|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-333 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 706.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 1 MTVKVGINGFGRIGRLALRAAFDWAEIEFVQINDVAGDTATLAHLLEFDSVQGRWNHEVAVEGDEMIIKGQRIRTTQERD 80
Cdd:PRK08955 1 MTIKVGINGFGRIGRLALRAAWDWPELEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 81 IDAIDWSGCDVVLEATGVHRKASFLNKYLEQGVKRVVVSAPVKEEGIANIVVGVNDNIFDPAVHKIVTAASCTTNCLAPV 160
Cdd:PRK08955 81 IADTDWSGCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLNIVMGVNDHLFDPAIHPIVTAASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 161 VKVINEKLGIENAAFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELENRINGHAVRVPLANAS 240
Cdd:PRK08955 161 VKVIHEKLGIKHGSMTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLANAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 241 LTDIIFEVKQDTTAEEVNAMLKEASENELKGILGFEERPLVSIDYKGDQRSTIVDALSTMLVGKRMVKIYAWYDNEMGYA 320
Cdd:PRK08955 241 LTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNEWGYA 320
|
330
....*....|...
gi 1330039263 321 TRTAELVRTVGLA 333
Cdd:PRK08955 321 NRTAELARKVGLA 333
|
|
| 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: 624.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 5 VGINGFGRIGRLALRAAFDWAEIEFVQINDVAGDTATLAHLLEFDSVQGRWNHEVAVEGDEMIIKGQRIRTTQERDIDAI 84
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 85 DWS-GCDVVLEATGVHRKASFLNKYLEQGVKRVVVSAPVKEEGIANIVVGVNDNIFDPAVHKIVTAASCTTNCLAPVVKV 163
Cdd:NF033735 81 PWGdGVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLNIVYGVNDHLYDPARHRIVTAASCTTNCLAPVVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 164 INEKLGIENAAFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELENRINGHAVRVPLANASLTD 243
Cdd:NF033735 161 IHEKIGIKHGSITTIHDITNTQTIVDAPHKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASLTD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 244 IIFEVKQDTTAEEVNAMLKEASENELKGILGFEERPLVSIDYKGDQRSTIVDALSTMLVGKRMVKIYAWYDNEMGYATRT 323
Cdd:NF033735 241 CVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYANRM 320
|
....
gi 1330039263 324 AELV 327
Cdd:NF033735 321 VDLA 324
|
|
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
1-331 |
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: 536.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 1 MTVKVGINGFGRIGRLALRAAFDWA-EIEFVQINDVaGDTATLAHLLEFDSVQGRWNHEVAVEGDEMIIKGQRIRTTQER 79
Cdd:COG0057 1 MTIRVAINGFGRIGRLVLRALLERGpDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 80 DIDAIDWS--GCDVVLEATGVHRKASFLNKYLEQGVKRVVVSAPVKEEgIANIVVGVNDNIFDPAvHKIVTAASCTTNCL 157
Cdd:COG0057 80 DPAELPWGelGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGD-DPTIVYGVNHDDYDAD-HRIISNASCTTNCL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 158 APVVKVINEKLGIENAAFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELENRINGHAVRVPLA 237
Cdd:COG0057 158 APVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 238 NASLTDIIFEVKQDTTAEEVNAMLKEASENELKGILGFEERPLVSIDYKGDQRSTIVDALSTMLVGKRMVKIYAWYDNEM 317
Cdd:COG0057 238 NVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEW 317
|
330
....*....|....
gi 1330039263 318 GYATRTAELVRTVG 331
Cdd:COG0057 318 GYSNRMVDLAEYMA 331
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
4-322 |
1.24e-146 |
|
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: 415.91 E-value: 1.24e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 4 KVGINGFGRIGRLALRAAF--DWAEIEFVQINDVaGDTATLAHLLEFDSVQGRWNHEVAVEGDEMIIKGQ-RIRTTQERD 80
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILekPGNDLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKeVISVFSERD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 81 IDAIDWS--GCDVVLEATGVHRKASFLNKYLEQGVKRVVVSAPVKEEGIaNIVVGVNDNIFDPAvHKIVTAASCTTNCLA 158
Cdd:TIGR01534 80 PSDLPWKalGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDVK-TIVYGVNHDEYDGE-ERIISNASCTTNCLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 159 PVVKVINEKLGIENAAFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELENRINGHAVRVPLAN 238
Cdd:TIGR01534 158 PLAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 239 ASLTDIIFEVKQDTTAEEVNAMLKEASENELKGILGFEERPLVSIDYKGDQRSTIVDALSTML--VGKRMVKIYAWYDNE 316
Cdd:TIGR01534 238 VSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNE 317
|
....*.
