LLNNRDPKELPWTDLGIDIVIEATGKFNSKEKAI-----------LHVEAGAKKVILTAPGKNE-DVTIVVGVNEDQLD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 161 PTT-TMISNASCTTNCLAPITKIINSKWKIITGFMTTVHAYTNDQQVADLAHQDMRRARAAAQNIIPTSTGAAKALPIVV 239
Cdd:PRK07729 141 IEKhTIISNASCTTNCLAPVVKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHKDLRRARACGQSIIPTTTGAAKALAKVL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 240 HDLRPKsLDGISIRVPVITGSLVDTSFNVEGTPTRDEINAALKAATlEGPLKGILGYTEDAIVSSDIINCTLSSIVDSLE 319
Cdd:PRK07729 221 PHLNGK-LHGMALRVPTPNVSLVDLVVDVKRDVTVEEINEAFKTAA-NGALKGILEFSEEPLVSIDFNTNTHSAIIDGLS 298
|
330 340 350
....*....|....*....|....*....|....*...
gi 128168587 320 TKVIPNPDgksalVKVLSWYDNEAGYSARCADIFHRIG 357
Cdd:PRK07729 299 TMVMGDRK-----VKVLAWYDNEWGYSCRVVDLVTLVA 331
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
5-352 |
5.33e-99 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 296.07 E-value: 5.33e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 5 IAINGFGRIGRLVFRAVrkLYPTECQVVAIHDLfAIDVN--IHLLKYDSAHGTWPEPITkIDNEHFQVGEGPTAWKVENm 82
Cdd:NF033735 1 IGINGFGRIGRLALRAL--WGRPGLEIVHINDL-AGDAAtlAHLLEFDSVHGRWDAEVT-AEEDSIVIDGKRISFSSNK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 83 vgriHPKDLKWGEKkVDVVLESTGVYKTKAQKGPdgkvtrdgydgHIAAGAKKVVLSVPAGDEIECTLVLGVNDEDVKPT 162
Cdd:NF033735 76 ----DIEDTPWGDG-VDVVIECTGKFKTPEKLQP-----------YFDQGVKKVVVSAPVKEEGVLNIVYGVNDHLYDPA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 163 T-TMISNASCTTNCLAPITKIINSKWKIITGFMTTVHAYTNDQQVADLAHQDMRRARAAAQNIIPTSTGAAKALPIVVHD 241
Cdd:NF033735 140 RhRIVTAASCTTNCLAPVVKVIHEKIGIKHGSITTIHDITNTQTIVDAPHKDLRRARSCGMSLIPTTTGSATAITLIFPE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 242 LRPKsLDGISIRVPVITGSLVDTSFNVEGTPTRDEINAALKAATlEGPLKGILGYTEDAIVSSDIINCTLSSIVDSLETK 321
Cdd:NF033735 220 LKGK-LNGHAVRVPLLNASLTDCVFEVERPTTVEEVNALFKAAA-EGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTM 297
|
330 340 350
....*....|....*....|....*....|.
gi 128168587 322 VIpnpDGksALVKVLSWYDNEAGYSARCADI 352
Cdd:NF033735 298 VV---NG--TQVKIYAWYDNEWGYANRMVDL 323
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
2-352 |
2.99e-96 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 289.50 E-value: 2.99e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 2 VVRIAINGFGRIGRLVFRAVRKLYPTECQVVAIHDLFAIDVNIHLLKYDSAHGTWPEPITKIDNEHFQVGegptawKVEN 81
Cdd:PRK07403 1 MIRVAINGFGRIGRNFLRCWLGRENSQLELVAINDTSDPRTNAHLLKYDSMLGKLNADISADENSITVNG------KTIK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 82 MVGRIHPKDLKWGEKKVDVVLESTGVYktkaqkgpdgkVTRDGYDGHIAAGAKKVVLSVPAGDEIECTLVLGVNDEDVKP 161
Cdd:PRK07403 75 CVSDRNPLNLPWKEWGIDLIIESTGVF-----------VTKEGASKHIQAGAKKVLITAPGKGEDIGTYVVGVNHHEYDH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 162 TT-TMISNASCTTNCLAPITKIINSKWKIITGFMTTVHAYTNDQQVADLAHQDMRRARAAAQNIIPTSTGAAKALPIVVH 240
Cdd:PRK07403 144 EDhNIISNASCTTNCLAPIAKVLHDNFGIIKGTMTTTHSYTGDQRILDASHRDLRRARAAAVNIVPTSTGAAKAVALVIP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 241 DLRPKsLDGISIRVPVITGSLVDTSFNVEGTPTRDEINAALKAATlEGPLKGILGYTEDAIVSSDIINCTLSSIVDSLET 320
Cdd:PRK07403 224 ELKGK-LNGIALRVPTPNVSVVDLVVQVEKRTITEQVNEVLKDAS-EGPLKGILEYSDLPLVSSDYRGTDASSIVDASLT 301
|
330 340 350
....*....|....*....|....*....|..
