|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
2-337 |
0e+00 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 746.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 2 TIRIAINGFGRIGRNVVRALYESGRRAEITVVAINELADAAGIAHLLKYDTSHGRFAWDVRQEREQLFVGDDAIRLLHES 81
Cdd:PRK13535 1 TIRVAINGFGRIGRNVLRALYESGRRAEITVVAINELADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 82 SLEALPWRELAVDVVLDCTGVYGSREHGEAHLQAGARKVLFSHPGGNDLDATIVFGVNHAELRTEHRIVSNASCTTNCII 161
Cdd:PRK13535 81 DIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSNDLDATVVYGVNHDQLRAEHRIVSNASCTTNCII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 162 PVIKLLDDAYGIESGTVTTIHSSMNDQQVIDSWHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVPTIN 241
Cdd:PRK13535 161 PVIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPTIN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 242 VTAIDLSVTVKKPVKASEVNQLLQKAALGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNEWG 321
Cdd:PRK13535 241 VTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNEWG 320
|
330
....*....|....*.
gi 2022055743 322 FANRMLDTTLAMAAQG 337
Cdd:PRK13535 321 FANRMLDTTLAMAAAG 336
|
|
| E4PD_g-proteo |
TIGR01532 |
erythrose-4-phosphate dehydrogenase; This model represents the small clade of dehydrogenases ... |
4-328 |
0e+00 |
|
erythrose-4-phosphate dehydrogenase; This model represents the small clade of dehydrogenases in gamma-proteobacteria 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. This enzyme activity appears to have evolved from glyceraldehyde-3-phosphate dehydrogenase, whose substrate differs only in the lack of one carbon relative to E4P. Accordingly, this model is very close to the corresponding models for GAPDH, and those sequences which hit above trusted here invariably hit between trusted and noise to the GAPDH model (TIGR01534). Similarly, it may be found that there are species outside of the gamma proteobacteria which synthesize pyridoxine and have more than one aparrent GAPDH gene of which one may have E4PD activity - this may necessitate a readjustment of these models. Alternatively, some of the GAPDH enzymes may prove to be bifunctional in certain species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
Pssm-ID: 130595 Cd Length: 325 Bit Score: 625.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 4 RIAINGFGRIGRNVVRALYESGRRAEITVVAINELADAAGIAHLLKYDTSHGRFAWDVRQEREQLFVGDDAIRLLHESSL 83
Cdd:TIGR01532 1 RVAINGFGRIGRNVLRALYESGRRAEITVVAINELADAAGMAHLLKYDTSHGRFAWEVRQDRDQLFVGDDAIRVLHERSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 84 EALPWRELAVDVVLDCTGVYGSREHGEAHLQAGARKVLFSHPGGNDLDATIVFGVNHAELRTEHRIVSNASCTTNCIIPV 163
Cdd:TIGR01532 81 QSLPWRELGVDLVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGASDLDATIVYGVNQDQLRAEHRIVSNASCTTNCIVPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 164 IKLLDDAYGIESGTVTTIHSSMNDQQVIDSWHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVPTINVT 243
Cdd:TIGR01532 161 IKLLDDAYGIESGTITTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGIERFFPQFNDRFEAIAVRVPTVNVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 244 AIDLSVTVKKPVKASEVNQLLQKAALGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNEWGFA 323
Cdd:TIGR01532 241 AIDLSVTVKKPVKANEVNLLLQKAAQGALRGIVDYTELPLVSVDFNHDPHSAIVDGTQTRVSGAHLVKTLVWCDNEWGFA 320
|
....*
gi 2022055743 324 NRMLD 328
Cdd:TIGR01532 321 NRMLD 325
|
|
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
1-337 |
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: 546.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 1 MTIRIAINGFGRIGRNVVRALYESGrrAEITVVAINELADAAGIAHLLKYDTSHGRFAWDVRQEREQLFVGDDAIRLLHE 80
Cdd:COG0057 1 MTIRVAINGFGRIGRLVLRALLERG--PDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 81 SSLEALPWRELAVDVVLDCTGVYGSREHGEAHLQAGARKVLFSHPGGNDlDATIVFGVNHAELRTEHRIVSNASCTTNCI 160
Cdd:COG0057 79 RDPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGD-DPTIVYGVNHDDYDADHRIISNASCTTNCL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 161 IPVIKLLDDAYGIESGTVTTIHSSMNDQQVIDSWHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVPTI 240
Cdd:COG0057 158 APVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 241 NVTAIDLSVTVKKPVKASEVNQLLQKAALGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNEW 320
Cdd:COG0057 238 NVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEW 317
|
330
....*....|....*..
