|
Name |
Accession |
Description |
Interval |
E-value |
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
1-333 |
0e+00 |
|
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]; Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 439827 [Multi-domain] Cd Length: 334 Bit Score: 610.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 1 MSIKVAINGFGRIGRLALRQI-EKAHGIEVVAVNDLTPAEMLLHLFKYDSTQGRFQGTAELKDDAIVVNGKEIKVFANPN 79
Cdd:COG0057 1 MTIRVAINGFGRIGRLVLRALlERGPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 80 PEELPWGELGVDVVLECTGFFTNKTKAEAHIRAGARKVVISAPGGNDVKTVVYGVNQDILDGSETVISAASCTTNCLAPM 159
Cdd:COG0057 81 PAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDDPTIVYGVNHDDYDADHRIISNASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 160 AAVLQKEFGVVEGLMTTIHAYTGDQNTLDAPHRkgDLRRARAAALNIVPNSTGAAKAIGLVIPELNGKLDGSAQRVPVAT 239
Cdd:COG0057 161 AKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHK--DLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 240 GSLTELVSVLERPVTKEEINAAMKAAASESY----GYNEDQIVSSDVVGIEYGSLFDATQTRVMtvgGKQLVKTVAWYDN 315
Cdd:COG0057 239 VSLVDLTVELEKETTVEEVNAALKEAAEGPLkgilGYTEEPLVSSDFNGDPHSSIFDALQTIVI---GGNLVKVLAWYDN 315
|
330
....*....|....*...
gi 488165058 316 EMSYTCQLVRTLEYFAGK 333
Cdd:COG0057 316 EWGYSNRMVDLAEYMAKL 333
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
4-325 |
0e+00 |
|
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: 507.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 4 KVAINGFGRIGRLALRQIEKAHG--IEVVAVNDLTPAEMLLHLFKYDSTQGRFQGTAELKDDAIVVNGKE-IKVFANPNP 80
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKPGndLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEvISVFSERDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 81 EELPWGELGVDVVLECTGFFTNKTKAEAHIRAGARKVVISAPGGNDVKTVVYGVNQDILDGSETVISAASCTTNCLAPMA 160
Cdd:TIGR01534 81 SDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDVKTIVYGVNHDEYDGEERIISNASCTTNCLAPLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 161 AVLQKEFGVVEGLMTTIHAYTGDQNTLDAPHRkgDLRRARAAALNIVPNSTGAAKAIGLVIPELNGKLDGSAQRVPVATG 240
Cdd:TIGR01534 161 KVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHK--DLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 241 SLTELVSVLERPVTKEEINAAMKAAA----SESYGYNEDQIVSSDVVGIEYGSLFDATQTRVMTVGGKQlVKTVAWYDNE 316
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKEASegelKGVLGYTEDELVSSDFIGSPYSSIVDATATKVTGLGDSL-VKVYAWYDNE 317
|
....*....
gi 488165058 317 MSYTCQLVR 325
Cdd:TIGR01534 318 WGYSNRLVD 326
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-334 |
9.66e-138 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 394.10 E-value: 9.66e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 1 MSIKVAINGFGRIGRLALRQIEKAHGIEVVAVNDLTPAEMLLHLFKYDSTQGRFQGTAELKDDAIVVNGKEIKVFANPNP 80
Cdd:PRK07729 1 MKTKVAINGFGRIGRMVFRKAIKESAFEIVAINASYPSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 81 EELPWGELGVDVVLECTGFFTNKTKAEAHIRAGARKVVISAPGGNDVKTVVYGVNQDILD-GSETVISAASCTTNCLAPM 159
Cdd:PRK07729 81 KELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVTIVVGVNEDQLDiEKHTIISNASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 160 AAVLQKEFGVVEGLMTTIHAYTGDQNTLDAPHRkgDLRRARAAALNIVPNSTGAAKAIGLVIPELNGKLDGSAQRVPVAT 239
Cdd:PRK07729 161 VKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHK--DLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 240 GSLTELVSVLERPVTKEEINAAMKAAASESY----GYNEDQIVSSDVVGIEYGSLFDATQTRVMtvGGKQlVKTVAWYDN 315
Cdd:PRK07729 239 VSLVDLVVDVKRDVTVEEINEAFKTAANGALkgilEFSEEPLVSIDFNTNTHSAIIDGLSTMVM--GDRK-VKVLAWYDN 315
|
330
....*....|....*....
gi 488165058 316 EMSYTCQLVRTLEYFAGKI 334
Cdd:PRK07729 316 EWGYSCRVVDLVTLVADEL 334
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
5-324 |
1.55e-118 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 344.61 E-value: 1.55e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 5 VAINGFGRIGRLALRQIEKAHGIEVVAVNDL-TPAEMLLHLFKYDSTQGRFQGTAELKDDAIVVNGKEIKVFANPNPEEL 83
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLaGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 84 PWGElGVDVVLECTGFFTNKTKAEAHIRAGARKVVISAP-GGNDVKTVVYGVNQDILDGSE-TVISAASCTTNCLAPMAA 161
Cdd:NF033735 81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvKEEGVLNIVYGVNDHLYDPARhRIVTAASCTTNCLAPVVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 162 VLQKEFGVVEGLMTTIHAYTGDQNTLDAPHRkgDLRRARAAALNIVPNSTGAAKAIGLVIPELNGKLDGSAQRVPVATGS 241
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAPHK--DLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNAS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 242 LTELVSVLERPVTKEEINAAMKAAAsESY-----GYNEDQIVSSDVVGIEYGSLFDATQTrvMTVGGKQlVKTVAWYDNE 316
Cdd:NF033735 238 LTDCVFEVERPTTVEEVNALFKAAA-EGPlkgilGYEERPLVSVDYVNDPRSSIIDALST--MVVNGTQ-VKIYAWYDNE 313
|
....*...