gi 1330039263 317 MGYATR 322
Cdd:TIGR01534 318 WGYSNR 323
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
152-316 |
2.87e-97 |
|
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: 284.73 E-value: 2.87e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 152 CTTNCLAPVVKVINEKLGIENAAFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELENRINGHA 231
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 232 VRVPLANASLTDIIFEVKQDTTAEEVNAMLKEASENELKGILGFEERPLVSIDYKGDQRSTIVDALSTMLVGKRMVKIYA 311
Cdd:cd18126 81 FRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVVA 160
|
....*
gi 1330039263 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 |
2.10e-70 |
|
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: 215.92 E-value: 2.10e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 157 LAPVVKVINEKLGIENAAFTTIHDLTNTQTILDAPH-KDLRRARACGMSLIPTTTGSAKAIVEIFPELENRINGHAVRVP 235
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHhKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330039263 236 LANASLTDIIFEVKQDTTAEEVNAMLKEASENELKGILGFEERPLVSIDYKGDQRSTIVDALSTMLVGKRMVKIYAWY 313
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-152 |
3.09e-63 |
|
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: 197.39 E-value: 3.09e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 3 VKVGINGFGRIGRLALRAAFDWAEIEFVQINDvAGDTATLAHLLEFDSVQGRWNHEVAVEGDEMIIKGQRIRTTQERDID 82
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAIND-LTDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1330039263 83 AIDWS--GCDVVLEATGVHRKASFLNKYLEQGVKRVVVSAPVKEEgIANIVVGVNDNIFDPAvHKIVTAASC 152
Cdd:smart00846 80 NLPWGelGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDA-DPTFVYGVNHDEYDGE-DHIISNASC 149
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-333 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 706.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 1 MTVKVGINGFGRIGRLALRAAFDWAEIEFVQINDVAGDTATLAHLLEFDSVQGRWNHEVAVEGDEMIIKGQRIRTTQERD 80
Cdd:PRK08955 1 MTIKVGINGFGRIGRLALRAAWDWPELEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 81 IDAIDWSGCDVVLEATGVHRKASFLNKYLEQGVKRVVVSAPVKEEGIANIVVGVNDNIFDPAVHKIVTAASCTTNCLAPV 160
Cdd:PRK08955 81 IADTDWSGCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLNIVMGVNDHLFDPAIHPIVTAASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 161 VKVINEKLGIENAAFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELENRINGHAVRVPLANAS 240
Cdd:PRK08955 161 VKVIHEKLGIKHGSMTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLANAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 241 LTDIIFEVKQDTTAEEVNAMLKEASENELKGILGFEERPLVSIDYKGDQRSTIVDALSTMLVGKRMVKIYAWYDNEMGYA 320
Cdd:PRK08955 241 LTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNEWGYA 320
|
330
....*....|...
gi 1330039263 321 TRTAELVRTVGLA 333
Cdd:PRK08955 321 NRTAELARKVGLA 333
|
|
| 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: 624.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 5 VGINGFGRIGRLALRAAFDWAEIEFVQINDVAGDTATLAHLLEFDSVQGRWNHEVAVEGDEMIIKGQRIRTTQERDIDAI 84
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 85 DWS-GCDVVLEATGVHRKASFLNKYLEQGVKRVVVSAPVKEEGIANIVVGVNDNIFDPAVHKIVTAASCTTNCLAPVVKV 163
Cdd:NF033735 81 PWGdGVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLNIVYGVNDHLYDPARHRIVTAASCTTNCLAPVVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 164 INEKLGIENAAFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELENRINGHAVRVPLANASLTD 243
Cdd:NF033735 161 IHEKIGIKHGSITTIHDITNTQTIVDAPHKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASLTD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 244 IIFEVKQDTTAEEVNAMLKEASENELKGILGFEERPLVSIDYKGDQRSTIVDALSTMLVGKRMVKIYAWYDNEMGYATRT 323
Cdd:NF033735 241 CVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYANRM 320
|
....
