|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-330 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 682.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 1 MTIKIGINGFGRMGRLALRSAWDWAEFEFVQINDPAGGAAALGHLLEFDSVHGRWGKDVVVDDDALIIDGKRIAVSSNTE 80
Cdd:PRK08955 1 MTIKVGINGFGRIGRLALRAAWDWPELEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 81 LETTDWSGCDMVIEASGKFKRKEVLQKYLDQGVKKVIVTAPVKQEGVLDAVYGVNHHWYDKAKHDIVTAASCTTNCLAPA 160
Cdd:PRK08955 81 IADTDWSGCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLNIVMGVNDHLFDPAIHPIVTAASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 161 VKVIHEKLGIKHGSMTTIHSITNTQTILDAPHKDLRRARACGESLIPTTTGSATAITHIFPELKGRLNGHAIRVPLCNAS 240
Cdd:PRK08955 161 VKVIHEKLGIKHGSMTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLANAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 241 ITDCVFEVERATSADEVNGLLQEAAEGELKGILGYETRPLVSIDYRTDPRSSVVDALSTMVVNDTQVKLYLWYDNEWGYA 320
Cdd:PRK08955 241 LTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNEWGYA 320
|
330
....*....|
gi 503109163 321 NRTVELARYV 330
Cdd:PRK08955 321 NRTAELARKV 330
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
5-327 |
0e+00 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 663.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 5 IGINGFGRMGRLALRSAWDWAEFEFVQINDPAGGAAALGHLLEFDSVHGRWGKDVVVDDDALIIDGKRIAVSSNTELETT 84
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 85 DWS-GCDMVIEASGKFKRKEVLQKYLDQGVKKVIVTAPVKQEGVLDAVYGVNHHWYDKAKHDIVTAASCTTNCLAPAVKV 163
Cdd:NF033735 81 PWGdGVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLNIVYGVNDHLYDPARHRIVTAASCTTNCLAPVVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 164 IHEKLGIKHGSMTTIHSITNTQTILDAPHKDLRRARACGESLIPTTTGSATAITHIFPELKGRLNGHAIRVPLCNASITD 243
Cdd:NF033735 161 IHEKIGIKHGSITTIHDITNTQTIVDAPHKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASLTD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 244 CVFEVERATSADEVNGLLQEAAEGELKGILGYETRPLVSIDYRTDPRSSVVDALSTMVVNDTQVKLYLWYDNEWGYANRT 323
Cdd:NF033735 241 CVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYANRM 320
|
....
gi 503109163 324 VELA 327
Cdd:NF033735 321 VDLA 324
|
|
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
1-334 |
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: 560.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 1 MTIKIGINGFGRMGRLALRSAWDWA-EFEFVQINDPaGGAAALGHLLEFDSVHGRWGKDVVVDDDALIIDGKRIAVSSNT 79
Cdd:COG0057 1 MTIRVAINGFGRIGRLVLRALLERGpDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 80 ELETTDWS--GCDMVIEASGKFKRKEVLQKYLDQGVKKVIVTAPVKQEgVLDAVYGVNHHWYDkAKHDIVTAASCTTNCL 157
Cdd:COG0057 80 DPAELPWGelGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGD-DPTIVYGVNHDDYD-ADHRIISNASCTTNCL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 158 APAVKVIHEKLGIKHGSMTTIHSITNTQTILDAPHKDLRRARACGESLIPTTTGSATAITHIFPELKGRLNGHAIRVPLC 237
Cdd:COG0057 158 APVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 238 NASITDCVFEVERATSADEVNGLLQEAAEGELKGILGYETRPLVSIDYRTDPRSSVVDALSTMVVNDTQVKLYLWYDNEW 317
Cdd:COG0057 238 NVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEW 317
|
330
....*....|....*..
gi 503109163 318 GYANRTVELARYVAEQG 334
Cdd:COG0057 318 GYSNRMVDLAEYMAKLL 334
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
4-324 |
3.20e-153 |
|
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: 432.86 E-value: 3.20e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 4 KIGINGFGRMGRLALRSAW--DWAEFEFVQINDPaGGAAALGHLLEFDSVHGRWGKDVVVDDDALIIDGK-RIAVSSNTE 80
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILekPGNDLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKeVISVFSERD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 81 LETTDWS--GCDMVIEASGKFKRKEVLQKYLDQGVKKVIVTAPVKQEgVLDAVYGVNHHWYDkAKHDIVTAASCTTNCLA 158
Cdd:TIGR01534 80 PSDLPWKalGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGD-VKTIVYGVNHDEYD-GEERIISNASCTTNCLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 159 PAVKVIHEKLGIKHGSMTTIHSITNTQTILDAPHKDLRRARACGESLIPTTTGSATAITHIFPELKGRLNGHAIRVPLCN 238
Cdd:TIGR01534 158 PLAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 239 ASITDCVFEVERATSADEVNGLLQEAAEGELKGILGYETRPLVSIDYRTDPRSSVVDALSTMVVN--DTQVKLYLWYDNE 316
Cdd:TIGR01534 238 VSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVTGlgDSLVKVYAWYDNE 317
|
....*...
