|
Name |
Accession |
Description |
Interval |
E-value |
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
1-333 |
0e+00 |
|
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]; Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 439827 [Multi-domain] Cd Length: 334 Bit Score: 674.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 1 AVKVGINGFGRIGRNVFRAALKN-PDIEVVAVNGLTDANTLAHLLKYDSVHGRLDAEVSVNGNNLVVNGKEIIVKAERDP 79
Cdd:COG0057 2 TIRVAINGFGRIGRLVLRALLERgPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 80 ENLAWGEIGVDIVVESTGRFTKREDAAKHLEAGAKKVIISAPAKNEDITIVMGVNQDKYDPKaHHVISNASCTTNCLAPF 159
Cdd:COG0057 82 AELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDDPTIVYGVNHDDYDAD-HRIISNASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 160 AKVLHEQFGIVRGMMTTVHSYTNDQRILDASHKDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGMAMRVPTPNVS 239
Cdd:COG0057 161 AKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 240 VVDLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMVIDGKMVKVVSWYDNETGYS 319
Cdd:COG0057 241 LVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGYS 320
|
330
....*....|....
2DBV_P 320 HRVVDLAAYIASKG 333
Cdd:COG0057 321 NRMVDLAEYMAKLL 334
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
2-332 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 530.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 2 VKVGINGFGRIGRNVFRAALKNPDIEVVAVNGLTDANTLAHLLKYDSVHGRLDAEVSVNGNNLVVNGKEIIVKAERDPEN 81
Cdd:PRK07729 3 TKVAINGFGRIGRMVFRKAIKESAFEIVAINASYPSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDPKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 82 LAWGEIGVDIVVESTGRFTKREDAAKHLEAGAKKVIISAPAKNEDITIVMGVNQDKYDPKAHHVISNASCTTNCLAPFAK 161
Cdd:PRK07729 83 LPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVTIVVGVNEDQLDIEKHTIISNASCTTNCLAPVVK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 162 VLHEQFGIVRGMMTTVHSYTNDQRILDASHKDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGMAMRVPTPNVSVV 241
Cdd:PRK07729 163 VLDEQFGIENGLMTTVHAYTNDQKNIDNPHKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNVSLV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 242 DLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMVIDGKMVKVVSWYDNETGYSHR 321
Cdd:PRK07729 243 DLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEWGYSCR 322
|
330
....*....|.
2DBV_P 322 VVDLAAYIASK 332
Cdd:PRK07729 323 VVDLVTLVADE 333
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
3-324 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the enzyme responsible for the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. Forms exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (1.2.1.59). In some species, NAD- and NADP- utilizing forms exist, generally being responsible for reactions in the anabolic and catabolic directions respectively. Two Pfam models cover the two functional domains of this protein; pfam00044 represents the N-terminal NAD(P)-binding domain and pfam02800 represents the C-terminal catalytic domain. An additional form of gap gene is found in gamma proteobacteria and is responsible for the conversion of erythrose-4-phosphate (E4P) to 4-phospho-erythronate in the biosynthesis of pyridoxine. This pathway of pyridoxine biosynthesis appears to be limited, however, to a relatively small number of bacterial species although it is prevalent among the gamma-proteobacteria. This enzyme is described by TIGR001532. These sequences generally score between trusted and noise to this GAPDH model due to the close evolutionary relationship. There exists the possiblity that some forms of GAPDH may be bifunctional and act on E4P in species which make pyridoxine and via hydroxythreonine and lack a separate E4PDH enzyme (for instance, the GAPDH from Bacillus stearothermophilus has been shown to posess a limited E4PD activity as well as a robust GAPDH activity). There are a great number of sequences in the databases which score between trusted and noise to this model, nearly all of them due to fragmentary sequences. It seems that study of this gene has been carried out in many species utilizing PCR probes which exclude the extreme ends of the consenses used to define this model. The noise level is set relative not to E4PD, but the next closest outliers, the class II GAPDH's (found in archaea, TIGR01546) and aspartate semialdehyde dehydrogenase (ASADH, TIGR01296) both of which have highest-scoring hits around -225 to the prior model. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 273675 [Multi-domain] Cd Length: 326 Bit Score: 520.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 3 KVGINGFGRIGRNVFRAALKNPD--IEVVAVNGLTDANTLAHLLKYDSVHGRLDAEVSVNGNNLVVNGKEII-VKAERDP 79
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKPGndLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEVIsVFSERDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 80 ENLAWGEIGVDIVVESTGRFTKREDAAKHLEAGAKKVIISAPAKNEDITIVMGVNQDKYDPKaHHVISNASCTTNCLAPF 159
Cdd:TIGR01534 81 SDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDVKTIVYGVNHDEYDGE-ERIISNASCTTNCLAPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 160 AKVLHEQFGIVRGMMTTVHSYTNDQRILDASHKDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGMAMRVPTPNVS 239
Cdd:TIGR01534 160 AKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 240 VVDLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMV--IDGKMVKVVSWYDNETG 317
Cdd:TIGR01534 240 LVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNEWG 319
|
....*..