gi 488165058 317 MSYTCQLV 324
Cdd:NF033735 314 WGYANRMV 321
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
151-316 |
1.64e-103 |
|
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: 300.53 E-value: 1.64e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 151 CTTNCLAPMAAVLQKEFGVVEGLMTTIHAYTGDQNTLDAPHRkgDLRRARAAALNIVPNSTGAAKAIGLVIPELNGKLDG 230
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHK--DLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 231 SAQRVPVATGSLTELVSVLERPVTKEEINAAMKAAASESY----GYNEDQIVSSDVVGIEYGSLFDATQTRVMtvgGKQL 306
Cdd:cd18126 79 MAFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLkgilGYTEDPLVSSDFVGDPHSSIFDATATIVL---GGNL 155
|
170
....*....|
gi 488165058 307 VKTVAWYDNE 316
Cdd:cd18126 156 VKVVAWYDNE 165
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-151 |
4.09e-82 |
|
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: 245.54 E-value: 4.09e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 3 IKVAINGFGRIGRLALRQIEKAHGIEVVAVNDLTPAEMLLHLFKYDSTQGRFQGTAELKDDAIVVNGKEIKVFANPNPEE 82
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPAN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488165058 83 LPWGELGVDVVLECTGFFTNKTKAEAHIRAGARKVVISAPGGNDVKTVVYGVNQDILDGSETVISAASC 151
Cdd:smart00846 81 LPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDADPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
156-313 |
1.84e-75 |
|
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: 229.02 E-value: 1.84e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 156 LAPMAAVLQKEFGVVEGLMTTIHAYTGDQNTLDAPHRKgDLRRARAAALNIVPNSTGAAKAIGLVIPELNGKLDGSAQRV 235
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHK-DLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 236 PVATGSLTELVSVLERPVTKEEINAAMKAAASESY----GYNEDQIVSSDVVGIEYGSLFDATQTRVMtvgGKQLVKTVA 311
Cdd:pfam02800 80 PTPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALkgilSYTEDPLVSSDFIGDPHSSIFDAKETIVV---NGNFVKVVA 156
|
..
gi 488165058 312 WY 313
Cdd:pfam02800 157 WY 158
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
1-333 |
0e+00 |
|
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]; Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 439827 [Multi-domain] Cd Length: 334 Bit Score: 610.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 1 MSIKVAINGFGRIGRLALRQI-EKAHGIEVVAVNDLTPAEMLLHLFKYDSTQGRFQGTAELKDDAIVVNGKEIKVFANPN 79
Cdd:COG0057 1 MTIRVAINGFGRIGRLVLRALlERGPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 80 PEELPWGELGVDVVLECTGFFTNKTKAEAHIRAGARKVVISAPGGNDVKTVVYGVNQDILDGSETVISAASCTTNCLAPM 159
Cdd:COG0057 81 PAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDDPTIVYGVNHDDYDADHRIISNASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 160 AAVLQKEFGVVEGLMTTIHAYTGDQNTLDAPHRkgDLRRARAAALNIVPNSTGAAKAIGLVIPELNGKLDGSAQRVPVAT 239
Cdd:COG0057 161 AKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHK--DLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 240 GSLTELVSVLERPVTKEEINAAMKAAASESY----GYNEDQIVSSDVVGIEYGSLFDATQTRVMtvgGKQLVKTVAWYDN 315
Cdd:COG0057 239 VSLVDLTVELEKETTVEEVNAALKEAAEGPLkgilGYTEEPLVSSDFNGDPHSSIFDALQTIVI---GGNLVKVLAWYDN 315
|
330
....*....|....*...
gi 488165058 316 EMSYTCQLVRTLEYFAGK 333
Cdd:COG0057 316 EWGYSNRMVDLAEYMAKL 333
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
4-325 |
0e+00 |
|
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: 507.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 4 KVAINGFGRIGRLALRQIEKAHG--IEVVAVNDLTPAEMLLHLFKYDSTQGRFQGTAELKDDAIVVNGKE-IKVFANPNP 80
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKPGndLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEvISVFSERDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 81 EELPWGELGVDVVLECTGFFTNKTKAEAHIRAGARKVVISAPGGNDVKTVVYGVNQDILDGSETVISAASCTTNCLAPMA 160
Cdd:TIGR01534 81 SDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDVKTIVYGVNHDEYDGEERIISNASCTTNCLAPLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 161 AVLQKEFGVVEGLMTTIHAYTGDQNTLDAPHRkgDLRRARAAALNIVPNSTGAAKAIGLVIPELNGKLDGSAQRVPVATG 240
Cdd:TIGR01534 161 KVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHK--DLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 241 SLTELVSVLERPVTKEEINAAMKAAA----SESYGYNEDQIVSSDVVGIEYGSLFDATQTRVMTVGGKQlVKTVAWYDNE 316
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKEASegelKGVLGYTEDELVSSDFIGSPYSSIVDATATKVTGLGDSL-VKVYAWYDNE 317
|
....*....