gi 2022055743 321 GFANRMLDTTLAMAAQG 337
Cdd:COG0057 318 GYSNRMVDLAEYMAKLL 334
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
4-328 |
2.31e-133 |
|
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: 382.78 E-value: 2.31e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 4 RIAINGFGRIGRNVVRALYESgRRAEITVVAINELADAAGIAHLLKYDTSHGRFAWDVR-QEREQLFVGDDAIRLLHESS 82
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEK-PGNDLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTvDEDGLVVNGKEVISVFSERD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 83 LEALPWRELAVDVVLDCTGVYGSREHGEAHLQAGARKVLFSHPGGNDlDATIVFGVNHAELRTEHRIVSNASCTTNCIIP 162
Cdd:TIGR01534 80 PSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGD-VKTIVYGVNHDEYDGEERIISNASCTTNCLAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 163 VIKLLDDAYGIESGTVTTIHSSMNDQQVIDSWHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVPTINV 242
Cdd:TIGR01534 159 LAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 243 TAIDLSVTVKKPVKASEVNQLLQKAALGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAH--LIKTLVWCDNEW 320
Cdd:TIGR01534 239 SLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVTGLGdsLVKVYAWYDNEW 318
|
....*...
gi 2022055743 321 GFANRMLD 328
Cdd:TIGR01534 319 GYSNRLVD 326
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-336 |
5.43e-132 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 379.85 E-value: 5.43e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 1 MTIRIAINGFGRIGRNVVRALYESGRraeITVVAINELADAAGIAHLLKYDTSHGRFAWDVRQEREQLFVGDDAIRLLHE 80
Cdd:PRK07729 1 MKTKVAINGFGRIGRMVFRKAIKESA---FEIVAINASYPSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 81 SSLEALPWRELAVDVVLDCTGVYGSREHGEAHLQAGARKVLFSHPGGNDlDATIVFGVNHAELR-TEHRIVSNASCTTNC 159
Cdd:PRK07729 78 RDPKELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNE-DVTIVVGVNEDQLDiEKHTIISNASCTTNC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 160 IIPVIKLLDDAYGIESGTVTTIHSSMNDQQVIDSWHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVPT 239
Cdd:PRK07729 157 LAPVVKVLDEQFGIENGLMTTVHAYTNDQKNIDNPHKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 240 INVTAIDLSVTVKKPVKASEVNQLLQKAALGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNE 319
Cdd:PRK07729 237 PNVSLVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNE 316
|
330
....*....|....*..
gi 2022055743 320 WGFANRMLDTTLAMAAQ 336
Cdd:PRK07729 317 WGYSCRVVDLVTLVADE 333
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
155-319 |
4.41e-113 |
|
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: 325.14 E-value: 4.41e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 155 CTTNCIIPVIKLLDDAYGIESGTVTTIHSSMNDQQVIDSWHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIA 234
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 235 VRVPTINVTAIDLSVTVKKPVKASEVNQLLQKAALGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLV 314
Cdd:cd23937 81 VRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLLV 160
|
....*
gi 2022055743 315 WCDNE 319
Cdd:cd23937 161 WCDNE 165
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
5-328 |
9.72e-110 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 322.65 E-value: 9.72e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 5 IAINGFGRIGRNVVRALYEsgrRAEITVVAINELA-DAAGIAHLLKYDTSHGRFAWDVRQEREQLFVGDDAIRLLHESSL 83
Cdd:NF033735 1 IGINGFGRIGRLALRALWG---RPGLEIVHINDLAgDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 84 EALPWRElAVDVVLDCTGVYGSREHGEAHLQAGARKVLFSHPGGNDLDATIVFGVNHAELRTE-HRIVSNASCTTNCIIP 162
Cdd:NF033735 78 EDTPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLNIVYGVNDHLYDPArHRIVTAASCTTNCLAP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 163 VIKLLDDAYGIESGTVTTIHSSMNDQQVIDSWHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVPTINV 242
Cdd:NF033735 157 VVKVIHEKIGIKHGSITTIHDITNTQTIVDAPHKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 243 TAIDLSVTVKKPVKASEVNQLLQKAALGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNEWGF 322
Cdd:NF033735 237 SLTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGY 316
|
....*.
