|
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: 555.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 1 MS-KVGINGFGRIGRLVLRRLLEVKSNIDVVAINDLTSPKILAYLLKHDSNYGPFPWSVDYTEDSLIVNGKSIAVYAEKE 79
Cdd:COG0057 1 MTiRVAINGFGRIGRLVLRALLERGPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 80 AKNIPWKAKGAEIIVECTGFYTSAEKSQAHLDAGAKKVLISAPA-GEMKTIVYNVNDDTLDGNDTIVSVASCTTNCLAPM 158
Cdd:COG0057 81 PAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAkGDDPTIVYGVNHDDYDADHRIISNASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 159 AKALHDSFGIEVGTMTTIHAYTGTQSLVDGPRgKDLRASRAAAENIIPHTTGAAKAIGLVIPELSGKLKGHAQRVPVKTG 238
Cdd:COG0057 161 AKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPH-KDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 239 SVTELVSILGKKVTAEEVNNALKKATNN--NESFGYTDEEIVSSDIIGSHFGSVFDATQTeiTAVGDlQLVKTVAWYDNE 316
Cdd:COG0057 240 SLVDLTVELEKETTVEEVNAALKEAAEGplKGILGYTEEPLVSSDFNGDPHSSIFDALQT--IVIGG-NLVKVLAWYDNE 316
|
330
....*....|....*..
gi 445970839 317 YGFVTQLIRTLEKFAKL 333
Cdd:COG0057 317 WGYSNRMVDLAEYMAKL 333
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
3-325 |
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: 516.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 3 KVGINGFGRIGRLVLRRLLEVKSN-IDVVAINDLTSPKILAYLLKHDSNYGPFPWSVDYTEDSLIVNGKSIAVYA-EKEA 80
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKPGNdLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEVISVFsERDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 81 KNIPWKAKGAEIIVECTGFYTSAEKSQAHLDAGAKKVLISAPA-GEMKTIVYNVNDDTLDGNDTIVSVASCTTNCLAPMA 159
Cdd:TIGR01534 81 SDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSkGDVKTIVYGVNHDEYDGEERIISNASCTTNCLAPLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 160 KALHDSFGIEVGTMTTIHAYTGTQSLVDGPRgKDLRASRAAAENIIPHTTGAAKAIGLVIPELSGKLKGHAQRVPVKTGS 239
Cdd:TIGR01534 161 KVLDEAFGIVSGLMTTVHAYTNDQNLLDGPH-KDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 240 VTELVSILGKKVTAEEVNNALKKATN--NNESFGYTDEEIVSSDIIGSHFGSVFDATQTEITAVGDLQlVKTVAWYDNEY 317
Cdd:TIGR01534 240 LVDLVVNLEKDVTVEEVNAALKEASEgeLKGVLGYTEDELVSSDFIGSPYSSIVDATATKVTGLGDSL-VKVYAWYDNEW 318
|
....*...
gi 445970839 318 GFVTQLIR 325
Cdd:TIGR01534 319 GYSNRLVD 326
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-325 |
5.29e-119 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 346.72 E-value: 5.29e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 1 MSKVGINGFGRIGRLVLRRLLEvKSNIDVVAINDLTSPKILAYLLKHDSNYGPFPWSVDYTEDSLIVNGKSIAVYAEKEA 80
Cdd:PRK07729 2 KTKVAINGFGRIGRMVFRKAIK-ESAFEIVAINASYPSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 81 KNIPWKAKGAEIIVECTGFYTSAEKSQAHLDAGAKKVLISAPA-GEMKTIVYNVNDDTLD-GNDTIVSVASCTTNCLAPM 158
Cdd:PRK07729 81 KELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGkNEDVTIVVGVNEDQLDiEKHTIISNASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 159 AKALHDSFGIEVGTMTTIHAYTGTQSLVDGPRgKDLRASRAAAENIIPHTTGAAKAIGLVIPELSGKLKGHAQRVPVKTG 238
Cdd:PRK07729 161 VKVLDEQFGIENGLMTTVHAYTNDQKNIDNPH-KDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 239 SVTELVSILGKKVTAEEVNNALKKATNNNES--FGYTDEEIVSSDIIGSHFGSVFDATQTEItaVGDLQlVKTVAWYDNE 316
Cdd:PRK07729 240 SLVDLVVDVKRDVTVEEINEAFKTAANGALKgiLEFSEEPLVSIDFNTNTHSAIIDGLSTMV--MGDRK-VKVLAWYDNE 316
|
330
....*....|..
gi 445970839 317 YGF---VTQLIR 325
Cdd:PRK07729 317 WGYscrVVDLVT 328
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
4-324 |
1.93e-105 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 311.48 E-value: 1.93e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 4 VGINGFGRIGRLVLRRLLEvKSNIDVVAINDL-TSPKILAYLLKHDSNYGPFPWSVDYTEDSLIVNGKSIAVYAEKEAKN 82
Cdd:NF033735 1 IGINGFGRIGRLALRALWG-RPGLEIVHINDLaGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 83 IPWKAkGAEIIVECTGFYTSAEKSQAHLDAGAKKVLISAP--AGEMKTIVYNVNDDTLDGN-DTIVSVASCTTNCLAPMA 159
Cdd:NF033735 80 TPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPArHRIVTAASCTTNCLAPVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 160 KALHDSFGIEVGTMTTIHAYTGTQSLVDGPRgKDLRASRAAAENIIPHTTGAAKAIGLVIPELSGKLKGHAQRVPVKTGS 239
Cdd:NF033735 159 KVIHEKIGIKHGSITTIHDITNTQTIVDAPH-KDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNAS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 240 VTELVSILGKKVTAEEVNNALKKATNN--NESFGYTDEEIVSSDIIGSHFGSVFDATQTEITavgDLQLVKTVAWYDNEY 317
Cdd:NF033735 238 LTDCVFEVERPTTVEEVNALFKAAAEGplKGILGYEERPLVSVDYVNDPRSSIIDALSTMVV---NGTQVKIYAWYDNEW 314
|
....*..
gi 445970839 318 GFVTQLI 324
Cdd:NF033735 315 GYANRMV 321
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
150-316 |
4.06e-97 |
|
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (1.2.1.12), NADP (1.2.1.13) or either (1.2.1.59). The family corresponds to the ubiquitous NAD+ or NADP+ utilizing type I GAPDH and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose.