gi 128168587 321 KVIPNPdgksaLVKVLSWYDNEAGYSARCADI 352
Cdd:PRK07403 302 MVMGGD-----MVKVIAWYDNEWGYSQRVVDL 328
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
3-352 |
2.54e-92 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 281.43 E-value: 2.54e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 3 VRIAINGFGRIGRLVFRAVRKLYPTECQVVAIHDLFAIDVNIHLLKYDSAHGTWPEPITKIDNEHFQVgEGptawKVENM 82
Cdd:PLN03096 61 IKVAINGFGRIGRNFLRCWHGRKDSPLDVVAINDTGGVKQASHLLKYDSTLGTFDADVKPVGDDAISV-DG----KVIKV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 83 VGRIHPKDLKWGEKKVDVVLESTGVYktkaqkgpdgkVTRDGYDGHIAAGAKKVVLSVPAGDEIEcTLVLGVNDEDVKPT 162
Cdd:PLN03096 136 VSDRNPLNLPWGELGIDLVIEGTGVF-----------VDREGAGKHIQAGAKKVLITAPGKGDIP-TYVVGVNADDYKHS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 163 TTMISNASCTTNCLAPITKIINSKWKIITGFMTTVHAYTNDQQVADLAHQDMRRARAAAQNIIPTSTGAAKALPIVVHDL 242
Cdd:PLN03096 204 DPIISNASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVALVLPNL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 243 RPKsLDGISIRVPVITGSLVDTSFNVEGTPTRDEINAALKAATlEGPLKGILGYTEDAIVSSDIINCTLSSIVDSLETKV 322
Cdd:PLN03096 284 KGK-LNGIALRVPTPNVSVVDLVVQVEKKTFAEEVNAAFRDAA-EKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMV 361
|
330 340 350
....*....|....*....|....*....|
gi 128168587 323 IPNPdgksaLVKVLSWYDNEAGYSARCADI 352
Cdd:PLN03096 362 MGDD-----MVKVVAWYDNEWGYSQRVVDL 386
|
|
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
3-352 |
9.98e-91 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 278.28 E-value: 9.98e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 3 VRIAINGFGRIGRLVFRAVrkLYPTECQVVAIHDLFaIDVN--IHLLKYDSAHGTWPEPITKIDNEHFQVGEgptawKVE 80
Cdd:PLN02272 86 TKIGINGFGRIGRLVLRIA--TSRDDIEVVAVNDPF-IDAKymAYMFKYDSTHGNFKGTINVVDDSTLEING-----KQI 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 81 NMVGRIHPKDLKWGEKKVDVVLESTGVYktkaqkgpdgkVTRDGYDGHIAAGAKKVVLSVPAGDEIecTLVLGVNDEDVK 160
Cdd:PLN02272 158 KVTSKRDPAEIPWGDFGAEYVVESSGVF-----------TTVEKASAHLKGGAKKVVISAPSADAP--MFVVGVNEKTYK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 161 PTTTMISNASCTTNCLAPITKIINSKWKIITGFMTTVHAYTNDQQVAD-LAHQDMRRARAAAQNIIPTSTGAAKALPIVV 239
Cdd:PLN02272 225 PNMNIVSNASCTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQKTVDgPSMKDWRGGRGASQNIIPSSTGAAKAVGKVL 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 240 HDLRPKsLDGISIRVPVITGSLVDTSFNVEGTPTRDEINAALKAATlEGPLKGILGYTEDAIVSSDIINCTLSSIVDSLE 319
Cdd:PLN02272 305 PELNGK-LTGMAFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYAS-EGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKA 382
|
330 340 350
....*....|....*....|....*....|...
