|
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: 719.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 1 MTIKVGINGFGRIGRLALRAAFDWEELEFVLINDVAGDTATLAHLLEFDSVQGRWHHEVAAEGDEMIINGQRIKTTQERD 80
Cdd:PRK08955 1 MTIKVGINGFGRIGRLALRAAWDWPELEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 81 IDAIDWSGCDVVIEATGVHRKTQFLNKYLEQGVKRVVVSAPVKEDGIANIVVGVNDEIFDPAIHKIVTAASCTTNCIAPV 160
Cdd:PRK08955 81 IADTDWSGCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLNIVMGVNDHLFDPAIHPIVTAASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 161 VKVIHEKLGIEQSSFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELEGKINGHAVRVPLANAS 240
Cdd:PRK08955 161 VKVIHEKLGIKHGSMTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLANAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 241 LTDIIFDVSRDTTAEEVNALLKEASEGELKGILGFEARPLVSIDYKGDQRSTIVDALSTMVVGGRMVKIYAWYDNEMGYA 320
Cdd:PRK08955 241 LTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNEWGYA 320
|
330
....*....|...
gi 2327038646 321 TRTAELVRKVGLA 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: 638.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 5 VGINGFGRIGRLALRAAFDWEELEFVLINDVAGDTATLAHLLEFDSVQGRWHHEVAAEGDEMIINGQRIKTTQERDIDAI 84
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 85 DWS-GCDVVIEATGVHRKTQFLNKYLEQGVKRVVVSAPVKEDGIANIVVGVNDEIFDPAIHKIVTAASCTTNCIAPVVKV 163
Cdd:NF033735 81 PWGdGVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLNIVYGVNDHLYDPARHRIVTAASCTTNCLAPVVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 164 IHEKLGIEQSSFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELEGKINGHAVRVPLANASLTD 243
Cdd:NF033735 161 IHEKIGIKHGSITTIHDITNTQTIVDAPHKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASLTD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 244 IIFDVSRDTTAEEVNALLKEASEGELKGILGFEARPLVSIDYKGDQRSTIVDALSTMVVGGRMVKIYAWYDNEMGYATRT 323
Cdd:NF033735 241 CVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYANRM 320
|
....
gi 2327038646 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: 550.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 1 MTIKVGINGFGRIGRLALRAAFDW-EELEFVLINDVaGDTATLAHLLEFDSVQGRWHHEVAAEGDEMIINGQRIKTTQER 79
Cdd:COG0057 1 MTIRVAINGFGRIGRLVLRALLERgPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 80 DIDAIDWS--GCDVVIEATGVHRKTQFLNKYLEQGVKRVVVSAPVKEDgIANIVVGVNDEIFDPAiHKIVTAASCTTNCI 157
Cdd:COG0057 80 DPAELPWGelGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGD-DPTIVYGVNHDDYDAD-HRIISNASCTTNCL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 158 APVVKVIHEKLGIEQSSFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELEGKINGHAVRVPLA 237
Cdd:COG0057 158 APVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 238 NASLTDIIFDVSRDTTAEEVNALLKEASEGELKGILGFEARPLVSIDYKGDQRSTIVDALSTMVVGGRMVKIYAWYDNEM 317
Cdd:COG0057 238 NVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEW 317
|
330
....*....|....
gi 2327038646 318 GYATRTAELVRKVG 331
Cdd:COG0057 318 GYSNRMVDLAEYMA 331
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
4-322 |
7.03e-151 |
|
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: 426.69 E-value: 7.03e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 4 KVGINGFGRIGRLALRAAF--DWEELEFVLINDVaGDTATLAHLLEFDSVQGRWHHEVAAEGDEMIINGQ-RIKTTQERD 80
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILekPGNDLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKeVISVFSERD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 81 IDAIDWS--GCDVVIEATGVHRKTQFLNKYLEQGVKRVVVSAPVKEDGIaNIVVGVNDEIFDPAiHKIVTAASCTTNCIA 158
Cdd:TIGR01534 80 PSDLPWKalGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDVK-TIVYGVNHDEYDGE-ERIISNASCTTNCLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 159 PVVKVIHEKLGIEQSSFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELEGKINGHAVRVPLAN 238
Cdd:TIGR01534 158 PLAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 239 ASLTDIIFDVSRDTTAEEVNALLKEASEGELKGILGFEARPLVSIDYKGDQRSTIVDALSTMV--VGGRMVKIYAWYDNE 316
Cdd:TIGR01534 238 VSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNE 317
|
....*.