gi 488165058 317 MSYTCQLVR 325
Cdd:TIGR01534 318 WGYSNRLVD 326
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-334 |
9.66e-138 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 394.10 E-value: 9.66e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 1 MSIKVAINGFGRIGRLALRQIEKAHGIEVVAVNDLTPAEMLLHLFKYDSTQGRFQGTAELKDDAIVVNGKEIKVFANPNP 80
Cdd:PRK07729 1 MKTKVAINGFGRIGRMVFRKAIKESAFEIVAINASYPSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 81 EELPWGELGVDVVLECTGFFTNKTKAEAHIRAGARKVVISAPGGNDVKTVVYGVNQDILD-GSETVISAASCTTNCLAPM 159
Cdd:PRK07729 81 KELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVTIVVGVNEDQLDiEKHTIISNASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 160 AAVLQKEFGVVEGLMTTIHAYTGDQNTLDAPHRkgDLRRARAAALNIVPNSTGAAKAIGLVIPELNGKLDGSAQRVPVAT 239
Cdd:PRK07729 161 VKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHK--DLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 240 GSLTELVSVLERPVTKEEINAAMKAAASESY----GYNEDQIVSSDVVGIEYGSLFDATQTRVMtvGGKQlVKTVAWYDN 315
Cdd:PRK07729 239 VSLVDLVVDVKRDVTVEEINEAFKTAANGALkgilEFSEEPLVSIDFNTNTHSAIIDGLSTMVM--GDRK-VKVLAWYDN 315
|
330
....*....|....*....
gi 488165058 316 EMSYTCQLVRTLEYFAGKI 334
Cdd:PRK07729 316 EWGYSCRVVDLVTLVADEL 334
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
5-324 |
1.55e-118 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 344.61 E-value: 1.55e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 5 VAINGFGRIGRLALRQIEKAHGIEVVAVNDL-TPAEMLLHLFKYDSTQGRFQGTAELKDDAIVVNGKEIKVFANPNPEEL 83
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLaGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 84 PWGElGVDVVLECTGFFTNKTKAEAHIRAGARKVVISAP-GGNDVKTVVYGVNQDILDGSE-TVISAASCTTNCLAPMAA 161
Cdd:NF033735 81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvKEEGVLNIVYGVNDHLYDPARhRIVTAASCTTNCLAPVVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 162 VLQKEFGVVEGLMTTIHAYTGDQNTLDAPHRkgDLRRARAAALNIVPNSTGAAKAIGLVIPELNGKLDGSAQRVPVATGS 241
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAPHK--DLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNAS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 242 LTELVSVLERPVTKEEINAAMKAAAsESY-----GYNEDQIVSSDVVGIEYGSLFDATQTrvMTVGGKQlVKTVAWYDNE 316
Cdd:NF033735 238 LTDCVFEVERPTTVEEVNALFKAAA-EGPlkgilGYEERPLVSVDYVNDPRSSIIDALST--MVVNGTQ-VKIYAWYDNE 313
|
....*...
gi 488165058 317 MSYTCQLV 324
Cdd:NF033735 314 WGYANRMV 321
|
|
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
3-332 |
2.92e-117 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 344.92 E-value: 2.92e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 3 IKVAINGFGRIGRLALRQIEKAHGIEVVAVND-LTPAEMLLHLFKYDSTQGRFQGTAELKDDAIV-VNGKEIKVFANPNP 80
Cdd:PLN02272 86 TKIGINGFGRIGRLVLRIATSRDDIEVVAVNDpFIDAKYMAYMFKYDSTHGNFKGTINVVDDSTLeINGKQIKVTSKRDP 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 81 EELPWGELGVDVVLECTGFFTNKTKAEAHIRAGARKVVISAPGGnDVKTVVYGVNQDILDGSETVISAASCTTNCLAPMA 160
Cdd:PLN02272 166 AEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSA-DAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 161 AVLQKEFGVVEGLMTTIHAYTGDQNTLDAPHRKgDLRRARAAALNIVPNSTGAAKAIGLVIPELNGKLDGSAQRVPVATG 240
Cdd:PLN02272 245 KVVHEEFGILEGLMTTVHATTATQKTVDGPSMK-DWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNV 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 241 SLTELVSVLERPVTKEEINAAMKaAASES-----YGYNEDQIVSSDVVGIEYGSLFDATQTRVMTvggKQLVKTVAWYDN 315
Cdd:PLN02272 324 SVVDLTCRLEKSASYEDVKAAIK-YASEGplkgiLGYTDEDVVSNDFVGDSRSSIFDAKAGIGLS---ASFMKLVSWYDN 399
|
330
....*....|....*..
gi 488165058 316 EMSYTCQLVRTLEYFAG 332
Cdd:PLN02272 400 EWGYSNRVLDLIEHMAL 416
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
3-333 |
4.63e-116 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 339.19 E-value: 4.63e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 3 IKVAINGFGRIGRLALRQI--EKAHGIEVVAVNDLTPAEMLLHLFKYDSTQGRFQGTAELKDDAIVVNGKEIKVFANPNP 80
Cdd:PRK07403 2 IRVAINGFGRIGRNFLRCWlgRENSQLELVAINDTSDPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDRNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 81 EELPWGELGVDVVLECTGFFTNKTKAEAHIRAGARKVVISAPG-GNDVKTVVYGVNQDILDGSE-TVISAASCTTNCLAP 158
Cdd:PRK07403 82 LNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPGkGEDIGTYVVGVNHHEYDHEDhNIISNASCTTNCLAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 159 MAAVLQKEFGVVEGLMTTIHAYTGDQNTLDAPHRkgDLRRARAAALNIVPNSTGAAKAIGLVIPELNGKLDGSAQRVPVA 238
Cdd:PRK07403 162 IAKVLHDNFGIIKGTMTTTHSYTGDQRILDASHR--DLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 239 TGSLTELVSVLERPVTKEEINAAMKAAASESY----GYNEDQIVSSDVVGIEYGSLFDATQTRVMtvgGKQLVKTVAWYD 314
Cdd:PRK07403 240 NVSVVDLVVQVEKRTITEQVNEVLKDASEGPLkgilEYSDLPLVSSDYRGTDASSIVDASLTMVM---GGDMVKVIAWYD 316
|
330
....*....|....*....
