|
Name |
Accession |
Description |
Interval |
E-value |
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
2-335 |
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: 596.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 2 IKVGINGFGRIGRFVFRAAQTR-NDIQIVGINDLCPVDYLAYMLKYDTMHGHFDGTIEadVEKSQLIVNGKTIRVTAEKN 80
Cdd:COG0057 3 IRVAINGFGRIGRLVLRALLERgPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVE--VEGDSLIVNGKKIKVLAERD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 81 PADLKWNEVGAEYVVESTGLFLTKEKAQAHIQAGAKYVVMSAPSKDDTPMFVCGVNENTYVKGTQFVSNASCTTNCLAPI 160
Cdd:COG0057 81 PAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDDPTIVYGVNHDDYDADHRIISNASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 161 AKVLNDKFGILDGLMTTVHSTTATQKTVDGPsMKDWRGGRAASGNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTLDV 240
Cdd:COG0057 161 AKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 241 SVVDLTVNLAKPATYAEICAAMKEASEGELKGILGYTEDAVVSSDFLGDTRTSIFDAKAGIALTDTFVKVVSWYDNEIGY 320
Cdd:COG0057 240 SLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGY 319
|
330
....*....|....*
gi 644097579 321 SNKVLDLIAHMAKVN 335
Cdd:COG0057 320 SNRMVDLAEYMAKLL 334
|
|
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
2-335 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 540.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 2 IKVGINGFGRIGRFVFRAAQTRNDIQIVGIND-LCPVDYLAYMLKYDTMHGHFDGTIEAdVEKSQLIVNGKTIRVTAEKN 80
Cdd:PLN02272 86 TKIGINGFGRIGRLVLRIATSRDDIEVVAVNDpFIDAKYMAYMFKYDSTHGNFKGTINV-VDDSTLEINGKQIKVTSKRD 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 81 PADLKWNEVGAEYVVESTGLFLTKEKAQAHIQAGAKYVVMSAPSKDdTPMFVCGVNENTYVKGTQFVSNASCTTNCLAPI 160
Cdd:PLN02272 165 PAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSAD-APMFVVGVNEKTYKPNMNIVSNASCTTNCLAPL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 161 AKVLNDKFGILDGLMTTVHSTTATQKTVDGPSMKDWRGGRAASGNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTLDV 240
Cdd:PLN02272 244 AKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNV 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 241 SVVDLTVNLAKPATYAEICAAMKEASEGELKGILGYTEDAVVSSDFLGDTRTSIFDAKAGIALTDTFVKVVSWYDNEIGY 320
Cdd:PLN02272 324 SVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGY 403
|
330
....*....|....*
gi 644097579 321 SNKVLDLIAHMAKVN 335
Cdd:PLN02272 404 SNRVLDLIEHMALVA 418
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
3-326 |
5.84e-177 |
|
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: 492.95 E-value: 5.84e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 3 KVGINGFGRIGRFVFRAAQTR--NDIQIVGINDLCPVDYLAYMLKYDTMHGHFDGTIEADVEKsqLIVNGK-TIRVTAEK 79
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKpgNDLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTVDEDG--LVVNGKeVISVFSER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 80 NPADLKWNEVGAEYVVESTGLFLTKEKAQAHIQAGAKYVVMSAPSKDDTPMFVCGVNENTYVKGTQFVSNASCTTNCLAP 159
Cdd:TIGR01534 79 DPSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDVKTIVYGVNHDEYDGEERIISNASCTTNCLAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 160 IAKVLNDKFGILDGLMTTVHSTTATQKTVDGPsMKDWRGGRAASGNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTLD 239
Cdd:TIGR01534 159 LAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 240 VSVVDLTVNLAKPATYAEICAAMKEASEGELKGILGYTEDAVVSSDFLGDTRTSIFDAKAGIA--LTDTFVKVVSWYDNE 317
Cdd:TIGR01534 238 VSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNE 317
|
....*....
gi 644097579 318 IGYSNKVLD 326
Cdd:TIGR01534 318 WGYSNRLVD 326
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
152-317 |
1.87e-118 |
|
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: 338.66 E-value: 1.87e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 152 CTTNCLAPIAKVLNDKFGILDGLMTTVHSTTATQKTVDGPSmKDWRGGRAASGNIIPSSTGAAKAVGKVIPSLNGKLTGM 231
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 232 SMRVPTLDVSVVDLTVNLAKPATYAEICAAMKEASEGELKGILGYTEDAVVSSDFLGDTRTSIFDAKAGIALTDTFVKVV 311
Cdd:cd18126 80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159
|
....*.
gi 644097579 312 SWYDNE 317
Cdd:cd18126 160 AWYDNE 165
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
4-327 |
5.99e-118 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 343.45 E-value: 5.99e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 4 VGINGFGRIGRFVFRAAQTRNDIQIVGINDL-CPVDYLAYMLKYDTMHGHFDGtiEADVEKSQLIVNGKTIRVTAEKNPA 82
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLaGDAATLAHLLEFDSVHGRWDA--EVTAEEDSIVIDGKRISFSSNKDIE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 83 DLKWNEvGAEYVVESTGLFLTKEKAQAHIQAGAKYVVMSAPSKDDTPM-FVCGVNENTYVKGT-QFVSNASCTTNCLAPI 160
Cdd:NF033735 79 DTPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLnIVYGVNDHLYDPARhRIVTAASCTTNCLAPV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 161 AKVLNDKFGILDGLMTTVHSTTATQKTVDGPSmKDWRGGRAASGNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTLDV 240
Cdd:NF033735 158 VKVIHEKIGIKHGSITTIHDITNTQTIVDAPH-KDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 241 SVVDLTVNLAKPATYAEICAAMKEASEGELKGILGYTEDAVVSSDFLGDTRTSIFDAKAGIALTDTFVKVVSWYDNEIGY 320
Cdd:NF033735 237 SLTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGY 316
|
....*..