gi 503109163 317 WGYANRTV 324
Cdd:TIGR01534 318 WGYSNRLV 325
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
152-316 |
2.60e-104 |
|
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: 302.45 E-value: 2.60e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 152 CTTNCLAPAVKVIHEKLGIKHGSMTTIHSITNTQTILDAPHKDLRRARACGESLIPTTTGSATAITHIFPELKGRLNGHA 231
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 232 IRVPLCNASITDCVFEVERATSADEVNGLLQEAAEGELKGILGYETRPLVSIDYRTDPRSSVVDALSTMVVNDTQVKLYL 311
Cdd:cd18126 81 FRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVVA 160
|
....*
gi 503109163 312 WYDNE 316
Cdd:cd18126 161 WYDNE 165
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
157-313 |
3.80e-76 |
|
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: 230.94 E-value: 3.80e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 157 LAPAVKVIHEKLGIKHGSMTTIHSITNTQTILDAPH-KDLRRARACGESLIPTTTGSATAITHIFPELKGRLNGHAIRVP 235
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHhKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503109163 236 LCNASITDCVFEVERATSADEVNGLLQEAAEGELKGILGYETRPLVSIDYRTDPRSSVVDALSTMVVNDTQVKLYLWY 313
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-152 |
4.33e-59 |
|
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: 186.99 E-value: 4.33e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 3 IKIGINGFGRMGRLALRSAWDWAEFEFVQINDPaGGAAALGHLLEFDSVHGRWGKDVVVDDDALIIDGKRIAVSSNTELE 82
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503109163 83 TTDWS--GCDMVIEASGKFKRKEVLQKYLDQGVKKVIVTAPVKqEGVLDAVYGVNHHWYDKAKHdIVTAASC 152
Cdd:smart00846 80 NLPWGelGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSK-DADPTFVYGVNHDEYDGEDH-IISNASC 149
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-330 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 682.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 1 MTIKIGINGFGRMGRLALRSAWDWAEFEFVQINDPAGGAAALGHLLEFDSVHGRWGKDVVVDDDALIIDGKRIAVSSNTE 80
Cdd:PRK08955 1 MTIKVGINGFGRIGRLALRAAWDWPELEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 81 LETTDWSGCDMVIEASGKFKRKEVLQKYLDQGVKKVIVTAPVKQEGVLDAVYGVNHHWYDKAKHDIVTAASCTTNCLAPA 160
Cdd:PRK08955 81 IADTDWSGCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLNIVMGVNDHLFDPAIHPIVTAASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 161 VKVIHEKLGIKHGSMTTIHSITNTQTILDAPHKDLRRARACGESLIPTTTGSATAITHIFPELKGRLNGHAIRVPLCNAS 240
Cdd:PRK08955 161 VKVIHEKLGIKHGSMTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLANAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 241 ITDCVFEVERATSADEVNGLLQEAAEGELKGILGYETRPLVSIDYRTDPRSSVVDALSTMVVNDTQVKLYLWYDNEWGYA 320
Cdd:PRK08955 241 LTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNEWGYA 320
|
330
....*....|
gi 503109163 321 NRTVELARYV 330
Cdd:PRK08955 321 NRTAELARKV 330
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
5-327 |
0e+00 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 663.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 5 IGINGFGRMGRLALRSAWDWAEFEFVQINDPAGGAAALGHLLEFDSVHGRWGKDVVVDDDALIIDGKRIAVSSNTELETT 84
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 85 DWS-GCDMVIEASGKFKRKEVLQKYLDQGVKKVIVTAPVKQEGVLDAVYGVNHHWYDKAKHDIVTAASCTTNCLAPAVKV 163
Cdd:NF033735 81 PWGdGVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLNIVYGVNDHLYDPARHRIVTAASCTTNCLAPVVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 164 IHEKLGIKHGSMTTIHSITNTQTILDAPHKDLRRARACGESLIPTTTGSATAITHIFPELKGRLNGHAIRVPLCNASITD 243
Cdd:NF033735 161 IHEKIGIKHGSITTIHDITNTQTIVDAPHKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASLTD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 244 CVFEVERATSADEVNGLLQEAAEGELKGILGYETRPLVSIDYRTDPRSSVVDALSTMVVNDTQVKLYLWYDNEWGYANRT 323
Cdd:NF033735 241 CVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYANRM 320
|
....