gi 488165058 315 NEMSYTCQLVRTLEYFAGK 333
Cdd:PRK07403 317 NEWGYSQRVVDLAELVARK 335
|
|
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-324 |
6.70e-110 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 323.33 E-value: 6.70e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 1 MSIKVAINGFGRIGRLALRQIEKAHGIEVVAVND-LTPAEMLLHLFKYDSTQGRFQGTAELKDDAIVVNGKEIKVFANPN 79
Cdd:PTZ00023 1 MVVKLGINGFGRIGRLVFRAALEREDVEVVAINDpFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 80 PEELPWGELGVDVVLECTGFFTNKTKAEAHIRAGARKVVISAPGGNDVKTVVYGVNQDILDGSETVISAASCTTNCLAPM 159
Cdd:PTZ00023 81 PAAIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKDDTPIYVMGVNHTQYDKSQRIVSNASCTTNCLAPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 160 AAVLQKEFGVVEGLMTTIHAYTGDQNTLDAPHRKG-DLRRARAAALNIVPNSTGAAKAIGLVIPELNGKLDGSAQRVPVA 238
Cdd:PTZ00023 161 AKVVNDKFGIVEGLMTTVHASTANQLTVDGPSKGGkDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 239 TGSLTELVSVLERPVTKEEINAAMKAAASESY----GYNEDQIVSSDVVGIEYGSLFDATQTRVMTvggKQLVKTVAWYD 314
Cdd:PTZ00023 241 DVSVVDLTCKLAKPAKYEEIVAAVKKAAEGPLkgilGYTDDEVVSSDFVHDKRSSIFDVKAGIALN---DTFVKLVSWYD 317
|
330
....*....|
gi 488165058 315 NEMSYTCQLV 324
Cdd:PTZ00023 318 NEWGYSNRLL 327
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
3-333 |
4.30e-109 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 323.42 E-value: 4.30e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 3 IKVAINGFGRIGRLALR--QIEKAHGIEVVAVNDLTPAEMLLHLFKYDSTQGRFQGTAELKDD-AIVVNGKEIKVFANPN 79
Cdd:PLN03096 61 IKVAINGFGRIGRNFLRcwHGRKDSPLDVVAINDTGGVKQASHLLKYDSTLGTFDADVKPVGDdAISVDGKVIKVVSDRN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 80 PEELPWGELGVDVVLECTGFFTNKTKAEAHIRAGARKVVISAPGGNDVKTVVYGVNQDILDGSETVISAASCTTNCLAPM 159
Cdd:PLN03096 141 PLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKGDIPTYVVGVNADDYKHSDPIISNASCTTNCLAPF 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 160 AAVLQKEFGVVEGLMTTIHAYTGDQNTLDAPHRkgDLRRARAAALNIVPNSTGAAKAIGLVIPELNGKLDGSAQRVPVAT 239
Cdd:PLN03096 221 VKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHR--DLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPN 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 240 GSLTELVSVLERPVTKEEINAAMK-AAASESYG---YNEDQIVSSDVVGIEYGSLFDATQTRVMtvgGKQLVKTVAWYDN 315
Cdd:PLN03096 299 VSVVDLVVQVEKKTFAEEVNAAFRdAAEKELKGilaVCDEPLVSVDFRCSDVSSTIDSSLTMVM---GDDMVKVVAWYDN 375
|
330
....*....|....*...
gi 488165058 316 EMSYTCQLVRTLEYFAGK 333
Cdd:PLN03096 376 EWGYSQRVVDLADIVANK 393
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
1-333 |
1.35e-106 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 315.84 E-value: 1.35e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 1 MSIKVAINGFGRIGRLALRQIEK----AHGIEVVAVNDL-TPAEMLLHLFKYDSTQGRFQGTAEL--------KDDAIVV 67
Cdd:PTZ00434 2 APIKVGINGFGRIGRMVFQAICDqgliGTEIDVVAVVDMsTNAEYFAYQMKYDTVHGRPKYTVETtksspsvkTDDVLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 68 NGKEIK-VFANPNPEELPWGELGVDVVLECTGFFTNKTKAEAHIRAGARKVVISAPGGNDVKTVVYGVNQDILDGSE-TV 145
Cdd:PTZ00434 82 NGHRIKcVKAQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPASGGAKTIVMGVNQHEYSPTEhHV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 146 ISAASCTTNCLAPMAAVLQKE-FGVVEGLMTTIHAYTGDQNTLDAPHRKgDLRRARAAALNIVPNSTGAAKAIGLVIPEL 224
Cdd:PTZ00434 162 VSNASCTTNCLAPIVHVLTKEgFGIETGLMTTIHSYTATQKTVDGVSVK-DWRGGRAAAVNIIPSTTGAAKAVGMVIPST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 225 NGKLDGSAQRVPVATGSLTELVSVLERPVTKEEINAAMKaAASESY-----GYNEDQIVSSDVVGIEYGSLFDATQTRVM 299
Cdd:PTZ00434 241 KGKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIK-RASQTYmkgilGFTDDELVSADFINDNRSSIYDSKATLQN 319
|
330 340 350
....*....|....*....|....*....|....*
gi 488165058 300 TV-GGKQLVKTVAWYDNEMSYTCQLVRTLEYFAGK 333
Cdd:PTZ00434 320 NLpGERRFFKIVSWYDNEWGYSHRVVDLVRYMAAK 354
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
3-316 |
8.49e-106 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 312.76 E-value: 8.49e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 3 IKVAINGFGRIGRLALRQI---EKAHGIEVVAVNDLTPAEMLLHLFKYDSTQGRFQGTAELKDDAIVVNGKEIKVFANPN 79
Cdd:PRK13535 2 IRVAINGFGRIGRNVLRALyesGRRAEITVVAINELADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 80 PEELPWGELGVDVVLECTGFFTNKTKAEAHIRAGARKVVISAPGGNDV-KTVVYGVNQDILDGSETVISAASCTTNCLAP 158
Cdd:PRK13535 82 IASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSNDLdATVVYGVNHDQLRAEHRIVSNASCTTNCIIP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 159 MAAVLQKEFGVVEGLMTTIHAYTGDQNTLDAPHRkgDLRRARAAALNIVPNSTGAAKAIGLVIPELNGKLDGSAQRVPVA 238
Cdd:PRK13535 162 VIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHP--DLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPTI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 239 TGSLTELVSVLERPVTKEEINAAMKAAASESY----GYNEDQIVSSDVVGIEYGSLFDATQTRvmtVGGKQLVKTVAWYD 314
Cdd:PRK13535 240 NVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFhgivDYTELPLVSIDFNHDPHSAIVDGTQTR---VSGAHLIKTLVWCD 316
|
..
