|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
1-422 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 888.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 1 MAFSTLLRSTPAAPLIEASRSDFSPSPSDRFEVSSIRFNSSKSIFGaSVPTGSSSLHTCSGRSIQPIKATATEMPPTVLR 80
Cdd:PLN02272 1 MAFSSLLRSAATAPAAAARGSDFSSSSSDPSKVSSVGFSSSLSFSG-SSSGASSSLQSCSARSVQPIKATATEAPPAVLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 81 SRADGKTKIGINGFGRIGRLVLRVATFRDDIDVVAVNDPFIDAEYMAYMFRYDSTHGVFNGTIKVLDDSTLEINGKQIKI 160
Cdd:PLN02272 80 SSSSGKTKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVVDDSTLEINGKQIKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 161 TSKRDPAEIPWGDFGAEFVVESSGVFTTLEKAAAHKKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMDVVSNASCTTNC 240
Cdd:PLN02272 160 TSKRDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 241 LAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVP 320
Cdd:PLN02272 240 LAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 321 TPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLMGILGYTDDDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDN 400
Cdd:PLN02272 320 TPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDN 399
|
410 420
....*....|....*....|..
gi 224101329 401 EWGYSNRVLDLIEHMALVAAHN 422
Cdd:PLN02272 400 EWGYSNRVLDLIEHMALVAASH 421
|
|
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
86-416 |
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: 582.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 86 KTKIGINGFGRIGRLVLRVATFR-DDIDVVAVNDPfIDAEYMAYMFRYDSTHGVFNGTIKVlDDSTLEINGKQIKITSKR 164
Cdd:COG0057 2 TIRVAINGFGRIGRLVLRALLERgPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEV-EGDSLIVNGKKIKVLAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 165 DPAEIPWGDFGAEFVVESSGVFTTLEKAAAHKKGGAKKVVISAPSADA-PMFVVGVNEKTYKPNMDVVSNASCTTNCLAP 243
Cdd:COG0057 80 DPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 244 LAKVVHEEFGILEGLMTTVHATTATQKTVDGPsMKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPN 323
Cdd:COG0057 160 VAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 324 VSVVDLTCRLEKSASYEDVKAAIKYASEGPLMGILGYTDDDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWG 403
Cdd:COG0057 239 VSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWG 318
|
330
....*....|...
gi 224101329 404 YSNRVLDLIEHMA 416
Cdd:COG0057 319 YSNRMVDLAEYMA 331
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
88-410 |
1.10e-173 |
|
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: 488.33 E-value: 1.10e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 88 KIGINGFGRIGRLVLRVATFRDD--IDVVAVNDPfIDAEYMAYMFRYDSTHGVFNGTIKVlDDSTLEINGKQ-IKITSKR 164
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKPGndLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTV-DEDGLVVNGKEvISVFSER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 165 DPAEIPWGDFGAEFVVESSGVFTTLEKAAAHKKGGAKKVVISAPSADA-PMFVVGVNEKTYKPNMDVVSNASCTTNCLAP 243
Cdd:TIGR01534 79 DPSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 244 LAKVVHEEFGILEGLMTTVHATTATQKTVDGPsMKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPN 323
Cdd:TIGR01534 159 LAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 324 VSVVDLTCRLEKSASYEDVKAAIKYASEGPLMGILGYTDDDVVSNDFVGDSRSSIFDAKAGI--GLSASFMKLVSWYDNE 401
Cdd:TIGR01534 238 VSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKvtGLGDSLVKVYAWYDNE 317
|
....*....
gi 224101329 402 WGYSNRVLD 410
Cdd:TIGR01534 318 WGYSNRLVD 326
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
89-411 |
2.81e-119 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 350.00 E-value: 2.81e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 89 IGINGFGRIGRLVLRVATFRDDIDVVAVNDPFIDAEYMAYMFRYDSTHGVFNGTIKVLDDStLEINGKQIKITSKRDPAE 168
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDS-IVIDGKRISFSSNKDIED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 169 IPWGDfGAEFVVESSGVFTTLEKAAAHKKGGAKKVVISAP--SADAPMFVVGVNEKTYKPNMD-VVSNASCTTNCLAPLA 245
Cdd:NF033735 80 TPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARHrIVTAASCTTNCLAPVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 246 KVVHEEFGILEGLMTTVHATTATQKTVDGPSmKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVS 325
Cdd:NF033735 159 KVIHEKIGIKHGSITTIHDITNTQTIVDAPH-KDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNAS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 326 VVDLTCRLEKSASYEDVKAAIKYASEGPLMGILGYTDDDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYS 405
Cdd:NF033735 238 LTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYA 317
|
....*.