gi 2327038646 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 |
2.88e-100 |
|
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: 292.44 E-value: 2.88e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 152 CTTNCIAPVVKVIHEKLGIEQSSFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELEGKINGHA 231
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 232 VRVPLANASLTDIIFDVSRDTTAEEVNALLKEASEGELKGILGFEARPLVSIDYKGDQRSTIVDALSTMVVGGRMVKIYA 311
Cdd:cd18126 81 FRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVVA 160
|
....*
gi 2327038646 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 |
2.93e-72 |
|
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: 220.93 E-value: 2.93e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 157 IAPVVKVIHEKLGIEQSSFTTIHDLTNTQTILDAPH-KDLRRARACGMSLIPTTTGSAKAIVEIFPELEGKINGHAVRVP 235
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHhKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2327038646 236 LANASLTDIIFDVSRDTTAEEVNALLKEASEGELKGILGFEARPLVSIDYKGDQRSTIVDALSTMVVGGRMVKIYAWY 313
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-152 |
8.99e-65 |
|
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. N-terminal domain is a Rossmann NAD(P) binding fold.
Pssm-ID: 214851 [Multi-domain] Cd Length: 149 Bit Score: 201.24 E-value: 8.99e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 3 IKVGINGFGRIGRLALRAAFDWEELEFVLINDvAGDTATLAHLLEFDSVQGRWHHEVAAEGDEMIINGQRIKTTQERDID 82
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAIND-LTDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2327038646 83 AIDWS--GCDVVIEATGVHRKTQFLNKYLEQGVKRVVVSAPVKEDgIANIVVGVNDEIFDPAiHKIVTAASC 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: 719.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 1 MTIKVGINGFGRIGRLALRAAFDWEELEFVLINDVAGDTATLAHLLEFDSVQGRWHHEVAAEGDEMIINGQRIKTTQERD 80
Cdd:PRK08955 1 MTIKVGINGFGRIGRLALRAAWDWPELEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 81 IDAIDWSGCDVVIEATGVHRKTQFLNKYLEQGVKRVVVSAPVKEDGIANIVVGVNDEIFDPAIHKIVTAASCTTNCIAPV 160
Cdd:PRK08955 81 IADTDWSGCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLNIVMGVNDHLFDPAIHPIVTAASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 161 VKVIHEKLGIEQSSFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELEGKINGHAVRVPLANAS 240
Cdd:PRK08955 161 VKVIHEKLGIKHGSMTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLANAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 241 LTDIIFDVSRDTTAEEVNALLKEASEGELKGILGFEARPLVSIDYKGDQRSTIVDALSTMVVGGRMVKIYAWYDNEMGYA 320
Cdd:PRK08955 241 LTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNEWGYA 320
|
330
....*....|...
gi 2327038646 321 TRTAELVRKVGLA 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: 638.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 5 VGINGFGRIGRLALRAAFDWEELEFVLINDVAGDTATLAHLLEFDSVQGRWHHEVAAEGDEMIINGQRIKTTQERDIDAI 84
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 85 DWS-GCDVVIEATGVHRKTQFLNKYLEQGVKRVVVSAPVKEDGIANIVVGVNDEIFDPAIHKIVTAASCTTNCIAPVVKV 163
Cdd:NF033735 81 PWGdGVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLNIVYGVNDHLYDPARHRIVTAASCTTNCLAPVVKV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 164 IHEKLGIEQSSFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELEGKINGHAVRVPLANASLTD 243
Cdd:NF033735 161 IHEKIGIKHGSITTIHDITNTQTIVDAPHKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASLTD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 244 IIFDVSRDTTAEEVNALLKEASEGELKGILGFEARPLVSIDYKGDQRSTIVDALSTMVVGGRMVKIYAWYDNEMGYATRT 323
Cdd:NF033735 241 CVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYANRM 320
|
....
gi 2327038646 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: 550.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 1 MTIKVGINGFGRIGRLALRAAFDW-EELEFVLINDVaGDTATLAHLLEFDSVQGRWHHEVAAEGDEMIINGQRIKTTQER 79
Cdd:COG0057 1 MTIRVAINGFGRIGRLVLRALLERgPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 80 DIDAIDWS--GCDVVIEATGVHRKTQFLNKYLEQGVKRVVVSAPVKEDgIANIVVGVNDEIFDPAiHKIVTAASCTTNCI 157
Cdd:COG0057 80 DPAELPWGelGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGD-DPTIVYGVNHDDYDAD-HRIISNASCTTNCL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 158 APVVKVIHEKLGIEQSSFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELEGKINGHAVRVPLA 237
Cdd:COG0057 158 APVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 238 NASLTDIIFDVSRDTTAEEVNALLKEASEGELKGILGFEARPLVSIDYKGDQRSTIVDALSTMVVGGRMVKIYAWYDNEM 317
Cdd:COG0057 238 NVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEW 317
|
330
....*....|....