gi 503109163 324 VELA 327
Cdd:NF033735 321 VDLA 324
|
|
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
1-334 |
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: 560.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 1 MTIKIGINGFGRMGRLALRSAWDWA-EFEFVQINDPaGGAAALGHLLEFDSVHGRWGKDVVVDDDALIIDGKRIAVSSNT 79
Cdd:COG0057 1 MTIRVAINGFGRIGRLVLRALLERGpDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 80 ELETTDWS--GCDMVIEASGKFKRKEVLQKYLDQGVKKVIVTAPVKQEgVLDAVYGVNHHWYDkAKHDIVTAASCTTNCL 157
Cdd:COG0057 80 DPAELPWGelGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGD-DPTIVYGVNHDDYD-ADHRIISNASCTTNCL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 158 APAVKVIHEKLGIKHGSMTTIHSITNTQTILDAPHKDLRRARACGESLIPTTTGSATAITHIFPELKGRLNGHAIRVPLC 237
Cdd:COG0057 158 APVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 238 NASITDCVFEVERATSADEVNGLLQEAAEGELKGILGYETRPLVSIDYRTDPRSSVVDALSTMVVNDTQVKLYLWYDNEW 317
Cdd:COG0057 238 NVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEW 317
|
330
....*....|....*..
gi 503109163 318 GYANRTVELARYVAEQG 334
Cdd:COG0057 318 GYSNRMVDLAEYMAKLL 334
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
4-324 |
3.20e-153 |
|
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: 432.86 E-value: 3.20e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 4 KIGINGFGRMGRLALRSAW--DWAEFEFVQINDPaGGAAALGHLLEFDSVHGRWGKDVVVDDDALIIDGK-RIAVSSNTE 80
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILekPGNDLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKeVISVFSERD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 81 LETTDWS--GCDMVIEASGKFKRKEVLQKYLDQGVKKVIVTAPVKQEgVLDAVYGVNHHWYDkAKHDIVTAASCTTNCLA 158
Cdd:TIGR01534 80 PSDLPWKalGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGD-VKTIVYGVNHDEYD-GEERIISNASCTTNCLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 159 PAVKVIHEKLGIKHGSMTTIHSITNTQTILDAPHKDLRRARACGESLIPTTTGSATAITHIFPELKGRLNGHAIRVPLCN 238
Cdd:TIGR01534 158 PLAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 239 ASITDCVFEVERATSADEVNGLLQEAAEGELKGILGYETRPLVSIDYRTDPRSSVVDALSTMVVN--DTQVKLYLWYDNE 316
Cdd:TIGR01534 238 VSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVTGlgDSLVKVYAWYDNE 317
|
....*...
gi 503109163 317 WGYANRTV 324
Cdd:TIGR01534 318 WGYSNRLV 325
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-333 |
2.02e-144 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 411.44 E-value: 2.02e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 1 MTIKIGINGFGRMGRLALRSAWDWAEFEFVQINdPAGGAAALGHLLEFDSVHGRWGKDVVVDDDALIIDGKRIAVSSNTE 80
Cdd:PRK07729 1 MKTKVAINGFGRIGRMVFRKAIKESAFEIVAIN-ASYPSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 81 LETTDWS--GCDMVIEASGKFKRKEVLQKYLDQGVKKVIVTAPVKQEGVlDAVYGVNHHWYDKAKHDIVTAASCTTNCLA 158
Cdd:PRK07729 80 PKELPWTdlGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDV-TIVVGVNEDQLDIEKHTIISNASCTTNCLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 159 PAVKVIHEKLGIKHGSMTTIHSITNTQTILDAPHKDLRRARACGESLIPTTTGSATAITHIFPELKGRLNGHAIRVPLCN 238
Cdd:PRK07729 159 PVVKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 239 ASITDCVFEVERATSADEVNGLLQEAAEGELKGILGYETRPLVSIDYRTDPRSSVVDALSTMVVNDTQVKLYLWYDNEWG 318
Cdd:PRK07729 239 VSLVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEWG 318
|
330
....*....|....*
gi 503109163 319 YANRTVELARYVAEQ 333
Cdd:PRK07729 319 YSCRVVDLVTLVADE 333
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
2-333 |
7.61e-118 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 343.43 E-value: 7.61e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 2 TIKIGINGFGRMGRLALRsAW---DWAEFEFVQINDPAGGAAAlGHLLEFDSVHGRWGKDVVVDDDALIIDGKRIAVSSN 78
Cdd:PRK07403 1 MIRVAINGFGRIGRNFLR-CWlgrENSQLELVAINDTSDPRTN-AHLLKYDSMLGKLNADISADENSITVNGKTIKCVSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 79 TELETTDWS--GCDMVIEASGKFKRKEVLQKYLDQGVKKVIVTAPVKQEGVLDAVYGVNHHWYDKAKHDIVTAASCTTNC 156
Cdd:PRK07403 79 RNPLNLPWKewGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPGKGEDIGTYVVGVNHHEYDHEDHNIISNASCTTNC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 157 LAPAVKVIHEKLGIKHGSMTTIHSITNTQTILDAPHKDLRRARACGESLIPTTTGSATAITHIFPELKGRLNGHAIRVPL 236
Cdd:PRK07403 159 LAPIAKVLHDNFGIIKGTMTTTHSYTGDQRILDASHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 237 CNASITDCVFEVERATSADEVNGLLQEAAEGELKGILGYETRPLVSIDYRTDPRSSVVDALSTMVVNDTQVKLYLWYDNE 316
Cdd:PRK07403 239 PNVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYDNE 318
|
330
....*....|....*..