gi 224101329 406 NRVLDL 411
Cdd:NF033735 318 NRMVDL 323
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
236-401 |
2.23e-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: 341.74 E-value: 2.23e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 236 CTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSmKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGM 315
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 316 AFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLMGILGYTDDDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLV 395
Cdd:cd18126 80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159
|
....*.
gi 224101329 396 SWYDNE 401
Cdd:cd18126 160 AWYDNE 165
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
241-398 |
4.01e-88 |
|
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: 264.45 E-value: 4.01e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 241 LAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVP 320
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224101329 321 TPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLMGILGYTDDDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWY 398
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
87-236 |
3.84e-79 |
|
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: 240.92 E-value: 3.84e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 87 TKIGINGFGRIGRLVLRVATFRDDIDVVAVNDPfIDAEYMAYMFRYDSTHGVFNGTIKVlDDSTLEINGKQIKITSKRDP 166
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEV-EGDGLVVNGKAIKVFAERDP 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224101329 167 AEIPWGDFGAEFVVESSGVFTTLEKAAAHKKGGAKKVVISAPSADA-PMFVVGVNEKTYKPNMDVVSNASC 236
Cdd:smart00846 79 ANLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
1-422 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 888.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 1 MAFSTLLRSTPAAPLIEASRSDFSPSPSDRFEVSSIRFNSSKSIFGaSVPTGSSSLHTCSGRSIQPIKATATEMPPTVLR 80
Cdd:PLN02272 1 MAFSSLLRSAATAPAAAARGSDFSSSSSDPSKVSSVGFSSSLSFSG-SSSGASSSLQSCSARSVQPIKATATEAPPAVLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 81 SRADGKTKIGINGFGRIGRLVLRVATFRDDIDVVAVNDPFIDAEYMAYMFRYDSTHGVFNGTIKVLDDSTLEINGKQIKI 160
Cdd:PLN02272 80 SSSSGKTKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVVDDSTLEINGKQIKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 161 TSKRDPAEIPWGDFGAEFVVESSGVFTTLEKAAAHKKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMDVVSNASCTTNC 240
Cdd:PLN02272 160 TSKRDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 241 LAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVP 320
Cdd:PLN02272 240 LAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 321 TPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLMGILGYTDDDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDN 400
Cdd:PLN02272 320 TPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDN 399
|
410 420
....*....|....*....|..
gi 224101329 401 EWGYSNRVLDLIEHMALVAAHN 422
Cdd:PLN02272 400 EWGYSNRVLDLIEHMALVAASH 421
|
|
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
86-416 |
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: 582.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 86 KTKIGINGFGRIGRLVLRVATFR-DDIDVVAVNDPfIDAEYMAYMFRYDSTHGVFNGTIKVlDDSTLEINGKQIKITSKR 164
Cdd:COG0057 2 TIRVAINGFGRIGRLVLRALLERgPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEV-EGDSLIVNGKKIKVLAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 165 DPAEIPWGDFGAEFVVESSGVFTTLEKAAAHKKGGAKKVVISAPSADA-PMFVVGVNEKTYKPNMDVVSNASCTTNCLAP 243
Cdd:COG0057 80 DPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 244 LAKVVHEEFGILEGLMTTVHATTATQKTVDGPsMKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPN 323
Cdd:COG0057 160 VAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 324 VSVVDLTCRLEKSASYEDVKAAIKYASEGPLMGILGYTDDDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWG 403
Cdd:COG0057 239 VSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWG 318
|
330
....*....|...
gi 224101329 404 YSNRVLDLIEHMA 416
Cdd:COG0057 319 YSNRMVDLAEYMA 331
|
|
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
87-415 |
8.38e-179 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 501.67 E-value: 8.38e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 87 TKIGINGFGRIGRLVLRVATFRDDIDVVAVNDPFIDAEYMAYMFRYDSTHGVFNGTIKVLDDsTLEINGKQIKITSKRDP 166
Cdd:PTZ00023 3 VKLGINGFGRIGRLVFRAALEREDVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDG-FLMIGSKKVHVFFEKDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 167 AEIPWGDFGAEFVVESSGVFTTLEKAAAHKKGGAKKVVISAP-SADAPMFVVGVNEKTYKPNMDVVSNASCTTNCLAPLA 245
Cdd:PTZ00023 82 AAIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPpKDDTPIYVMGVNHTQYDKSQRIVSNASCTTNCLAPLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 246 KVVHEEFGILEGLMTTVHATTATQKTVDGPSM--KDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPN 323
Cdd:PTZ00023 162 KVVNDKFGIVEGLMTTVHASTANQLTVDGPSKggKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVPD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 324 VSVVDLTCRLEKSASYEDVKAAIKYASEGPLMGILGYTDDDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWG 403
Cdd:PTZ00023 242 VSVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDNEWG 321
|
330
....*....|..