gi 2327038646 318 GYATRTAELVRKVG 331
Cdd:COG0057 318 GYSNRMVDLAEYMA 331
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
4-322 |
7.03e-151 |
|
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: 426.69 E-value: 7.03e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 4 KVGINGFGRIGRLALRAAF--DWEELEFVLINDVaGDTATLAHLLEFDSVQGRWHHEVAAEGDEMIINGQ-RIKTTQERD 80
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILekPGNDLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKeVISVFSERD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 81 IDAIDWS--GCDVVIEATGVHRKTQFLNKYLEQGVKRVVVSAPVKEDGIaNIVVGVNDEIFDPAiHKIVTAASCTTNCIA 158
Cdd:TIGR01534 80 PSDLPWKalGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDVK-TIVYGVNHDEYDGE-ERIISNASCTTNCLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 159 PVVKVIHEKLGIEQSSFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELEGKINGHAVRVPLAN 238
Cdd:TIGR01534 158 PLAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 239 ASLTDIIFDVSRDTTAEEVNALLKEASEGELKGILGFEARPLVSIDYKGDQRSTIVDALSTMV--VGGRMVKIYAWYDNE 316
Cdd:TIGR01534 238 VSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNE 317
|
....*.
gi 2327038646 317 MGYATR 322
Cdd:TIGR01534 318 WGYSNR 323
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-331 |
1.52e-138 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 396.41 E-value: 1.52e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 1 MTIKVGINGFGRIGRLALRAAFDWEELEFVLINdVAGDTATLAHLLEFDSVQGRWHHEVAAEGDEMIINGQRIKTTQERD 80
Cdd:PRK07729 1 MKTKVAINGFGRIGRMVFRKAIKESAFEIVAIN-ASYPSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 81 IDAIDWS--GCDVVIEATGVHRKTQFLNKYLEQGVKRVVVSAPVKEDGIAnIVVGVNDEIFDPAIHKIVTAASCTTNCIA 158
Cdd:PRK07729 80 PKELPWTdlGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVT-IVVGVNEDQLDIEKHTIISNASCTTNCLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 159 PVVKVIHEKLGIEQSSFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELEGKINGHAVRVPLAN 238
Cdd:PRK07729 159 PVVKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 239 ASLTDIIFDVSRDTTAEEVNALLKEASEGELKGILGFEARPLVSIDYKGDQRSTIVDALSTMVVGGRMVKIYAWYDNEMG 318
Cdd:PRK07729 239 VSLVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEWG 318
|
330
....*....|...
gi 2327038646 319 YATRTAELVRKVG 331
Cdd:PRK07729 319 YSCRVVDLVTLVA 331
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
2-329 |
2.91e-115 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 336.88 E-value: 2.91e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 2 TIKVGINGFGRIGRLALRAAFDWE--ELEFVLINDVAgDTATLAHLLEFDSVQGRWHHEVAAEGDEMIINGQRIKTTQER 79
Cdd:PRK07403 1 MIRVAINGFGRIGRNFLRCWLGREnsQLELVAINDTS-DPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 80 DIDAIDWS--GCDVVIEATGVHRKTQFLNKYLEQGVKRVVVSAPVKEDGIANIVVGVNDEIFDPAIHKIVTAASCTTNCI 157
Cdd:PRK07403 80 NPLNLPWKewGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPGKGEDIGTYVVGVNHHEYDHEDHNIISNASCTTNCL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 158 APVVKVIHEKLGIEQSSFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELEGKINGHAVRVPLA 237
Cdd:PRK07403 160 APIAKVLHDNFGIIKGTMTTTHSYTGDQRILDASHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 238 NASLTDIIFDVSRDTTAEEVNALLKEASEGELKGILGFEARPLVSIDYKGDQRSTIVDALSTMVVGGRMVKIYAWYDNEM 317
Cdd:PRK07403 240 NVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYDNEW 319
|
330
....*....|....*
gi 2327038646 318 GYATRT---AELVRK 329
Cdd:PRK07403 320 GYSQRVvdlAELVAR 334
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
152-316 |
2.88e-100 |
|
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: 292.44 E-value: 2.88e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 152 CTTNCIAPVVKVIHEKLGIEQSSFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELEGKINGHA 231