gi 1330039263 324 AELV 327
Cdd:NF033735 321 VDLA 324
|
|
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
1-331 |
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: 536.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 1 MTVKVGINGFGRIGRLALRAAFDWA-EIEFVQINDVaGDTATLAHLLEFDSVQGRWNHEVAVEGDEMIIKGQRIRTTQER 79
Cdd:COG0057 1 MTIRVAINGFGRIGRLVLRALLERGpDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 80 DIDAIDWS--GCDVVLEATGVHRKASFLNKYLEQGVKRVVVSAPVKEEgIANIVVGVNDNIFDPAvHKIVTAASCTTNCL 157
Cdd:COG0057 80 DPAELPWGelGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGD-DPTIVYGVNHDDYDAD-HRIISNASCTTNCL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 158 APVVKVINEKLGIENAAFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELENRINGHAVRVPLA 237
Cdd:COG0057 158 APVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 238 NASLTDIIFEVKQDTTAEEVNAMLKEASENELKGILGFEERPLVSIDYKGDQRSTIVDALSTMLVGKRMVKIYAWYDNEM 317
Cdd:COG0057 238 NVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEW 317
|
330
....*....|....
gi 1330039263 318 GYATRTAELVRTVG 331
Cdd:COG0057 318 GYSNRMVDLAEYMA 331
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
4-322 |
1.24e-146 |
|
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: 415.91 E-value: 1.24e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 4 KVGINGFGRIGRLALRAAF--DWAEIEFVQINDVaGDTATLAHLLEFDSVQGRWNHEVAVEGDEMIIKGQ-RIRTTQERD 80
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILekPGNDLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKeVISVFSERD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 81 IDAIDWS--GCDVVLEATGVHRKASFLNKYLEQGVKRVVVSAPVKEEGIaNIVVGVNDNIFDPAvHKIVTAASCTTNCLA 158
Cdd:TIGR01534 80 PSDLPWKalGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDVK-TIVYGVNHDEYDGE-ERIISNASCTTNCLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 159 PVVKVINEKLGIENAAFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELENRINGHAVRVPLAN 238
Cdd:TIGR01534 158 PLAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 239 ASLTDIIFEVKQDTTAEEVNAMLKEASENELKGILGFEERPLVSIDYKGDQRSTIVDALSTML--VGKRMVKIYAWYDNE 316
Cdd:TIGR01534 238 VSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNE 317
|
....*.
gi 1330039263 317 MGYATR 322
Cdd:TIGR01534 318 WGYSNR 323
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-331 |
8.99e-134 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 384.09 E-value: 8.99e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 1 MTVKVGINGFGRIGRLALRAAFDWAEIEFVQINdVAGDTATLAHLLEFDSVQGRWNHEVAVEGDEMIIKGQRIRTTQERD 80
Cdd:PRK07729 1 MKTKVAINGFGRIGRMVFRKAIKESAFEIVAIN-ASYPSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 81 IDAIDWS--GCDVVLEATGVHRKASFLNKYLEQGVKRVVVSAPVKEEGIAnIVVGVNDNIFDPAVHKIVTAASCTTNCLA 158
Cdd:PRK07729 80 PKELPWTdlGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVT-IVVGVNEDQLDIEKHTIISNASCTTNCLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 159 PVVKVINEKLGIENAAFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELENRINGHAVRVPLAN 238
Cdd:PRK07729 159 PVVKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 239 ASLTDIIFEVKQDTTAEEVNAMLKEASENELKGILGFEERPLVSIDYKGDQRSTIVDALSTMLVGKRMVKIYAWYDNEMG 318
Cdd:PRK07729 239 VSLVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEWG 318
|
330
....*....|...
gi 1330039263 319 YATRTAELVRTVG 331
Cdd:PRK07729 319 YSCRVVDLVTLVA 331
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
2-330 |
1.18e-109 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 322.63 E-value: 1.18e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 2 TVKVGINGFGRIGRLALRAAF--DWAEIEFVQINDVAgDTATLAHLLEFDSVQGRWNHEVAVEGDEMIIKGQRIRTTQER 79
Cdd:PRK07403 1 MIRVAINGFGRIGRNFLRCWLgrENSQLELVAINDTS-DPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 80 DIDAIDWS--GCDVVLEATGVHRKASFLNKYLEQGVKRVVVSAPVKEEGIANIVVGVNDNIFDPAVHKIVTAASCTTNCL 157
Cdd:PRK07403 80 NPLNLPWKewGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPGKGEDIGTYVVGVNHHEYDHEDHNIISNASCTTNCL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 158 APVVKVINEKLGIENAAFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELENRINGHAVRVPLA 237
Cdd:PRK07403 160 APIAKVLHDNFGIIKGTMTTTHSYTGDQRILDASHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 238 NASLTDIIFEVKQDTTAEEVNAMLKEASENELKGILGFEERPLVSIDYKGDQRSTIVDALSTMLVGKRMVKIYAWYDNEM 317
Cdd:PRK07403 240 NVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYDNEW 319
|
330
....*....|...