gi 224101329 404 YSNRVLDLIEHM 415
Cdd:PTZ00023 322 YSNRLLDLAHYI 333
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
88-410 |
1.10e-173 |
|
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: 488.33 E-value: 1.10e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 88 KIGINGFGRIGRLVLRVATFRDD--IDVVAVNDPfIDAEYMAYMFRYDSTHGVFNGTIKVlDDSTLEINGKQ-IKITSKR 164
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKPGndLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTV-DEDGLVVNGKEvISVFSER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 165 DPAEIPWGDFGAEFVVESSGVFTTLEKAAAHKKGGAKKVVISAPSADA-PMFVVGVNEKTYKPNMDVVSNASCTTNCLAP 243
Cdd:TIGR01534 79 DPSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 244 LAKVVHEEFGILEGLMTTVHATTATQKTVDGPsMKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPN 323
Cdd:TIGR01534 159 LAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 324 VSVVDLTCRLEKSASYEDVKAAIKYASEGPLMGILGYTDDDVVSNDFVGDSRSSIFDAKAGI--GLSASFMKLVSWYDNE 401
Cdd:TIGR01534 238 VSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKvtGLGDSLVKVYAWYDNE 317
|
....*....
gi 224101329 402 WGYSNRVLD 410
Cdd:TIGR01534 318 WGYSNRLVD 326
|
|
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
83-416 |
1.81e-173 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 488.46 E-value: 1.81e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 83 ADGKTKIGINGFGRIGRLVLRVATFRDDIDVVAVNDPFIDAEYMAYMFRYDSTHGVF-NGTIKVLDDSTLEINGKQIKIT 161
Cdd:PLN02358 2 ADKKIRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWkHHELKVKDDKTLLFGEKPVTVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 162 SKRDPAEIPWGDFGAEFVVESSGVFTTLEKAAAHKKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMDVVSNASCTTNCL 241
Cdd:PLN02358 82 GIRNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCTTNCL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 242 APLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPT 321
Cdd:PLN02358 162 APLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 322 PNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLMGILGYTDDDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNE 401
Cdd:PLN02358 242 VDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNE 321
|
330
....*....|....*
gi 224101329 402 WGYSNRVLDLIEHMA 416
Cdd:PLN02358 322 WGYSSRVVDLIVHMS 336
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
88-416 |
1.02e-161 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 458.43 E-value: 1.02e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 88 KIGINGFGRIGRLVLRVATFRDDIDVVAVNDpFIDAEYMAYMFRYDSTHGVFNGTIKVlDDSTLEINGKQIKITSKRDPA 167
Cdd:PRK15425 4 KVGINGFGRIGRIVFRAAQKRSDIEIVAIND-LLDADYMAYMLKYDSTHGRFDGTVEV-KDGHLIVNGKKIRVTAERDPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 168 EIPWGDFGAEFVVESSGVFTTLEKAAAHKKGGAKKVVISAPSAD-APMFVVGVNEKTYKpNMDVVSNASCTTNCLAPLAK 246
Cdd:PRK15425 82 NLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDnTPMFVKGANFDKYA-GQDIVSNASCTTNCLAPLAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 247 VVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSV 326
Cdd:PRK15425 161 VINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 327 VDLTCRLEKSASYEDVKAAIKYASEGPLMGILGYTDDDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYSN 406
Cdd:PRK15425 241 VDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYSN 320
|
330
....*....|
gi 224101329 407 RVLDLIEHMA 416
Cdd:PRK15425 321 KVLDLIAHIS 330
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
88-416 |
1.18e-144 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 415.99 E-value: 1.18e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 88 KIGINGFGRIGRLVLRVATFRD----DIDVVAVNDPFIDAEYMAYMFRYDSTHGVFNGTIK-------VLDDSTLEINGK 156
Cdd:PTZ00434 5 KVGINGFGRIGRMVFQAICDQGligtEIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVEttksspsVKTDDVLVVNGH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 157 QIK-ITSKRDPAEIPWGDFGAEFVVESSGVFTTLEKAAAHKKGGAKKVVISAP-SADAPMFVVGVNEKTYKP-NMDVVSN 233
Cdd:PTZ00434 85 RIKcVKAQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPaSGGAKTIVMGVNQHEYSPtEHHVVSN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 234 ASCTTNCLAPLAKV-VHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKL 312
Cdd:PTZ00434 165 ASCTTNCLAPIVHVlTKEGFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGKL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 313 TGMAFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLMGILGYTDDDVVSNDFVGDSRSSIFDAKA----GIGLS 388
Cdd:PTZ00434 245 TGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKAtlqnNLPGE 324
|
330 340
....*....|....*....|....*...