2DBV_P 318 YSHRVVD 324
Cdd:TIGR01534 320 YSNRLVD 326
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
4-326 |
4.70e-168 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 470.18 E-value: 4.70e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 4 VGINGFGRIGRNVFRAALKNPDIEVVAVNGL-TDANTLAHLLKYDSVHGRLDAEVSVNGNNLVVNGKEIIVKAERDPENL 82
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLaGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 83 AWGEiGVDIVVESTGRFTKREDAAKHLEAGAKKVIISAPAKNEDI-TIVMGVNQDKYDPKAHHVISNASCTTNCLAPFAK 161
Cdd:NF033735 81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVlNIVYGVNDHLYDPARHRIVTAASCTTNCLAPVVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 162 VLHEQFGIVRGMMTTVHSYTNDQRILDASHKDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGMAMRVPTPNVSVV 241
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAPHKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASLT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 242 DLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMVIDGKMVKVVSWYDNETGYSHR 321
Cdd:NF033735 240 DCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYANR 319
|
....*
2DBV_P 322 VVDLA 326
Cdd:NF033735 320 MVDLA 324
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
151-315 |
1.16e-120 |
|
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: 344.05 E-value: 1.16e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 151 CTTNCLAPFAKVLHEQFGIVRGMMTTVHSYTNDQRILDASHKDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGMA 230
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 231 MRVPTPNVSVVDLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMVIDGKMVKVVS 310
Cdd:cd18126 81 FRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVVA 160
|
....*
2DBV_P 311 WYDNE 315
Cdd:cd18126 161 WYDNE 165
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
156-312 |
7.71e-91 |
|
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: 268.31 E-value: 7.71e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 156 LAPFAKVLHEQFGIVRGMMTTVHSYTNDQRILDA-SHKDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGMAMRVP 234
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGpHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
2DBV_P 235 TPNVSVVDLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMVIDGKMVKVVSWY 312
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
2-151 |
2.26e-89 |
|
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: 264.03 E-value: 2.26e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 2 VKVGINGFGRIGRNVFRAALKNPDIEVVAVNGLTDANTLAHLLKYDSVHGRLDAEVSVNGNNLVVNGKEIIVKAERDPEN 81
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPAN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 82 LAWGEIGVDIVVESTGRFTKREDAAKHLEAGAKKVIISAPAKNEDITIVMGVNQDKYDPKaHHVISNASC 151
Cdd:smart00846 81 LPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDADPTFVYGVNHDEYDGE-DHIISNASC 149
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
1-333 |
0e+00 |
|
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]; Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 439827 [Multi-domain] Cd Length: 334 Bit Score: 674.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 1 AVKVGINGFGRIGRNVFRAALKN-PDIEVVAVNGLTDANTLAHLLKYDSVHGRLDAEVSVNGNNLVVNGKEIIVKAERDP 79
Cdd:COG0057 2 TIRVAINGFGRIGRLVLRALLERgPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 80 ENLAWGEIGVDIVVESTGRFTKREDAAKHLEAGAKKVIISAPAKNEDITIVMGVNQDKYDPKaHHVISNASCTTNCLAPF 159
Cdd:COG0057 82 AELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDDPTIVYGVNHDDYDAD-HRIISNASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 160 AKVLHEQFGIVRGMMTTVHSYTNDQRILDASHKDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGMAMRVPTPNVS 239
Cdd:COG0057 161 AKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPHKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 240 VVDLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMVIDGKMVKVVSWYDNETGYS 319
Cdd:COG0057 241 LVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGYS 320
|
330
....*....|....
2DBV_P 320 HRVVDLAAYIASKG 333
Cdd:COG0057 321 NRMVDLAEYMAKLL 334
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
2-332 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 530.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 2 VKVGINGFGRIGRNVFRAALKNPDIEVVAVNGLTDANTLAHLLKYDSVHGRLDAEVSVNGNNLVVNGKEIIVKAERDPEN 81
Cdd:PRK07729 3 TKVAINGFGRIGRMVFRKAIKESAFEIVAINASYPSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDPKE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 82 LAWGEIGVDIVVESTGRFTKREDAAKHLEAGAKKVIISAPAKNEDITIVMGVNQDKYDPKAHHVISNASCTTNCLAPFAK 161
Cdd:PRK07729 83 LPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVTIVVGVNEDQLDIEKHTIISNASCTTNCLAPVVK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 162 VLHEQFGIVRGMMTTVHSYTNDQRILDASHKDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGMAMRVPTPNVSVV 241
Cdd:PRK07729 163 VLDEQFGIENGLMTTVHAYTNDQKNIDNPHKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNVSLV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 242 DLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMVIDGKMVKVVSWYDNETGYSHR 321
Cdd:PRK07729 243 DLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEWGYSCR 322
|
330
....*....|.
2DBV_P 322 VVDLAAYIASK 332
Cdd:PRK07729 323 VVDLVTLVADE 333
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
3-324 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the enzyme responsible for the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. Forms exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (1.2.1.59). In some species, NAD- and NADP- utilizing forms exist, generally being responsible for reactions in the anabolic and catabolic directions respectively. Two Pfam models cover the two functional domains of this protein; pfam00044 represents the N-terminal NAD(P)-binding domain and pfam02800 represents the C-terminal catalytic domain. An additional form of gap gene is found in gamma proteobacteria and is responsible for the conversion of erythrose-4-phosphate (E4P) to 4-phospho-erythronate in the biosynthesis of pyridoxine. This pathway of pyridoxine biosynthesis appears to be limited, however, to a relatively small number of bacterial species although it is prevalent among the gamma-proteobacteria. This enzyme is described by TIGR001532. These sequences generally score between trusted and noise to this GAPDH model due to the close evolutionary relationship. There exists the possiblity that some forms of GAPDH may be bifunctional and act on E4P in species which make pyridoxine and via hydroxythreonine and lack a separate E4PDH enzyme (for instance, the GAPDH from Bacillus stearothermophilus has been shown to posess a limited E4PD activity as well as a robust GAPDH activity). There are a great number of sequences in the databases which score between trusted and noise to this model, nearly all of them due to fragmentary sequences. It seems that study of this gene has been carried out in many species utilizing PCR probes which exclude the extreme ends of the consenses used to define this model. The noise level is set relative not to E4PD, but the next closest outliers, the class II GAPDH's (found in archaea, TIGR01546) and aspartate semialdehyde dehydrogenase (ASADH, TIGR01296) both of which have highest-scoring hits around -225 to the prior model. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 273675 [Multi-domain] Cd Length: 326 Bit Score: 520.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 3 KVGINGFGRIGRNVFRAALKNPD--IEVVAVNGLTDANTLAHLLKYDSVHGRLDAEVSVNGNNLVVNGKEII-VKAERDP 79
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKPGndLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEVIsVFSERDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 80 ENLAWGEIGVDIVVESTGRFTKREDAAKHLEAGAKKVIISAPAKNEDITIVMGVNQDKYDPKaHHVISNASCTTNCLAPF 159
Cdd:TIGR01534 81 SDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDVKTIVYGVNHDEYDGE-ERIISNASCTTNCLAPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 160 AKVLHEQFGIVRGMMTTVHSYTNDQRILDASHKDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGMAMRVPTPNVS 239
Cdd:TIGR01534 160 AKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPHKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 240 VVDLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMV--IDGKMVKVVSWYDNETG 317
Cdd:TIGR01534 240 LVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNEWG 319
|
....*..