Pssm-ID: 467676 Cd Length: 165 Bit Score: 284.35 E-value: 4.06e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 150 CTTNCLAPMAKALHDSFGIEVGTMTTIHAYTGTQSLVDGPRgKDLRASRAAAENIIPHTTGAAKAIGLVIPELSGKLKGH 229
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 230 AQRVPVKTGSVTELVSILGKKVTAEEVNNALKKATNNN--ESFGYTDEEIVSSDIIGSHFGSVFDATQTEitaVGDLQLV 307
Cdd:cd18126 80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPlkGILGYTEDPLVSSDFVGDPHSSIFDATATI---VLGGNLV 156
|
....*....
gi 445970839 308 KTVAWYDNE 316
Cdd:cd18126 157 KVVAWYDNE 165
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-150 |
5.01e-75 |
|
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: 227.43 E-value: 5.01e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 3 KVGINGFGRIGRLVLRRLLEvKSNIDVVAINDLTSPKILAYLLKHDSNYGPFPWSVDYTEDSLIVNGKSIAVYAEKEAKN 82
Cdd:smart00846 2 KVGINGFGRIGRLVLRAALE-RPDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPAN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445970839 83 IPWKAKGAEIIVECTGFYTSAEKSQAHLDAGAKKVLISAP-AGEMKTIVYNVNDDTLDGNDTIVSVASC 150
Cdd:smart00846 81 LPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPsKDADPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
155-313 |
2.93e-72 |
|
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. C-terminal domain is a mixed alpha/antiparallel beta fold.
Pssm-ID: 460700 Cd Length: 158 Bit Score: 220.93 E-value: 2.93e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 155 LAPMAKALHDSFGIEVGTMTTIHAYTGTQSLVDGPRGKDLRASRAAAENIIPHTTGAAKAIGLVIPELSGKLKGHAQRVP 234
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 235 VKTGSVTELVSILGKKVTAEEVNNALKKATNN--NESFGYTDEEIVSSDIIGSHFGSVFDATQTEitaVGDLQLVKTVAW 312
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGalKGILSYTEDPLVSSDFIGDPHSSIFDAKETI---VVNGNFVKVVAW 157
|
.
gi 445970839 313 Y 313
Cdd:pfam02800 158 Y 158
|
|
| |
|
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: 555.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 1 MS-KVGINGFGRIGRLVLRRLLEVKSNIDVVAINDLTSPKILAYLLKHDSNYGPFPWSVDYTEDSLIVNGKSIAVYAEKE 79
Cdd:COG0057 1 MTiRVAINGFGRIGRLVLRALLERGPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 80 AKNIPWKAKGAEIIVECTGFYTSAEKSQAHLDAGAKKVLISAPA-GEMKTIVYNVNDDTLDGNDTIVSVASCTTNCLAPM 158
Cdd:COG0057 81 PAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAkGDDPTIVYGVNHDDYDADHRIISNASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 159 AKALHDSFGIEVGTMTTIHAYTGTQSLVDGPRgKDLRASRAAAENIIPHTTGAAKAIGLVIPELSGKLKGHAQRVPVKTG 238
Cdd:COG0057 161 AKVLNDAFGIEKGLMTTIHAYTNDQNLLDAPH-KDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 239 SVTELVSILGKKVTAEEVNNALKKATNN--NESFGYTDEEIVSSDIIGSHFGSVFDATQTeiTAVGDlQLVKTVAWYDNE 316
Cdd:COG0057 240 SLVDLTVELEKETTVEEVNAALKEAAEGplKGILGYTEEPLVSSDFNGDPHSSIFDALQT--IVIGG-NLVKVLAWYDNE 316
|
330
....*....|....*..
gi 445970839 317 YGFVTQLIRTLEKFAKL 333
Cdd:COG0057 317 WGYSNRMVDLAEYMAKL 333
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
3-325 |
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: 516.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 3 KVGINGFGRIGRLVLRRLLEVKSN-IDVVAINDLTSPKILAYLLKHDSNYGPFPWSVDYTEDSLIVNGKSIAVYA-EKEA 80
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKPGNdLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEVISVFsERDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 81 KNIPWKAKGAEIIVECTGFYTSAEKSQAHLDAGAKKVLISAPA-GEMKTIVYNVNDDTLDGNDTIVSVASCTTNCLAPMA 159
Cdd:TIGR01534 81 SDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSkGDVKTIVYGVNHDEYDGEERIISNASCTTNCLAPLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 160 KALHDSFGIEVGTMTTIHAYTGTQSLVDGPRgKDLRASRAAAENIIPHTTGAAKAIGLVIPELSGKLKGHAQRVPVKTGS 239
Cdd:TIGR01534 161 KVLDEAFGIVSGLMTTVHAYTNDQNLLDGPH-KDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 240 VTELVSILGKKVTAEEVNNALKKATN--NNESFGYTDEEIVSSDIIGSHFGSVFDATQTEITAVGDLQlVKTVAWYDNEY 317
Cdd:TIGR01534 240 LVDLVVNLEKDVTVEEVNAALKEASEgeLKGVLGYTEDELVSSDFIGSPYSSIVDATATKVTGLGDSL-VKVYAWYDNEW 318
|
....*...