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 232 VRVPLANASLTDIIFDVSRDTTAEEVNALLKEASEGELKGILGFEARPLVSIDYKGDQRSTIVDALSTMVVGGRMVKIYA 311
Cdd:cd18126 81 FRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVVA 160
|
....*
gi 2327038646 312 WYDNE 316
Cdd:cd18126 161 WYDNE 165
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
3-326 |
7.51e-100 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 299.92 E-value: 7.51e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 3 IKVGINGFGRIGRLALRAafdWE-----ELEFVLINDVAGdTATLAHLLEFDSVQGRWHHEVAAEGDEMI-INGQRIKTT 76
Cdd:PLN03096 61 IKVAINGFGRIGRNFLRC---WHgrkdsPLDVVAINDTGG-VKQASHLLKYDSTLGTFDADVKPVGDDAIsVDGKVIKVV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 77 QERDIDAIDWS--GCDVVIEATGVHRKTQFLNKYLEQGVKRVVVSAPVKEDgIANIVVGVNDEIFDPAiHKIVTAASCTT 154
Cdd:PLN03096 137 SDRNPLNLPWGelGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKGD-IPTYVVGVNADDYKHS-DPIISNASCTT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 155 NCIAPVVKVIHEKLGIEQSSFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELEGKINGHAVRV 234
Cdd:PLN03096 215 NCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRV 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 235 PLANASLTDIIFDVSRDTTAEEVNALLKEASEGELKGILGFEARPLVSIDYKGDQRSTIVDALSTMVVGGRMVKIYAWYD 314
Cdd:PLN03096 295 PTPNVSVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAWYD 374
|
330
....*....|..
gi 2327038646 315 NEMGYATRTAEL 326
Cdd:PLN03096 375 NEWGYSQRVVDL 386
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
3-330 |
7.70e-99 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 298.74 E-value: 7.70e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 3 IKVGINGFGRIGRLALRAafdWEE-----LEFVLINDvAGDTATLAHLLEFDSVQGRWHHEVAAEGDEMI-INGQRIKTT 76
Cdd:PLN02237 76 LKVAINGFGRIGRNFLRC---WHGrkdspLDVVVVND-SGGVKNASHLLKYDSMLGTFKADVKIVDDETIsVDGKPIKVV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 77 QERDIDAIDWS--GCDVVIEATGVHRKTQFLNKYLEQGVKRVVVSAPVKEDGIANIVVGVNDEIFDPAIHKIVTAASCTT 154
Cdd:PLN02237 152 SNRDPLKLPWAelGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAKGADIPTYVVGVNEDDYDHEVANIVSNASCTT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 155 NCIAPVVKVIHEKLGIEQSSFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELEGKINGHAVRV 234
Cdd:PLN02237 232 NCLAPFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRV 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 235 PLANASLTDIIFDVSRD-TTAEEVNALLKEASEGELKGILGFEARPLVSIDYKGDQRSTIVDALSTMVVGGRMVKIYAWY 313
Cdd:PLN02237 312 PTPNVSVVDLVVNVEKKgITAEDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVAWY 391
|
330
....*....|....*..
gi 2327038646 314 DNEMGYATRTAELVRKV 330
Cdd:PLN02237 392 DNEWGYSQRVVDLAHLV 408
|
|
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
3-332 |
8.69e-98 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 295.23 E-value: 8.69e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 3 IKVGINGFGRIGRLALRAAFDWEELEFVLINDVAGDTATLAHLLEFDSVQGRWHHEVAAEGDEMI-INGQRIKTTQERDI 81
Cdd:PLN02272 86 TKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVVDDSTLeINGKQIKVTSKRDP 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 82 DAIDWS--GCDVVIEATGVHRKTQFLNKYLEQGVKRVVVSAPVKEDGIanIVVGVNDEIFDPAIHkIVTAASCTTNCIAP 159
Cdd:PLN02272 166 AEIPWGdfGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPM--FVVGVNEKTYKPNMN-IVSNASCTTNCLAP 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 160 VVKVIHEKLGIEQSSFTTIHDLTNTQTILDAPH-KDLRRARACGMSLIPTTTGSAKAIVEIFPELEGKINGHAVRVPLAN 238
Cdd:PLN02272 243 LAKVVHEEFGILEGLMTTVHATTATQKTVDGPSmKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPN 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 239 ASLTDIIFDVSRDTTAEEVNALLKEASEGELKGILGFEARPLVSIDYKGDQRSTIVDALSTMVVGGRMVKIYAWYDNEMG 318
Cdd:PLN02272 323 VSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWG 402
|
330
....*....|....