gi 644097579 321 SNKVLDL 327
Cdd:NF033735 317 ANRMVDL 323
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
157-314 |
7.31e-90 |
|
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: 265.61 E-value: 7.31e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 157 LAPIAKVLNDKFGILDGLMTTVHSTTATQKTVDGPSMKDWRGGRAASGNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVP 236
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 644097579 237 TLDVSVVDLTVNLAKPATYAEICAAMKEASEGELKGILGYTEDAVVSSDFLGDTRTSIFDAKAGIALTDTFVKVVSWY 314
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
2-152 |
5.95e-78 |
|
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: 235.14 E-value: 5.95e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 2 IKVGINGFGRIGRFVFRAAQTRNDIQIVGINDLCPVDYLAYMLKYDTMHGHFDGTIEADveKSQLIVNGKTIRVTAEKNP 81
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEVE--GDGLVVNGKAIKVFAERDP 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 644097579 82 ADLKWNEVGAEYVVESTGLFLTKEKAQAHIQAGAKYVVMSAPSKDDTPMFVCGVNENTYVKGTQFVSNASC 152
Cdd:smart00846 79 ANLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDADPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
2-335 |
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: 596.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 2 IKVGINGFGRIGRFVFRAAQTR-NDIQIVGINDLCPVDYLAYMLKYDTMHGHFDGTIEadVEKSQLIVNGKTIRVTAEKN 80
Cdd:COG0057 3 IRVAINGFGRIGRLVLRALLERgPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVE--VEGDSLIVNGKKIKVLAERD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 81 PADLKWNEVGAEYVVESTGLFLTKEKAQAHIQAGAKYVVMSAPSKDDTPMFVCGVNENTYVKGTQFVSNASCTTNCLAPI 160
Cdd:COG0057 81 PAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDDPTIVYGVNHDDYDADHRIISNASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 161 AKVLNDKFGILDGLMTTVHSTTATQKTVDGPsMKDWRGGRAASGNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTLDV 240
Cdd:COG0057 161 AKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 241 SVVDLTVNLAKPATYAEICAAMKEASEGELKGILGYTEDAVVSSDFLGDTRTSIFDAKAGIALTDTFVKVVSWYDNEIGY 320
Cdd:COG0057 240 SLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGY 319
|
330
....*....|....*
gi 644097579 321 SNKVLDLIAHMAKVN 335
Cdd:COG0057 320 SNRMVDLAEYMAKLL 334
|
|
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
2-335 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 540.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 2 IKVGINGFGRIGRFVFRAAQTRNDIQIVGIND-LCPVDYLAYMLKYDTMHGHFDGTIEAdVEKSQLIVNGKTIRVTAEKN 80
Cdd:PLN02272 86 TKIGINGFGRIGRLVLRIATSRDDIEVVAVNDpFIDAKYMAYMFKYDSTHGNFKGTINV-VDDSTLEINGKQIKVTSKRD 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 81 PADLKWNEVGAEYVVESTGLFLTKEKAQAHIQAGAKYVVMSAPSKDdTPMFVCGVNENTYVKGTQFVSNASCTTNCLAPI 160
Cdd:PLN02272 165 PAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSAD-APMFVVGVNEKTYKPNMNIVSNASCTTNCLAPL 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 161 AKVLNDKFGILDGLMTTVHSTTATQKTVDGPSMKDWRGGRAASGNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTLDV 240
Cdd:PLN02272 244 AKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNV 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 241 SVVDLTVNLAKPATYAEICAAMKEASEGELKGILGYTEDAVVSSDFLGDTRTSIFDAKAGIALTDTFVKVVSWYDNEIGY 320
Cdd:PLN02272 324 SVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGY 403
|
330
....*....|....*
gi 644097579 321 SNKVLDLIAHMAKVN 335
Cdd:PLN02272 404 SNRVLDLIEHMALVA 418
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
3-326 |
5.84e-177 |
|
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: 492.95 E-value: 5.84e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 3 KVGINGFGRIGRFVFRAAQTR--NDIQIVGINDLCPVDYLAYMLKYDTMHGHFDGTIEADVEKsqLIVNGK-TIRVTAEK 79
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKpgNDLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTVDEDG--LVVNGKeVISVFSER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 80 NPADLKWNEVGAEYVVESTGLFLTKEKAQAHIQAGAKYVVMSAPSKDDTPMFVCGVNENTYVKGTQFVSNASCTTNCLAP 159
Cdd:TIGR01534 79 DPSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDVKTIVYGVNHDEYDGEERIISNASCTTNCLAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 160 IAKVLNDKFGILDGLMTTVHSTTATQKTVDGPsMKDWRGGRAASGNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTLD 239
Cdd:TIGR01534 159 LAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 240 VSVVDLTVNLAKPATYAEICAAMKEASEGELKGILGYTEDAVVSSDFLGDTRTSIFDAKAGIA--LTDTFVKVVSWYDNE 317
Cdd:TIGR01534 238 VSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNE 317
|
....*....