gi 488165058 315 NE 316
Cdd:PRK13535 317 NE 318
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
151-316 |
1.64e-103 |
|
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: 300.53 E-value: 1.64e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 151 CTTNCLAPMAAVLQKEFGVVEGLMTTIHAYTGDQNTLDAPHRkgDLRRARAAALNIVPNSTGAAKAIGLVIPELNGKLDG 230
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHK--DLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 231 SAQRVPVATGSLTELVSVLERPVTKEEINAAMKAAASESY----GYNEDQIVSSDVVGIEYGSLFDATQTRVMtvgGKQL 306
Cdd:cd18126 79 MAFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLkgilGYTEDPLVSSDFVGDPHSSIFDATATIVL---GGNL 155
|
170
....*....|
gi 488165058 307 VKTVAWYDNE 316
Cdd:cd18126 156 VKVVAWYDNE 165
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
3-324 |
1.93e-103 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 310.68 E-value: 1.93e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 3 IKVAINGFGRIGRLALR--QIEKAHGIEVVAVNDLTPAEMLLHLFKYDSTQGRFQGTAELKDDA-IVVNGKEIKVFANPN 79
Cdd:PLN02237 76 LKVAINGFGRIGRNFLRcwHGRKDSPLDVVVVNDSGGVKNASHLLKYDSMLGTFKADVKIVDDEtISVDGKPIKVVSNRD 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 80 PEELPWGELGVDVVLECTGFFTNKTKAEAHIRAGARKVVISAPG-GNDVKTVVYGVNQDILDGSET-VISAASCTTNCLA 157
Cdd:PLN02237 156 PLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAkGADIPTYVVGVNEDDYDHEVAnIVSNASCTTNCLA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 158 PMAAVLQKEFGVVEGLMTTIHAYTGDQNTLDAPHRkgDLRRARAAALNIVPNSTGAAKAIGLVIPELNGKLDGSAQRVPV 237
Cdd:PLN02237 236 PFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDASHR--DLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPT 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 238 ATGSLTELV-SVLERPVTKEEINAAMKAAASESY----GYNEDQIVSSDVVGIEYGSLFDATQTRVMtvgGKQLVKTVAW 312
Cdd:PLN02237 314 PNVSVVDLVvNVEKKGITAEDVNAAFRKAADGPLkgilAVCDVPLVSVDFRCSDVSSTIDASLTMVM---GDDMVKVVAW 390
|
330
....*....|..
gi 488165058 313 YDNEMSYTCQLV 324
Cdd:PLN02237 391 YDNEWGYSQRVV 402
|
|
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-326 |
1.16e-102 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 304.73 E-value: 1.16e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 1 MSIKVAINGFGRIGRLALRQIEKAHGIEVVAVNDLT-PAEMLLHLFKYDSTQGRFQGTAELKDDAIVVNGKEIKVFANPN 79
Cdd:PRK08955 1 MTIKVGINGFGRIGRLALRAAWDWPELEFVQINDPAgDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 80 PEELPWGelGVDVVLECTGFFTNKTKAEAHIRAGARKVVISAPGGND-VKTVVYGVNQDILDGSE-TVISAASCTTNCLA 157
Cdd:PRK08955 81 IADTDWS--GCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEgVLNIVMGVNDHLFDPAIhPIVTAASCTTNCLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 158 PMAAVLQKEFGVVEGLMTTIHAYTGDQNTLDAPHRkgDLRRARAAALNIVPNSTGAAKAIGLVIPELNGKLDGSAQRVPV 237
Cdd:PRK08955 159 PVVKVIHEKLGIKHGSMTTIHDLTNTQTILDAPHK--DLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 238 ATGSLTELVSVLERPVTKEEINAAMKAAASES----YGYNEDQIVSSDVVGIEYGSLFDATQTrvMTVGGKQlVKTVAWY 313
Cdd:PRK08955 237 ANASLTDCVFEVERDTTVEEVNALLKEAAEGElkgiLGYEERPLVSIDYKTDPRSSIVDALST--MVVNGTQ-VKLYAWY 313
|
330
....*....|....*.