2DBV_P 318 YSHRVVD 324
Cdd:TIGR01534 320 YSNRLVD 326
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
2-332 |
1.36e-168 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 472.08 E-value: 1.36e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 2 VKVGINGFGRIGRNVFRAAL--KNPDIEVVAVNGLTDANTLAHLLKYDSVHGRLDAEVSVNGNNLVVNGKEIIVKAERDP 79
Cdd:PRK07403 2 IRVAINGFGRIGRNFLRCWLgrENSQLELVAINDTSDPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDRNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 80 ENLAWGEIGVDIVVESTGRFTKREDAAKHLEAGAKKVIISAPAKNEDI-TIVMGVNQDKYDPKAHHVISNASCTTNCLAP 158
Cdd:PRK07403 82 LNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPGKGEDIgTYVVGVNHHEYDHEDHNIISNASCTTNCLAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 159 FAKVLHEQFGIVRGMMTTVHSYTNDQRILDASHKDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGMAMRVPTPNV 238
Cdd:PRK07403 162 IAKVLHDNFGIIKGTMTTTHSYTGDQRILDASHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTPNV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 239 SVVDLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMVIDGKMVKVVSWYDNETGY 318
Cdd:PRK07403 242 SVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYDNEWGY 321
|
330
....*....|....
2DBV_P 319 SHRVVDLAAYIASK 332
Cdd:PRK07403 322 SQRVVDLAELVARK 335
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
4-326 |
4.70e-168 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 470.18 E-value: 4.70e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 4 VGINGFGRIGRNVFRAALKNPDIEVVAVNGL-TDANTLAHLLKYDSVHGRLDAEVSVNGNNLVVNGKEIIVKAERDPENL 82
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLaGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 83 AWGEiGVDIVVESTGRFTKREDAAKHLEAGAKKVIISAPAKNEDI-TIVMGVNQDKYDPKAHHVISNASCTTNCLAPFAK 161
Cdd:NF033735 81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVlNIVYGVNDHLYDPARHRIVTAASCTTNCLAPVVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 162 VLHEQFGIVRGMMTTVHSYTNDQRILDASHKDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGMAMRVPTPNVSVV 241
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAPHKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASLT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 242 DLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMVIDGKMVKVVSWYDNETGYSHR 321
Cdd:NF033735 240 DCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYANR 319
|
....*
2DBV_P 322 VVDLA 326
Cdd:NF033735 320 MVDLA 324
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
2-332 |
5.46e-152 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 434.33 E-value: 5.46e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 2 VKVGINGFGRIGRNVFRAALKNPD--IEVVAVNGLTDANTLAHLLKYDSVHGRLDAEVSVNGNNLV-VNGKEIIVKAERD 78
Cdd:PLN02237 76 LKVAINGFGRIGRNFLRCWHGRKDspLDVVVVNDSGGVKNASHLLKYDSMLGTFKADVKIVDDETIsVDGKPIKVVSNRD 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 79 PENLAWGEIGVDIVVESTGRFTKREDAAKHLEAGAKKVIISAPAKNEDI-TIVMGVNQDKYDPKAHHVISNASCTTNCLA 157
Cdd:PLN02237 156 PLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAKGADIpTYVVGVNEDDYDHEVANIVSNASCTTNCLA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 158 PFAKVLHEQFGIVRGMMTTVHSYTNDQRILDASHKDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGMAMRVPTPN 237
Cdd:PLN02237 236 PFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTPN 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 238 VSVVDLVAELEKE-VTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMVIDGKMVKVVSWYDNET 316
Cdd:PLN02237 316 VSVVDLVVNVEKKgITAEDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVAWYDNEW 395
|
330
....*....|....*.
2DBV_P 317 GYSHRVVDLAAYIASK 332
Cdd:PLN02237 396 GYSQRVVDLAHLVAAK 411
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
2-332 |
3.59e-151 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 430.51 E-value: 3.59e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 2 VKVGINGFGRIGRNVFRA--ALKNPDIEVVAVNGLTDANTLAHLLKYDSVHGRLDAEVSVNGNN-LVVNGKEIIVKAERD 78
Cdd:PLN03096 61 IKVAINGFGRIGRNFLRCwhGRKDSPLDVVAINDTGGVKQASHLLKYDSTLGTFDADVKPVGDDaISVDGKVIKVVSDRN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 79 PENLAWGEIGVDIVVESTGRFTKREDAAKHLEAGAKKVIISAPAKNEDITIVMGVNQDKYDPkAHHVISNASCTTNCLAP 158
Cdd:PLN03096 141 PLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKGDIPTYVVGVNADDYKH-SDPIISNASCTTNCLAP 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 159 FAKVLHEQFGIVRGMMTTVHSYTNDQRILDASHKDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGMAMRVPTPNV 238
Cdd:PLN03096 220 FVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNV 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 239 SVVDLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMVIDGKMVKVVSWYDNETGY 318
Cdd:PLN03096 300 SVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAWYDNEWGY 379
|
330
....*....|....