gi 644097579 318 IGYSNKVLD 326
Cdd:TIGR01534 318 WGYSNRLVD 326
|
|
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
2-333 |
4.25e-169 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 473.55 E-value: 4.25e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 2 IKVGINGFGRIGRFVFRAAQTRNDIQIVGIND-LCPVDYLAYMLKYDTMHGHFDGtiEADVEKSQLIVNGKTIRVTAEKN 80
Cdd:PTZ00023 3 VKLGINGFGRIGRLVFRAALEREDVEVVAINDpFMTLDYMCYLLKYDSVHGSLPA--EVSVTDGFLMIGSKKVHVFFEKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 81 PADLKWNEVGAEYVVESTGLFLTKEKAQAHIQAGAKYVVMSAPSKDDTPMFVCGVNENTYVKGTQFVSNASCTTNCLAPI 160
Cdd:PTZ00023 81 PAAIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKDDTPIYVMGVNHTQYDKSQRIVSNASCTTNCLAPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 161 AKVLNDKFGILDGLMTTVHSTTATQKTVDGPSM--KDWRGGRAASGNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTL 238
Cdd:PTZ00023 161 AKVVNDKFGIVEGLMTTVHASTANQLTVDGPSKggKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 239 DVSVVDLTVNLAKPATYAEICAAMKEASEGELKGILGYTEDAVVSSDFLGDTRTSIFDAKAGIALTDTFVKVVSWYDNEI 318
Cdd:PTZ00023 241 DVSVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDNEW 320
|
330
....*....|....*
gi 644097579 319 GYSNKVLDLIAHMAK 333
Cdd:PTZ00023 321 GYSNRLLDLAHYITQ 335
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
2-333 |
2.00e-168 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 471.91 E-value: 2.00e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 2 IKVGINGFGRIGRFVFRAAQTRNDIQIVGINDLCPVDYLAYMLKYDTMHGHFDGTIEadVEKSQLIVNGKTIRVTAEKNP 81
Cdd:PRK15425 3 IKVGINGFGRIGRIVFRAAQKRSDIEIVAINDLLDADYMAYMLKYDSTHGRFDGTVE--VKDGHLIVNGKKIRVTAERDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 82 ADLKWNEVGAEYVVESTGLFLTKEKAQAHIQAGAKYVVMSAPSKDDTPMFVCGVNENTYVkGTQFVSNASCTTNCLAPIA 161
Cdd:PRK15425 81 ANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDNTPMFVKGANFDKYA-GQDIVSNASCTTNCLAPLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 162 KVLNDKFGILDGLMTTVHSTTATQKTVDGPSMKDWRGGRAASGNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTLDVS 241
Cdd:PRK15425 160 KVINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 242 VVDLTVNLAKPATYAEICAAMKEASEGELKGILGYTEDAVVSSDFLGDTRTSIFDAKAGIALTDTFVKVVSWYDNEIGYS 321
Cdd:PRK15425 240 VVDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYS 319
|
330
....*....|..
gi 644097579 322 NKVLDLIAHMAK 333
Cdd:PRK15425 320 NKVLDLIAHISK 331
|
|
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
2-333 |
7.73e-156 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 440.31 E-value: 7.73e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 2 IKVGINGFGRIGRFVFRAAQTRNDIQIVGIND-LCPVDYLAYMLKYDTMHGHFDGTIEADVEKSQLIVNGKTIRVTAEKN 80
Cdd:PLN02358 6 IRIGINGFGRIGRLVARVVLQRDDVELVAVNDpFITTEYMTYMFKYDSVHGQWKHHELKVKDDKTLLFGEKPVTVFGIRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 81 PADLKWNEVGAEYVVESTGLFLTKEKAQAHIQAGAKYVVMSAPSKDdTPMFVCGVNENTYVKGTQFVSNASCTTNCLAPI 160
Cdd:PLN02358 86 PEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKD-APMFVVGVNEHEYKSDLDIVSNASCTTNCLAPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 161 AKVLNDKFGILDGLMTTVHSTTATQKTVDGPSMKDWRGGRAASGNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTLDV 240
Cdd:PLN02358 165 AKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 241 SVVDLTVNLAKPATYAEICAAMKEASEGELKGILGYTEDAVVSSDFLGDTRTSIFDAKAGIALTDTFVKVVSWYDNEIGY 320
Cdd:PLN02358 245 SVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEWGY 324
|
330
....*....|...