gi 2327038646 319 YATRTAELVRKVGL 332
Cdd:PLN02272 403 YSNRVLDLIEHMAL 416
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
2-322 |
3.81e-96 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 288.11 E-value: 3.81e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 2 TIKVGINGFGRIGRLALRAAFD---WEELEFVLINDVAgDTATLAHLLEFDSVQGRWHHEVAAEGDEMIINGQRIKTTQE 78
Cdd:PRK13535 1 TIRVAINGFGRIGRNVLRALYEsgrRAEITVVAINELA-DAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 79 RDIDAIDWS--GCDVVIEATGVHRKTQFLNKYLEQGVKRVVVSAPVKEDGIANIVVGVNDEIFDPAiHKIVTAASCTTNC 156
Cdd:PRK13535 80 RDIASLPWRelGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSNDLDATVVYGVNHDQLRAE-HRIVSNASCTTNC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 157 IAPVVKVIHEKLGIEQSSFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELEGKINGHAVRVPL 236
Cdd:PRK13535 159 IIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 237 ANASLTDIIFDVSRDTTAEEVNALLKEASEGELKGILGFEARPLVSIDYKGDQRSTIVDALSTMVVGGRMVKIYAWYDNE 316
Cdd:PRK13535 239 INVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNE 318
|
....*.
gi 2327038646 317 MGYATR 322
Cdd:PRK13535 319 WGFANR 324
|
|
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-326 |
2.92e-90 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 273.25 E-value: 2.92e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 1 MTIKVGINGFGRIGRLALRAAFDWEELEFVLINDVAGDTATLAHLLEFDSVQGRWHHEVAAEGDEMIINGQRIKTTQERD 80
Cdd:PTZ00023 1 MVVKLGINGFGRIGRLVFRAALEREDVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 81 IDAIDW--SGCDVVIEATGVHRKTQFLNKYLEQGVKRVVVSAPVKEDgIANIVVGVNDEIFDPAiHKIVTAASCTTNCIA 158
Cdd:PTZ00023 81 PAAIPWgkNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKDD-TPIYVMGVNHTQYDKS-QRIVSNASCTTNCLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 159 PVVKVIHEKLGIEQSSFTTIHDLTNTQTILDAPH---KDLRRARACGMSLIPTTTGSAKAIVEIFPELEGKINGHAVRVP 235
Cdd:PTZ00023 159 PLAKVVNDKFGIVEGLMTTVHASTANQLTVDGPSkggKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 236 LANASLTDIIFDVSRDTTAEEVNALLKEASEGELKGILGFEARPLVSIDYKGDQRSTIVDALSTMVVGGRMVKIYAWYDN 315
Cdd:PTZ00023 239 VPDVSVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDN 318
|
330
....*....|.
gi 2327038646 316 EMGYATRTAEL 326
Cdd:PTZ00023 319 EWGYSNRLLDL 329
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
1-328 |
2.61e-89 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 271.54 E-value: 2.61e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 1 MTIKVGINGFGRIGRLALRAAFD----WEELEFVLINDVAGDTATLAHLLEFDSVQGRWHHEVA--------AEGDEMII 68
Cdd:PTZ00434 2 APIKVGINGFGRIGRMVFQAICDqgliGTEIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVEttksspsvKTDDVLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 69 NGQRIKTTQ-ERDIDAIDWS--GCDVVIEATGVHRKTQFLNKYLEQGVKRVVVSAPVkEDGIANIVVGVNDEIFDPAIHK 145
Cdd:PTZ00434 82 NGHRIKCVKaQRNPADLPWGklGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPA-SGGAKTIVMGVNQHEYSPTEHH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 146 IVTAASCTTNCIAPVVKVI-HEKLGIEQSSFTTIHDLTNTQTILDAPH-KDLRRARACGMSLIPTTTGSAKAIVEIFPEL 223
Cdd:PTZ00434 161 VVSNASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSvKDWRGGRAAAVNIIPSTTGAAKAVGMVIPST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 224 EGKINGHAVRVPLANASLTDIIFDVSRDTTAEEVNALLKEASEGELKGILGFEARPLVSIDYKGDQRSTIVDALSTMVVG 303
Cdd:PTZ00434 241 KGKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKATLQNN 320
|
330 340
....*....|....*....|....*....