2DBV_P 319 SHRVVDLAAYIASK 332
Cdd:PLN03096 380 SQRVVDLADIVANK 393
|
|
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-326 |
8.28e-151 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 427.22 E-value: 8.28e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 1 AVKVGINGFGRIGRNVFRAALKNPDIEVVAVNGLT-DANTLAHLLKYDSVHGRLDAEVSVNGNNLVVNGKEIIVKAERDP 79
Cdd:PRK08955 2 TIKVGINGFGRIGRLALRAAWDWPELEFVQINDPAgDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 80 ENLAWGeiGVDIVVESTGRFTKREDAAKHLEAGAKKVIISAPAKNEDI-TIVMGVNQDKYDPKAHHVISNASCTTNCLAP 158
Cdd:PRK08955 82 ADTDWS--GCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVlNIVMGVNDHLFDPAIHPIVTAASCTTNCLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 159 FAKVLHEQFGIVRGMMTTVHSYTNDQRILDASHKDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGMAMRVPTPNV 238
Cdd:PRK08955 160 VVKVIHEKLGIKHGSMTTIHDLTNTQTILDAPHKDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLANA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 239 SVVDLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMVIDGKMVKVVSWYDNETGY 318
Cdd:PRK08955 240 SLTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNEWGY 319
|
....*...
2DBV_P 319 SHRVVDLA 326
Cdd:PRK08955 320 ANRTAELA 327
|
|
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
2-330 |
6.53e-143 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 410.40 E-value: 6.53e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 2 VKVGINGFGRIGRNVFRAALKNPDIEVVAVNG-LTDANTLAHLLKYDSVHGRLDAEVSV-NGNNLVVNGKEIIVKAERDP 79
Cdd:PLN02272 86 TKIGINGFGRIGRLVLRIATSRDDIEVVAVNDpFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDP 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 80 ENLAWGEIGVDIVVESTGRFTKREDAAKHLEAGAKKVIISAPAKNEDItIVMGVNQDKYDPKAHhVISNASCTTNCLAPF 159
Cdd:PLN02272 166 AEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPM-FVVGVNEKTYKPNMN-IVSNASCTTNCLAPL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 160 AKVLHEQFGIVRGMMTTVHSYTNDQRILDA-SHKDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGMAMRVPTPNV 238
Cdd:PLN02272 244 AKVVHEEFGILEGLMTTVHATTATQKTVDGpSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNV 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 239 SVVDLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMVIDGKMVKVVSWYDNETGY 318
Cdd:PLN02272 324 SVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGY 403
|
330
....*....|..
2DBV_P 319 SHRVVDLAAYIA 330
Cdd:PLN02272 404 SNRVLDLIEHMA 415
|
|
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-332 |
1.32e-132 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 381.10 E-value: 1.32e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 1 AVKVGINGFGRIGRNVFRAALKNPDIEVVAVNG-LTDANTLAHLLKYDSVHGRLDAEVSVNGNNLVVNGKEIIVKAERDP 79
Cdd:PTZ00023 2 VVKLGINGFGRIGRLVFRAALEREDVEVVAINDpFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 80 ENLAWGEIGVDIVVESTGRFTKREDAAKHLEAGAKKVIISAPAKNEDITIVMGVNQDKYDPKaHHVISNASCTTNCLAPF 159
Cdd:PTZ00023 82 AAIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKDDTPIYVMGVNHTQYDKS-QRIVSNASCTTNCLAPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 160 AKVLHEQFGIVRGMMTTVHSYTNDQRILDASH---KDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGMAMRVPTP 236
Cdd:PTZ00023 161 AKVVNDKFGIVEGLMTTVHASTANQLTVDGPSkggKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 237 NVSVVDLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMVIDGKMVKVVSWYDNET 316
Cdd:PTZ00023 241 DVSVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDNEW 320
|
330
....*....|....*.
2DBV_P 317 GYSHRVVDLAAYIASK 332
Cdd:PTZ00023 321 GYSNRLLDLAHYITQK 336
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
2-330 |
4.15e-129 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 372.14 E-value: 4.15e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 2 VKVGINGFGRIGRNVFRAALKNPDIEVVAVNGLTDANTLAHLLKYDSVHGRLDAEVSVNGNNLVVNGKEIIVKAERDPEN 81
Cdd:PRK15425 3 IKVGINGFGRIGRIVFRAAQKRSDIEIVAINDLLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPAN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 82 LAWGEIGVDIVVESTGRFTKREDAAKHLEAGAKKVIISAPAKNEDITIVMGVNQDKYdpKAHHVISNASCTTNCLAPFAK 161
Cdd:PRK15425 83 LKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDNTPMFVKGANFDKY--AGQDIVSNASCTTNCLAPLAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 162 VLHEQFGIVRGMMTTVHSYTNDQRILDA-SHKDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGMAMRVPTPNVSV 240
Cdd:PRK15425 161 VINDNFGIIEGLMTTVHATTATQKTVDGpSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 241 VDLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMVIDGKMVKVVSWYDNETGYSH 320
Cdd:PRK15425 241 VDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYSN 320
|
330
....*....|
2DBV_P 321 RVVDLAAYIA 330
Cdd:PRK15425 321 KVLDLIAHIS 330
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
2-332 |
4.66e-129 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 372.85 E-value: 4.66e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 2 VKVGINGFGRIGRNVFRA----ALKNPDIEVVAVNGL-TDANTLAHLLKYDSVHGRLDAEVSVNGNN--------LVVNG 68
Cdd:PTZ00434 4 IKVGINGFGRIGRMVFQAicdqGLIGTEIDVVAVVDMsTNAEYFAYQMKYDTVHGRPKYTVETTKSSpsvktddvLVVNG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 69 KEII-VKAERDPENLAWGEIGVDIVVESTGRFTKREDAAKHLEAGAKKVIISAPAKNEDITIVMGVNQDKYDPKAHHVIS 147
Cdd:PTZ00434 84 HRIKcVKAQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPASGGAKTIVMGVNQHEYSPTEHHVVS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 148 NASCTTNCLAPFAKVL-HEQFGIVRGMMTTVHSYTNDQRILDA-SHKDLRRARAAAESIIPTTTGAAKAVALVLPELKGK 225
Cdd:PTZ00434 164 NASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGvSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 226 LNGMAMRVPTPNVSVVDLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMVI---- 301
Cdd:PTZ00434 244 LTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKATLQNnlpg 323
|
330 340 350
....*....|....*....|....*....|.