gi 1330039263 318 GYATRTAELVRTV 330
Cdd:PRK07403 320 GYSQRVVDLAELV 332
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
152-316 |
2.87e-97 |
|
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: 284.73 E-value: 2.87e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 152 CTTNCLAPVVKVINEKLGIENAAFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELENRINGHA 231
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 232 VRVPLANASLTDIIFEVKQDTTAEEVNAMLKEASENELKGILGFEERPLVSIDYKGDQRSTIVDALSTMLVGKRMVKIYA 311
Cdd:cd18126 81 FRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVVA 160
|
....*
gi 1330039263 312 WYDNE 316
Cdd:cd18126 161 WYDNE 165
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
3-330 |
2.12e-96 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 292.57 E-value: 2.12e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 3 VKVGINGFGRIGRLALRAAFDWAE--IEFVQINDvAGDTATLAHLLEFDSVQGRWNHEVAVEGDEMI-IKGQRIRTTQER 79
Cdd:PLN02237 76 LKVAINGFGRIGRNFLRCWHGRKDspLDVVVVND-SGGVKNASHLLKYDSMLGTFKADVKIVDDETIsVDGKPIKVVSNR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 80 DIDAIDWS--GCDVVLEATGVHRKASFLNKYLEQGVKRVVVSAPVKEEGIANIVVGVNDNIFDPAVHKIVTAASCTTNCL 157
Cdd:PLN02237 155 DPLKLPWAelGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAKGADIPTYVVGVNEDDYDHEVANIVSNASCTTNCL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 158 APVVKVINEKLGIENAAFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELENRINGHAVRVPLA 237
Cdd:PLN02237 235 APFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 238 NASLTDIIFEV-KQDTTAEEVNAMLKEASENELKGILGFEERPLVSIDYKGDQRSTIVDALSTMLVGKRMVKIYAWYDNE 316
Cdd:PLN02237 315 NVSVVDLVVNVeKKGITAEDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVAWYDNE 394
|
330
....*....|....
gi 1330039263 317 MGYATRTAELVRTV 330
Cdd:PLN02237 395 WGYSQRVVDLAHLV 408
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
2-322 |
3.60e-96 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 288.11 E-value: 3.60e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 2 TVKVGINGFGRIGRLALRAAFD---WAEIEFVQINDVAgDTATLAHLLEFDSVQGRWNHEVAVEGDEMIIKGQRIRTTQE 78
Cdd:PRK13535 1 TIRVAINGFGRIGRNVLRALYEsgrRAEITVVAINELA-DAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 79 RDIDAIDWS--GCDVVLEATGVHRKASFLNKYLEQGVKRVVVSAPVKEEGIANIVVGVNDNIFDpAVHKIVTAASCTTNC 156
Cdd:PRK13535 80 RDIASLPWRelGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSNDLDATVVYGVNHDQLR-AEHRIVSNASCTTNC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 157 LAPVVKVINEKLGIENAAFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELENRINGHAVRVPL 236
Cdd:PRK13535 159 IIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 237 ANASLTDIIFEVKQDTTAEEVNAMLKEASENELKGILGFEERPLVSIDYKGDQRSTIVDALSTMLVGKRMVKIYAWYDNE 316
Cdd:PRK13535 239 INVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNE 318
|
....*.
gi 1330039263 317 MGYATR 322
Cdd:PRK13535 319 WGFANR 324
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
3-330 |
3.18e-95 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 287.98 E-value: 3.18e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 3 VKVGINGFGRIGRLALRAafdW-----AEIEFVQINDVAGdTATLAHLLEFDSVQGRWNHEVAVEGDEMI-IKGQRIRTT 76
Cdd:PLN03096 61 IKVAINGFGRIGRNFLRC---WhgrkdSPLDVVAINDTGG-VKQASHLLKYDSTLGTFDADVKPVGDDAIsVDGKVIKVV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 77 QERDIDAIDWS--GCDVVLEATGVHRKASFLNKYLEQGVKRVVVSAPVKEEgIANIVVGVNDNIFDPAvHKIVTAASCTT 154
Cdd:PLN03096 137 SDRNPLNLPWGelGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKGD-IPTYVVGVNADDYKHS-DPIISNASCTT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 155 NCLAPVVKVINEKLGIENAAFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELENRINGHAVRV 234
Cdd:PLN03096 215 NCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 235 PLANASLTDIIFEVKQDTTAEEVNAMLKEASENELKGILGFEERPLVSIDYKGDQRSTIVDALSTMLVGKRMVKIYAWYD 314
Cdd:PLN03096 295 PTPNVSVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAWYD 374
|
330
....*....|....*.