gi 445970839 318 GFVTQLIR 325
Cdd:TIGR01534 319 GYSNRLVD 326
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-325 |
5.29e-119 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 346.72 E-value: 5.29e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 1 MSKVGINGFGRIGRLVLRRLLEvKSNIDVVAINDLTSPKILAYLLKHDSNYGPFPWSVDYTEDSLIVNGKSIAVYAEKEA 80
Cdd:PRK07729 2 KTKVAINGFGRIGRMVFRKAIK-ESAFEIVAINASYPSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 81 KNIPWKAKGAEIIVECTGFYTSAEKSQAHLDAGAKKVLISAPA-GEMKTIVYNVNDDTLD-GNDTIVSVASCTTNCLAPM 158
Cdd:PRK07729 81 KELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGkNEDVTIVVGVNEDQLDiEKHTIISNASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 159 AKALHDSFGIEVGTMTTIHAYTGTQSLVDGPRgKDLRASRAAAENIIPHTTGAAKAIGLVIPELSGKLKGHAQRVPVKTG 238
Cdd:PRK07729 161 VKVLDEQFGIENGLMTTVHAYTNDQKNIDNPH-KDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 239 SVTELVSILGKKVTAEEVNNALKKATNNNES--FGYTDEEIVSSDIIGSHFGSVFDATQTEItaVGDLQlVKTVAWYDNE 316
Cdd:PRK07729 240 SLVDLVVDVKRDVTVEEINEAFKTAANGALKgiLEFSEEPLVSIDFNTNTHSAIIDGLSTMV--MGDRK-VKVLAWYDNE 316
|
330
....*....|..
gi 445970839 317 YGF---VTQLIR 325
Cdd:PRK07729 317 WGYscrVVDLVT 328
|
|
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
2-331 |
5.51e-115 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 339.14 E-value: 5.51e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 2 SKVGINGFGRIGRLVLRrLLEVKSNIDVVAIND-LTSPKILAYLLKHDSNYGPFPWSVDYTEDS-LIVNGKSIAVYAEKE 79
Cdd:PLN02272 86 TKIGINGFGRIGRLVLR-IATSRDDIEVVAVNDpFIDAKYMAYMFKYDSTHGNFKGTINVVDDStLEINGKQIKVTSKRD 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 80 AKNIPWKAKGAEIIVECTGFYTSAEKSQAHLDAGAKKVLISAPAGEMKTIVYNVNDDTLDGNDTIVSVASCTTNCLAPMA 159
Cdd:PLN02272 165 PAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 160 KALHDSFGIEVGTMTTIHAYTGTQSLVDGPRGKDLRASRAAAENIIPHTTGAAKAIGLVIPELSGKLKGHAQRVPVKTGS 239
Cdd:PLN02272 245 KVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVS 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 240 VTELVSILGKKVTAEEVNNALKKATNN--NESFGYTDEEIVSSDIIGSHFGSVFDATqteiTAVG-DLQLVKTVAWYDNE 316
Cdd:PLN02272 325 VVDLTCRLEKSASYEDVKAAIKYASEGplKGILGYTDEDVVSNDFVGDSRSSIFDAK----AGIGlSASFMKLVSWYDNE 400
|
330
....*....|....*
gi 445970839 317 YGFVTQLIRTLEKFA 331
Cdd:PLN02272 401 WGYSNRVLDLIEHMA 415
|
|
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
3-324 |
1.32e-110 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 325.25 E-value: 1.32e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 3 KVGINGFGRIGRLVLRRLLEvKSNIDVVAIND-LTSPKILAYLLKHDSNYGPFPWSVDYTEDSLIVNGKSIAVYAEKEAK 81
Cdd:PTZ00023 4 KLGINGFGRIGRLVFRAALE-REDVEVVAINDpFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKDPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 82 NIPWKAKGAEIIVECTGFYTSAEKSQAHLDAGAKKVLISAPAGEMKTI-VYNVNDDTLDGNDTIVSVASCTTNCLAPMAK 160
Cdd:PTZ00023 83 AIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKDDTPIyVMGVNHTQYDKSQRIVSNASCTTNCLAPLAK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 161 ALHDSFGIEVGTMTTIHAYTGTQSLVDGPR--GKDLRASRAAAENIIPHTTGAAKAIGLVIPELSGKLKGHAQRVPVKTG 238
Cdd:PTZ00023 163 VVNDKFGIVEGLMTTVHASTANQLTVDGPSkgGKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVPDV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 239 SVTELVSILGKKVTAEEVNNALKKATNNNES--FGYTDEEIVSSDIIGSHFGSVFDATQTeiTAVGDlQLVKTVAWYDNE 316
Cdd:PTZ00023 243 SVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKgiLGYTDDEVVSSDFVHDKRSSIFDVKAG--IALND-TFVKLVSWYDNE 319
|
....*...