gi 503109163 317 WGYANRTVELARYVAEQ 333
Cdd:PRK07403 319 WGYSQRVVDLAELVARK 335
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
152-316 |
2.60e-104 |
|
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: 302.45 E-value: 2.60e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 152 CTTNCLAPAVKVIHEKLGIKHGSMTTIHSITNTQTILDAPHKDLRRARACGESLIPTTTGSATAITHIFPELKGRLNGHA 231
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 232 IRVPLCNASITDCVFEVERATSADEVNGLLQEAAEGELKGILGYETRPLVSIDYRTDPRSSVVDALSTMVVNDTQVKLYL 311
Cdd:cd18126 81 FRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVVA 160
|
....*
gi 503109163 312 WYDNE 316
Cdd:cd18126 161 WYDNE 165
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
3-333 |
5.06e-104 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 310.32 E-value: 5.06e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 3 IKIGINGFGRMGRLALRSawdW-----AEFEFVQINDpAGGAAALGHLLEFDSVHGRWGKDV-VVDDDALIIDGKRIAVS 76
Cdd:PLN03096 61 IKVAINGFGRIGRNFLRC---WhgrkdSPLDVVAIND-TGGVKQASHLLKYDSTLGTFDADVkPVGDDAISVDGKVIKVV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 77 SNTELETTDWS--GCDMVIEASGKFKRKEVLQKYLDQGVKKVIVTAPVKQEgVLDAVYGVNHHWYdKAKHDIVTAASCTT 154
Cdd:PLN03096 137 SDRNPLNLPWGelGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKGD-IPTYVVGVNADDY-KHSDPIISNASCTT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 155 NCLAPAVKVIHEKLGIKHGSMTTIHSITNTQTILDAPHKDLRRARACGESLIPTTTGSATAITHIFPELKGRLNGHAIRV 234
Cdd:PLN03096 215 NCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 235 PLCNASITDCVFEVERATSADEVNGLLQEAAEGELKGILGYETRPLVSIDYRTDPRSSVVDALSTMVVNDTQVKLYLWYD 314
Cdd:PLN03096 295 PTPNVSVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAWYD 374
|
330
....*....|....*....
gi 503109163 315 NEWGYANRTVELARYVAEQ 333
Cdd:PLN03096 375 NEWGYSQRVVDLADIVANK 393
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
3-335 |
3.44e-103 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 309.91 E-value: 3.44e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 3 IKIGINGFGRMGRLALRSawdWAE-----FEFVQINDpAGGAAALGHLLEFDSVHGRWGKDV-VVDDDALIIDGKRIAVS 76
Cdd:PLN02237 76 LKVAINGFGRIGRNFLRC---WHGrkdspLDVVVVND-SGGVKNASHLLKYDSMLGTFKADVkIVDDETISVDGKPIKVV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 77 SNTELETTDWS--GCDMVIEASGKFKRKEVLQKYLDQGVKKVIVTAPVKQEGVLDAVYGVNHHWYDKAKHDIVTAASCTT 154
Cdd:PLN02237 152 SNRDPLKLPWAelGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAKGADIPTYVVGVNEDDYDHEVANIVSNASCTT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 155 NCLAPAVKVIHEKLGIKHGSMTTIHSITNTQTILDAPHKDLRRARACGESLIPTTTGSATAITHIFPELKGRLNGHAIRV 234
Cdd:PLN02237 232 NCLAPFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRV 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 235 PLCNASITDCVFEVER-ATSADEVNGLLQEAAEGELKGILGYETRPLVSIDYRTDPRSSVVDALSTMVVNDTQVKLYLWY 313
Cdd:PLN02237 312 PTPNVSVVDLVVNVEKkGITAEDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVAWY 391
|
330 340
....*....|....*....|..