gi 128168587 320 TKVIpnpdgKSALVKVLSWYDNEAGYSARCADI 352
Cdd:PLN02272 383 GIGL-----SASFMKLVSWYDNEWGYSNRVLDL 410
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
3-351 |
1.67e-90 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 274.63 E-value: 1.67e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 3 VRIAINGFGRIGRLVFRAvrkLYPT----ECQVVAIHDLFAIDVNIHLLKYDSAHGTWPEPItKIDNEHFQVGEgptawk 78
Cdd:PRK13535 2 IRVAINGFGRIGRNVLRA---LYESgrraEITVVAINELADAEGMAHLLKYDTSHGRFAWDV-RQERDQLFVGD------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 79 veNMVGRIHPKD---LKWGEKKVDVVLESTGVYKTKAqkgpdgkvtrDGyDGHIAAGAKKVVLSVPAGDEIECTLVLGVN 155
Cdd:PRK13535 72 --DAIRLLHERDiasLPWRELGVDVVLDCTGVYGSRE----------DG-EAHIAAGAKKVLFSHPGSNDLDATVVYGVN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 156 DEDVKPTTTMISNASCTTNCLAPITKIINSKWKIITGFMTTVHAYTNDQQVADLAHQDMRRARAAAQNIIPTSTGAAKAL 235
Cdd:PRK13535 139 HDQLRAEHRIVSNASCTTNCIIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 236 PIVVHDLRPKsLDGISIRVPVITGSLVDTSFNVEGTPTRDEINAALKAATlEGPLKGILGYTEDAIVSSDIINCTLSSIV 315
Cdd:PRK13535 219 TRIFPQFNDR-FEAISVRVPTINVTAIDLSVTVKKPVKVNEVNQLLQKAA-QGAFHGIVDYTELPLVSIDFNHDPHSAIV 296
|
330 340 350
....*....|....*....|....*....|....*.
gi 128168587 316 DSLETKVipnPDGKsaLVKVLSWYDNEAGYSARCAD 351
Cdd:PRK13535 297 DGTQTRV---SGAH--LIKTLVWCDNEWGFANRMLD 327
|
|
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-356 |
6.03e-90 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 273.25 E-value: 6.03e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 1 MVVRIAINGFGRIGRLVFRAvrKLYPTECQVVAIHDLF-AIDVNIHLLKYDSAHGTWPEPITKIDnEHFQVGEgptawKV 79
Cdd:PTZ00023 1 MVVKLGINGFGRIGRLVFRA--ALEREDVEVVAINDPFmTLDYMCYLLKYDSVHGSLPAEVSVTD-GFLMIGS-----KK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 80 ENMVGRIHPKDLKWGEKKVDVVLESTGVYKTKAQKgpdgkvtrdgyDGHIAAGAKKVVLSVPAGDEIEcTLVLGVNDEDV 159
Cdd:PTZ00023 73 VHVFFEKDPAAIPWGKNGVDVVCESTGVFLTKEKA-----------QAHLKGGAKKVIMSAPPKDDTP-IYVMGVNHTQY 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 160 KPTTTMISNASCTTNCLAPITKIINSKWKIITGFMTTVHAYTNDQQVADLAH---QDMRRARAAAQNIIPTSTGAAKALP 236
Cdd:PTZ00023 141 DKSQRIVSNASCTTNCLAPLAKVVNDKFGIVEGLMTTVHASTANQLTVDGPSkggKDWRAGRCAGVNIIPASTGAAKAVG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 237 IVVHDLRPKsLDGISIRVPVITGSLVDTSFNVEGTPTRDEINAALKAATlEGPLKGILGYTEDAIVSSDIINCTLSSIVD 316
Cdd:PTZ00023 221 KVIPELNGK-LTGMAFRVPVPDVSVVDLTCKLAKPAKYEEIVAAVKKAA-EGPLKGILGYTDDEVVSSDFVHDKRSSIFD 298
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 128168587 317 sLETKVIPNpdgkSALVKVLSWYDNEAGYSARCADIFHRI 356
Cdd:PTZ00023 299 -VKAGIALN----DTFVKLVSWYDNEWGYSNRLLDLAHYI 333
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
171-342 |
4.69e-88 |
|
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: 262.39 E-value: 4.69e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 171 CTTNCLAPITKIINSKWKIITGFMTTVHAYTNDQQVADLAHQDMRRARAAAQNIIPTSTGAAKALPIVVHDLRPKsLDGI 250
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGK-LTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 251 SIRVPVITGSLVDTSFNVEGTPTRDEINAALKAATlEGPLKGILGYTEDAIVSSDIINCTLSSIVDSLETKVIpnpDGKs 330
Cdd:cd18126 80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAA-EGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVL---GGN- 154
|
170
....*....|..