gi 445970839 317 YGFVTQLI 324
Cdd:PTZ00023 320 WGYSNRLL 327
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
1-332 |
1.92e-106 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 314.54 E-value: 1.92e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 1 MSKVGINGFGRIGRLVLRRLL-EVKSNIDVVAINDLTSPKILAYLLKHDSNYGPFPWSVDYTEDSLIVNGKSIAVYAEKE 79
Cdd:PRK07403 1 MIRVAINGFGRIGRNFLRCWLgRENSQLELVAINDTSDPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 80 AKNIPWKAKGAEIIVECTGFYTSAEKSQAHLDAGAKKVLISAPA--GEMKTIVYNVNDDTLDGND-TIVSVASCTTNCLA 156
Cdd:PRK07403 81 PLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPGkgEDIGTYVVGVNHHEYDHEDhNIISNASCTTNCLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 157 PMAKALHDSFGIEVGTMTTIHAYTGTQSLVDGPRgKDLRASRAAAENIIPHTTGAAKAIGLVIPELSGKLKGHAQRVPVK 236
Cdd:PRK07403 161 PIAKVLHDNFGIIKGTMTTTHSYTGDQRILDASH-RDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 237 TGSVTELVSILGKKVTAEEVNNALKKATNNNES--FGYTDEEIVSSDIIGSHFGSVFDATqteITAVGDLQLVKTVAWYD 314
Cdd:PRK07403 240 NVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKgiLEYSDLPLVSSDYRGTDASSIVDAS---LTMVMGGDMVKVIAWYD 316
|
330
....*....|....*...
gi 445970839 315 NEYGFVTQLIRTLEKFAK 332
Cdd:PRK07403 317 NEWGYSQRVVDLAELVAR 334
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
4-324 |
1.93e-105 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 311.48 E-value: 1.93e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 4 VGINGFGRIGRLVLRRLLEvKSNIDVVAINDL-TSPKILAYLLKHDSNYGPFPWSVDYTEDSLIVNGKSIAVYAEKEAKN 82
Cdd:NF033735 1 IGINGFGRIGRLALRALWG-RPGLEIVHINDLaGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 83 IPWKAkGAEIIVECTGFYTSAEKSQAHLDAGAKKVLISAP--AGEMKTIVYNVNDDTLDGN-DTIVSVASCTTNCLAPMA 159
Cdd:NF033735 80 TPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPArHRIVTAASCTTNCLAPVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 160 KALHDSFGIEVGTMTTIHAYTGTQSLVDGPRgKDLRASRAAAENIIPHTTGAAKAIGLVIPELSGKLKGHAQRVPVKTGS 239
Cdd:NF033735 159 KVIHEKIGIKHGSITTIHDITNTQTIVDAPH-KDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNAS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 240 VTELVSILGKKVTAEEVNNALKKATNN--NESFGYTDEEIVSSDIIGSHFGSVFDATQTEITavgDLQLVKTVAWYDNEY 317
Cdd:NF033735 238 LTDCVFEVERPTTVEEVNALFKAAAEGplKGILGYEERPLVSVDYVNDPRSSIIDALSTMVV---NGTQVKIYAWYDNEW 314
|
....*..
gi 445970839 318 GFVTQLI 324
Cdd:NF033735 315 GYANRMV 321
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
150-316 |
4.06e-97 |
|
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (1.2.1.12), NADP (1.2.1.13) or either (1.2.1.59). The family corresponds to the ubiquitous NAD+ or NADP+ utilizing type I GAPDH and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose.
Pssm-ID: 467676 Cd Length: 165 Bit Score: 284.35 E-value: 4.06e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 150 CTTNCLAPMAKALHDSFGIEVGTMTTIHAYTGTQSLVDGPRgKDLRASRAAAENIIPHTTGAAKAIGLVIPELSGKLKGH 229
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 230 AQRVPVKTGSVTELVSILGKKVTAEEVNNALKKATNNN--ESFGYTDEEIVSSDIIGSHFGSVFDATQTEitaVGDLQLV 307
Cdd:cd18126 80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPlkGILGYTEDPLVSSDFVGDPHSSIFDATATI---VLGGNLV 156
|
....*....
gi 445970839 308 KTVAWYDNE 316
Cdd:cd18126 157 KVVAWYDNE 165
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
1-326 |
5.50e-97 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 290.42 E-value: 5.50e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 1 MSKVGINGFGRIGRLVLRRLLEV--KSNIDVVAINDLTSPKILAYLLKHDSNYGPFPWSVDYTEDSLIVNGKSIAVYAEK 78
Cdd:PRK13535 1 TIRVAINGFGRIGRNVLRALYESgrRAEITVVAINELADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 79 EAKNIPWKAKGAEIIVECTGFYTSAEKSQAHLDAGAKKVLISAPAGEM--KTIVYNVNDDTLDGNDTIVSVASCTTNCLA 156
Cdd:PRK13535 81 DIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSNDldATVVYGVNHDQLRAEHRIVSNASCTTNCII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 157 PMAKALHDSFGIEVGTMTTIHAYTGTQSLVDGPRgKDLRASRAAAENIIPHTTGAAKAIGLVIPELSGKLKGHAQRVPvk 236
Cdd:PRK13535 161 PVIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYH-PDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVP-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 237 TGSVT--ELVSILGKKVTAEEVNNALKKATNNneSF----GYTDEEIVSSDIIGSHFGSVFDATQTEitaVGDLQLVKTV 310
Cdd:PRK13535 238 TINVTaiDLSVTVKKPVKVNEVNQLLQKAAQG--AFhgivDYTELPLVSIDFNHDPHSAIVDGTQTR---VSGAHLIKTL 312
|
330
....*....|....*.