gi 503109163 314 DNEWGYANRTVELARYVAEqGW 335
Cdd:PLN02237 392 DNEWGYSQRVVDLAHLVAA-KW 412
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
2-334 |
1.63e-101 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 301.98 E-value: 1.63e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 2 TIKIGINGFGRMGRLALRSAWD---WAEFEFVQINDPAGgAAALGHLLEFDSVHGRWGKDVVVDDDALIIDGKRIAVSSN 78
Cdd:PRK13535 1 TIRVAINGFGRIGRNVLRALYEsgrRAEITVVAINELAD-AEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 79 TELETTDWS--GCDMVIEASGKFKRKEVLQKYLDQGVKKVIVTAPVKQEgvLDA--VYGVNHHWYdKAKHDIVTAASCTT 154
Cdd:PRK13535 80 RDIASLPWRelGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSND--LDAtvVYGVNHDQL-RAEHRIVSNASCTT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 155 NCLAPAVKVIHEKLGIKHGSMTTIHSITNTQTILDAPHKDLRRARACGESLIPTTTGSATAITHIFPELKGRLNGHAIRV 234
Cdd:PRK13535 157 NCIIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 235 PLCNASITDCVFEVERATSADEVNGLLQEAAEGELKGILGYETRPLVSIDYRTDPRSSVVDALSTMVVNDTQVKLYLWYD 314
Cdd:PRK13535 237 PTINVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCD 316
|
330 340
....*....|....*....|
gi 503109163 315 NEWGYANRTVELARYVAEQG 334
Cdd:PRK13535 317 NEWGFANRMLDTTLAMAAAG 336
|
|
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-333 |
3.44e-101 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 301.37 E-value: 3.44e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 1 MTIKIGINGFGRMGRLALRSAWDWAEFEFVQINDPAGGAAALGHLLEFDSVHGRWGKDVVVDDDALIIDGKRIAVSSNTE 80
Cdd:PTZ00023 1 MVVKLGINGFGRIGRLVFRAALEREDVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 81 LETTDW--SGCDMVIEASGKFKRKEVLQKYLDQGVKKVIVTAPVKQEGVLdAVYGVNHHWYDKaKHDIVTAASCTTNCLA 158
Cdd:PTZ00023 81 PAAIPWgkNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKDDTPI-YVMGVNHTQYDK-SQRIVSNASCTTNCLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 159 PAVKVIHEKLGIKHGSMTTIHSITNTQTILDAPH---KDLRRARACGESLIPTTTGSATAITHIFPELKGRLNGHAIRVP 235
Cdd:PTZ00023 159 PLAKVVNDKFGIVEGLMTTVHASTANQLTVDGPSkggKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 236 LCNASITDCVFEVERATSADEVNGLLQEAAEGELKGILGYETRPLVSIDYRTDPRSSVVDALSTMVVNDTQVKLYLWYDN 315
Cdd:PTZ00023 239 VPDVSVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDN 318
|
330
....*....|....*...
gi 503109163 316 EWGYANRTVELARYVAEQ 333
Cdd:PTZ00023 319 EWGYSNRLLDLAHYITQK 336
|
|
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
3-331 |
3.22e-100 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 301.78 E-value: 3.22e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 3 IKIGINGFGRMGRLALRSAWDWAEFEFVQINDPAGGAAALGHLLEFDSVHGRWGKDV-VVDDDALIIDGKRIAVSSNTEL 81
Cdd:PLN02272 86 TKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTInVVDDSTLEINGKQIKVTSKRDP 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 82 ETTDWS--GCDMVIEASGKFKRKEVLQKYLDQGVKKVIVTAPVKqegvlDA---VYGVNHHWYdKAKHDIVTAASCTTNC 156
Cdd:PLN02272 166 AEIPWGdfGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSA-----DApmfVVGVNEKTY-KPNMNIVSNASCTTNC 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 157 LAPAVKVIHEKLGIKHGSMTTIHSITNTQTILDAPH-KDLRRARACGESLIPTTTGSATAITHIFPELKGRLNGHAIRVP 235
Cdd:PLN02272 240 LAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSmKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVP 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 236 LCNASITDCVFEVERATSADEVNGLLQEAAEGELKGILGYETRPLVSIDYRTDPRSSVVDALSTMVVNDTQVKLYLWYDN 315
Cdd:PLN02272 320 TPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDN 399
|
330
....*....|....*.