gi 128168587 331 aLVKVLSWYDNE 342
Cdd:cd18126 155 -LVKVVAWYDNE 165
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
3-354 |
2.81e-86 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 267.54 E-value: 2.81e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 3 VRIAINGFGRIGRLVFRAVRKLYPTECQVVAIHDLFAIDVNIHLLKYDSAHGTWPEPITKIDNEHFQVGEGPTAwkvenM 82
Cdd:PLN02237 76 LKVAINGFGRIGRNFLRCWHGRKDSPLDVVVVNDSGGVKNASHLLKYDSMLGTFKADVKIVDDETISVDGKPIK-----V 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 83 VGRIHPKDLKWGEKKVDVVLESTGVYktkaQKGPdgkvtrdGYDGHIAAGAKKVVLSVPA-GDEIEcTLVLGVNDEDVKP 161
Cdd:PLN02237 151 VSNRDPLKLPWAELGIDIVIEGTGVF----VDGP-------GAGKHIQAGAKKVIITAPAkGADIP-TYVVGVNEDDYDH 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 162 TTT-MISNASCTTNCLAPITKIINSKWKIITGFMTTVHAYTNDQQVADLAHQDMRRARAAAQNIIPTSTGAAKALPIVVH 240
Cdd:PLN02237 219 EVAnIVSNASCTTNCLAPFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVSLVLP 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 241 DLRPKsLDGISIRVPVITGSLVDTSFNVEGTP-TRDEINAALKAATlEGPLKGILGYTEDAIVSSDIINCTLSSIVDSLE 319
Cdd:PLN02237 299 QLKGK-LNGIALRVPTPNVSVVDLVVNVEKKGiTAEDVNAAFRKAA-DGPLKGILAVCDVPLVSVDFRCSDVSSTIDASL 376
|
330 340 350
....*....|....*....|....*....|....*
gi 128168587 320 TKVIPNPdgksaLVKVLSWYDNEAGYSARCADIFH 354
Cdd:PLN02237 377 TMVMGDD-----MVKVVAWYDNEWGYSQRVVDLAH 406
|
|
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-359 |
1.34e-83 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 256.97 E-value: 1.34e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 1 MVVRIAINGFGRIGRLVFRAVRKlYPtECQVVAIHDLfAIDVNI--HLLKYDSAHGTWPEPITkIDNEHFQVGEGPTAWK 78
Cdd:PRK08955 1 MTIKVGINGFGRIGRLALRAAWD-WP-ELEFVQINDP-AGDAATlaHLLEFDSVHGRWHHEVT-AEGDAIVINGKRIRTT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 79 VENMVGrihpkDLKWGekKVDVVLESTGVYKTKAQkgpdgkvtrdgYDGHIAAGAKKVVLSVPAGDEIECTLVLGVNDED 158
Cdd:PRK08955 77 QNKAIA-----DTDWS--GCDVVIEASGVMKTKAL-----------LQAYLDQGVKRVVVTAPVKEEGVLNIVMGVNDHL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 159 VKPTTTMI-SNASCTTNCLAPITKIINSKWKIITGFMTTVHAYTNDQQVADLAHQDMRRARAAAQNIIPTSTGAAKALPI 237
Cdd:PRK08955 139 FDPAIHPIvTAASCTTNCLAPVVKVIHEKLGIKHGSMTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSATAITE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 238 VVHDLRPKsLDGISIRVPVITGSLVDTSFNVEGTPTRDEINAALKAATlEGPLKGILGYTEDAIVSSDIINCTLSSIVDS 317
Cdd:PRK08955 219 IFPELKGK-LNGHAVRVPLANASLTDCVFEVERDTTVEEVNALLKEAA-EGELKGILGYEERPLVSIDYKTDPRSSIVDA 296
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 128168587 318 LETKVIpnpdgKSALVKVLSWYDNEAGYSARCADIFHRIGTM 359