gi 488165058 314 DNEMSY---TCQLVRT 326
Cdd:PRK08955 314 DNEWGYanrTAELARK 329
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
1-331 |
1.17e-100 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 299.73 E-value: 1.17e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 1 MSIKVAINGFGRIGRLALRQIEKAHGIEVVAVNDLTPAEMLLHLFKYDSTQGRFQGTAELKDDAIVVNGKEIKVFANPNP 80
Cdd:PRK15425 1 MTIKVGINGFGRIGRIVFRAAQKRSDIEIVAINDLLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 81 EELPWGELGVDVVLECTGFFTNKTKAEAHIRAGARKVVISAPGGNDVKTVVYGVNQDILDGSEtVISAASCTTNCLAPMA 160
Cdd:PRK15425 81 ANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDNTPMFVKGANFDKYAGQD-IVSNASCTTNCLAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 161 AVLQKEFGVVEGLMTTIHAYTGDQNTLDAPHRKgDLRRARAAALNIVPNSTGAAKAIGLVIPELNGKLDGSAQRVPVATG 240
Cdd:PRK15425 160 KVINDNFGIIEGLMTTVHATTATQKTVDGPSHK-DWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 241 SLTELVSVLERPVTKEEINAAMKAAASESY----GYNEDQIVSSDVVGIEYGSLFDATQTRVMTvggKQLVKTVAWYDNE 316
Cdd:PRK15425 239 SVVDLTVRLEKAATYEQIKAAVKAAAEGEMkgvlGYTEDDVVSTDFNGEVCTSVFDAKAGIALN---DNFVKLVSWYDNE 315
|
330
....*....|....*
gi 488165058 317 MSYTCQLVRTLEYFA 331
Cdd:PRK15425 316 TGYSNKVLDLIAHIS 330
|
|
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
3-324 |
7.60e-92 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 277.37 E-value: 7.60e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 3 IKVAINGFGRIGRLALRQIEKAHGIEVVAVND-LTPAEMLLHLFKYDSTQGRFQ-GTAELKDDAIVVNG-KEIKVFANPN 79
Cdd:PLN02358 6 IRIGINGFGRIGRLVARVVLQRDDVELVAVNDpFITTEYMTYMFKYDSVHGQWKhHELKVKDDKTLLFGeKPVTVFGIRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 80 PEELPWGELGVDVVLECTGFFTNKTKAEAHIRAGARKVVISAPGgNDVKTVVYGVNQDILDGSETVISAASCTTNCLAPM 159
Cdd:PLN02358 86 PEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPS-KDAPMFVVGVNEHEYKSDLDIVSNASCTTNCLAPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 160 AAVLQKEFGVVEGLMTTIHAYTGDQNTLDAPHRKgDLRRARAAALNIVPNSTGAAKAIGLVIPELNGKLDGSAQRVPVAT 239
Cdd:PLN02358 165 AKVINDRFGIVEGLMTTVHSITATQKTVDGPSMK-DWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 240 GSLTELVSVLERPVTKEEINAAMKAAASES----YGYNEDQIVSSDVVGIEYGSLFDATQTRVMTvggKQLVKTVAWYDN 315
Cdd:PLN02358 244 VSVVDLTVRLEKAATYDEIKKAIKEESEGKlkgiLGYTEDDVVSTDFVGDNRSSIFDAKAGIALS---DKFVKLVSWYDN 320
|
....*....
gi 488165058 316 EMSYTCQLV 324
Cdd:PLN02358 321 EWGYSSRVV 329
|
|
| GAPDH_I_N |
cd05214 |
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
3-150 |
5.95e-89 |
|
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: 263.48 E-value: 5.95e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 3 IKVAINGFGRIGRLALRQIEKAHGIEVVAVNDLTPAEMLLHLFKYDSTQGRFQGTAELKDDAIVVNGKEIKVFANPNPEE 82
Cdd:cd05214 1 IKVGINGFGRIGRLVFRAALERDDIEVVAINDLTDDETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488165058 83 LPWGELGVDVVLECTGFFTNKTKAEAHIRAGARKVVISAPGGNDVKTVVYGVNQDILDGSETVISAAS 150
Cdd:cd05214 81 LPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDDDPTIVMGVNHDKYDADDKIISNAS 148
|
|
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
5-332 |
6.71e-88 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 271.80 E-value: 6.71e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 5 VAINGFGRIGRLALRQ-IEKAHGIE-------VV---AVNDLTPAEMLLhlfKYDSTQGRFQGTAELKDD--AIVVNGKE 71
Cdd:PRK08289 130 VVLYGFGRIGRLLARLlIEKTGGGNglrlraiVVrkgSEGDLEKRASLL---RRDSVHGPFNGTITVDEEnnAIIANGNY 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 72 IKVFANPNPEELPWGELGVD--VVLECTGFFTNKTKAEAHIRA-GARKVVISAPGGNDVKTVVYGVNQDILDGSETVISA 148
Cdd:PRK08289 207 IQVIYANSPEEVDYTAYGINnaLVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGKGDIKNIVHGVNHSDITDEDKIVSA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 149 ASCTTNCLAPMAAVLQKEFGVVEGLMTTIHAYTGDQNTLDAPHrKGDlRRARAAALNIVPNSTGAAKAIGLVIPELNGKL 228
Cdd:PRK08289 287 ASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYH-KGD-RRGRSAPLNMVITETGAAKAVAKALPELAGKL 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 229 DGSAQRVPVATGSLTELVSVLERPVTKEEINAAMKAAASESY-----GY-NEDQIVSSDVVGIEYGSLFDATQTrvmTVG 302
Cdd:PRK08289 365 TGNAIRVPTPNVSMAILNLNLEKETSREELNEYLRQMSLHSPlqnqiDYtDSTEVVSSDFVGSRHAGVVDSQAT---IVN 441
|
330 340 350
....*....|....*....|....*....|
gi 488165058 303 GKQLVKTVaWYDNEMSYTCQLVRTLEYFAG 332
Cdd:PRK08289 442 GNRAVLYV-WYDNEFGYSCQVVRVMEQMAG 470
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-151 |
4.09e-82 |
|
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: 245.54 E-value: 4.09e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 3 IKVAINGFGRIGRLALRQIEKAHGIEVVAVNDLTPAEMLLHLFKYDSTQGRFQGTAELKDDAIVVNGKEIKVFANPNPEE 82
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPAN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488165058 83 LPWGELGVDVVLECTGFFTNKTKAEAHIRAGARKVVISAPGGNDVKTVVYGVNQDILDGSETVISAASC 151
Cdd:smart00846 81 LPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDADPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
156-313 |
1.84e-75 |
|
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: 229.02 E-value: 1.84e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 156 LAPMAAVLQKEFGVVEGLMTTIHAYTGDQNTLDAPHRKgDLRRARAAALNIVPNSTGAAKAIGLVIPELNGKLDGSAQRV 235
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHK-DLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 236 PVATGSLTELVSVLERPVTKEEINAAMKAAASESY----GYNEDQIVSSDVVGIEYGSLFDATQTRVMtvgGKQLVKTVA 311
Cdd:pfam02800 80 PTPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALkgilSYTEDPLVSSDFIGDPHSSIFDAKETIVV---NGNFVKVVA 156
|
..