gi 503109163 316 EWGYANRTVELARYVA 331
Cdd:PLN02272 400 EWGYSNRVLDLIEHMA 415
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
1-332 |
2.08e-88 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 268.53 E-value: 2.08e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 1 MTIKIGINGFGRMGRLALRSAWDWAEFEFVQINDPAGgAAALGHLLEFDSVHGRWGKDVVVDDDALIIDGKRIAVSSNTE 80
Cdd:PRK15425 1 MTIKVGINGFGRIGRIVFRAAQKRSDIEIVAINDLLD-ADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 81 LETTDWS--GCDMVIEASGKFKRKEVLQKYLDQGVKKVIVTAPVKQEGVLdAVYGVNHHWYdkAKHDIVTAASCTTNCLA 158
Cdd:PRK15425 80 PANLKWDevGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDNTPM-FVKGANFDKY--AGQDIVSNASCTTNCLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 159 PAVKVIHEKLGIKHGSMTTIHSITNTQTILDAP-HKDLRRARACGESLIPTTTGSATAITHIFPELKGRLNGHAIRVPLC 237
Cdd:PRK15425 157 PLAKVINDNFGIIEGLMTTVHATTATQKTVDGPsHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 238 NASITDCVFEVERATSADEVNGLLQEAAEGELKGILGYETRPLVSIDYRTDPRSSVVDALSTMVVNDTQVKLYLWYDNEW 317
Cdd:PRK15425 237 NVSVVDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNET 316
|
330
....*....|....*
gi 503109163 318 GYANRTVELARYVAE 332
Cdd:PRK15425 317 GYSNKVLDLIAHISK 331
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
1-331 |
4.99e-88 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 268.46 E-value: 4.99e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 1 MTIKIGINGFGRMGRLALRSAWDWA----EFEFVQINDPAGGAAALGHLLEFDSVHGRWGKDV--------VVDDDALII 68
Cdd:PTZ00434 2 APIKVGINGFGRIGRMVFQAICDQGligtEIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVettksspsVKTDDVLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 69 DGKRI-AVSSNTELETTDWS--GCDMVIEASGKFKRKEVLQKYLDQGVKKVIVTAPVKQeGVLDAVYGVNHHWYDKAKHD 145
Cdd:PTZ00434 82 NGHRIkCVKAQRNPADLPWGklGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPASG-GAKTIVMGVNQHEYSPTEHH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 146 IVTAASCTTNCLAPAVKVI-HEKLGIKHGSMTTIHSITNTQTILDAPH-KDLRRARACGESLIPTTTGSATAITHIFPEL 223
Cdd:PTZ00434 161 VVSNASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSvKDWRGGRAAAVNIIPSTTGAAKAVGMVIPST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 224 KGRLNGHAIRVPLCNASITDCVFEVERATSADEVNGLLQEAAEGELKGILGYETRPLVSIDYRTDPRSSVVDALSTMVVN 303
Cdd:PTZ00434 241 KGKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKATLQNN 320
|
330 340 350
....*....|....*....|....*....|..
gi 503109163 304 DTQVKLYL----WYDNEWGYANRTVELARYVA 331
Cdd:PTZ00434 321 LPGERRFFkivsWYDNEWGYSHRVVDLVRYMA 352
|
|
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
3-332 |
8.49e-87 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 264.66 E-value: 8.49e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 3 IKIGINGFGRMGRLALRSAWDWAEFEFVQINDPAGGAAALGHLLEFDSVHGRWGKD--VVVDDDALIIDGKRIAVSSNTE 80
Cdd:PLN02358 6 IRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKHHelKVKDDKTLLFGEKPVTVFGIRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 81 LETTDWS--GCDMVIEASGKFKRKEVLQKYLDQGVKKVIVTAPVKQEGVLdaVYGVNHHWYdKAKHDIVTAASCTTNCLA 158
Cdd:PLN02358 86 PEDIPWGeaGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMF--VVGVNEHEY-KSDLDIVSNASCTTNCLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 159 PAVKVIHEKLGIKHGSMTTIHSITNTQTILDAPH-KDLRRARACGESLIPTTTGSATAITHIFPELKGRLNGHAIRVPLC 237
Cdd:PLN02358 163 PLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSmKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 238 NASITDCVFEVERATSADEVNGLLQEAAEGELKGILGYETRPLVSIDYRTDPRSSVVDALSTMVVNDTQVKLYLWYDNEW 317
Cdd:PLN02358 243 DVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEW 322
|
330
....*....|....*
gi 503109163 318 GYANRTVELARYVAE 332
Cdd:PLN02358 323 GYSSRVVDLIVHMSK 337
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
157-313 |
3.80e-76 |
|
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: 230.94 E-value: 3.80e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 157 LAPAVKVIHEKLGIKHGSMTTIHSITNTQTILDAPH-KDLRRARACGESLIPTTTGSATAITHIFPELKGRLNGHAIRVP 235