Cdd:PRK08955 297 LSTMVV-----NGTQVKLYAWYDNEWGYANRTAELARKVGLA 333
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
1-352 |
1.41e-83 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 258.06 E-value: 1.41e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 1 MVVRIAINGFGRIGRLVFRAV--RKLYPTECQVVAIHDLFA-IDVNIHLLKYDSAHGTWPEPITKIDNEhfqvgegPTAW 77
Cdd:PTZ00434 2 APIKVGINGFGRIGRMVFQAIcdQGLIGTEIDVVAVVDMSTnAEYFAYQMKYDTVHGRPKYTVETTKSS-------PSVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 78 KVENMVGRIH----------PKDLKWGEKKVDVVLESTGVYKTKAQKgpdgkvtrdgyDGHIAAGAKKVVLSVPAGDEIE 147
Cdd:PTZ00434 75 TDDVLVVNGHrikcvkaqrnPADLPWGKLGVDYVIESTGLFTDKLAA-----------EGHLKGGAKKVVISAPASGGAK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 148 cTLVLGVNDEDVKPTTT-MISNASCTTNCLAPITKIINSK-WKIITGFMTTVHAYTNDQQVAD-LAHQDMRRARAAAQNI 224
Cdd:PTZ00434 144 -TIVMGVNQHEYSPTEHhVVSNASCTTNCLAPIVHVLTKEgFGIETGLMTTIHSYTATQKTVDgVSVKDWRGGRAAAVNI 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 225 IPTSTGAAKALPIVVHDLRPKsLDGISIRVPVITGSLVDTSFNVEGTPTRDEINAALKAATlEGPLKGILGYTEDAIVSS 304
Cdd:PTZ00434 223 IPSTTGAAKAVGMVIPSTKGK-LTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRAS-QTYMKGILGFTDDELVSA 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 128168587 305 DIINCTLSSIVDSLETkVIPNPDGKSALVKVLSWYDNEAGYSARCADI 352
Cdd:PTZ00434 301 DFINDNRSSIYDSKAT-LQNNLPGERRFFKIVSWYDNEWGYSHRVVDL 347
|
|
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
3-352 |
1.64e-79 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 246.94 E-value: 1.64e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 3 VRIAINGFGRIGRLVFRAVrkLYPTECQVVAIHDLF-AIDVNIHLLKYDSAHGTWPEPITKIDNEH-FQVGEGPTAwkve 80
Cdd:PLN02358 6 IRIGINGFGRIGRLVARVV--LQRDDVELVAVNDPFiTTEYMTYMFKYDSVHGQWKHHELKVKDDKtLLFGEKPVT---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 81 nMVGRIHPKDLKWGEKKVDVVLESTGVYKTKaqkgpdgkvtrDGYDGHIAAGAKKVVLSVPAGDEIecTLVLGVNDEDVK 160
Cdd:PLN02358 80 -VFGIRNPEDIPWGEAGADFVVESTGVFTDK-----------DKAAAHLKGGAKKVVISAPSKDAP--MFVVGVNEHEYK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 161 PTTTMISNASCTTNCLAPITKIINSKWKIITGFMTTVHAYTNDQQVAD-LAHQDMRRARAAAQNIIPTSTGAAKALPIVV 239
Cdd:PLN02358 146 SDLDIVSNASCTTNCLAPLAKVINDRFGIVEGLMTTVHSITATQKTVDgPSMKDWRGGRAASFNIIPSSTGAAKAVGKVL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 240 HDLRPKsLDGISIRVPVITGSLVDTSFNVEGTPTRDEINAALKAATlEGPLKGILGYTEDAIVSSDIINCTLSSIVDSLE 319
Cdd:PLN02358 226 PSLNGK-LTGMSFRVPTVDVSVVDLTVRLEKAATYDEIKKAIKEES-EGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKA 303
|
330 340 350
....*....|....*....|....*....|...