gi 644097579 321 SNKVLDLIAHMAK 333
Cdd:PLN02358 325 SSRVVDLIVHMSK 337
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
2-332 |
5.13e-139 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 398.27 E-value: 5.13e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 2 IKVGINGFGRIGRFVFRAAQTR----NDIQIVGINDL-CPVDYLAYMLKYDTMHGHFDGTIEADVEKSQ------LIVNG 70
Cdd:PTZ00434 4 IKVGINGFGRIGRMVFQAICDQgligTEIDVVAVVDMsTNAEYFAYQMKYDTVHGRPKYTVETTKSSPSvktddvLVVNG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 71 KTIR-VTAEKNPADLKWNEVGAEYVVESTGLFLTKEKAQAHIQAGAKYVVMSAPSKDDTPMFVCGVNENTYVKGTQ-FVS 148
Cdd:PTZ00434 84 HRIKcVKAQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPASGGAKTIVMGVNQHEYSPTEHhVVS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 149 NASCTTNCLAPIAKVL-NDKFGILDGLMTTVHSTTATQKTVDGPSMKDWRGGRAASGNIIPSSTGAAKAVGKVIPSLNGK 227
Cdd:PTZ00434 164 NASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 228 LTGMSMRVPTLDVSVVDLTVNLAKPATYAEICAAMKEASEGELKGILGYTEDAVVSSDFLGDTRTSIFDAKA----GIAL 303
Cdd:PTZ00434 244 LTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKAtlqnNLPG 323
|
330 340
....*....|....*....|....*....
gi 644097579 304 TDTFVKVVSWYDNEIGYSNKVLDLIAHMA 332
Cdd:PTZ00434 324 ERRFFKIVSWYDNEWGYSHRVVDLVRYMA 352
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-333 |
6.80e-138 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 394.87 E-value: 6.80e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 1 MIKVGINGFGRIGRFVFRAAQTRNDIQIVGINDLCPVDYLAYMLKYDTMHGHFDGTIEAdvEKSQLIVNGKTIRVTAEKN 80
Cdd:PRK07729 2 KTKVAINGFGRIGRMVFRKAIKESAFEIVAINASYPSETLAHLIKYDTVHGKFDGTVEA--FEDHLLVDGKKIRLLNNRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 81 PADLKWNEVGAEYVVESTGLFLTKEKAQAHIQAGAKYVVMSAPSKDDTPMFVCGVNENTYVKGTQFV-SNASCTTNCLAP 159
Cdd:PRK07729 80 PKELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVTIVVGVNEDQLDIEKHTIiSNASCTTNCLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 160 IAKVLNDKFGILDGLMTTVHSTTATQKTVDGPSmKDWRGGRAASGNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTLD 239
Cdd:PRK07729 160 VVKVLDEQFGIENGLMTTVHAYTNDQKNIDNPH-KDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 240 VSVVDLTVNLAKPATYAEICAAMKEASEGELKGILGYTEDAVVSSDFLGDTRTSIFDAKAGIALTDTFVKVVSWYDNEIG 319
Cdd:PRK07729 239 VSLVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEWG 318
|
330
....*....|....
gi 644097579 320 YSNKVLDLIAHMAK 333
Cdd:PRK07729 319 YSCRVVDLVTLVAD 332
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
152-317 |
1.87e-118 |
|
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: 338.66 E-value: 1.87e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 152 CTTNCLAPIAKVLNDKFGILDGLMTTVHSTTATQKTVDGPSmKDWRGGRAASGNIIPSSTGAAKAVGKVIPSLNGKLTGM 231
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 232 SMRVPTLDVSVVDLTVNLAKPATYAEICAAMKEASEGELKGILGYTEDAVVSSDFLGDTRTSIFDAKAGIALTDTFVKVV 311
Cdd:cd18126 80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159
|
....*.
gi 644097579 312 SWYDNE 317
Cdd:cd18126 160 AWYDNE 165
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
4-327 |
5.99e-118 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 343.45 E-value: 5.99e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 4 VGINGFGRIGRFVFRAAQTRNDIQIVGINDL-CPVDYLAYMLKYDTMHGHFDGtiEADVEKSQLIVNGKTIRVTAEKNPA 82
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLaGDAATLAHLLEFDSVHGRWDA--EVTAEEDSIVIDGKRISFSSNKDIE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 83 DLKWNEvGAEYVVESTGLFLTKEKAQAHIQAGAKYVVMSAPSKDDTPM-FVCGVNENTYVKGT-QFVSNASCTTNCLAPI 160
Cdd:NF033735 79 DTPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLnIVYGVNDHLYDPARhRIVTAASCTTNCLAPV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 161 AKVLNDKFGILDGLMTTVHSTTATQKTVDGPSmKDWRGGRAASGNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTLDV 240
Cdd:NF033735 158 VKVIHEKIGIKHGSITTIHDITNTQTIVDAPH-KDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 241 SVVDLTVNLAKPATYAEICAAMKEASEGELKGILGYTEDAVVSSDFLGDTRTSIFDAKAGIALTDTFVKVVSWYDNEIGY 320
Cdd:NF033735 237 SLTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGY 316
|
....*..