gi 445970839 311 AWYDNEYGFVTQLIRT 326
Cdd:PRK13535 313 VWCDNEWGFANRMLDT 328
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
3-325 |
1.13e-95 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 288.11 E-value: 1.13e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 3 KVGINGFGRIGRLVLRRLLE---VKSNIDVVAINDL-TSPKILAYLLKHDSNYGPFPWSVDYTE--------DSLIVNGK 70
Cdd:PTZ00434 5 KVGINGFGRIGRMVFQAICDqglIGTEIDVVAVVDMsTNAEYFAYQMKYDTVHGRPKYTVETTKsspsvktdDVLVVNGH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 71 SI-AVYAEKEAKNIPWKAKGAEIIVECTGFYTSAEKSQAHLDAGAKKVLISAPA-GEMKTIVYNVNDDTLDGNDT-IVSV 147
Cdd:PTZ00434 85 RIkCVKAQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPAsGGAKTIVMGVNQHEYSPTEHhVVSN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 148 ASCTTNCLAPMAKAL-HDSFGIEVGTMTTIHAYTGTQSLVDGPRGKDLRASRAAAENIIPHTTGAAKAIGLVIPELSGKL 226
Cdd:PTZ00434 165 ASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGKL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 227 KGHAQRVPVKTGSVTELVSILGKKVTAEEVNNALKKATNN--NESFGYTDEEIVSSDIIGSHFGSVFDATQT-EITAVGD 303
Cdd:PTZ00434 245 TGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTymKGILGFTDDELVSADFINDNRSSIYDSKATlQNNLPGE 324
|
330 340
....*....|....*....|....*
gi 445970839 304 LQLVKTVAWYDNEYGF---VTQLIR 325
Cdd:PTZ00434 325 RRFFKIVSWYDNEWGYshrVVDLVR 349
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
3-332 |
8.99e-91 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 274.30 E-value: 8.99e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 3 KVGINGFGRIGRLVLRRLlEVKSNIDVVAINDLTSPKILAYLLKHDSNYGPFPWSVDYTEDSLIVNGKSIAVYAEKEAKN 82
Cdd:PRK15425 4 KVGINGFGRIGRIVFRAA-QKRSDIEIVAINDLLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPAN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 83 IPWKAKGAEIIVECTGFYTSAEKSQAHLDAGAKKVLISAPAGE-MKTIVYNVNDDTLDGNDtIVSVASCTTNCLAPMAKA 161
Cdd:PRK15425 83 LKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDnTPMFVKGANFDKYAGQD-IVSNASCTTNCLAPLAKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 162 LHDSFGIEVGTMTTIHAYTGTQSLVDGPRGKDLRASRAAAENIIPHTTGAAKAIGLVIPELSGKLKGHAQRVPVKTGSVT 241
Cdd:PRK15425 162 INDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 242 ELVSILGKKVTAEEVNNALKKATNNNES--FGYTDEEIVSSDIIGSHFGSVFDATQTeiTAVGDlQLVKTVAWYDNEYGF 319
Cdd:PRK15425 242 DLTVRLEKAATYEQIKAAVKAAAEGEMKgvLGYTEDDVVSTDFNGEVCTSVFDAKAG--IALND-NFVKLVSWYDNETGY 318
|
330
....*....|...
gi 445970839 320 VTQLIRTLEKFAK 332
Cdd:PRK15425 319 SNKVLDLIAHISK 331
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
3-319 |
1.17e-90 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 276.43 E-value: 1.17e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 3 KVGINGFGRIGRLVLRRLLEVK-SNIDVVAINDLTSPKILAYLLKHDSNYGPFPWSVDYTEDSLI-VNGKSIAVYAEKEA 80
Cdd:PLN03096 62 KVAINGFGRIGRNFLRCWHGRKdSPLDVVAINDTGGVKQASHLLKYDSTLGTFDADVKPVGDDAIsVDGKVIKVVSDRNP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 81 KNIPWKAKGAEIIVECTGFYTSAEKSQAHLDAGAKKVLISAPA-GEMKTIVYNVNDDTLDGNDTIVSVASCTTNCLAPMA 159
Cdd:PLN03096 142 LNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGkGDIPTYVVGVNADDYKHSDPIISNASCTTNCLAPFV 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 160 KALHDSFGIEVGTMTTIHAYTGTQSLVDGPRgKDLRASRAAAENIIPHTTGAAKAIGLVIPELSGKLKGHAQRVPVKTGS 239
Cdd:PLN03096 222 KVLDQKFGIIKGTMTTTHSYTGDQRLLDASH-RDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVS 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 240 VTELVSILGKKVTAEEVNNALKKATNN--NESFGYTDEEIVSSDIIGSHFGSVFDATQTEItaVGDlQLVKTVAWYDNEY 317
Cdd:PLN03096 301 VVDLVVQVEKKTFAEEVNAAFRDAAEKelKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMV--MGD-DMVKVVAWYDNEW 377
|
..
gi 445970839 318 GF 319
Cdd:PLN03096 378 GY 379
|
|
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
3-328 |
3.22e-89 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 270.45 E-value: 3.22e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 3 KVGINGFGRIGRLVLRRLLEvKSNIDVVAINDLTS-PKILAYLLKHDSNYGPFPWSVDYTEDSLIVNGKSIAVYAEKEAK 81
Cdd:PRK08955 4 KVGINGFGRIGRLALRAAWD-WPELEFVQINDPAGdAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKAIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 82 NIPWKakGAEIIVECTGFYTSAEKSQAHLDAGAKKVLISAPAGE--MKTIVYNVNDDTLD-GNDTIVSVASCTTNCLAPM 158
Cdd:PRK08955 83 DTDWS--GCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEegVLNIVMGVNDHLFDpAIHPIVTAASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 159 AKALHDSFGIEVGTMTTIHAYTGTQSLVDGPRgKDLRASRAAAENIIPHTTGAAKAIGLVIPELSGKLKGHAQRVPVKTG 238
Cdd:PRK08955 161 VKVIHEKLGIKHGSMTTIHDLTNTQTILDAPH-KDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLANA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 239 SVTELVSILGKKVTAEEVNNALKKATNN--NESFGYTDEEIVSSDIIGSHFGSVFDATQTEItaVGDLQlVKTVAWYDNE 316
Cdd:PRK08955 240 SLTDCVFEVERDTTVEEVNALLKEAAEGelKGILGYEERPLVSIDYKTDPRSSIVDALSTMV--VNGTQ-VKLYAWYDNE 316
|
330
....*....|..