gi 128168587 320 TKVIPNpdgksALVKVLSWYDNEAGYSARCADI 352
Cdd:PLN02358 304 GIALSD-----KFVKLVSWYDNEWGYSSRVVDL 331
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
1-356 |
1.04e-75 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 236.94 E-value: 1.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 1 MVVRIAINGFGRIGRLVFRAVRKlyPTECQVVAIHDLFAIDVNIHLLKYDSAHGTWpEPITKIDNEHFQVGEgptawKVE 80
Cdd:PRK15425 1 MTIKVGINGFGRIGRIVFRAAQK--RSDIEIVAINDLLDADYMAYMLKYDSTHGRF-DGTVEVKDGHLIVNG-----KKI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 81 NMVGRIHPKDLKWGEKKVDVVLESTGVYktkaqkgpdgkVTRDGYDGHIAAGAKKVVLSVPAGDEIEcTLVLGVNDEdVK 160
Cdd:PRK15425 73 RVTAERDPANLKWDEVGVDVVAEATGLF-----------LTDETARKHITAGAKKVVMTGPSKDNTP-MFVKGANFD-KY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 161 PTTTMISNASCTTNCLAPITKIINSKWKIITGFMTTVHAYTNDQQVAD-LAHQDMRRARAAAQNIIPTSTGAAKALPIVV 239
Cdd:PRK15425 140 AGQDIVSNASCTTNCLAPLAKVINDNFGIIEGLMTTVHATTATQKTVDgPSHKDWRGGRGASQNIIPSSTGAAKAVGKVL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 240 HDLRPKsLDGISIRVPVITGSLVDTSFNVEGTPTRDEINAALKAATlEGPLKGILGYTEDAIVSSDIINCTLSSIVDSlE 319
Cdd:PRK15425 220 PELNGK-LTGMAFRVPTPNVSVVDLTVRLEKAATYEQIKAAVKAAA-EGEMKGVLGYTEDDVVSTDFNGEVCTSVFDA-K 296
|
330 340 350
....*....|....*....|....*....|....*..
gi 128168587 320 TKVIPNPDgksaLVKVLSWYDNEAGYSARCADIFHRI 356
Cdd:PRK15425 297 AGIALNDN----FVKLVSWYDNETGYSNKVLDLIAHI 329
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
176-339 |
7.46e-63 |
|
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: 197.82 E-value: 7.46e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 176 LAPITKIINSKWKIITGFMTTVHAYTNDQQVADLAHQ-DMRRARAAAQNIIPTSTGAAKALPIVVHDLRPKsLDGISIRV 254
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHkDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGK-LDGMAVRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 255 PVITGSLVDTSFNVEGTPTRDEINAALKAATlEGPLKGILGYTEDAIVSSDIINCTLSSIVDSLETKVIPNPdgksaLVK 334
Cdd:pfam02800 80 PTPNVSVVDLVVELEKPVTVEEVNAALKEAA-EGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGN-----FVK 153
|
....*
gi 128168587 335 VLSWY 339
Cdd:pfam02800 154 VVAWY 158
|
|
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
9-346 |
5.39e-62 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 205.54 E-value: 5.39e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 9 GFGRIGRLVFR-----------------AVRKLYPTECQVVAihdlfaidvniHLLKYDSAHGTWPEPITkIDNEHfqvg 71
Cdd:PRK08289 134 GFGRIGRLLARlliektgggnglrlraiVVRKGSEGDLEKRA-----------SLLRRDSVHGPFNGTIT-VDEEN---- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 72 egPTAWKVENMVGRIH---PKDLKWGEKKVD--VVLESTGVYKTkaqkgpdgkvtRDGYDGHIAA-GAKKVVLSVPAGDE 145
Cdd:PRK08289 198 --NAIIANGNYIQVIYansPEEVDYTAYGINnaLVVDNTGKWRD-----------EEGLSQHLKSkGVAKVLLTAPGKGD 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 146 IEcTLVLGVNDEDVKPTTTMISNASCTTNCLAPITKIINSKWKIITGFMTTVHAYTNDQQVADLAHQDMRRARAAAQNII 225
Cdd:PRK08289 265 IK-NIVHGVNHSDITDEDKIVSAASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKGDRRGRSAPLNMV 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 226 PTSTGAAKALPIVVHDLRPKsLDGISIRVPVITGSLVDTSFNVEGTPTRDEINAALKAATLEGPLKGILGYTEDA-IVSS 304
Cdd:PRK08289 344 ITETGAAKAVAKALPELAGK-LTGNAIRVPTPNVSMAILNLNLEKETSREELNEYLRQMSLHSPLQNQIDYTDSTeVVSS 422
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 128168587 305 DIINCTLSSIVDSLETKVipnpDGKSALVKVlsWYDNEAGYS 346
Cdd:PRK08289 423 DFVGSRHAGVVDSQATIV----NGNRAVLYV--WYDNEFGYS 458
|
|
| GAPDH_I_N |
cd05214 |
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
3-170 |
8.99e-53 |
|
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: 171.81 E-value: 8.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 3 VRIAINGFGRIGRLVFRAVRKLypTECQVVAIHDLFAIDVNIHLLKYDSAHGTWPEPITkIDNEHFQVGEgptawkvenm 82
Cdd:cd05214 1 IKVGINGFGRIGRLVFRAALER--DDIEVVAINDLTDDETLAYLLKYDSVHGRFDGEVE-VDDDALIVNG---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 83 vGRIH------PKDLKWGEKKVDVVLESTGVYKtkaqkgpdgkvTRDGYDGHIAAGAKKVVLSVPAGDEIeCTLVLGVND 156
Cdd:cd05214 68 -KKIKvfaerdPAELPWGELGVDIVIESTGVFT-----------TKEKASAHLKAGAKKVIISAPAKDDD-PTIVMGVNH 134
|
170
....*....|....