gi 1330039263 315 NEMGYATRTAELVRTV 330
Cdd:PLN03096 375 NEWGYSQRVVDLADIV 390
|
|
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
3-327 |
5.38e-94 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 285.60 E-value: 5.38e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 3 VKVGINGFGRIGRLALRAAFDWAEIEFVQINDVAGDTATLAHLLEFDSVQGRWNHEVAVEGDEMI-IKGQRIRTTQERDI 81
Cdd:PLN02272 86 TKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVVDDSTLeINGKQIKVTSKRDP 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 82 DAIDWS--GCDVVLEATGVHRKASFLNKYLEQGVKRVVVSAPVKEEGIanIVVGVNDNIFDPAVHkIVTAASCTTNCLAP 159
Cdd:PLN02272 166 AEIPWGdfGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPM--FVVGVNEKTYKPNMN-IVSNASCTTNCLAP 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 160 VVKVINEKLGIENAAFTTIHDLTNTQTILDAPH-KDLRRARACGMSLIPTTTGSAKAIVEIFPELENRINGHAVRVPLAN 238
Cdd:PLN02272 243 LAKVVHEEFGILEGLMTTVHATTATQKTVDGPSmKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPN 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 239 ASLTDIIFEVKQDTTAEEVNAMLKEASENELKGILGFEERPLVSIDYKGDQRSTIVDALSTMLVGKRMVKIYAWYDNEMG 318
Cdd:PLN02272 323 VSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWG 402
|
....*....
gi 1330039263 319 YATRTAELV 327
Cdd:PLN02272 403 YSNRVLDLI 411
|
|
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-326 |
3.35e-88 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 267.86 E-value: 3.35e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 1 MTVKVGINGFGRIGRLALRAAFDWAEIEFVQINDVAGDTATLAHLLEFDSVQGRWNHEVAVEGDEMIIKGQRIRTTQERD 80
Cdd:PTZ00023 1 MVVKLGINGFGRIGRLVFRAALEREDVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 81 IDAIDW--SGCDVVLEATGVHRKASFLNKYLEQGVKRVVVSAPVKEEgIANIVVGVNDNIFDPAVhKIVTAASCTTNCLA 158
Cdd:PTZ00023 81 PAAIPWgkNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKDD-TPIYVMGVNHTQYDKSQ-RIVSNASCTTNCLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 159 PVVKVINEKLGIENAAFTTIHDLTNTQTILDAPH---KDLRRARACGMSLIPTTTGSAKAIVEIFPELENRINGHAVRVP 235
Cdd:PTZ00023 159 PLAKVVNDKFGIVEGLMTTVHASTANQLTVDGPSkggKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 236 LANASLTDIIFEVKQDTTAEEVNAMLKEASENELKGILGFEERPLVSIDYKGDQRSTIVDALSTMLVGKRMVKIYAWYDN 315
Cdd:PTZ00023 239 VPDVSVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDN 318
|
330
....*....|.
gi 1330039263 316 EMGYATRTAEL 326
Cdd:PTZ00023 319 EWGYSNRLLDL 329
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
1-328 |
3.75e-88 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 268.85 E-value: 3.75e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 1 MTVKVGINGFGRIGRLALRAAFDWA----EIEFVQINDVAGDTATLAHLLEFDSVQGRWNHEVAV--------EGDEMII 68
Cdd:PTZ00434 2 APIKVGINGFGRIGRMVFQAICDQGligtEIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVETtksspsvkTDDVLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 69 KGQRIRTTQ-ERDIDAIDWS--GCDVVLEATGVHRKASFLNKYLEQGVKRVVVSAPVkEEGIANIVVGVNDNIFDPAVHK 145
Cdd:PTZ00434 82 NGHRIKCVKaQRNPADLPWGklGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPA-SGGAKTIVMGVNQHEYSPTEHH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 146 IVTAASCTTNCLAPVVKVI-NEKLGIENAAFTTIHDLTNTQTILDAPH-KDLRRARACGMSLIPTTTGSAKAIVEIFPEL 223
Cdd:PTZ00434 161 VVSNASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSvKDWRGGRAAAVNIIPSTTGAAKAVGMVIPST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 224 ENRINGHAVRVPLANASLTDIIFEVKQDTTAEEVNAMLKEASENELKGILGFEERPLVSIDYKGDQRSTIVDALSTM--- 300
Cdd:PTZ00434 241 KGKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKATLqnn 320
|
330 340
....*....|....*....|....*....