gi 644097579 321 SNKVLDL 327
Cdd:NF033735 317 ANRMVDL 323
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
1-333 |
2.77e-117 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 342.27 E-value: 2.77e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 1 MIKVGINGFGRIGRFVFRAAQTRND--IQIVGINDLCPVDYLAYMLKYDTMHGHFDGTIEADveKSQLIVNGKTIRVTAE 78
Cdd:PRK07403 1 MIRVAINGFGRIGRNFLRCWLGRENsqLELVAINDTSDPRTNAHLLKYDSMLGKLNADISAD--ENSITVNGKTIKCVSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 79 KNPADLKWNEVGAEYVVESTGLFLTKEKAQAHIQAGAKYVVMSAPSK-DDTPMFVCGVNENTYVKGT-QFVSNASCTTNC 156
Cdd:PRK07403 79 RNPLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPGKgEDIGTYVVGVNHHEYDHEDhNIISNASCTTNC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 157 LAPIAKVLNDKFGILDGLMTTVHSTTATQKTVDGpSMKDWRGGRAASGNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVP 236
Cdd:PRK07403 159 LAPIAKVLHDNFGIIKGTMTTTHSYTGDQRILDA-SHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 237 TLDVSVVDLTVNLAKPATYAEICAAMKEASEGELKGILGYTEDAVVSSDFLGDTRTSIFDAKAGIALTDTFVKVVSWYDN 316
Cdd:PRK07403 238 TPNVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYDN 317
|
330
....*....|....*..
gi 644097579 317 EIGYSNKVLDLIAHMAK 333
Cdd:PRK07403 318 EWGYSQRVVDLAELVAR 334
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
2-327 |
6.00e-109 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 323.04 E-value: 6.00e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 2 IKVGINGFGRIGRFVFRAAQTRND--IQIVGINDLCPVDYLAYMLKYDTMHGHFDGTIEAdVEKSQLIVNGKTIRVTAEK 79
Cdd:PLN03096 61 IKVAINGFGRIGRNFLRCWHGRKDspLDVVAINDTGGVKQASHLLKYDSTLGTFDADVKP-VGDDAISVDGKVIKVVSDR 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 80 NPADLKWNEVGAEYVVESTGLFLTKEKAQAHIQAGAKYVVMSAPSKDDTPMFVCGVNENTYVKGTQFVSNASCTTNCLAP 159
Cdd:PLN03096 140 NPLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKGDIPTYVVGVNADDYKHSDPIISNASCTTNCLAP 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 160 IAKVLNDKFGILDGLMTTVHSTTATQKTVDGpSMKDWRGGRAASGNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTLD 239
Cdd:PLN03096 220 FVKVLDQKFGIIKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPN 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 240 VSVVDLTVNLAKPATYAEICAAMKEASEGELKGILGYTEDAVVSSDFLGDTRTSIFDAKAGIALTDTFVKVVSWYDNEIG 319
Cdd:PLN03096 299 VSVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAWYDNEWG 378
|
....*...
gi 644097579 320 YSNKVLDL 327
Cdd:PLN03096 379 YSQRVVDL 386
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
2-331 |
1.37e-103 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 311.06 E-value: 1.37e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 2 IKVGINGFGRIGRFVFRAAQTRND--IQIVGINDLCPVDYLAYMLKYDTMHGHFDGTIEAdVEKSQLIVNGKTIRVTAEK 79
Cdd:PLN02237 76 LKVAINGFGRIGRNFLRCWHGRKDspLDVVVVNDSGGVKNASHLLKYDSMLGTFKADVKI-VDDETISVDGKPIKVVSNR 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 80 NPADLKWNEVGAEYVVESTGLFLTKEKAQAHIQAGAKYVVMSAPSK-DDTPMFVCGVNENTYV-KGTQFVSNASCTTNCL 157
Cdd:PLN02237 155 DPLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAKgADIPTYVVGVNEDDYDhEVANIVSNASCTTNCL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 158 APIAKVLNDKFGILDGLMTTVHSTTATQKTVDGpSMKDWRGGRAASGNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPT 237
Cdd:PLN02237 235 APFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPT 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 238 LDVSVVDLTVNLAKPATYAE-ICAAMKEASEGELKGILGYTEDAVVSSDFLGDTRTSIFDAKAGIALTDTFVKVVSWYDN 316
Cdd:PLN02237 314 PNVSVVDLVVNVEKKGITAEdVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVAWYDN 393
|
330
....*....|....*
gi 644097579 317 EIGYSNKVLDLiAHM 331
Cdd:PLN02237 394 EWGYSQRVVDL-AHL 407
|
|
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
2-328 |
1.80e-102 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 304.35 E-value: 1.80e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 2 IKVGINGFGRIGRFVFRAAQTRNDIQIVGINDLC-PVDYLAYMLKYDTMHGHFDGtiEADVEKSQLIVNGKTIRVTAEKN 80
Cdd:PRK08955 3 IKVGINGFGRIGRLALRAAWDWPELEFVQINDPAgDAATLAHLLEFDSVHGRWHH--EVTAEGDAIVINGKRIRTTQNKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 81 PADLKWNevGAEYVVESTGLFLTKEKAQAHIQAGAKYVVMSAPSKDDTPM-FVCGVNENTYVKGT-QFVSNASCTTNCLA 158
Cdd:PRK08955 81 IADTDWS--GCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLnIVMGVNDHLFDPAIhPIVTAASCTTNCLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 159 PIAKVLNDKFGILDGLMTTVHSTTATQKTVDGPSmKDWRGGRAASGNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTL 238
Cdd:PRK08955 159 PVVKVIHEKLGIKHGSMTTIHDLTNTQTILDAPH-KDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 239 DVSVVDLTVNLAKPATYAEICAAMKEASEGELKGILGYTEDAVVSSDFLGDTRTSIFDAKAGIALTDTFVKVVSWYDNEI 318
Cdd:PRK08955 238 NASLTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNEW 317
|
330
....*....|
gi 644097579 319 GYSNKVLDLI 328
Cdd:PRK08955 318 GYANRTAELA 327
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
1-333 |
1.66e-95 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 286.57 E-value: 1.66e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 1 MIKVGINGFGRIGRFVFRA---AQTRNDIQIVGINDLCPVDYLAYMLKYDTMHGHFDGTIEADVEksQLIVNGKTIRVTA 77
Cdd:PRK13535 1 TIRVAINGFGRIGRNVLRAlyeSGRRAEITVVAINELADAEGMAHLLKYDTSHGRFAWDVRQERD--QLFVGDDAIRLLH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 78 EKNPADLKWNEVGAEYVVESTGLFLTKEKAQAHIQAGAKYVVMSAPSKDDT-PMFVCGVNENTYVKGTQFVSNASCTTNC 156
Cdd:PRK13535 79 ERDIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSNDLdATVVYGVNHDQLRAEHRIVSNASCTTNC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 157 LAPIAKVLNDKFGILDGLMTTVHSTTATQKTVDGpSMKDWRGGRAASGNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVP 236
Cdd:PRK13535 159 IIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 237 TLDVSVVDLTVNLAKPATYAEICAAMKEASEGELKGILGYTEDAVVSSDFLGDTRTSIFDAKAGIALTDTFVKVVSWYDN 316
Cdd:PRK13535 238 TINVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDN 317
|
330
....*....|....*..