gi 128168587 157 EDVKPTTTMISNAS 170
Cdd:cd05214 135 DKYDADDKIISNAS 148
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-171 |
3.78e-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: 156.94 E-value: 3.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 3 VRIAINGFGRIGRLVFRAVRKlyPTECQVVAIHDLFAIDVNIHLLKYDSAHGTWPEPITkIDNEHFQVGEgptawKVENM 82
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALE--RPDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVE-VEGDGLVVNG-----KAIKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 83 VGRIHPKDLKWGEKKVDVVLESTGVYKTKAQKGPdgkvtrdgydgHIAAGAKKVVLSVPAGDEIEcTLVLGVNDEDVKPT 162
Cdd:smart00846 73 FAERDPANLPWGELGVDIVVECTGGFTTREKASA-----------HLKAGAKKVIISAPSKDADP-TFVYGVNHDEYDGE 140
|
....*....
gi 128168587 163 TTMISNASC 171
Cdd:smart00846 141 DHIISNASC 149
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
171-342 |
9.67e-45 |
|
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: 151.41 E-value: 9.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 171 CTTNCLAPITKIINSKWKIITGFMTTVHAYTNDQQVADLAHQDMRRARAAAQNIIPTSTGAAKALPIVVHDLRPKsLDGI 250
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGR-FEAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 251 SIRVPVITGSLVDTSFNVEGTPTRDEINAALKAATlEGPLKGILGYTEDAIVSSDIINCTLSSIVDSLETKVipnpdGKS 330
Cdd:cd23937 80 AVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQAS-QGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRV-----SGK 153
|
170
....*....|..
gi 128168587 331 ALVKVLSWYDNE 342
Cdd:cd23937 154 RLVKLLVWCDNE 165
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
171-342 |
9.84e-43 |
|
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: 146.22 E-value: 9.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 171 CTTNCLAPITKIINSKWKIITGFMTTVHAYTNDQQVAD-LAHQDMRRARAAAQNIIPTSTGAAKALPIVVHDLRPKsLDG 249
Cdd:cd18123 1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDgPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGK-LTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 250 ISIRVPVITGSLVDTSFNVEGTPTRDEINAALKAATLEgplKGILGYTEDAIVSSDIINCTLSSIVDSLETKVipnpdGK 329
Cdd:cd18123 80 MAVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG---KGRLGYTEAEDVSSDFRGDIFESVFDAESIIA-----VN 151
|
170
....*....|...
gi 128168587 330 SALVKVLSWYDNE 342
Cdd:cd18123 152 DNEVKLMQWYDNE 164
|
|
| GAPDH_N_E4PDH |
cd17892 |
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
3-170 |
6.67e-41 |
|
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: 141.25 E-value: 6.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 3 VRIAINGFGRIGRLVFRAvrkLYPT----ECQVVAIHDLFAIDVNIHLLKYDSAHGTWPEPItKIDNEHFQVGegptawk 78
Cdd:cd17892 1 YRVAINGYGRIGRNVLRA---LYESgrraEFQVVAINELADAETIAHLTKYDTTHGRFPGEV-RVENDQLFVN------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 79 venmVGRIH------PKDLKWGEKKVDVVLESTGVYKTkaqkgpdgkvtRDGYDGHIAAGAKKVVLSVPAGDEIECTLVL 152
Cdd:cd17892 70 ----GDKIRvlhepdPENLPWRELGIDLVLECTGVFGS-----------REDAERHLAAGAKKVLFSHPASNDVDATIVY 134
|
170
....*....|....*...
gi 128168587 153 GVNDEDVKPTTTMISNAS 170
Cdd:cd17892 135 GINQDLLRAEHRIVSNAS 152
|
|
| Gp_dh_N |
pfam00044 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-111 |
3.31e-32 |
|
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: 116.43 E-value: 3.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 3 VRIAINGFGRIGRLVFRAVrkLYPTECQVVAIHDLFAIDVNIHLLKYDSAHGTWPEPITkIDNEHFQVGEGPTAWKVENm 82
Cdd:pfam00044 1 VKVGINGFGRIGRLVLRAA--LERPDIEVVAINDLTDPETLAYLLKYDSVHGRFPGEVE-AEEDGLVVNGKKIKVFAER- 76
|
90 100
....*....|....*....|....*....