gi 2022055743 323 ANRMLD 328
Cdd:NF033735 317 ANRMVD 322
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
2-328 |
1.98e-106 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 314.54 E-value: 1.98e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 2 TIRIAINGFGRIGRNVVRALYesGRR-AEITVVAINELADAAGIAHLLKYDTSHGRFAWDVRQEREQLFVGDDAIRLLHE 80
Cdd:PRK07403 1 MIRVAINGFGRIGRNFLRCWL--GREnSQLELVAINDTSDPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 81 SSLEALPWRELAVDVVLDCTGVYGSREHGEAHLQAGARKVLFSHPGGNDLDATIVFGVNHAELRTE-HRIVSNASCTTNC 159
Cdd:PRK07403 79 RNPLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPGKGEDIGTYVVGVNHHEYDHEdHNIISNASCTTNC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 160 IIPVIKLLDDAYGIESGTVTTIHSSMNDQQVIDSWHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVPT 239
Cdd:PRK07403 159 LAPIAKVLHDNFGIIKGTMTTTHSYTGDQRILDASHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 240 INVTAIDLSVTVKKPVKASEVNQLLQKAALGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNE 319
Cdd:PRK07403 239 PNVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYDNE 318
|
....*....
gi 2022055743 320 WGFANRMLD 328
Cdd:PRK07403 319 WGYSQRVVD 327
|
|
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-325 |
2.39e-98 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 293.95 E-value: 2.39e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 1 MTIRIAINGFGRIGRNVVRALYESgrrAEITVVAINELA-DAAGIAHLLKYDTSHGRFAWDVRQEREQLFVGDDAIRLLH 79
Cdd:PRK08955 1 MTIKVGINGFGRIGRLALRAAWDW---PELEFVQINDPAgDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 80 ESSLEALPWRelAVDVVLDCTGVYGSREHGEAHLQAGARKVLFSHPGGNDLDATIVFGVNHaEL--RTEHRIVSNASCTT 157
Cdd:PRK08955 78 NKAIADTDWS--GCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLNIVMGVND-HLfdPAIHPIVTAASCTT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 158 NCIIPVIKLLDDAYGIESGTVTTIHSSMNDQQVIDSWHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRV 237
Cdd:PRK08955 155 NCLAPVVKVIHEKLGIKHGSMTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 238 PTINVTAIDLSVTVKKPVKASEVNQLLQKAALGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCD 317
Cdd:PRK08955 235 PLANASLTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYD 314
|
....*...
gi 2022055743 318 NEWGFANR 325
Cdd:PRK08955 315 NEWGYANR 322
|
|
| GAPDH_N_E4PDH |
cd17892 |
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
3-154 |
8.56e-94 |
|
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: 276.07 E-value: 8.56e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 3 IRIAINGFGRIGRNVVRALYESGRRAEITVVAINELADAAGIAHLLKYDTSHGRFAWDVRQEREQLFVGDDAIRLLHESS 82
Cdd:cd17892 1 YRVAINGYGRIGRNVLRALYESGRRAEFQVVAINELADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2022055743 83 LEALPWRELAVDVVLDCTGVYGSREHGEAHLQAGARKVLFSHPGGNDLDATIVFGVNHAELRTEHRIVSNAS 154
Cdd:cd17892 81 PENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASNDVDATIVYGINQDLLRAEHRIVSNAS 152
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
3-328 |
5.82e-92 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 279.89 E-value: 5.82e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 3 IRIAINGFGRIGRNVVRALYesGRR-AEITVVAINELADAAGIAHLLKYDTSHGRFAWDVRqereqlFVGDDA------- 74
Cdd:PLN03096 61 IKVAINGFGRIGRNFLRCWH--GRKdSPLDVVAINDTGGVKQASHLLKYDSTLGTFDADVK------PVGDDAisvdgkv 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 75 IRLLHESSLEALPWRELAVDVVLDCTGVYGSREHGEAHLQAGARKVLFSHPGGNDLdATIVFGVNHAELRTEHRIVSNAS 154
Cdd:PLN03096 133 IKVVSDRNPLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKGDI-PTYVVGVNADDYKHSDPIISNAS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 155 CTTNCIIPVIKLLDDAYGIESGTVTTIHSSMNDQQVIDSWHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIA 234
Cdd:PLN03096 212 CTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 235 VRVPTINVTAIDLSVTVKKPVKASEVNQLLQKAALGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLV 314
Cdd:PLN03096 292 LRVPTPNVSVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVA 371
|
330
....*....|....