gi 1330039263 301 LVG-KRMVKIYAWYDNEMGYATRTAELVR 328
Cdd:PTZ00434 321 LPGeRRFFKIVSWYDNEWGYSHRVVDLVR 349
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
1-327 |
3.50e-83 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 255.04 E-value: 3.50e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 1 MTVKVGINGFGRIGRLALRAAFDWAEIEFVQINDVAgDTATLAHLLEFDSVQGRWNHEVAVEGDEMIIKGQRIRTTQERD 80
Cdd:PRK15425 1 MTIKVGINGFGRIGRIVFRAAQKRSDIEIVAINDLL-DADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 81 IDAIDWS--GCDVVLEATGVHRKASFLNKYLEQGVKRVVVSAPVKEEgIANIVVGVNDNIFdpAVHKIVTAASCTTNCLA 158
Cdd:PRK15425 80 PANLKWDevGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDN-TPMFVKGANFDKY--AGQDIVSNASCTTNCLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 159 PVVKVINEKLGIENAAFTTIHDLTNTQTILDAP-HKDLRRARACGMSLIPTTTGSAKAIVEIFPELENRINGHAVRVPLA 237
Cdd:PRK15425 157 PLAKVINDNFGIIEGLMTTVHATTATQKTVDGPsHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 238 NASLTDIIFEVKQDTTAEEVNAMLKEASENELKGILGFEERPLVSIDYKGDQRSTIVDALSTMLVGKRMVKIYAWYDNEM 317
Cdd:PRK15425 237 NVSVVDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNET 316
|
330
....*....|
gi 1330039263 318 GYATRTAELV 327
Cdd:PRK15425 317 GYSNKVLDLI 326
|
|
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
3-327 |
1.82e-80 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 248.48 E-value: 1.82e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 3 VKVGINGFGRIGRLALRAAFDWAEIEFVQINDVAGDTATLAHLLEFDSVQGRWNH-EVAVEGDEMIIKGQR-IRTTQERD 80
Cdd:PLN02358 6 IRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKHhELKVKDDKTLLFGEKpVTVFGIRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 81 IDAIDWS--GCDVVLEATGVHRKASFLNKYLEQGVKRVVVSAPVKEEGIanIVVGVNDNIFDPAVhKIVTAASCTTNCLA 158
Cdd:PLN02358 86 PEDIPWGeaGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPM--FVVGVNEHEYKSDL-DIVSNASCTTNCLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 159 PVVKVINEKLGIENAAFTTIHDLTNTQTILDAPH-KDLRRARACGMSLIPTTTGSAKAIVEIFPELENRINGHAVRVPLA 237
Cdd:PLN02358 163 PLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSmKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 238 NASLTDIIFEVKQDTTAEEVNAMLKEASENELKGILGFEERPLVSIDYKGDQRSTIVDALSTMLVGKRMVKIYAWYDNEM 317
Cdd:PLN02358 243 DVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEW 322
|
330
....*....|
gi 1330039263 318 GYATRTAELV 327
Cdd:PLN02358 323 GYSSRVVDLI 332
|
|
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
9-330 |
8.46e-71 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 227.50 E-value: 8.46e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 9 GFGRIGRL---------------ALRAafdwaeieFVQINDVAGDTATLAHLLEFDSVQGRWNHEVAVEGDE--MIIKGQ 71
Cdd:PRK08289 134 GFGRIGRLlarlliektgggnglRLRA--------IVVRKGSEGDLEKRASLLRRDSVHGPFNGTITVDEENnaIIANGN 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 72 RIRTTQERDIDAIDWS--GCD--VVLEATGVHRKASFLNKYLE-QGVKRVVVSAPVKEEgIANIVVGVNDNIFDPAvHKI 146
Cdd:PRK08289 206 YIQVIYANSPEEVDYTayGINnaLVVDNTGKWRDEEGLSQHLKsKGVAKVLLTAPGKGD-IKNIVHGVNHSDITDE-DKI 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 147 VTAASCTTNCLAPVVKVINEKLGIENAAFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELENR 226
Cdd:PRK08289 284 VSAASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKGDRRGRSAPLNMVITETGAAKAVAKALPELAGK 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 227 INGHAVRVPLANASLTDIIFEVKQDTTAEEVNAMLKEAS-ENELKGILGFEERP-LVSIDYKGDQRSTIVDALSTMLVGK 304
Cdd:PRK08289 364 LTGNAIRVPTPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQIDYTDSTeVVSSDFVGSRHAGVVDSQATIVNGN 443
|
330 340
....*....|....*....|....*.