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHhKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503109163 236 LCNASITDCVFEVERATSADEVNGLLQEAAEGELKGILGYETRPLVSIDYRTDPRSSVVDALSTMVVNDTQVKLYLWY 313
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
9-331 |
4.13e-73 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 233.66 E-value: 4.13e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 9 GFGRMGRLALRsawdwaefefvQINDPAGGAAAL------------------GHLLEFDSVHGRWGKDVVVDDD--ALII 68
Cdd:PRK08289 134 GFGRIGRLLAR-----------LLIEKTGGGNGLrlraivvrkgsegdlekrASLLRRDSVHGPFNGTITVDEEnnAIIA 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 69 DGKRIAV---SSNTELETTDWsGCD--MVIEASGKFKRKEVLQKYLD-QGVKKVIVTAPVKQEgVLDAVYGVNHHWYdKA 142
Cdd:PRK08289 203 NGNYIQViyaNSPEEVDYTAY-GINnaLVVDNTGKWRDEEGLSQHLKsKGVAKVLLTAPGKGD-IKNIVHGVNHSDI-TD 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 143 KHDIVTAASCTTNCLAPAVKVIHEKLGIKHGSMTTIHSITNTQTILDAPHKDLRRARACGESLIPTTTGSATAITHIFPE 222
Cdd:PRK08289 280 EDKIVSAASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKGDRRGRSAPLNMVITETGAAKAVAKALPE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 223 LKGRLNGHAIRVPLCNASITDCVFEVERATSADEVNGLLQEAA-EGELKGILGYETRP-LVSIDYRTDPRSSVVDALSTm 300
Cdd:PRK08289 360 LAGKLTGNAIRVPTPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQIDYTDSTeVVSSDFVGSRHAGVVDSQAT- 438
|
330 340 350
....*....|....*....|....*....|.
gi 503109163 301 VVNDTQVKLYLWYDNEWGYANRTVELARYVA 331
Cdd:PRK08289 439 IVNGNRAVLYVWYDNEFGYSCQVVRVMEQMA 469
|
|
| GAPDH_I_N |
cd05214 |
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
3-151 |
1.99e-61 |
|
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: 193.38 E-value: 1.99e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 3 IKIGINGFGRMGRLALRSAWDWAEFEFVQINDPaGGAAALGHLLEFDSVHGRWGKDVVVDDDALIIDGKRIAVSSNTELE 82
Cdd:cd05214 1 IKVGINGFGRIGRLVFRAALERDDIEVVAINDL-TDDETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503109163 83 TTDWS--GCDMVIEASGKFKRKEVLQKYLDQGVKKVIVTAPVKqEGVLDAVYGVNHHWYDkAKHDIVTAAS 151
Cdd:cd05214 80 ELPWGelGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAK-DDDPTIVMGVNHDKYD-ADDKIISNAS 148
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
152-316 |
5.65e-60 |
|
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: 189.93 E-value: 5.65e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 152 CTTNCLAPAVKVIHEKLGIKHGSMTTIHSITNTQTILDAPHKDLRRARACGESLIPTTTGSATAITHIFPELKGRLNGHA 231
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 232 IRVPLCNASITDCVFEVERATSADEVNGLLQEAAEGELKGILGYETRPLVSIDYRTDPRSSVVDALSTMVVNDTQVKLYL 311
Cdd:cd23937 81 VRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLLV 160
|
....*
gi 503109163 312 WYDNE 316
Cdd:cd23937 161 WCDNE 165
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-152 |
4.33e-59 |
|
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: 186.99 E-value: 4.33e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 3 IKIGINGFGRMGRLALRSAWDWAEFEFVQINDPaGGAAALGHLLEFDSVHGRWGKDVVVDDDALIIDGKRIAVSSNTELE 82
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503109163 83 TTDWS--GCDMVIEASGKFKRKEVLQKYLDQGVKKVIVTAPVKqEGVLDAVYGVNHHWYDKAKHdIVTAASC 152
Cdd:smart00846 80 NLPWGelGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSK-DADPTFVYGVNHDEYDGEDH-IISNASC 149
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
152-316 |
1.61e-47 |
|
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: 157.78 E-value: 1.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 152 CTTNCLAPAVKVIHEKLGIKHGSMTTIHSITNTQTILDAP-HKDLRRARACGESLIPTTTGSATAITHIFPELKGRLNGH 230
Cdd:cd18123 1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPsGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 231 AIRVPLCNASITDCVFEVERATSADEVNGLLQEAAEGelKGILGYETRPLVSIDYRTDPRSSVVDALSTMVVNDTQVKLY 310
Cdd:cd18123 81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLM 158
|
....*.