gi 2022055743 315 WCDNEWGFANRMLD 328
Cdd:PLN03096 372 WYDNEWGYSQRVVD 385
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
3-336 |
7.72e-89 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 273.31 E-value: 7.72e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 3 IRIAINGFGRIGRNVVRAlYESGRRAEITVVAINELADAAGIAHLLKYDTSHGRFAWDVR-QEREQLFVGDDAIRLLHES 81
Cdd:PLN02237 76 LKVAINGFGRIGRNFLRC-WHGRKDSPLDVVVVNDSGGVKNASHLLKYDSMLGTFKADVKiVDDETISVDGKPIKVVSNR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 82 SLEALPWRELAVDVVLDCTGVYGSREHGEAHLQAGARKVLFSHPG-GNDLdATIVFGVNHAELRTEH-RIVSNASCTTNC 159
Cdd:PLN02237 155 DPLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAkGADI-PTYVVGVNEDDYDHEVaNIVSNASCTTNC 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 160 IIPVIKLLDDAYGIESGTVTTIHSSMNDQQVIDSWHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVPT 239
Cdd:PLN02237 234 LAPFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPT 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 240 INVTAIDLSVTV-KKPVKASEVNQLLQKAALGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDN 318
Cdd:PLN02237 314 PNVSVVDLVVNVeKKGITAEDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVAWYDN 393
|
330
....*....|....*...
gi 2022055743 319 EWGFANRMLDTTLAMAAQ 336
Cdd:PLN02237 394 EWGYSQRVVDLAHLVAAK 411
|
|
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-336 |
2.77e-86 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 263.23 E-value: 2.77e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 1 MTIRIAINGFGRIGRNVVRALYEsgrRAEITVVAINE-LADAAGIAHLLKYDTSHGRFAWDVRQEREQLFVGDDAIRLLH 79
Cdd:PTZ00023 1 MVVKLGINGFGRIGRLVFRAALE---REDVEVVAINDpFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 80 ESSLEALPWRELAVDVVLDCTGVYGSREHGEAHLQAGARKVLFSHPGGNDlDATIVFGVNHAELRTEHRIVSNASCTTNC 159
Cdd:PTZ00023 78 EKDPAAIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKDD-TPIYVMGVNHTQYDKSQRIVSNASCTTNC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 160 IIPVIKLLDDAYGIESGTVTTIHSSMNDQQVIDSWH---PDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVR 236
Cdd:PTZ00023 157 LAPLAKVVNDKFGIVEGLMTTVHASTANQLTVDGPSkggKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 237 VPTINVTAIDLSVTVKKPVKASEVNQLLQKAALGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWC 316
Cdd:PTZ00023 237 VPVPDVSVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWY 316
|
330 340
....*....|....*....|
gi 2022055743 317 DNEWGFANRMLDTTLAMAAQ 336
Cdd:PTZ00023 317 DNEWGYSNRLLDLAHYITQK 336
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
155-319 |
1.10e-84 |
|
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: 252.76 E-value: 1.10e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 155 CTTNCIIPVIKLLDDAYGIESGTVTTIHSSMNDQQVIDSWHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIA 234
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 235 VRVPTINVTAIDLSVTVKKPVKASEVNQLLQKAALGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLV 314
Cdd:cd18126 81 FRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVVA 160
|
....*
gi 2022055743 315 WCDNE 319
Cdd:cd18126 161 WYDNE 165
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
1-328 |
1.98e-78 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 243.10 E-value: 1.98e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 1 MTIRIAINGFGRIGRNVVRAlyeSGRRAEITVVAINELADAAGIAHLLKYDTSHGRFAWDVRQEREQLFVGDDAIRLLHE 80
Cdd:PRK15425 1 MTIKVGINGFGRIGRIVFRA---AQKRSDIEIVAINDLLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 81 SSLEALPWRELAVDVVLDCTGVYGSREHGEAHLQAGARKVLFSHPGgNDLDATIVFGVNHaELRTEHRIVSNASCTTNCI 160
Cdd:PRK15425 78 RDPANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPS-KDNTPMFVKGANF-DKYAGQDIVSNASCTTNCL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 161 IPVIKLLDDAYGIESGTVTTIHSSMNDQQVIDS-WHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVPT 239
Cdd:PRK15425 156 APLAKVINDNFGIIEGLMTTVHATTATQKTVDGpSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 240 INVTAIDLSVTVKKPVKASEVNQLLQKAALGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNE 319
Cdd:PRK15425 236 PNVSVVDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNE 315
|
....*....