gi 488165058 312 WY 313
Cdd:pfam02800 157 WY 158
|
|
| GAPDH_N_E4PDH |
cd17892 |
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
3-150 |
4.38e-65 |
|
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: 202.88 E-value: 4.38e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 3 IKVAINGFGRIGRLALRQI---EKAHGIEVVAVNDLTPAEMLLHLFKYDSTQGRFQGTAELKDDAIVVNGKEIKVFANPN 79
Cdd:cd17892 1 YRVAINGYGRIGRNVLRALyesGRRAEFQVVAINELADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488165058 80 PEELPWGELGVDVVLECTGFFTNKTKAEAHIRAGARKVVISAPGGNDVK-TVVYGVNQDILDGSETVISAAS 150
Cdd:cd17892 81 PENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASNDVDaTIVYGINQDLLRAEHRIVSNAS 152
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
151-316 |
4.02e-59 |
|
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: 187.44 E-value: 4.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 151 CTTNCLAPMAAVLQKEFGVVEGLMTTIHAYTGDQNTLDAPHRKgDLRRARAAALNIVPNSTGAAKAIGLVIPELNGKLDG 230
Cdd:cd18123 1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGK-DWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 231 SAQRVPVATGSLTELVSVLERPVTKEEINAAMKAAAS--ESYGYNEDQIVSSDVVGIEYGSLFDATQTrvmTVGGKQLVK 308
Cdd:cd18123 80 MAVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEgkGRLGYTEAEDVSSDFRGDIFESVFDAESI---IAVNDNEVK 156
|
....*...
gi 488165058 309 TVAWYDNE 316
Cdd:cd18123 157 LMQWYDNE 164
|
|
| Gp_dh_N |
pfam00044 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-103 |
2.16e-55 |
|
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: 175.75 E-value: 2.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 3 IKVAINGFGRIGRLALRQIEKAHGIEVVAVNDLTPAEMLLHLFKYDSTQGRFQGTAELKDDAIVVNGKEIKVFANPNPEE 82
Cdd:pfam00044 1 VKVGINGFGRIGRLVLRAALERPDIEVVAINDLTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAE 80
|
90 100
....*....|....*....|.
gi 488165058 83 LPWGELGVDVVLECTGFFTNK 103
Cdd:pfam00044 81 LPWGDLGVDVVIESTGVFTTK 101
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-324 |
9.65e-44 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 153.49 E-value: 9.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 1 MSIKVAINGFGRIGRLALRQIEKAHGIEVVAVNDLT-PAEMLLHLFKYDSTQGRFQGTA-ELKDDAIVVNGKE-IKVFAN 77
Cdd:PTZ00353 1 LPITVGINGFGPVGKAVLFASLTDPLVTVVAVNDASvSIAYIAYVLEQESPLSAPDGASiRVVGEQIVLNGTQkIRVSAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 78 PNPEELPWGELGVDVVLECTGFFTNKTKAEAHIRAGARKVVISAPGGnDVKTVVYGVNQDILDGSETVISAASCTTNCLA 157
Cdd:PTZ00353 81 HDLVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSA-DAPTVMAGSNDERLSASLPVCCAGAPIAVALA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 158 PMAAVLQKEFGVVEGLMTTIHAYTGDQNTLDAPHRKGDLRRARAAALNIVPNSTGAAKAIGLVIPELNGKLDGSAQRVPV 237
Cdd:PTZ00353 160 PVIRALHEVYGVEECSYTAIHGMQPQEPIAARSKNSQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 238 ATGSLTELVSVLERPVTKEEINAAMKAAASESYG----YNEDQIVSSDVVGieYGSL-FDATQTRVMTVGgkQLVKTVAW 312
Cdd:PTZ00353 240 KKGCAIDMLVRTKQPVSKEVVDSALAEAASDRLNgvlcISKRDMISVDCIP--NGKLcYDATSSSSSREG--EVHKMVLW 315
|
330
....*....|..
gi 488165058 313 YDNEMSYTCQLV 324
Cdd:PTZ00353 316 FDVECYYAARLL 327
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
151-316 |
8.01e-42 |
|
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: 142.94 E-value: 8.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 151 CTTNCLAPMAAVLQKEFGVVEGLMTTIHAYTGDQNTLDAPHRkgDLRRARAAALNIVPNSTGAAKAIGLVIPELNGKLDG 230
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDAYHP--DLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 231 SAQRVPVATGSLTELVSVLERPVTKEEINAAMKAAASESY----GYNEDQIVSSDVVGIEYGSLFDATQTRvmtVGGKQL 306
Cdd:cd23937 79 IAVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLkgilGYTEEPLVSVDFNHDPHSCIVDGTQTR---VSGKRL 155
|
170
....*....|
gi 488165058 307 VKTVAWYDNE 316
Cdd:cd23937 156 VKLLVWCDNE 165
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
151-316 |
1.11e-37 |
|
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: 132.26 E-value: 1.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 151 CTTNCLAPMAAVLQKEFGVVEGLMTTIHAYTGDQNTLDAPHRKGDlrrARAAALNIVPNSTGAAKAIGLVIPELN--GKL 228
Cdd:cd18122 1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE---VRAIIPNIPKNETKHAPETGKVLGEIGkpIKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 229 DGSAQRVPVATGSLTELVSVLERPVTKEEINAAMKAAASESYGYNED----QIVSSDVVGIEYGSLFDATQTRVMtvgGK 304
Cdd:cd18122 78 DGIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDgltyAKVSTRSVGGVYGVPVGRQREFAF---DD 154
|
170
....*....|..