gi 2327038646 304 ----GRMVKIYAWYDNEMGYATRTAELVR 328
Cdd:PTZ00434 321 lpgeRRFFKIVSWYDNEWGYSHRVVDLVR 349
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
1-330 |
3.02e-84 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 257.74 E-value: 3.02e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 1 MTIKVGINGFGRIGRLALRAAFDWEELEFVLINDVAgDTATLAHLLEFDSVQGRWHHEVAAEGDEMIINGQRIKTTQERD 80
Cdd:PRK15425 1 MTIKVGINGFGRIGRIVFRAAQKRSDIEIVAINDLL-DADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 81 IDAIDWS--GCDVVIEATGVHRKTQFLNKYLEQGVKRVVVSAPVKeDGIANIVVGVNDEIFdpAIHKIVTAASCTTNCIA 158
Cdd:PRK15425 80 PANLKWDevGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSK-DNTPMFVKGANFDKY--AGQDIVSNASCTTNCLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 159 PVVKVIHEKLGIEQSSFTTIHDLTNTQTILDAP-HKDLRRARACGMSLIPTTTGSAKAIVEIFPELEGKINGHAVRVPLA 237
Cdd:PRK15425 157 PLAKVINDNFGIIEGLMTTVHATTATQKTVDGPsHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 238 NASLTDIIFDVSRDTTAEEVNALLKEASEGELKGILGFEARPLVSIDYKGDQRSTIVDALSTMVVGGRMVKIYAWYDNEM 317
Cdd:PRK15425 237 NVSVVDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNET 316
|
330
....*....|...
gi 2327038646 318 GYATRTAELVRKV 330
Cdd:PRK15425 317 GYSNKVLDLIAHI 329
|
|
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
3-327 |
2.08e-80 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 248.10 E-value: 2.08e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 3 IKVGINGFGRIGRLALRAAFDWEELEFVLINDVAGDTATLAHLLEFDSVQGRW-HHEVAAEGDEMIINGQR-IKTTQERD 80
Cdd:PLN02358 6 IRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWkHHELKVKDDKTLLFGEKpVTVFGIRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 81 IDAIDWS--GCDVVIEATGVHRKTQFLNKYLEQGVKRVVVSAPVKEDGIanIVVGVNDEIFDPAIhKIVTAASCTTNCIA 158
Cdd:PLN02358 86 PEDIPWGeaGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPM--FVVGVNEHEYKSDL-DIVSNASCTTNCLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 159 PVVKVIHEKLGIEQSSFTTIHDLTNTQTILDAPH-KDLRRARACGMSLIPTTTGSAKAIVEIFPELEGKINGHAVRVPLA 237
Cdd:PLN02358 163 PLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSmKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 238 NASLTDIIFDVSRDTTAEEVNALLKEASEGELKGILGFEARPLVSIDYKGDQRSTIVDALSTMVVGGRMVKIYAWYDNEM 317
Cdd:PLN02358 243 DVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEW 322
|
330
....*....|
gi 2327038646 318 GYATRTAELV 327
Cdd:PLN02358 323 GYSSRVVDLI 332
|
|
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
9-330 |
7.78e-75 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 237.90 E-value: 7.78e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 9 GFGRIGRL---------------ALRAafdweeleFVLINDVAGDTATLAHLLEFDSVQGRWHH--EVAAEGDEMIINGQ 71
Cdd:PRK08289 134 GFGRIGRLlarlliektgggnglRLRA--------IVVRKGSEGDLEKRASLLRRDSVHGPFNGtiTVDEENNAIIANGN 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 72 RIKTTQERDIDAIDWS--GCD--VVIEATGVHRKTQFLNKYLE-QGVKRVVVSAPVKEDgIANIVVGVNDEIFDPAiHKI 146
Cdd:PRK08289 206 YIQVIYANSPEEVDYTayGINnaLVVDNTGKWRDEEGLSQHLKsKGVAKVLLTAPGKGD-IKNIVHGVNHSDITDE-DKI 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 147 VTAASCTTNCIAPVVKVIHEKLGIEQSSFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELEGK 226
Cdd:PRK08289 284 VSAASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKGDRRGRSAPLNMVITETGAAKAVAKALPELAGK 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 227 INGHAVRVPLANASLTDIIFDVSRDTTAEEVNALLKEAS-EGELKGILGFEARP-LVSIDYKGDQRSTIVDALSTMVVGG 304
Cdd:PRK08289 364 LTGNAIRVPTPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQIDYTDSTeVVSSDFVGSRHAGVVDSQATIVNGN 443
|
330 340
....*....|....*....|....*.