gi 2022055743 320 WGFANRMLD 328
Cdd:PRK15425 316 TGYSNKVLD 324
|
|
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
3-334 |
3.04e-77 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 242.84 E-value: 3.04e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 3 IRIAINGFGRIGRNVVRAlyeSGRRAEITVVAINE-LADAAGIAHLLKYDTSHGRFAWDVRQ-EREQLFVGDDAIRLLHE 80
Cdd:PLN02272 86 TKIGINGFGRIGRLVLRI---ATSRDDIEVVAVNDpFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSK 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 81 SSLEALPWRELAVDVVLDCTGVYGSREHGEAHLQAGARKVLFSHPGGndlDATI-VFGVNHAELRTEHRIVSNASCTTNC 159
Cdd:PLN02272 163 RDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSA---DAPMfVVGVNEKTYKPNMNIVSNASCTTNC 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 160 IIPVIKLLDDAYGIESGTVTTIHSSMNDQQVIDSwhP---DLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVR 236
Cdd:PLN02272 240 LAPLAKVVHEEFGILEGLMTTVHATTATQKTVDG--PsmkDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFR 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 237 VPTINVTAIDLSVTVKKPVKASEVNQLLQKAALGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWC 316
Cdd:PLN02272 318 VPTPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWY 397
|
330
....*....|....*...
gi 2022055743 317 DNEWGFANRMLDTTLAMA 334
Cdd:PLN02272 398 DNEWGYSNRVLDLIEHMA 415
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
1-339 |
1.49e-76 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 239.19 E-value: 1.49e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 1 MTIRIAINGFGRIGRNVVRALYESGRRA-EITVVAINELA-DAAGIAHLLKYDTSHGRFAWDVRQEREQLFVGDDAIRLL 78
Cdd:PTZ00434 2 APIKVGINGFGRIGRMVFQAICDQGLIGtEIDVVAVVDMStNAEYFAYQMKYDTVHGRPKYTVETTKSSPSVKTDDVLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 79 HESSLEA---------LPWRELAVDVVLDCTGVYGSREHGEAHLQAGARKVLFSHPGGNDLDaTIVFGVNHAELR-TEHR 148
Cdd:PTZ00434 82 NGHRIKCvkaqrnpadLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPASGGAK-TIVMGVNQHEYSpTEHH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 149 IVSNASCTTNCIIPVIKLL-DDAYGIESGTVTTIHSSMNDQQVIDSWH-PDLRRTRAASQSIIPVDTKLAAGITRFFPQF 226
Cdd:PTZ00434 161 VVSNASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSvKDWRGGRAAAVNIIPSTTGAAKAVGMVIPST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 227 NDRFEAIAVRVPTINVTAIDLSVTVKKPVKASEVNQLLQKAALGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSG 306
Cdd:PTZ00434 241 KGKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKATLQNN 320
|
330 340 350
....*....|....*....|....*....|....*..
gi 2022055743 307 ----AHLIKTLVWCDNEWGFANRMLDTTLAMAAQGFR 339
Cdd:PTZ00434 321 lpgeRRFFKIVSWYDNEWGYSHRVVDLVRYMAAKDAA 357
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-155 |
1.31e-70 |
|
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: 216.65 E-value: 1.31e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 3 IRIAINGFGRIGRNVVRALYEsgrRAEITVVAINELADAAGIAHLLKYDTSHGRFAWDVRQEREQLFVGDDAIRLLHESS 82
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALE---RPDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERD 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2022055743 83 LEALPWRELAVDVVLDCTGVYGSREHGEAHLQAGARKVLFSHPGGNDlDATIVFGVNHAELRTEHRIVSNASC 155
Cdd:smart00846 78 PANLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDA-DPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
3-334 |
3.56e-70 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 222.29 E-value: 3.56e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 3 IRIAINGFGRIGRNVVRALYEsgrRAEITVVAINE-LADAAGIAHLLKYDTSHGRFAWD---VRQEREQLFvGDDAIRLL 78
Cdd:PLN02358 6 IRIGINGFGRIGRLVARVVLQ---RDDVELVAVNDpFITTEYMTYMFKYDSVHGQWKHHelkVKDDKTLLF-GEKPVTVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 79 HESSLEALPWRELAVDVVLDCTGVYGSREHGEAHLQAGARKVLFSHPGGNDldATIVFGVNHAELRTEHRIVSNASCTTN 158
Cdd:PLN02358 82 GIRNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDA--PMFVVGVNEHEYKSDLDIVSNASCTTN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 159 CIIPVIKLLDDAYGIESGTVTTIHSSMNDQQVIDS-WHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRV 237
Cdd:PLN02358 160 CLAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGpSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 238 PTINVTAIDLSVTVKKPVKASEVNQLLQKAALGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCD 317
Cdd:PLN02358 240 PTVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYD 319
|
330
....*....|....*..