gi 644097579 317 EIGYSNKVLDLIAHMAK 333
Cdd:PRK13535 318 EWGFANRMLDTTLAMAA 334
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
157-314 |
7.31e-90 |
|
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: 265.61 E-value: 7.31e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 157 LAPIAKVLNDKFGILDGLMTTVHSTTATQKTVDGPSMKDWRGGRAASGNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVP 236
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 644097579 237 TLDVSVVDLTVNLAKPATYAEICAAMKEASEGELKGILGYTEDAVVSSDFLGDTRTSIFDAKAGIALTDTFVKVVSWY 314
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
8-335 |
4.46e-89 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 274.88 E-value: 4.46e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 8 GFGRIGRFV---------------FRAAQTRNDiqivGINDLcpvDYLAYMLKYDTMHGHFDGTIEADVEKSQLIVNGKT 72
Cdd:PRK08289 134 GFGRIGRLLarlliektgggnglrLRAIVVRKG----SEGDL---EKRASLLRRDSVHGPFNGTITVDEENNAIIANGNY 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 73 IRVTAEKNPADLKWNEVGAE--YVVESTGLFLTKEKAQAHIQA-GAKYVVMSAPSKDDTPMFVCGVNENTYVKGTQFVSN 149
Cdd:PRK08289 207 IQVIYANSPEEVDYTAYGINnaLVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGKGDIKNIVHGVNHSDITDEDKIVSA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 150 ASCTTNCLAPIAKVLNDKFGILDGLMTTVHSTTATQKTVDGPSMKDwRGGRAASGNIIPSSTGAAKAVGKVIPSLNGKLT 229
Cdd:PRK08289 287 ASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKGD-RRGRSAPLNMVITETGAAKAVAKALPELAGKLT 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 230 GMSMRVPTLDVSVVDLTVNLAKPATYAEICAAMKEAS-EGELKGILGYTEDA-VVSSDFLGDTRTSIFDAKAGIALTDTF 307
Cdd:PRK08289 366 GNAIRVPTPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQIDYTDSTeVVSSDFVGSRHAGVVDSQATIVNGNRA 445
|
330 340
....*....|....*....|....*...
gi 644097579 308 VKVVsWYDNEIGYSNKVLDLIAHMAKVN 335
Cdd:PRK08289 446 VLYV-WYDNEFGYSCQVVRVMEQMAGVR 472
|
|
| GAPDH_I_N |
cd05214 |
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
2-151 |
4.68e-88 |
|
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: 261.17 E-value: 4.68e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 2 IKVGINGFGRIGRFVFRAAQTRNDIQIVGINDLCPVDYLAYMLKYDTMHGHFDGTIEADVEKsqLIVNGKTIRVTAEKNP 81
Cdd:cd05214 1 IKVGINGFGRIGRLVFRAALERDDIEVVAINDLTDDETLAYLLKYDSVHGRFDGEVEVDDDA--LIVNGKKIKVFAERDP 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 82 ADLKWNEVGAEYVVESTGLFLTKEKAQAHIQAGAKYVVMSAPSKDDTPMFVCGVNENTYVKGTQFVSNAS 151
Cdd:cd05214 79 AELPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDDDPTIVMGVNHDKYDADDKIISNAS 148
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
2-152 |
5.95e-78 |
|
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: 235.14 E-value: 5.95e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 2 IKVGINGFGRIGRFVFRAAQTRNDIQIVGINDLCPVDYLAYMLKYDTMHGHFDGTIEADveKSQLIVNGKTIRVTAEKNP 81
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEVE--GDGLVVNGKAIKVFAERDP 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 644097579 82 ADLKWNEVGAEYVVESTGLFLTKEKAQAHIQAGAKYVVMSAPSKDDTPMFVCGVNENTYVKGTQFVSNASC 152
Cdd:smart00846 79 ANLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDADPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
152-317 |
3.83e-75 |
|
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: 228.66 E-value: 3.83e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 152 CTTNCLAPIAKVLNDKFGILDGLMTTVHSTTATQKTVDGPSMKDWRGGRAASGNIIPSSTGAAKAVGKVIPSLNGKLTGM 231
Cdd:cd18123 1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 232 SMRVPTLDVSVVDLTVNLAKPATYAEICAAMKEASEGelKGILGYTEDAVVSSDFLGDTRTSIFDAKAGIALTDTFVKVV 311
Cdd:cd18123 81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLM 158
|
....*.