gi 1330039263 305 RMVkIYAWYDNEMGYatrTAELVRTV 330
Cdd:PRK08289 444 RAV-LYVWYDNEFGY---SCQVVRVM 465
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
157-313 |
2.10e-70 |
|
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: 215.92 E-value: 2.10e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 157 LAPVVKVINEKLGIENAAFTTIHDLTNTQTILDAPH-KDLRRARACGMSLIPTTTGSAKAIVEIFPELENRINGHAVRVP 235
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHhKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330039263 236 LANASLTDIIFEVKQDTTAEEVNAMLKEASENELKGILGFEERPLVSIDYKGDQRSTIVDALSTMLVGKRMVKIYAWY 313
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-152 |
3.09e-63 |
|
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: 197.39 E-value: 3.09e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 3 VKVGINGFGRIGRLALRAAFDWAEIEFVQINDvAGDTATLAHLLEFDSVQGRWNHEVAVEGDEMIIKGQRIRTTQERDID 82
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAIND-LTDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1330039263 83 AIDWS--GCDVVLEATGVHRKASFLNKYLEQGVKRVVVSAPVKEEgIANIVVGVNDNIFDPAvHKIVTAASC 152
Cdd:smart00846 80 NLPWGelGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDA-DPTFVYGVNHDEYDGE-DHIISNASC 149
|
|
| GAPDH_I_N |
cd05214 |
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
3-151 |
7.43e-63 |
|
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: 196.85 E-value: 7.43e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 3 VKVGINGFGRIGRLALRAAFDWAEIEFVQINDVaGDTATLAHLLEFDSVQGRWNHEVAVEGDEMIIKGQRIRTTQERDID 82
Cdd:cd05214 1 IKVGINGFGRIGRLVFRAALERDDIEVVAINDL-TDDETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1330039263 83 AIDWS--GCDVVLEATGVHRKASFLNKYLEQGVKRVVVSAPVKEEgIANIVVGVNDNIFDPAvHKIVTAAS 151
Cdd:cd05214 80 ELPWGelGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDD-DPTIVMGVNHDKYDAD-DKIISNAS 148
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
152-316 |
7.39e-62 |
|
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: 194.56 E-value: 7.39e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 152 CTTNCLAPVVKVINEKLGIENAAFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELENRINGHA 231
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 232 VRVPLANASLTDIIFEVKQDTTAEEVNAMLKEASENELKGILGFEERPLVSIDYKGDQRSTIVDALSTMLVGKRMVKIYA 311
Cdd:cd23937 81 VRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLLV 160
|
....*
gi 1330039263 312 WYDNE 316
Cdd:cd23937 161 WCDNE 165
|
|
| Gp_dh_N |
pfam00044 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-98 |
4.36e-43 |
|
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. N-terminal domain is a Rossmann NAD(P) binding fold.
Pssm-ID: 459648 [Multi-domain] Cd Length: 101 Bit Score: 144.17 E-value: 4.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 3 VKVGINGFGRIGRLALRAAFDWAEIEFVQINDVaGDTATLAHLLEFDSVQGRWNHEVAVEGDEMIIKGQRIRTTQERDID 82
Cdd:pfam00044 1 VKVGINGFGRIGRLVLRAALERPDIEVVAINDL-TDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPA 79
|
90
....*....|....*...
gi 1330039263 83 AIDWS--GCDVVLEATGV 98
Cdd:pfam00044 80 ELPWGdlGVDVVIESTGV 97
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
152-316 |
3.74e-42 |
|
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: 143.91 E-value: 3.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 152 CTTNCLAPVVKVINEKLGIENAAFTTIHDLTNTQTILDAP-HKDLRRARACGMSLIPTTTGSAKAIVEIFPELENRINGH 230
Cdd:cd18123 1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPsGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 231 AVRVPLANASLTDIIFEVKQDTTAEEVNAMLKEASENelKGILGFEERPLVSIDYKGDQRSTIVDALSTMLVGKRMVKIY 310
Cdd:cd18123 81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLM 158
|
....*.