2DBV_P 302 DGKMVKVVSWYDNETGYSHRVVDLAAYIASK 332
Cdd:PTZ00434 324 ERRFFKIVSWYDNEWGYSHRVVDLVRYMAAK 354
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
2-332 |
2.26e-122 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 355.13 E-value: 2.26e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 2 VKVGINGFGRIGRNVFRAAL---KNPDIEVVAVNGLTDANTLAHLLKYDSVHGRLDAEVSVNGNNLVVNGKEIIVKAERD 78
Cdd:PRK13535 2 IRVAINGFGRIGRNVLRALYesgRRAEITVVAINELADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 79 PENLAWGEIGVDIVVESTGRFTKREDAAKHLEAGAKKVIISAPAKNE-DITIVMGVNQDKYDPKaHHVISNASCTTNCLA 157
Cdd:PRK13535 82 IASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSNDlDATVVYGVNHDQLRAE-HRIVSNASCTTNCII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 158 PFAKVLHEQFGIVRGMMTTVHSYTNDQRILDASHKDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGMAMRVPTPN 237
Cdd:PRK13535 161 PVIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPTIN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 238 VSVVDLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMVIDGKMVKVVSWYDNETG 317
Cdd:PRK13535 241 VTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNEWG 320
|
330
....*....|....*.
2DBV_P 318 YSHRVVDLA-AYIASK 332
Cdd:PRK13535 321 FANRMLDTTlAMAAAG 336
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
151-315 |
1.16e-120 |
|
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: 344.05 E-value: 1.16e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 151 CTTNCLAPFAKVLHEQFGIVRGMMTTVHSYTNDQRILDASHKDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGMA 230
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGMA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 231 MRVPTPNVSVVDLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMVIDGKMVKVVS 310
Cdd:cd18126 81 FRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVVA 160
|
....*
2DBV_P 311 WYDNE 315
Cdd:cd18126 161 WYDNE 165
|
|
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
2-330 |
6.32e-105 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 310.88 E-value: 6.32e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 2 VKVGINGFGRIGRNVFRAALKNPDIEVVAVNG-LTDANTLAHLLKYDSVHGRLD-AEVSVNGNNLVVNG-KEIIVKAERD 78
Cdd:PLN02358 6 IRIGINGFGRIGRLVARVVLQRDDVELVAVNDpFITTEYMTYMFKYDSVHGQWKhHELKVKDDKTLLFGeKPVTVFGIRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 79 PENLAWGEIGVDIVVESTGRFTKREDAAKHLEAGAKKVIISAPAKNEDItIVMGVNQDKYDPKAHhVISNASCTTNCLAP 158
Cdd:PLN02358 86 PEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPM-FVVGVNEHEYKSDLD-IVSNASCTTNCLAP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 159 FAKVLHEQFGIVRGMMTTVHSYTNDQRILDA-SHKDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGMAMRVPTPN 237
Cdd:PLN02358 164 LAKVINDRFGIVEGLMTTVHSITATQKTVDGpSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 238 VSVVDLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMVIDGKMVKVVSWYDNETG 317
Cdd:PLN02358 244 VSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEWG 323
|
330
....*....|...
2DBV_P 318 YSHRVVDLAAYIA 330
Cdd:PLN02358 324 YSSRVVDLIVHMS 336
|
|
| GAPDH_I_N |
cd05214 |
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
2-150 |
2.23e-93 |
|
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: 274.66 E-value: 2.23e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 2 VKVGINGFGRIGRNVFRAALKNPDIEVVAVNGLTDANTLAHLLKYDSVHGRLDAEVSVNGNNLVVNGKEIIVKAERDPEN 81
Cdd:cd05214 1 IKVGINGFGRIGRLVFRAALERDDIEVVAINDLTDDETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
2DBV_P 82 LAWGEIGVDIVVESTGRFTKREDAAKHLEAGAKKVIISAPAKNEDITIVMGVNQDKYDPKaHHVISNAS 150
Cdd:cd05214 81 LPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDDDPTIVMGVNHDKYDAD-DKIISNAS 148
|
|
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
8-330 |
4.37e-92 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 282.58 E-value: 4.37e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 8 GFGRIGRNVFR-----AALKNP----DIeVVAVNGLTDANTLAHLLKYDSVHGRLDAEVSVNGNN--LVVNGKEIIVKAE 76
Cdd:PRK08289 134 GFGRIGRLLARlliekTGGGNGlrlrAI-VVRKGSEGDLEKRASLLRRDSVHGPFNGTITVDEENnaIIANGNYIQVIYA 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 77 RDPENLAWGEIGVD--IVVESTGRFTKREDAAKHLEA-GAKKVIISAPAKNEDITIVMGVNQDKYDPkAHHVISNASCTT 153
Cdd:PRK08289 213 NSPEEVDYTAYGINnaLVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGKGDIKNIVHGVNHSDITD-EDKIVSAASCTT 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 154 NCLAPFAKVLHEQFGIVRGMMTTVHSYTNDQRILDASHKDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGMAMRV 233
Cdd:PRK08289 292 NAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKGDRRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNAIRV 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 234 PTPNVSVVDLVAELEKEVTVEEVNAALKAAA-EGELKGILAYSEEP-LVSRDYNGSTVSSTIDALSTMViDGKMVKVVSW 311
Cdd:PRK08289 372 PTPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQIDYTDSTeVVSSDFVGSRHAGVVDSQATIV-NGNRAVLYVW 450
|
330
....*....|....*....