gi 2022055743 318 NEWGFANRMLDTTLAMA 334
Cdd:PLN02358 320 NEWGYSSRVVDLIVHMS 336
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
160-316 |
1.64e-68 |
|
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: 211.30 E-value: 1.64e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 160 IIPVIKLLDDAYGIESGTVTTIHSSMNDQQVIDSWHP-DLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVP 238
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHkDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2022055743 239 TINVTAIDLSVTVKKPVKASEVNQLLQKAALGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWC 316
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| GAPDH_I_N |
cd05214 |
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
3-154 |
5.72e-68 |
|
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: 210.33 E-value: 5.72e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 3 IRIAINGFGRIGRNVVRALYEsgrRAEITVVAINELADAAGIAHLLKYDTSHGRFAWDVRQEREQLFVGDDAIRLLHESS 82
Cdd:cd05214 1 IKVGINGFGRIGRLVFRAALE---RDDIEVVAINDLTDDETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERD 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2022055743 83 LEALPWRELAVDVVLDCTGVYGSREHGEAHLQAGARKVLFSHPGGNDlDATIVFGVNHAELRTEHRIVSNAS 154
Cdd:cd05214 78 PAELPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDD-DPTIVMGVNHDKYDADDKIISNAS 148
|
|
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
9-334 |
4.90e-65 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 212.86 E-value: 4.90e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 9 GFGRIGRNVVRALYE-----SGRRAEITVVAINELADAAGIAHLLKYDTSHGRFAW--DVRQEREQLFVGDDAIRLLHES 81
Cdd:PRK08289 134 GFGRIGRLLARLLIEktgggNGLRLRAIVVRKGSEGDLEKRASLLRRDSVHGPFNGtiTVDEENNAIIANGNYIQVIYAN 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 82 SLEALPWRELAVD--VVLDCTGVYGSREHGEAHLQA-GARKVLFSHPGGNDLdATIVFGVNHAELRTEHRIVSNASCTTN 158
Cdd:PRK08289 214 SPEEVDYTAYGINnaLVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGKGDI-KNIVHGVNHSDITDEDKIVSAASCTTN 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 159 CIIPVIKLLDDAYGIESGTVTTIHSSMNDQQVIDSWHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAIAVRVP 238
Cdd:PRK08289 293 AITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKGDRRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNAIRVP 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 239 TINVTAIDLSVTVKKPVKASEVNQLLQKAAL-GAFHGIVDYTELP-LVSIDFNHDPHSAIVDGTQTRVSGAHLIkTLVWC 316
Cdd:PRK08289 373 TPNVSMAILNLNLEKETSREELNEYLRQMSLhSPLQNQIDYTDSTeVVSSDFVGSRHAGVVDSQATIVNGNRAV-LYVWY 451
|
330
....*....|....*...
gi 2022055743 317 DNEWGFANRMLDTTLAMA 334
Cdd:PRK08289 452 DNEFGYSCQVVRVMEQMA 469
|
|
| Gp_dh_N |
pfam00044 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-106 |
5.84e-45 |
|
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: 149.17 E-value: 5.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 3 IRIAINGFGRIGRNVVRALYEsgrRAEITVVAINELADAAGIAHLLKYDTSHGRFAWDVRQEREQLFVGDDAIRLLHESS 82
Cdd:pfam00044 1 VKVGINGFGRIGRLVLRAALE---RPDIEVVAINDLTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERD 77
|
90 100
....*....|....*....|....