gi 503109163 311 LWYDNE 316
Cdd:cd18123 159 QWYDNE 164
|
|
| Gp_dh_N |
pfam00044 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-100 |
3.44e-39 |
|
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: 134.15 E-value: 3.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 3 IKIGINGFGRMGRLALRSAWDWAEFEFVQINDPaGGAAALGHLLEFDSVHGRWGKDVVVDDDALIIDGKRIAVSSNTELE 82
Cdd:pfam00044 1 VKVGINGFGRIGRLVLRAALERPDIEVVAINDL-TDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPA 79
|
90 100
....*....|....*....|
gi 503109163 83 TTDWS--GCDMVIEASGKFK 100
Cdd:pfam00044 80 ELPWGdlGVDVVIESTGVFT 99
|
|
| GAPDH_N_E4PDH |
cd17892 |
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
3-151 |
8.26e-37 |
|
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: 130.08 E-value: 8.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 3 IKIGINGFGRMGRLALRSAWD---WAEFEFVQINDPAGgAAALGHLLEFDSVHGRWGKDVVVDDDALIIDGKRIAVSSNT 79
Cdd:cd17892 1 YRVAINGYGRIGRNVLRALYEsgrRAEFQVVAINELAD-AETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEP 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503109163 80 ELETTDWS--GCDMVIEASGKFKRKEVLQKYLDQGVKKVIVTAPVKQEgvLDA--VYGVNHHWYdKAKHDIVTAAS 151
Cdd:cd17892 80 DPENLPWRelGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASND--VDAtiVYGINQDLL-RAEHRIVSNAS 152
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-330 |
5.35e-36 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 133.08 E-value: 5.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 1 MTIKIGINGFGRMGRLALRSAWDWAEFEFVQINDPAGGAAALGHLLEFDSVHGRWGKD--VVVDDDALIIDGKRIAVSSN 78
Cdd:PTZ00353 1 LPITVGINGFGPVGKAVLFASLTDPLVTVVAVNDASVSIAYIAYVLEQESPLSAPDGAsiRVVGEQIVLNGTQKIRVSAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 79 TELETTDWS--GCDMVIEASGKFKRKEVLQKYLDQGVKKVIVTApvkQEGVLDAVYGVNHHWYDKAKHDIVTAASCTTNC 156
Cdd:PTZ00353 81 HDLVEIAWRdyGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAG---QSADAPTVMAGSNDERLSASLPVCCAGAPIAVA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 157 LAPAVKVIHEKLGIKHGSMTTIHSITNTQTIL--DAPHKDLRRARACGESLIPTTTGSATAITHIFPELKGRLNGHAIRV 234
Cdd:PTZ00353 158 LAPVIRALHEVYGVEECSYTAIHGMQPQEPIAarSKNSQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 235 PLCNASITDCVFEVERATSADEVNGLLQEAAEGELKGILGYETRPLVSIDyrTDPRSSVV-DALSTMVVNDTQV-KLYLW 312
Cdd:PTZ00353 238 PVKKGCAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVD--CIPNGKLCyDATSSSSSREGEVhKMVLW 315
|
330
....*....|....*...
gi 503109163 313 YDNEWGYANRTVELARYV 330
Cdd:PTZ00353 316 FDVECYYAARLLSLVKQL 333
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
152-316 |
7.07e-24 |
|
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: 96.05 E-value: 7.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 152 CTTNCLAPAVKVIHEKLGIKHGSMTTIHSITNTQTILDAPHkDLRRARACGESLIPTTTGSATAITHIFPEL--KGRLNG 229
Cdd:cd18122 1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPI-LKSEVRAIIPNIPKNETKHAPETGKVLGEIgkPIKVDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 230 HAIRVPLCNASITDCVFEVERATSADEVNGLLQEAAEGELKGILGYETRPLVSIDYRTDPRSSVVDALSTMVVNDTQVKL 309
Cdd:cd18122 80 IAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLKV 159
|
....*..
gi 503109163 310 YLWYDNE 316
Cdd:cd18122 160 FSAVDNE 166
|
|
| GAPDH-like_N |
cd05192 |
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ... |
3-156 |
4.77e-03 |
|
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: 36.18 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503109163 3 IKIGINGFGRMGRLAlrsawdwaefefvqindpaggaaalghlleFDSVHGRWGKDVVVDDDALiidgkriavssntele 82
Cdd:cd05192 1 IRVAINGFGRIGRIV------------------------------FRAIADQDDLDVVAINDRR---------------- 34
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503109163 83 ttdwsgcDMVIEASGKFKRKEVLQKYLDQGVKKVIVTAPVKQEgvlDAVYGVNHHWYDK-AKHDIVTAASCTTNC 156
Cdd:cd05192 35 -------DVVIECTGSFTDDDNAEKHIKAGGKKAVITAPEKGD---IPTIVVVLNELAKsAGATVVSNANETSYS 99
|
|
| |