2DBV_P 312 YDNETGYSHRVVDLAAYIA 330
Cdd:PRK08289 451 YDNEFGYSCQVVRVMEQMA 469
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
156-312 |
7.71e-91 |
|
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: 268.31 E-value: 7.71e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 156 LAPFAKVLHEQFGIVRGMMTTVHSYTNDQRILDA-SHKDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGMAMRVP 234
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGpHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
2DBV_P 235 TPNVSVVDLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMVIDGKMVKVVSWY 312
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
2-151 |
2.26e-89 |
|
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: 264.03 E-value: 2.26e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 2 VKVGINGFGRIGRNVFRAALKNPDIEVVAVNGLTDANTLAHLLKYDSVHGRLDAEVSVNGNNLVVNGKEIIVKAERDPEN 81
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPAN 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 82 LAWGEIGVDIVVESTGRFTKREDAAKHLEAGAKKVIISAPAKNEDITIVMGVNQDKYDPKaHHVISNASC 151
Cdd:smart00846 81 LPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDADPTFVYGVNHDEYDGE-DHIISNASC 149
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
151-315 |
7.25e-65 |
|
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: 202.26 E-value: 7.25e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 151 CTTNCLAPFAKVLHEQFGIVRGMMTTVHSYTNDQRILDASHKDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGMA 230
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDAYHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 231 MRVPTPNVSVVDLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMVIDGKMVKVVS 310
Cdd:cd23937 81 VRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLLV 160
|
....*
2DBV_P 311 WYDNE 315
Cdd:cd23937 161 WCDNE 165
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
151-315 |
4.98e-60 |
|
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: 189.75 E-value: 4.98e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 151 CTTNCLAPFAKVLHEQFGIVRGMMTTVHSYTNDQRILDA-SHKDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGM 229
Cdd:cd18123 1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGpSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 230 AMRVPTPNVSVVDLVAELEKEVTVEEVNAALKAAAEGelKGILAYSEEPLVSRDYNGSTVSSTIDALSTMVIDGKMVKVV 309
Cdd:cd18123 81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLM 158
|
....*.
2DBV_P 310 SWYDNE 315
Cdd:cd18123 159 QWYDNE 164
|
|
| Gp_dh_N |
pfam00044 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
2-102 |
7.20e-58 |
|
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: 181.92 E-value: 7.20e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 2 VKVGINGFGRIGRNVFRAALKNPDIEVVAVNGLTDANTLAHLLKYDSVHGRLDAEVSVNGNNLVVNGKEIIVKAERDPEN 81
Cdd:pfam00044 1 VKVGINGFGRIGRLVLRAALERPDIEVVAINDLTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAE 80
|
90 100
....*....|....*....|.
2DBV_P 82 LAWGEIGVDIVVESTGRFTKR 102
Cdd:pfam00044 81 LPWGDLGVDVVIESTGVFTTK 101
|
|
| GAPDH_N_E4PDH |
cd17892 |
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
2-150 |
3.58e-57 |
|
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: 182.85 E-value: 3.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 2 VKVGINGFGRIGRNVFRAALKNP---DIEVVAVNGLTDANTLAHLLKYDSVHGRLDAEVSVNGNNLVVNGKEIIVKAERD 78
Cdd:cd17892 1 YRVAINGYGRIGRNVLRALYESGrraEFQVVAINELADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
2DBV_P 79 PENLAWGEIGVDIVVESTGRFTKREDAAKHLEAGAKKVIISAPAKNE-DITIVMGVNQDKYDPkAHHVISNAS 150
Cdd:cd17892 81 PENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASNDvDATIVYGINQDLLRA-EHRIVSNAS 152
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
2-326 |
2.56e-53 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 178.53 E-value: 2.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 2 VKVGINGFGRIGRNVFRAALKNPDIEVVAVNGLT-DANTLAHLLKYDSVHGRLD-AEVSVNGNNLVVNGKEII-VKAERD 78
Cdd:PTZ00353 3 ITVGINGFGPVGKAVLFASLTDPLVTVVAVNDASvSIAYIAYVLEQESPLSAPDgASIRVVGEQIVLNGTQKIrVSAKHD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 79 PENLAWGEIGVDIVVESTGRFTKREDAAKHLEAGAKKVIISApaKNEDITIVMGVNQDKYDPKAHHVISNASCTTNCLAP 158
Cdd:PTZ00353 83 LVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAG--QSADAPTVMAGSNDERLSASLPVCCAGAPIAVALAP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 159 FAKVLHEQFGIVRGMMTTVHSYTNDQRILDASH--KDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGMAMRVPTP 236
Cdd:PTZ00353 161 VIRALHEVYGVEECSYTAIHGMQPQEPIAARSKnsQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 237 NVSVVDLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMVIDGKMVKVVSWYDNET 316
Cdd:PTZ00353 241 KGCAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCIPNGKLCYDATSSSSSREGEVHKMVLWFDVEC 320
|
330
....*....|
2DBV_P 317 GYSHRVVDLA 326
Cdd:PTZ00353 321 YYAARLLSLV 330
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
151-315 |
1.47e-33 |
|
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: 121.47 E-value: 1.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 151 CTTNCLAPFAKVLHEQFGIVRGMMTTVHSYTNDQRILDASHkDLRRARAAAESIIPTTTGAAKAVALVLPEL--KGKLNG 228
Cdd:cd18122 1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPI-LKSEVRAIIPNIPKNETKHAPETGKVLGEIgkPIKVDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 229 MAMRVPTPNVSVVDLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTMVIDGKMVKV 308
Cdd:cd18122 80 IAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLKV 159
|
....*..