gi 2327038646 305 RMVkIYAWYDNEMGYATRTAELVRKV 330
Cdd:PRK08289 444 RAV-LYVWYDNEFGYSCQVVRVMEQM 468
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
157-313 |
2.93e-72 |
|
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: 220.93 E-value: 2.93e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 157 IAPVVKVIHEKLGIEQSSFTTIHDLTNTQTILDAPH-KDLRRARACGMSLIPTTTGSAKAIVEIFPELEGKINGHAVRVP 235
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHhKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2327038646 236 LANASLTDIIFDVSRDTTAEEVNALLKEASEGELKGILGFEARPLVSIDYKGDQRSTIVDALSTMVVGGRMVKIYAWY 313
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-152 |
8.99e-65 |
|
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. N-terminal domain is a Rossmann NAD(P) binding fold.
Pssm-ID: 214851 [Multi-domain] Cd Length: 149 Bit Score: 201.24 E-value: 8.99e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 3 IKVGINGFGRIGRLALRAAFDWEELEFVLINDvAGDTATLAHLLEFDSVQGRWHHEVAAEGDEMIINGQRIKTTQERDID 82
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAIND-LTDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2327038646 83 AIDWS--GCDVVIEATGVHRKTQFLNKYLEQGVKRVVVSAPVKEDgIANIVVGVNDEIFDPAiHKIVTAASC 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 |
6.15e-64 |
|
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: 199.93 E-value: 6.15e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 3 IKVGINGFGRIGRLALRAAFDWEELEFVLINDVaGDTATLAHLLEFDSVQGRWHHEVAAEGDEMIINGQRIKTTQERDID 82
Cdd:cd05214 1 IKVGINGFGRIGRLVFRAALERDDIEVVAINDL-TDDETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPA 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2327038646 83 AIDWS--GCDVVIEATGVHRKTQFLNKYLEQGVKRVVVSAPVKeDGIANIVVGVNDEIFDPAiHKIVTAAS 151
Cdd:cd05214 80 ELPWGelGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAK-DDDPTIVMGVNHDKYDAD-DKIISNAS 148
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
152-316 |
2.14e-61 |
|
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: 193.40 E-value: 2.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 152 CTTNCIAPVVKVIHEKLGIEQSSFTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELEGKINGHA 231
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 232 VRVPLANASLTDIIFDVSRDTTAEEVNALLKEASEGELKGILGFEARPLVSIDYKGDQRSTIVDALSTMVVGGRMVKIYA 311
Cdd:cd23937 81 VRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLLV 160
|
....*
gi 2327038646 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 |
4.83e-44 |
|
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: 146.48 E-value: 4.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 3 IKVGINGFGRIGRLALRAAFDWEELEFVLINDVaGDTATLAHLLEFDSVQGRWHHEVAAEGDEMIINGQRIKTTQERDID 82
Cdd:pfam00044 1 VKVGINGFGRIGRLVLRAALERPDIEVVAINDL-TDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPA 79
|
90
....*....|....*...
gi 2327038646 83 AIDWS--GCDVVIEATGV 98
Cdd:pfam00044 80 ELPWGdlGVDVVIESTGV 97
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
152-316 |
1.35e-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: 145.07 E-value: 1.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 152 CTTNCIAPVVKVIHEKLGIEQSSFTTIHDLTNTQTILDAP-HKDLRRARACGMSLIPTTTGSAKAIVEIFPELEGKINGH 230
Cdd:cd18123 1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPsGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 231 AVRVPLANASLTDIIFDVSRDTTAEEVNALLKEASEGelKGILGFEARPLVSIDYKGDQRSTIVDALSTMVVGGRMVKIY 310
Cdd:cd18123 81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLM 158
|
....*.