gi 488165058 305 QLVKTVAWYDNE 316
Cdd:cd18122 155 NKLKVFSAVDNE 166
|
|
| GAPDH-like_N |
cd05192 |
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ... |
3-155 |
1.47e-16 |
|
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: 74.31 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 3 IKVAINGFGRIGRLALRQIEKAHGIEVVAVNDLTpaemllhlfkydstqgrfqgtaelkddaivvngkeikvfanpnpee 82
Cdd:cd05192 1 IRVAINGFGRIGRIVFRAIADQDDLDVVAINDRR---------------------------------------------- 34
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488165058 83 lpwgelgvDVVLECTGFFTNKTKAEAHIRAGARKVVISAPGGNDVKTVVYGVNQDILDGSETVISAASCTTNC 155
Cdd:cd05192 35 --------DVVIECTGSFTDDDNAEKHIKAGGKKAVITAPEKGDIPTIVVVLNELAKSAGATVVSNANETSYS 99
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|
| MDR |
cd05188 |
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ... |
4-161 |
8.29e-07 |
|
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.
Pssm-ID: 176178 [Multi-domain] Cd Length: 271 Bit Score: 49.63 E-value: 8.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 4 KVAINGFGRIGRLALrQIEKAHGIEVVAVndltpaemllhlfkyDSTQGRFQGTAELKDDAIVVNGKEikvfaNPNPEEL 83
Cdd:cd05188 137 TVLVLGAGGVGLLAA-QLAKAAGARVIVT---------------DRSDEKLELAKELGADHVIDYKEE-----DLEEELR 195
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488165058 84 PWGELGVDVVLECTGFFTNKTKAEAHIRAGARKVVISAPGGNDVKTVVygvnQDILDGSETVISAASCTTNCLAPMAA 161
Cdd:cd05188 196 LTGGGGADVVIDAVGGPETLAQALRLLRPGGRIVVVGGTSGGPPLDDL----RRLLFKELTIIGSTGGTREDFEEALD 269
|
|
| COG4091 |
COG4091 |
Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and ... |
3-115 |
1.06e-05 |
|
Predicted homoserine dehydrogenase, contains C-terminal SAF domain [Amino acid transport and metabolism];
Pssm-ID: 443267 [Multi-domain] Cd Length: 429 Bit Score: 46.68 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 3 IKVAINGFGRIGRLALRQIEKAHGIEVVAVNDLTP--AEMLLHLFKYDSTQGRFQGTAELKDDAIvvngKEIKVFANPNP 80
Cdd:COG4091 16 IRVGLIGAGQMGRGLLAQIRRMPGMEVVAIADRNPerARAALREAGIPEEDIRVVDTAAEADAAI----AAGKTVVTDDA 91
|
90 100 110
....*....|....*....|....*....|....*
gi 488165058 81 EELPwGELGVDVVLECTGfftnktkaeaHIRAGAR 115
Cdd:COG4091 92 ELLI-AADGIDVVVEATG----------VPEAGAR 115
|
|
| nat-AmDH_N_like |
cd24146 |
N-terminal NAD(P)-binding domain of native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs) ... |
3-120 |
1.54e-04 |
|
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: 41.37 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 3 IKVAINGFGRIGRLALRQIEKAHGIEVVAVNDLTPAEmllhlfkydstQGRFQGTAELKDDAIVVngkeikvfANPNPEE 82
Cdd:cd24146 1 IRVVVWGLGAMGRGIARYLLEKPGLEIVGAVDRDPAK-----------VGKDLGELGGGAPLGVK--------VTDDLDA 61
|
90 100 110
....*....|....*....|....*....|....*...
gi 488165058 83 LpWGELGVDVVLECTGFFTNKTKAEAHIRAGARKVVIS 120
Cdd:cd24146 62 V-LAATKPDVVVHATTSFLADVAPQIERLLEAGLNVIT 98
|
|
| MviM |
COG0673 |
Predicted dehydrogenase [General function prediction only]; |
1-38 |
1.66e-03 |
|
Predicted dehydrogenase [General function prediction only];
Pssm-ID: 440437 [Multi-domain] Cd Length: 295 Bit Score: 39.52 E-value: 1.66e-03
10 20 30
....*....|....*....|....*....|....*...
gi 488165058 1 MSIKVAINGFGRIGRLALRQIEKAHGIEVVAVNDLTPA 38
Cdd:COG0673 2 DKLRVGIIGAGGIGRAHAPALAALPGVELVAVADRDPE 39
|
|
| DHDPR_N |
cd02274 |
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; ... |
3-119 |
4.71e-03 |
|
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: 36.77 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488165058 3 IKVAINGF-GRIGRLALRQIEKAHGIEVVAVNDLTPAEMLLhlfkydstqgrfqgtaelkDDAIVVNGKEIKVFANPNPE 81
Cdd:cd02274 1 IKVAVAGAtGRMGRELVKAILEAPDLELVGAVDRPGSGLLG-------------------GDAGGLAGIGTGVIVSLDLE 61
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 488165058 82 ELpwgELGVDVVLEctgfFTNKTKAEAHIRAGARK---VVI 119
Cdd:cd02274 62 LA---AADADVVID----FTTPEATLENLEAAAKAgvpLVI 95
|
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