gi 1330039263 311 AWYDNE 316
Cdd:cd18123 159 QWYDNE 164
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-330 |
1.55e-39 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 142.32 E-value: 1.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 1 MTVKVGINGFGRIGRLALRAAFDWAEIEFVQINDVAGDTATLAHLLEFDS-VQGRWNHEVAVEGDEMIIKG-QRIRTTQE 78
Cdd:PTZ00353 1 LPITVGINGFGPVGKAVLFASLTDPLVTVVAVNDASVSIAYIAYVLEQESpLSAPDGASIRVVGEQIVLNGtQKIRVSAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 79 RDIDAIDWS--GCDVVLEATGVHRKASFLNKYLEQGVKRVVVSApvKEEGIANIVVGVNDNIFDpAVHKIVTAASCTTNC 156
Cdd:PTZ00353 81 HDLVEIAWRdyGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAG--QSADAPTVMAGSNDERLS-ASLPVCCAGAPIAVA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 157 LAPVVKVINEKLGIENAAFTTIHDLTNTQTIL--DAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELENRINGHAVRV 234
Cdd:PTZ00353 158 LAPVIRALHEVYGVEECSYTAIHGMQPQEPIAarSKNSQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 235 PLANASLTDIIFEVKQDTTAEEVNAMLKEASENELKGILGFEERPLVSIDYKGDQRSTIVDALSTMLVGKRMVKIYAWYD 314
Cdd:PTZ00353 238 PVKKGCAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCIPNGKLCYDATSSSSSREGEVHKMVLWFD 317
|
330
....*....|....*.
gi 1330039263 315 NEMGYATRTAELVRTV 330
Cdd:PTZ00353 318 VECYYAARLLSLVKQL 333
|
|
| GAPDH_N_E4PDH |
cd17892 |
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
3-151 |
1.77e-38 |
|
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: 134.32 E-value: 1.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 3 VKVGINGFGRIGRLALRAAFD---WAEIEFVQINDVAgDTATLAHLLEFDSVQGRWNHEVAVEGDEMIIKGQRIRTTQER 79
Cdd:cd17892 1 YRVAINGYGRIGRNVLRALYEsgrRAEFQVVAINELA-DAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEP 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1330039263 80 DIDAIDWS--GCDVVLEATGVHRKASFLNKYLEQGVKRVVVSAPVKEEGIANIVVGVNDNIFDPAvHKIVTAAS 151
Cdd:cd17892 80 DPENLPWRelGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASNDVDATIVYGINQDLLRAE-HRIVSNAS 152
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
152-316 |
2.55e-21 |
|
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: 89.12 E-value: 2.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 152 CTTNCLAPVVKVINEKLGIENAAFTTIHDLTNTQTILDAPHkDLRRARACGMSLIPTTTGSAKAIVEIFPELENRIN--G 229
Cdd:cd18122 1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPI-LKSEVRAIIPNIPKNETKHAPETGKVLGEIGKPIKvdG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 230 HAVRVPLANASLTDIIFEVKQDTTAEEVNAMLKEASENELKGILGFEERPLVSIDYKGDQRSTIVDALSTMLVGKRMVKI 309
Cdd:cd18122 80 IAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLKV 159
|
....*..
gi 1330039263 310 YAWYDNE 316
Cdd:cd18122 160 FSAVDNE 166
|
|
| Asd |
COG0136 |
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ... |
63-264 |
6.53e-04 |
|
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; Aspartate-semialdehyde dehydrogenase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439906 [Multi-domain] Cd Length: 333 Bit Score: 41.17 E-value: 6.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 63 GDEMIIKGQRIRTtqeRDIDAIDWSGCDVVLEATGvhrkASFLNKYLEQGVKR--VVV---SAPVKEEGIANIVVGVN-D 136
Cdd:COG0136 40 GKTVSFGGKELTV---EDATDFDFSGVDIALFSAG----GSVSKEYAPKAAAAgaVVIdnsSAFRMDPDVPLVVPEVNpE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330039263 137 NIFDPAVHKIVTAASCTTNCLAPVVKVINEKLGIENAAFTT-----------IHDLTN-TQTILDAPHKDLRR-ARACGM 203
Cdd:COG0136 113 ALADHLPKGIIANPNCSTIQMLVALKPLHDAAGIKRVVVSTyqavsgagaaaMDELAEqTAALLNGEEIEPEVfPHPIAF 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330039263 204 SLIP-----TTTGSA----KAIVE---IF--PELenRINGHAVRVPLANA---SLTdiiFEVKQDTTAEEVNAMLKEA 264
Cdd:COG0136 193 NLIPqidvfLENGYTkeemKMVNEtrkILgdPDI--PVSATCVRVPVFRGhseAVN---IEFERPVSLEEARELLAAA 265
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| GAPDH-like_N |
cd05192 |
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ... |
3-34 |
9.01e-04 |
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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: 38.49 E-value: 9.01e-04
10 20 30
....*....|....*....|....*....|..
gi 1330039263 3 VKVGINGFGRIGRLALRAAFDWAEIEFVQIND 34
Cdd:cd05192 1 IRVAINGFGRIGRIVFRAIADQDDLDVVAIND 32
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