gi 128168587 83 vgriHPKDLKWGEKKVDVVLESTGVYKTK 111
Cdd:pfam00044 77 ----DPAELPWGDLGVDVVIESTGVFTTK 101
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
171-342 |
4.17e-23 |
|
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: 94.12 E-value: 4.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 171 CTTNCLAPITKIINSKWKIITGFMTTVHAYTNDQQVADLAHqDMRRARAAAQNIIPTSTGAAKALPIVVHDL-RPKSLDG 249
Cdd:cd18122 1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPI-LKSEVRAIIPNIPKNETKHAPETGKVLGEIgKPIKVDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 250 ISIRVPVITGSLVDTSFNVEGTPTRDEINAALKAATlEGPLKGILGYTEDAIVSSDIINCTLSSIVDSL-ETKVIPNpdg 328
Cdd:cd18122 80 IAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAV-EEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQrEFAFDDN--- 155
|
170
....*....|....
gi 128168587 329 ksaLVKVLSWYDNE 342
Cdd:cd18122 156 ---KLKVFSAVDNE 166
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-348 |
3.48e-18 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 84.54 E-value: 3.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 1 MVVRIAINGFGRIGRLVFRAvrKLYPTECQVVAIHDL-FAIDVNIHLLKYDSAHGTWPEPITKIDNEHFqvgegptawkV 79
Cdd:PTZ00353 1 LPITVGINGFGPVGKAVLFA--SLTDPLVTVVAVNDAsVSIAYIAYVLEQESPLSAPDGASIRVVGEQI----------V 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 80 ENMVGRIH------PKDLKWGEKKVDVVLESTGVYKtkaqkgpdgkvTRDGYDGHIAAGAKKVVLSVPAGDeiECTLVLG 153
Cdd:PTZ00353 69 LNGTQKIRvsakhdLVEIAWRDYGVQYVVECTGLYS-----------TRSRCWGHVTGGAKGVFVAGQSAD--APTVMAG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 154 VNDEDVKPTTTMISNASCTTNCLAPITKIINSKWKIITGFMTTVHAYTNDQQVADLAH--QDMRRARAAAQNIIPTSTGA 231
Cdd:PTZ00353 136 SNDERLSASLPVCCAGAPIAVALAPVIRALHEVYGVEECSYTAIHGMQPQEPIAARSKnsQDWRQTRVAIDAIAPYRDNG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 232 AKALPIVVHDLRPKsLDGISIRVPVITGSLVDTSFNVEGTPTRDEINAALKAATlEGPLKGILGYTEDAIVSSDIINctl 311
Cdd:PTZ00353 216 AETVCKLLPHLVGR-ISGSAFQVPVKKGCAIDMLVRTKQPVSKEVVDSALAEAA-SDRLNGVLCISKRDMISVDCIP--- 290
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 128168587 312 ssivdslETKVIPNPDGKSALV-----KVLSWYDNEAGYSAR 348
Cdd:PTZ00353 291 -------NGKLCYDATSSSSSRegevhKMVLWFDVECYYAAR 325
|
|
| GAPDH-like_N |
cd05192 |
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ... |
3-175 |
2.19e-06 |
|
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: 45.81 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 3 VRIAINGFGRIGRLVFRAVRKlyPTECQVVAIHDLfaidvnihllkydsahgtwpepitkidnehfqvgegptawkvenm 82
Cdd:cd05192 1 IRVAINGFGRIGRIVFRAIAD--QDDLDVVAINDR--------------------------------------------- 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 128168587 83 vgrihpkdlkwgekkVDVVLESTGVYktkaqkgpdgkVTRDGYDGHIAAGAKKVVLSVPAGDEIEcTLVLGVNDEDVKPT 162
Cdd:cd05192 34 ---------------RDVVIECTGSF-----------TDDDNAEKHIKAGGKKAVITAPEKGDIP-TIVVVLNELAKSAG 86
|
170
....*....|...
gi 128168587 163 TTMISNASCTTNC 175
Cdd:cd05192 87 ATVVSNANETSYS 99
|
|
| |