gi 445970839 317 YGFVTqliRTLE 328
Cdd:PRK08955 317 WGYAN---RTAE 325
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
3-324 |
6.92e-86 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 265.61 E-value: 6.92e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 3 KVGINGFGRIGRLVLRRLLEVK-SNIDVVAINDLTSPKILAYLLKHDSNYGPFPWSVDYTEDSLI-VNGKSIAVYAEKEA 80
Cdd:PLN02237 77 KVAINGFGRIGRNFLRCWHGRKdSPLDVVVVNDSGGVKNASHLLKYDSMLGTFKADVKIVDDETIsVDGKPIKVVSNRDP 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 81 KNIPWKAKGAEIIVECTGFYTSAEKSQAHLDAGAKKVLISAPA--GEMKTIVYNVNDDTLDGNDT-IVSVASCTTNCLAP 157
Cdd:PLN02237 157 LKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAkgADIPTYVVGVNEDDYDHEVAnIVSNASCTTNCLAP 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 158 MAKALHDSFGIEVGTMTTIHAYTGTQSLVDGPRgKDLRASRAAAENIIPHTTGAAKAIGLVIPELSGKLKGHAQRVPVKT 237
Cdd:PLN02237 237 FVKVLDEEFGIVKGTMTTTHSYTGDQRLLDASH-RDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTPN 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 238 GSVTELVSILGKK-VTAEEVNNALKKATNNNES--FGYTDEEIVSSDIIGSHFGSVFDATQTEItaVGDlQLVKTVAWYD 314
Cdd:PLN02237 316 VSVVDLVVNVEKKgITAEDVNAAFRKAADGPLKgiLAVCDVPLVSVDFRCSDVSSTIDASLTMV--MGD-DMVKVVAWYD 392
|
330
....*....|
gi 445970839 315 NEYGFVTQLI 324
Cdd:PLN02237 393 NEWGYSQRVV 402
|
|
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
3-332 |
5.32e-85 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 260.04 E-value: 5.32e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 3 KVGINGFGRIGRLVLRRLLEvKSNIDVVAIND-LTSPKILAYLLKHDSNYGPFPWSVDYTED--SLIVNGKSIAVYAEKE 79
Cdd:PLN02358 7 RIGINGFGRIGRLVARVVLQ-RDDVELVAVNDpFITTEYMTYMFKYDSVHGQWKHHELKVKDdkTLLFGEKPVTVFGIRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 80 AKNIPWKAKGAEIIVECTGFYTSAEKSQAHLDAGAKKVLISAPAGEMKTIVYNVNDDTLDGNDTIVSVASCTTNCLAPMA 159
Cdd:PLN02358 86 PEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCTTNCLAPLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 160 KALHDSFGIEVGTMTTIHAYTGTQSLVDGPRGKDLRASRAAAENIIPHTTGAAKAIGLVIPELSGKLKGHAQRVPVKTGS 239
Cdd:PLN02358 166 KVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 240 VTELVSILGKKVTAEEVNNALKKATNNNES--FGYTDEEIVSSDIIGSHFGSVFDATQTeiTAVGDlQLVKTVAWYDNEY 317
Cdd:PLN02358 246 VVDLTVRLEKAATYDEIKKAIKEESEGKLKgiLGYTEDDVVSTDFVGDNRSSIFDAKAG--IALSD-KFVKLVSWYDNEW 322
|
330
....*....|....*
gi 445970839 318 GFVTQLIRTLEKFAK 332
Cdd:PLN02358 323 GYSSRVVDLIVHMSK 337
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
150-316 |
3.41e-84 |
|
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: 251.38 E-value: 3.41e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 150 CTTNCLAPMAKALHDSFGIEVGTMTTIHAYTGTQSLVDGPRGKDLRASRAAAENIIPHTTGAAKAIGLVIPELSGKLKGH 229
Cdd:cd18123 1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 230 AQRVPVKTGSVTELVSILGKKVTAEEVNNALKKATNNNESFGYTDEEIVSSDIIGSHFGSVFDATQTEitaVGDLQLVKT 309
Cdd:cd18123 81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEGKGRLGYTEAEDVSSDFRGDIFESVFDAESII---AVNDNEVKL 157
|
....*..