gi 2022055743 83 LEALPWRELAVDVVLDCTGVYGSR 106
Cdd:pfam00044 78 PAELPWGDLGVDVVIESTGVFTTK 101
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-327 |
1.36e-37 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 137.31 E-value: 1.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 1 MTIRIAINGFGRIGRNVvraLYESGRRAEITVVAINELA-DAAGIAHLLKYDTSHGRFAW-DVRQEREQLFV-GDDAIRL 77
Cdd:PTZ00353 1 LPITVGINGFGPVGKAV---LFASLTDPLVTVVAVNDASvSIAYIAYVLEQESPLSAPDGaSIRVVGEQIVLnGTQKIRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 78 LHESSLEALPWRELAVDVVLDCTGVYGSREHGEAHLQAGARKVLFShpgGNDLDA-TIVFGVNHAELRTEHRIVSNASCT 156
Cdd:PTZ00353 78 SAKHDLVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVA---GQSADApTVMAGSNDERLSASLPVCCAGAPI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 157 TNCIIPVIKLLDDAYGIESGTVTTIHSsMNDQQVI--DSWHP-DLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAI 233
Cdd:PTZ00353 155 AVALAPVIRALHEVYGVEECSYTAIHG-MQPQEPIaaRSKNSqDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 234 AVRVPTINVTAIDLSVTVKKPVKASEVNQLLQKAALGAFHGIVDYTELPLVSIDFNHDpHSAIVDGTQTR-VSGAHLIKT 312
Cdd:PTZ00353 234 AFQVPVKKGCAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCIPN-GKLCYDATSSSsSREGEVHKM 312
|
330
....*....|....*
gi 2022055743 313 LVWCDNEWGFANRML 327
Cdd:PTZ00353 313 VLWFDVECYYAARLL 327
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
155-319 |
3.28e-35 |
|
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: 125.81 E-value: 3.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 155 CTTNCIIPVIKLLDDAYGIESGTVTTIHSSMNDQQVIDS-WHPDLRRTRAASQSIIPVDTKLAAGITRFFPQFNDRFEAI 233
Cdd:cd18123 1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGpSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 234 AVRVPTINVTAIDLSVTVKKPVKASEVNQLLQKAALGafHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTL 313
Cdd:cd18123 81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLM 158
|
....*.
gi 2022055743 314 VWCDNE 319
Cdd:cd18123 159 QWYDNE 164
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
155-319 |
6.67e-18 |
|
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: 79.87 E-value: 6.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 155 CTTNCIIPVIKLLDDAYGIESGTVTTIHSSMNDQQVIDSWHpDLRRTRAASQSIIPVDTKLAAGITRFFPQFND--RFEA 232
Cdd:cd18122 1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPI-LKSEVRAIIPNIPKNETKHAPETGKVLGEIGKpiKVDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 233 IAVRVPTINVTAIDLSVTVKKPVKASEVNQLLQKAALGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKT 312
Cdd:cd18122 80 IAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLKV 159
|
....*..
gi 2022055743 313 LVWCDNE 319
Cdd:cd18122 160 FSAVDNE 166
|
|
| GAPDH-like_N |
cd05192 |
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ... |
3-159 |
2.39e-11 |
|
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: 60.06 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 3 IRIAINGFGRIGRNVVRALYEsgrRAEITVVAINELADaagiahllkydtshgrfawdvrqereqlfvgddairllhess 82
Cdd:cd05192 1 IRVAINGFGRIGRIVFRAIAD---QDDLDVVAINDRRD------------------------------------------ 35
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2022055743 83 lealpwrelavdVVLDCTGVYGSREHGEAHLQAGARKVLFSHPGGNDlDATIVFGVNHAELRTEHRIVSNASCTTNC 159
Cdd:cd05192 36 ------------VVIECTGSFTDDDNAEKHIKAGGKKAVITAPEKGD-IPTIVVVLNELAKSAGATVVSNANETSYS 99
|
|
| Asd |
COG0136 |
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ... |
134-267 |
1.02e-03 |
|
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: 40.40 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 134 IVFGVNHAEL--RTEHRIVSNASCTTNCIIPVIKLLDDAYGIESGTVTTIHS-SMNDQQVIDswhpDLRRTRAASQSIIP 210
Cdd:COG0136 105 VVPEVNPEALadHLPKGIIANPNCSTIQMLVALKPLHDAAGIKRVVVSTYQAvSGAGAAAMD----ELAEQTAALLNGEE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 211 VDTKlaagitrFFPQ---FN-----DRFE---------------------------AIAVRVPTINVTAIDLSVTVKKPV 255
Cdd:COG0136 181 IEPE-------VFPHpiaFNlipqiDVFLengytkeemkmvnetrkilgdpdipvsATCVRVPVFRGHSEAVNIEFERPV 253
|
170
....*....|..
gi 2022055743 256 KASEVNQLLQKA 267
Cdd:COG0136 254 SLEEARELLAAA 265
|
|
| GFO_IDH_MocA |
pfam01408 |
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. ... |
3-116 |
2.72e-03 |
|
Oxidoreductase family, NAD-binding Rossmann fold; This family of enzymes utilize NADP or NAD. This family is called the GFO/IDH/MOCA family in swiss-prot.