gi 644097579 312 SWYDNE 317
Cdd:cd18123 159 QWYDNE 164
|
|
| Gp_dh_N |
pfam00044 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
2-104 |
1.39e-54 |
|
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: 173.83 E-value: 1.39e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 2 IKVGINGFGRIGRFVFRAAQTRNDIQIVGINDLCPVDYLAYMLKYDTMHGHFDGTIEADVEKsqLIVNGKTIRVTAEKNP 81
Cdd:pfam00044 1 VKVGINGFGRIGRLVLRAALERPDIEVVAINDLTDPETLAYLLKYDSVHGRFPGEVEAEEDG--LVVNGKKIKVFAERDP 78
|
90 100
....*....|....*....|...
gi 644097579 82 ADLKWNEVGAEYVVESTGLFLTK 104
Cdd:pfam00044 79 AELPWGDLGVDVVIESTGVFTTK 101
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
2-331 |
7.23e-54 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 180.07 E-value: 7.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 2 IKVGINGFGRIGRFVFRAAQTRNDIQIVGIND--LCpVDYLAYMLKYDTMHGHFDGTiEADVEKSQLIVNG-KTIRVTAE 78
Cdd:PTZ00353 3 ITVGINGFGPVGKAVLFASLTDPLVTVVAVNDasVS-IAYIAYVLEQESPLSAPDGA-SIRVVGEQIVLNGtQKIRVSAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 79 KNPADLKWNEVGAEYVVESTGLFLTKEKAQAHIQAGAKYVVMSAPSKDdTPMFVCGVNENTYVKGTQFVSNASCTTNCLA 158
Cdd:PTZ00353 81 HDLVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSAD-APTVMAGSNDERLSASLPVCCAGAPIAVALA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 159 PIAKVLNDKFGILDGLMTTVHSTTATQKT-VDGPSMKDWRGGRAASGNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPT 237
Cdd:PTZ00353 160 PVIRALHEVYGVEECSYTAIHGMQPQEPIaARSKNSQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 238 LDVSVVDLTVNLAKPATYAEICAAMKEASEGELKGILGYTEDAVVSSDFLGDTRTsIFDAKAGIALTDTFV-KVVSWYDN 316
Cdd:PTZ00353 240 KKGCAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCIPNGKL-CYDATSSSSSREGEVhKMVLWFDV 318
|
330
....*....|....*
gi 644097579 317 EIGYSNKVLDLIAHM 331
Cdd:PTZ00353 319 ECYYAARLLSLVKQL 333
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
152-317 |
2.06e-48 |
|
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: 160.27 E-value: 2.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 152 CTTNCLAPIAKVLNDKFGILDGLMTTVHSTTATQKTVDGpSMKDWRGGRAASGNIIPSSTGAAKAVGKVIPSLNGKLTGM 231
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 232 SMRVPTLDVSVVDLTVNLAKPATYAEICAAMKEASEGELKGILGYTEDAVVSSDFLGDTRTSIFDAKAGIALTDTFVKVV 311
Cdd:cd23937 80 AVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLL 159
|
....*.
gi 644097579 312 SWYDNE 317
Cdd:cd23937 160 VWCDNE 165
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
152-317 |
8.58e-47 |
|
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: 156.14 E-value: 8.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 152 CTTNCLAPIAKVLNDKFGILDGLMTTVHSTTATQKTVDGPSMKDWrgGRAASGNIIPSSTGAAKAVGKVIPSLN--GKLT 229
Cdd:cd18122 1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIGkpIKVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 230 GMSMRVPTLDVSVVDLTVNLAKPATYAEICAAMKEASEGELKGILGYTEDAVVSSDFLGDTRTSIFDAKAGIALTDTFVK 309
Cdd:cd18122 79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLK 158
|
....*...