gi 445970839 310 VAWYDNE 316
Cdd:cd18123 158 MQWYDNE 164
|
|
| GAPDH_I_N |
cd05214 |
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
3-149 |
1.13e-80 |
|
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: 242.30 E-value: 1.13e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 3 KVGINGFGRIGRLVLRRLLEvKSNIDVVAINDLTSPKILAYLLKHDSNYGPFPWSVDYTEDSLIVNGKSIAVYAEKEAKN 82
Cdd:cd05214 2 KVGINGFGRIGRLVFRAALE-RDDIEVVAINDLTDDETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 445970839 83 IPWKAKGAEIIVECTGFYTSAEKSQAHLDAGAKKVLISAPA-GEMKTIVYNVNDDTLDGNDTIVSVAS 149
Cdd:cd05214 81 LPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAkDDDPTIVMGVNHDKYDADDKIISNAS 148
|
|
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
8-333 |
1.20e-79 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 250.61 E-value: 1.20e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 8 GFGRIGRLVLRRLLE---VKSNIDVVAI-------NDLTSPkilAYLLKHDSNYGPFPWS--VDYTEDSLIVNGKSIAV- 74
Cdd:PRK08289 134 GFGRIGRLLARLLIEktgGGNGLRLRAIvvrkgseGDLEKR---ASLLRRDSVHGPFNGTitVDEENNAIIANGNYIQVi 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 75 YAEKEAkNIPWKAKGAE--IIVECTGFYTSAEKSQAHLDA-GAKKVLISAPA-GEMKTIVYNVNDDTLDGNDTIVSVASC 150
Cdd:PRK08289 211 YANSPE-EVDYTAYGINnaLVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGkGDIKNIVHGVNHSDITDEDKIVSAASC 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 151 TTNCLAPMAKALHDSFGIEVGTMTTIHAYTGTQSLVDGPRGKDlRASRAAAENIIPHTTGAAKAIGLVIPELSGKLKGHA 230
Cdd:PRK08289 290 TTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKGD-RRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNA 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 231 QRVPVKTGSVTELVSILGKKVTAEEVNNALKKATNNNE---SFGYTDE-EIVSSDIIGSHFGSVFDAtqtEITAVGDLQL 306
Cdd:PRK08289 369 IRVPTPNVSMAILNLNLEKETSREELNEYLRQMSLHSPlqnQIDYTDStEVVSSDFVGSRHAGVVDS---QATIVNGNRA 445
|
330 340
....*....|....*....|....*..
gi 445970839 307 VKTVaWYDNEYGFVTQLIRTLEKFAKL 333
Cdd:PRK08289 446 VLYV-WYDNEFGYSCQVVRVMEQMAGV 471
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-150 |
5.01e-75 |
|
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: 227.43 E-value: 5.01e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 3 KVGINGFGRIGRLVLRRLLEvKSNIDVVAINDLTSPKILAYLLKHDSNYGPFPWSVDYTEDSLIVNGKSIAVYAEKEAKN 82
Cdd:smart00846 2 KVGINGFGRIGRLVLRAALE-RPDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPAN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 445970839 83 IPWKAKGAEIIVECTGFYTSAEKSQAHLDAGAKKVLISAP-AGEMKTIVYNVNDDTLDGNDTIVSVASC 150
Cdd:smart00846 81 LPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPsKDADPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
155-313 |
2.93e-72 |
|
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. C-terminal domain is a mixed alpha/antiparallel beta fold.
Pssm-ID: 460700 Cd Length: 158 Bit Score: 220.93 E-value: 2.93e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 155 LAPMAKALHDSFGIEVGTMTTIHAYTGTQSLVDGPRGKDLRASRAAAENIIPHTTGAAKAIGLVIPELSGKLKGHAQRVP 234
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 235 VKTGSVTELVSILGKKVTAEEVNNALKKATNN--NESFGYTDEEIVSSDIIGSHFGSVFDATQTEitaVGDLQLVKTVAW 312
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGalKGILSYTEDPLVSSDFIGDPHSSIFDAKETI---VVNGNFVKVVAW 157
|
.
gi 445970839 313 Y 313
Cdd:pfam02800 158 Y 158
|
|
| GAPDH_N_E4PDH |
cd17892 |
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
3-149 |
5.18e-56 |
|
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: 179.77 E-value: 5.18e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 3 KVGINGFGRIGRLVLRRLLE--VKSNIDVVAINDLTSPKILAYLLKHDSNYGPFPWSVDYTEDSLIVNGKSIAVYAEKEA 80
Cdd:cd17892 2 RVAINGYGRIGRNVLRALYEsgRRAEFQVVAINELADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPDP 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 445970839 81 KNIPWKAKGAEIIVECTGFYTSAEKSQAHLDAGAKKVLISAPAGEM--KTIVYNVNDDTLDGNDTIVSVAS 149
Cdd:cd17892 82 ENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASNDvdATIVYGINQDLLRAEHRIVSNAS 152
|
|
| Gp_dh_N |
pfam00044 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-103 |
7.07e-50 |
|
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: 161.50 E-value: 7.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 3 KVGINGFGRIGRLVLRRLLEvKSNIDVVAINDLTSPKILAYLLKHDSNYGPFPWSVDYTEDSLIVNGKSIAVYAEKEAKN 82
Cdd:pfam00044 2 KVGINGFGRIGRLVLRAALE-RPDIEVVAINDLTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAE 80
|
90 100
....*....|....*....|.
gi 445970839 83 IPWKAKGAEIIVECTGFYTSA 103
Cdd:pfam00044 81 LPWGDLGVDVVIESTGVFTTK 101
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
4-324 |
5.60e-49 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 166.97 E-value: 5.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 4 VGINGFGRIGRLVLRRLLeVKSNIDVVAINDLT-SPKILAYLLKHDSNY-GPFPWSVDYTEDSLIVNG-KSIAVYAEKEA 80
Cdd:PTZ00353 5 VGINGFGPVGKAVLFASL-TDPLVTVVAVNDASvSIAYIAYVLEQESPLsAPDGASIRVVGEQIVLNGtQKIRVSAKHDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 81 KNIPWKAKGAEIIVECTGFYTSAEKSQAHLDAGAKKVLISAPAGEMKTIVYNVNDDTLDGNDTIVSVASCTTNCLAPMAK 160
Cdd:PTZ00353 84 VEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDERLSASLPVCCAGAPIAVALAPVIR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 161 ALHDSFGIEVGTMTTIHAY-----TGTQSlvDGPRgkDLRASRAAAENIIPHTTGAAKAIGLVIPELSGKLKGHAQRVPV 235
Cdd:PTZ00353 164 ALHEVYGVEECSYTAIHGMqpqepIAARS--KNSQ--DWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 236 KTGSVTELVSILGKKVTAEEVNNALKKATNNNES--FGYTDEEIVSSDIIGShfGSV-FDATQTEITAVGDLQlvKTVAW 312
Cdd:PTZ00353 240 KKGCAIDMLVRTKQPVSKEVVDSALAEAASDRLNgvLCISKRDMISVDCIPN--GKLcYDATSSSSSREGEVH--KMVLW 315
|
330
....*....|..