gi 2327038646 311 AWYDNE 316
Cdd:cd18123 159 QWYDNE 164
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-330 |
5.65e-41 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 146.17 E-value: 5.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 1 MTIKVGINGFGRIGRLALRAAFDWEELEFVLINDVAGDTATLAHLLEFDS-VQGRWHHEVAAEGDEMIING-QRIKTTQE 78
Cdd:PTZ00353 1 LPITVGINGFGPVGKAVLFASLTDPLVTVVAVNDASVSIAYIAYVLEQESpLSAPDGASIRVVGEQIVLNGtQKIRVSAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 79 RDIDAIDWS--GCDVVIEATGVHRKTQFLNKYLEQGVKRVVVSAPVKEdgIANIVVGVNDEIFDpAIHKIVTAASCTTNC 156
Cdd:PTZ00353 81 HDLVEIAWRdyGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSAD--APTVMAGSNDERLS-ASLPVCCAGAPIAVA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 157 IAPVVKVIHEKLGIEQSSFTTIHDLTNTQTIL--DAPHKDLRRARACGMSLIPTTTGSAKAIVEIFPELEGKINGHAVRV 234
Cdd:PTZ00353 158 LAPVIRALHEVYGVEECSYTAIHGMQPQEPIAarSKNSQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 235 PLANASLTDIIFDVSRDTTAEEVNALLKEASEGELKGILGFEARPLVSIDYKGDQRSTIVDALSTMVVGGRMVKIYAWYD 314
Cdd:PTZ00353 238 PVKKGCAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCIPNGKLCYDATSSSSSREGEVHKMVLWFD 317
|
330
....*....|....*.
gi 2327038646 315 NEMGYATRTAELVRKV 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 |
1.00e-40 |
|
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: 140.09 E-value: 1.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 3 IKVGINGFGRIGRLALRAAFD---WEELEFVLINDVAgDTATLAHLLEFDSVQGRWHHEVAAEGDEMIINGQRIKTTQER 79
Cdd:cd17892 1 YRVAINGYGRIGRNVLRALYEsgrRAEFQVVAINELA-DAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEP 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2327038646 80 DIDAIDWS--GCDVVIEATGVHRKTQFLNKYLEQGVKRVVVSAPVKEDGIANIVVGVNDEIFDPAiHKIVTAAS 151
Cdd:cd17892 80 DPENLPWRelGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASNDVDATIVYGINQDLLRAE-HRIVSNAS 152
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
152-316 |
5.72e-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: 87.96 E-value: 5.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 152 CTTNCIAPVVKVIHEKLGIEQSSFTTIHDLTNTQTILDAPHkDLRRARACGMSLIPTTTGSAKAIVEIFPELEGKIN--G 229
Cdd:cd18122 1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPI-LKSEVRAIIPNIPKNETKHAPETGKVLGEIGKPIKvdG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 230 HAVRVPLANASLTDIIFDVSRDTTAEEVNALLKEASEGELKGILGFEARPLVSIDYKGDQRSTIVDALSTMVVGGRMVKI 309
Cdd:cd18122 80 IAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLKV 159
|
....*..
gi 2327038646 310 YAWYDNE 316
Cdd:cd18122 160 FSAVDNE 166
|
|
| GAPDH-like_N |
cd05192 |
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ... |
3-34 |
1.65e-04 |
|
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: 40.41 E-value: 1.65e-04
10 20 30
....*....|....*....|....*....|..
gi 2327038646 3 IKVGINGFGRIGRLALRAAFDWEELEFVLIND 34
Cdd:cd05192 1 IRVAINGFGRIGRIVFRAIADQDDLDVVAIND 32
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| Asd |
COG0136 |
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ... |
63-264 |
4.00e-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: 41.56 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 63 GDEMIINGQRIKTtqeRDIDAIDWSGCDVVIEATGVHRKTQFLNKYLEQGVkrVVV---SAPVKEDGIANIVVGVN-DEI 138
Cdd:COG0136 40 GKTVSFGGKELTV---EDATDFDFSGVDIALFSAGGSVSKEYAPKAAAAGA--VVIdnsSAFRMDPDVPLVVPEVNpEAL 114
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2327038646 139 FDPAIHKIVTAASCTTNCIAPVVKVIHEKLGIEQSSFTT-----------IHDLTN-TQTILDAPHKDLRR-ARACGMSL 205
Cdd:COG0136 115 ADHLPKGIIANPNCSTIQMLVALKPLHDAAGIKRVVVSTyqavsgagaaaMDELAEqTAALLNGEEIEPEVfPHPIAFNL 194
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170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2327038646 206 IP-----TTTGSA----KAIVE---IF--PELegKINGHAVRVPLANA---SLTdIIFDvsRDTTAEEVNALLKEA 264
Cdd:COG0136 195 IPqidvfLENGYTkeemKMVNEtrkILgdPDI--PVSATCVRVPVFRGhseAVN-IEFE--RPVSLEEARELLAAA 265
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