2DBV_P 309 VSWYDNE 315
Cdd:cd18122 160 FSAVDNE 166
|
|
| GAPDH-like_N |
cd05192 |
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ... |
2-155 |
3.61e-16 |
|
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like family; The GAPDH-like family includes glyceraldehyde-3-phosphate dehydrogenase (GAPDH), native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs), 2,4-diaminopentanoate dehydrogenase (DAPDH), meso-diaminopimelate D-dehydrogenase (meso-DAPDH), and dihydrodipicolinate reductase (DHDPR). GAPDH plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. nat-AmDHs catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. They play important roles in the efficient asymmetric synthesis of alpha-chiral amines. DAPDH is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). DHDPR catalyzes the NAD(P)H-dependent reduction of 2,3-dihydrodipicolinate (DHDP) to 2,3,4,5-tetrahydrodipicolinate (THDP). It could also function as a dehydratase in addition to the role of a nucleotide dependent reductase. The model corresponds to the N-terminal NAD(P)-binding domain of GAPDH-like family proteins. It contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft.
Pssm-ID: 467613 [Multi-domain] Cd Length: 109 Bit Score: 73.16 E-value: 3.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 2 VKVGINGFGRIGRNVFRAALKNPDIEVVAVNGLTDantlahllkydsvhgrldaevsvngnnlvvngkeiivkaerdpen 81
Cdd:cd05192 1 IRVAINGFGRIGRIVFRAIADQDDLDVVAINDRRD--------------------------------------------- 35
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2DBV_P 82 lawgeigvdIVVESTGRFTKREDAAKHLEAGAKKVIISAPAKNEDITIVMGVNQDKYDPkAHHVISNASCTTNC 155
Cdd:cd05192 36 ---------VVIECTGSFTDDDNAEKHIKAGGKKAVITAPEKGDIPTIVVVLNELAKSA-GATVVSNANETSYS 99
|
|
| Asd |
COG0136 |
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ... |
61-263 |
3.13e-06 |
|
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: 48.10 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 61 GNNLVVNGKEIIVKaERDPENLAwgeiGVDIVVESTGRFTKREDAAKHLEAGAkkVII---SAPAKNEDITIVM-GVNQD 136
Cdd:COG0136 40 GKTVSFGGKELTVE-DATDFDFS----GVDIALFSAGGSVSKEYAPKAAAAGA--VVIdnsSAFRMDPDVPLVVpEVNPE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 137 ---KYDPKAhhVISNASCTTNCLAPFAKVLHEQFGIVRGMMTTVHSytndqrildASH------KDLRR-ARAAAESIIP 206
Cdd:COG0136 113 alaDHLPKG--IIANPNCSTIQMLVALKPLHDAAGIKRVVVSTYQA---------VSGagaaamDELAEqTAALLNGEEI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 207 TTTGAAKAVAL-VLP-------------ELKG-------------KLNGMAMRVPTPN---VSVvdlVAELEKEVTVEEV 256
Cdd:COG0136 182 EPEVFPHPIAFnLIPqidvflengytkeEMKMvnetrkilgdpdiPVSATCVRVPVFRghsEAV---NIEFERPVSLEEA 258
|
....*..
2DBV_P 257 NAALKAA 263
Cdd:COG0136 259 RELLAAA 265
|
|
| PRK14874 |
PRK14874 |
aspartate-semialdehyde dehydrogenase; Provisional |
67-171 |
2.39e-05 |
|
aspartate-semialdehyde dehydrogenase; Provisional
Pssm-ID: 237845 [Multi-domain] Cd Length: 334 Bit Score: 45.53 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 67 NGKEIIVK--AERDPEnlawgeiGVDIVVESTGRFTKREDAAKHLEAGAkkVII---SAPAKNEDIT-IVMGVN-QDKYD 139
Cdd:PRK14874 47 KGKELKVEdlTTFDFS-------GVDIALFSAGGSVSKKYAPKAAAAGA--VVIdnsSAFRMDPDVPlVVPEVNpEALAE 117
|
90 100 110
....*....|....*....|....*....|..
2DBV_P 140 PKAHHVISNASCTTNCLAPFAKVLHEQFGIVR 171
Cdd:PRK14874 118 HRKKGIIANPNCSTIQMVVALKPLHDAAGIKR 149
|
|
| PRK04207 |
PRK04207 |
type II glyceraldehyde-3-phosphate dehydrogenase; |
2-31 |
4.05e-04 |
|
type II glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 179786 [Multi-domain] Cd Length: 341 Bit Score: 41.74 E-value: 4.05e-04
10 20 30
....*....|....*....|....*....|
2DBV_P 2 VKVGINGFGRIGRNVFRAALKNPDIEVVAV 31
Cdd:PRK04207 2 IKVGVNGYGTIGKRVADAVAAQPDMELVGV 31
|
|
| meso-DAPDH_N |
cd02270 |
N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and ... |
3-31 |
6.54e-04 |
|
N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and similar proteins; Meso-DAPDH (EC 1.4.1.16), also called diaminopimelate dehydrogenase, or meso-DAP dehydrogenase, probably plays a role in lysine biosynthesis. It catalyzes the reversible NADP(H)-dependent reductive amination of L-2-amino-6-oxopimelate, the acyclic form of L-tetrahydrodipicolinate, to generate the meso compound, D,L-2,6-diaminopimelate. DAPDH is a homodimer which is highly specific for meso-DAP and NADP(+) as substrates. Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.