Pssm-ID: 426248 [Multi-domain] Cd Length: 120 Bit Score: 37.19 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 3 IRIAINGFGRIGRNVVRALYESGRRAEITVVaineladaagiahllkydtshgrfaWDVRQEREQLFVGDDAIRLLheSS 82
Cdd:pfam01408 1 IRVGIIGAGKIGSKHARALNASQPGAELVAI-------------------------LDPNSERAEAVAESFGVEVY--SD 53
|
90 100 110
....*....|....*....|....*....|....
gi 2022055743 83 LEALPwRELAVDVVLDCTGVYGSREHGEAHLQAG 116
Cdd:pfam01408 54 LEELL-NDPEIDAVIVATPNGLHYDLAIAALEAG 86
|
|
| PRK06270 |
PRK06270 |
homoserine dehydrogenase; Provisional |
1-46 |
3.58e-03 |
|
homoserine dehydrogenase; Provisional
Pssm-ID: 235763 [Multi-domain] Cd Length: 341 Bit Score: 38.69 E-value: 3.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2022055743 1 MTIRIAINGFGRIGRNVVRALYESGRR------AEITVVAInelADAAGIAH 46
Cdd:PRK06270 1 MEMKIALIGFGGVGQGVAELLAEKREYlkkrygLDLKVVAI---ADSSGSAI 49
|
|
| MDR |
cd05188 |
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ... |
4-167 |
4.86e-03 |
|
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.
Pssm-ID: 176178 [Multi-domain] Cd Length: 271 Bit Score: 38.07 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 4 RIAINGFGRIGRNVVRALYESGrrAEITVVAIN----ELADAAGIAHLLKYDTshgrfAWDVRQEREQLFVGddairllh 79
Cdd:cd05188 137 TVLVLGAGGVGLLAAQLAKAAG--ARVIVTDRSdeklELAKELGADHVIDYKE-----EDLEEELRLTGGGG-------- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 80 esslealpwrelaVDVVLDCTGVYGSREHGEAHLQAGARKVLFSHPGGNDLdATIVFGVNHAELrtehRIVSNASCTTNC 159
Cdd:cd05188 202 -------------ADVVIDAVGGPETLAQALRLLRPGGRIVVVGGTSGGPP-LDDLRRLLFKEL----TIIGSTGGTRED 263
|
....*...
gi 2022055743 160 IIPVIKLL 167
Cdd:cd05188 264 FEEALDLL 271
|
|
| NAD_binding_3 |
pfam03447 |
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. ... |
9-116 |
7.20e-03 |
|
Homoserine dehydrogenase, NAD binding domain; This domain adopts a Rossmann NAD binding fold. The C-terminal domain of homoserine dehydrogenase contributes a single helix to this structural domain, which is not included in the Pfam model.
Pssm-ID: 281446 [Multi-domain] Cd Length: 116 Bit Score: 35.74 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 9 GFGRIGRNVVRALYESGRRAEITVVAIneladaaGIAHLLKYDTshGRFAWDVRQEreqlfvgddairllheSSLEALpW 88
Cdd:pfam03447 1 GCGAIGSGVLEQLLRQQSEIPLELVAV-------ADRDLLSKDP--LALLPDEPLT----------------LDLDDL-I 54
|
90 100
....*....|....*....|....*...
gi 2022055743 89 RELAVDVVLDCTGVYGSREHGEAHLQAG 116
Cdd:pfam03447 55 AHPDPDVVVECASSEAVAELVLDALKAG 82
|
|
| AspD |
COG1712 |
L-aspartate dehydrogenase, NAD(P)-dependent [Amino acid transport and metabolism]; |
3-116 |
8.43e-03 |
|
L-aspartate dehydrogenase, NAD(P)-dependent [Amino acid transport and metabolism];
Pssm-ID: 441318 [Multi-domain] Cd Length: 263 Bit Score: 37.47 E-value: 8.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2022055743 3 IRIAINGFGRIGRNVVRALyesgRRAEITVVAIneladaagiahllkYDTSHGRfawdvrqeREQLFVGDDAIRLlheSS 82
Cdd:COG1712 1 MRIGLIGCGAIGSEVAEAL----ADAGVELVAV--------------YDRDPER--------AEALLASLGARVV---SD 51
|
90 100 110
....*....|....*....|....*....|....
gi 2022055743 83 LEALpwRELAVDVVLDCTGVYGSREHGEAHLQAG 116
Cdd:COG1712 52 VDEL--LAADPDLVVEAASQAAVREHGPAVLEAG 83
|
|
| |