gi 445970839 313 YDNEYGFVTQLI 324
Cdd:PTZ00353 316 FDVECYYAARLL 327
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
150-316 |
1.35e-40 |
|
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: 139.86 E-value: 1.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 150 CTTNCLAPMAKALHDSFGIEVGTMTTIHAYTGTQSLVDGPRgKDLRASRAAAENIIPHTTGAAKAIGLVIPELSGKLKGH 229
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDAYH-PDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 230 AQRVPVKTGSVTELVSILGKKVTAEEVNNALKKATNNNES--FGYTDEEIVSSDIIGSHFGSVFDATQTEitaVGDLQLV 307
Cdd:cd23937 80 AVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKgiLGYTEEPLVSVDFNHDPHSCIVDGTQTR---VSGKRLV 156
|
....*....
gi 445970839 308 KTVAWYDNE 316
Cdd:cd23937 157 KLLVWCDNE 165
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
150-316 |
4.21e-31 |
|
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: 114.92 E-value: 4.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 150 CTTNCLAPMAKALHDSFGIEVGTMTTIHAYTGTQSLVDGPRGKDLraSRAAAENIIPHTTGAAKAIGLVIPELS--GKLK 227
Cdd:cd18122 1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIGkpIKVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 228 GHAQRVPVKTGSVTELVSILGKKVTAEEVNNALkKATNNNESFGYTDEEI---VSSDIIGSHFGSVFDATQTEitaVGDL 304
Cdd:cd18122 79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAV-AEAVEEVQISAEDGLTyakVSTRSVGGVYGVPVGRQREF---AFDD 154
|
170
....*....|..
gi 445970839 305 QLVKTVAWYDNE 316
Cdd:cd18122 155 NKLKVFSAVDNE 166
|
|
| GAPDH-like_N |
cd05192 |
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ... |
3-154 |
3.10e-14 |
|
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: 67.76 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 3 KVGINGFGRIGRLVLRRLLEvKSNIDVVAINDLTspkilayllkhdsnygpfpwsvdytedslivngksiavyaekeakn 82
Cdd:cd05192 2 RVAINGFGRIGRIVFRAIAD-QDDLDVVAINDRR---------------------------------------------- 34
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 445970839 83 ipwkakgaEIIVECTGFYTSAEKSQAHLDAGAKKVLISAPA-GEMKTIVYNVNDDTLDGNDTIVSVASCTTNC 154
Cdd:cd05192 35 --------DVVIECTGSFTDDDNAEKHIKAGGKKAVITAPEkGDIPTIVVVLNELAKSAGATVVSNANETSYS 99
|
|
| ASADH_C_arch_fung_like |
cd18130 |
C-terminal catalytic domain of fungal/archaeal aspartate beta-semialdehyde dehydrogenase ... |
150-265 |
6.54e-08 |
|
C-terminal catalytic domain of fungal/archaeal aspartate beta-semialdehyde dehydrogenase (ASADH) and similar proteins; The family corresponds to a new branch of aspartate beta-semialdehyde dehydrogenase (ASADH) enzymes that has a similar overall fold and domain organization but share very little sequence homology with the typical bacterial ASADHs. They are mainly from archaea and fungi. ASADH (EC 1.2.1.11), also called ASA dehydrogenase (ASD), or aspartate-beta-semialdehyde dehydrogenase, catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate, which is the second step of the aspartate biosynthetic pathway. ASA can either be further reduced to homoserine, which leads to methionine, threonine, or isoleucine, or it can be condensed with pyruvate and cyclized into dihydrodipicolinate, and then converted into diaminopimelate, a component of bacterial cell walls, and finally decarboxylated to produce lysine. ASADH contains an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins. This family also includes NADP-dependent malonyl-CoA reductase (MCR, EC 1.2.1.75), which catalyzes the reduction of malonyl-CoA to malonate semialdehyde, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutyrate cycles. It can also use succinyl-CoA and succinate semialdehyde as substrates but at a lower rate than malonyl-CoA.
Pssm-ID: 467680 [Multi-domain] Cd Length: 180 Bit Score: 51.85 E-value: 6.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445970839 150 CTTNCLAPMAKALHDSFGIEVGTMTTIHA-----YTGTQSLvdgprgkdlrasrAAAENIIPHTTGAAKAIGLVIPELSG 224
Cdd:cd18130 1 CSTAGLALPLKPLHDFFGIEAVIVTTMQAisgagYPGVPSL-------------DILDNVIPYIGGEEEKIESETKKILG 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 445970839 225 KLKG------------HAQRVPVKTGSvTELVSI-LGKKVTAEEVNNALKKATN 265
Cdd:cd18130 68 TLNEdkiepadfkvsaTCNRVPVIDGH-TESVSVkFKERPDPEEVKEALENYEP 120
|
|
| |