Pssm-ID: 467610 [Multi-domain] Cd Length: 151 Bit Score: 39.48 E-value: 6.54e-04
10 20
....*....|....*....|....*....
2DBV_P 3 KVGINGFGRIGRNVFRAALKNPDIEVVAV 31
Cdd:cd02270 2 RVAIVGYGNLGRGVEEAIQANPDMELVGV 30
|
|
| DapB_N |
pfam01113 |
Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the ... |
2-120 |
1.51e-03 |
|
Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the alpha,beta-unsaturated cyclic imine, dihydro-dipicolinate. This reaction is the second committed step in the biosynthesis of L-lysine and its precursor meso-diaminopimelate, which are critical for both protein and cell wall biosynthesis. The N-terminal domain of DapB binds the dinucleotide NADPH.
Pssm-ID: 460069 [Multi-domain] Cd Length: 121 Bit Score: 37.98 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 2 VKVGINGF-GRIGRNVFRAALKNPDIEVVAVnglTDANTLAHLLKYDSVHGRLDAEVSVNGNNLVVNGkEIIV---KAER 77
Cdd:pfam01113 1 IKIAVAGAsGRMGRELIKAVLEAPDLELVAA---VDRPGSSLLGSDAGELAPLGVPVTDDLEEVLADA-DVLIdftTPEA 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
2DBV_P 78 DPENLAW-GEIGVDIVVESTGrFTKREDAAkhLEAGAKK--VIISA 120
Cdd:pfam01113 77 TLENLEFaLKHGVPLVIGTTG-FTEEQLAE--LKEAAKKipIVIAP 119
|
|
| MviM |
COG0673 |
Predicted dehydrogenase [General function prediction only]; |
2-31 |
2.36e-03 |
|
Predicted dehydrogenase [General function prediction only];
Pssm-ID: 440437 [Multi-domain] Cd Length: 295 Bit Score: 39.14 E-value: 2.36e-03
10 20 30
....*....|....*....|....*....|
2DBV_P 2 VKVGINGFGRIGRNVFRAALKNPDIEVVAV 31
Cdd:COG0673 4 LRVGIIGAGGIGRAHAPALAALPGVELVAV 33
|
|
| GAPDH_II_N |
cd02278 |
N-terminal NAD(P)-binding domain of type II glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
2-31 |
6.15e-03 |
|
N-terminal NAD(P)-binding domain of type II 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 type II NADP+ utilizing GAPDHs mainly from archaea.
Pssm-ID: 467612 Cd Length: 171 Bit Score: 37.16 E-value: 6.15e-03
10 20 30
....*....|....*....|....*....|
2DBV_P 2 VKVGINGFGRIGRNVFRAALKNPDIEVVAV 31
Cdd:cd02278 1 IKVGVNGYGTIGKRVADAVLLQDDMELVGV 30
|
|
| GAPDH_II_C |
cd18127 |
C-terminal catalytic domain of type II glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
150-263 |
8.98e-03 |
|
C-terminal catalytic domain of type II 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 type II NADP+ utilizing GAPDHs, mainly from archaea.
Pssm-ID: 467677 Cd Length: 162 Bit Score: 36.41 E-value: 8.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 150 SCTTNCLAPFAKVLHEQFGIVRGMMTTVhsytndqrildashkdlRRA-------RAAAESIIPTTTGA---AKAVALVL 219
Cdd:cd18127 1 SCNTTGLSRVLKALDRAFGLKRVRATIV-----------------RRAadpgkhkKGVINAIVPEPKDPshhAPDVKTVF 63
|
90 100 110 120
....*....|....*....|....*....|....*....|....
2DBV_P 220 PELKgkLNGMAMRVPTPNVSVVDLVAELEKEVTVEEVNAALKAA 263
Cdd:cd18127 64 PDLD--ITTSAVKVPTTLMHLHTINVELKRKVSREEVLEALASN 105
|
|
| DHDPR_N |
cd02274 |
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; ... |
2-115 |
9.36e-03 |
|
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; DHDPR (EC 1.17.1.8), also called 4-hydroxy-tetrahydrodipicolinate reductase, or HTPA reductase, is a product of an essential gene referred to as dapB. It catalyzes the NAD(P)H-dependent reduction of 2,3-dihydrodipicolinate (DHDP) to 2,3,4,5-tetrahydrodipicolinate (THDP). DHDPR could also function as a dehydratase in addition to the role of a nucleotide dependent reductase. DHDPR is a component of the biosynthetic pathway that generates meso-diaminopimelate, a component of bacterial cell walls, and the amino acid L-lysine in various bacteria, archaea, cyanobacteria and higher plants. The enzyme is a homotetramer where each monomer is composed of two domains, an N-terminal NAD(P)-binding domain which forms a Rossmann fold, and a C-terminal substrate-binding domain that forms an open, mixed alpha-beta sandwich.
Pssm-ID: 467611 [Multi-domain] Cd Length: 139 Bit Score: 36.00 E-value: 9.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2DBV_P 2 VKVGINGF-GRIGRNVFRAALKNPDIEVVAVNGLTDANTLahllkydsvhGRLDAEVSVNGNNLVVNGKEIIVKAerdpe 80
Cdd:cd02274 1 IKVAVAGAtGRMGRELVKAILEAPDLELVGAVDRPGSGLL----------GGDAGGLAGIGTGVIVSLDLELAAA----- 65
|
90 100 110
....*....|....*....|....*....|....*
2DBV_P 81 nlawgeiGVDIVVEstgrFTKREDAAKHLEAGAKK 115
Cdd:cd02274 66 -------DADVVID----FTTPEATLENLEAAAKA 89
|
|
| |