gi 644097579 310 VVSWYDNE 317
Cdd:cd18122 159 VFSAVDNE 166
|
|
| GAPDH_N_E4PDH |
cd17892 |
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
2-151 |
1.02e-45 |
|
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: 153.19 E-value: 1.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 2 IKVGINGFGRIGRFVFRA---AQTRNDIQIVGINDLCPVDYLAYMLKYDTMHGHFDGtiEADVEKSQLIVNGKTIRVTAE 78
Cdd:cd17892 1 YRVAINGYGRIGRNVLRAlyeSGRRAEFQVVAINELADAETIAHLTKYDTTHGRFPG--EVRVENDQLFVNGDKIRVLHE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 644097579 79 KNPADLKWNEVGAEYVVESTGLFLTKEKAQAHIQAGAKYVVMSAPSKDDT-PMFVCGVNENTYVKGTQFVSNAS 151
Cdd:cd17892 79 PDPENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASNDVdATIVYGINQDLLRAEHRIVSNAS 152
|
|
| GAPDH-like_N |
cd05192 |
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ... |
2-156 |
1.80e-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: 73.93 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 2 IKVGINGFGRIGRFVFRAAQTRNDIQIVGINDLcpvdylaymlkydtmhghfdgtieadveksqlivngktirvtaeknp 81
Cdd:cd05192 1 IRVAINGFGRIGRIVFRAIADQDDLDVVAINDR----------------------------------------------- 33
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 644097579 82 adlkwnevgAEYVVESTGLFLTKEKAQAHIQAGAKYVVMSAPSKDDTPMFVCGVNENTYVKGTQFVSNASCTTNC 156
Cdd:cd05192 34 ---------RDVVIECTGSFTDDDNAEKHIKAGGKKAVITAPEKGDIPTIVVVLNELAKSAGATVVSNANETSYS 99
|
|
| PRK04207 |
PRK04207 |
type II glyceraldehyde-3-phosphate dehydrogenase; |
1-266 |
1.91e-06 |
|
type II glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 179786 [Multi-domain] Cd Length: 341 Bit Score: 49.06 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 1 MIKVGINGFGRIGRFVFRAAQTRNDIQIVGINDLCPvDYLAYMLK------Y---DTMHGHFD-------GTIEADVEKS 64
Cdd:PRK04207 1 MIKVGVNGYGTIGKRVADAVAAQPDMELVGVAKTKP-DYEARVAVekgyplYvadPEREKAFEeagipvaGTIEDLLEKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 65 QLIVNGktirvTAEKnpadlkwneVGAEYvvestglfltKEKAQAHiqaGAKYVVMSAPSKDdtpmfVCGVNENTYV--- 141
Cdd:PRK04207 80 DIVVDA-----TPGG---------VGAKN----------KELYEKA---GVKAIFQGGEKAE-----VAGVSFNALAnye 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 142 --KGTQFVSNASCTTNCLAPIAKVLNDKFGILDGLMTTVHSTTATQKTVDGPSMkdwrggraasgNIIPSSTGA----AK 215
Cdd:PRK04207 128 eaLGKDYVRVVSCNTTGLCRTLCALDRAFGVKKVRATLVRRAADPKEVKRGPIN-----------AIVPDPVTVpshhGP 196
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 644097579 216 AVGKVIPSLNgkLTGMSMRVPTLDVSVVDLTVNLAKPATYAEICAAMKEAS 266
Cdd:PRK04207 197 DVKTVLPDLD--ITTMAVKVPTTLMHMHSVNVELKKPVTKEEVLEALENTP 245
|
|
| ASADH_C_arch_fung_like |
cd18130 |
C-terminal catalytic domain of fungal/archaeal aspartate beta-semialdehyde dehydrogenase ... |
152-271 |
1.03e-04 |
|
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: 42.22 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 152 CTTNCLAPIAKVLNDKFGIldglmTTVHSTT------ATQKTVdgPSMkdwrggrAASGNIIPSSTGAAKAVGKVIPSLN 225
Cdd:cd18130 1 CSTAGLALPLKPLHDFFGI-----EAVIVTTmqaisgAGYPGV--PSL-------DILDNVIPYIGGEEEKIESETKKIL 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 644097579 226 GKLTG------------MSMRVPTLDVSVVDLTVNLAKPATYAEICAAMKEASEGELK 271
Cdd:cd18130 67 GTLNEdkiepadfkvsaTCNRVPVIDGHTESVSVKFKERPDPEEVKEALENYEPEPQV 124
|
|
| meso-DAPDH_N |
cd02270 |
N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and ... |
2-31 |
4.12e-03 |
|
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: 37.17 E-value: 4.12e-03
10 20 30
....*....|....*....|....*....|
gi 644097579 2 IKVGINGFGRIGRFVFRAAQTRNDIQIVGI 31
Cdd:cd02270 1 IRVAIVGYGNLGRGVEEAIQANPDMELVGV 30
|
|
| GAPDH_II_N |
cd02278 |
N-terminal NAD(P)-binding domain of type II glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
2-68 |
7.91e-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: 36.77 E-value: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644097579 2 IKVGINGFGRIGRFVFRAAQTRNDIQIVGINDLCPvDYLAYML----------------KYDTMHGHFDGTIEADVEKSQ 65
Cdd:cd02278 1 IKVGVNGYGTIGKRVADAVLLQDDMELVGVAKRSP-DYEAKPAvergiplyvpdesraeKFEEAGIPVAGTLEDLLEKAD 79
|
...
gi 644097579 66 LIV 68
Cdd:cd02278 80 VVV 82
|
|
| MviM |
COG0673 |
Predicted dehydrogenase [General function prediction only]; |
1-36 |
9.78e-03 |
|
Predicted dehydrogenase [General function prediction only];
Pssm-ID: 440437 [Multi-domain] Cd Length: 295 Bit Score: 37.21 E-value: 9.78e-03
10 20 30
....*....|....*....|....*....|....*.
gi 644097579 1 MIKVGINGFGRIGRFVFRAAQTRNDIQIVGINDLCP 36
Cdd:COG0673 3 KLRVGIIGAGGIGRAHAPALAALPGVELVAVADRDP 38
|
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