gi 224101329 389 ASFMKLVSWYDNEWGYSNRVLDLIEHMA 416
Cdd:PTZ00434 325 RRFFKIVSWYDNEWGYSHRVVDLVRYMA 352
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
86-416 |
3.31e-143 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 411.82 E-value: 3.31e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 86 KTKIGINGFGRIGRLVLRVATFRDDIDVVAVNDPFiDAEYMAYMFRYDSTHGVFNGTIKVLDDStLEINGKQIKITSKRD 165
Cdd:PRK07729 2 KTKVAINGFGRIGRMVFRKAIKESAFEIVAINASY-PSETLAHLIKYDTVHGKFDGTVEAFEDH-LLVDGKKIRLLNNRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 166 PAEIPWGDFGAEFVVESSGVFTTLEKAAAHKKGGAKKVVISAPSADAPM-FVVGVNEKTYKPNMD-VVSNASCTTNCLAP 243
Cdd:PRK07729 80 PKELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVtIVVGVNEDQLDIEKHtIISNASCTTNCLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 244 LAKVVHEEFGILEGLMTTVHATTATQKTVDGPSmKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPN 323
Cdd:PRK07729 160 VVKVLDEQFGIENGLMTTVHAYTNDQKNIDNPH-KDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 324 VSVVDLTCRLEKSASYEDVKAAIKYASEGPLMGILGYTDDDVVSNDFVGDSRSSIFDakagiGLSASFM-----KLVSWY 398
Cdd:PRK07729 239 VSLVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIID-----GLSTMVMgdrkvKVLAWY 313
|
330
....*....|....*...
gi 224101329 399 DNEWGYSNRVLDLIEHMA 416
Cdd:PRK07729 314 DNEWGYSCRVVDLVTLVA 331
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
87-416 |
1.01e-120 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 354.21 E-value: 1.01e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 87 TKIGINGFGRIGRLVLRVATFRDD--IDVVAVNDPfIDAEYMAYMFRYDSTHGVFNGTIKVlDDSTLEINGKQIKITSKR 164
Cdd:PRK07403 2 IRVAINGFGRIGRNFLRCWLGRENsqLELVAINDT-SDPRTNAHLLKYDSMLGKLNADISA-DENSITVNGKTIKCVSDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 165 DPAEIPWGDFGAEFVVESSGVFTTLEKAAAHKKGGAKKVVISAP--SADAPMFVVGVNEKTYKPNM-DVVSNASCTTNCL 241
Cdd:PRK07403 80 NPLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPgkGEDIGTYVVGVNHHEYDHEDhNIISNASCTTNCL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 242 APLAKVVHEEFGILEGLMTTVHATTATQKTVDGpSMKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPT 321
Cdd:PRK07403 160 APIAKVLHDNFGIIKGTMTTTHSYTGDQRILDA-SHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 322 PNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLMGILGYTDDDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNE 401
Cdd:PRK07403 239 PNVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYDNE 318
|
330
....*....|....*
gi 224101329 402 WGYSNRVLDLIEHMA 416
Cdd:PRK07403 319 WGYSQRVVDLAELVA 333
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
89-411 |
2.81e-119 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 350.00 E-value: 2.81e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 89 IGINGFGRIGRLVLRVATFRDDIDVVAVNDPFIDAEYMAYMFRYDSTHGVFNGTIKVLDDStLEINGKQIKITSKRDPAE 168
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDS-IVIDGKRISFSSNKDIED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 169 IPWGDfGAEFVVESSGVFTTLEKAAAHKKGGAKKVVISAP--SADAPMFVVGVNEKTYKPNMD-VVSNASCTTNCLAPLA 245
Cdd:NF033735 80 TPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARHrIVTAASCTTNCLAPVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 246 KVVHEEFGILEGLMTTVHATTATQKTVDGPSmKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVS 325
Cdd:NF033735 159 KVIHEKIGIKHGSITTIHDITNTQTIVDAPH-KDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNAS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 326 VVDLTCRLEKSASYEDVKAAIKYASEGPLMGILGYTDDDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYS 405
Cdd:NF033735 238 LTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYA 317
|
....*.
gi 224101329 406 NRVLDL 411
Cdd:NF033735 318 NRMVDL 323
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
236-401 |
2.23e-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: 341.74 E-value: 2.23e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 236 CTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSmKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGM 315
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 316 AFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLMGILGYTDDDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLV 395
Cdd:cd18126 80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159
|
....*.
gi 224101329 396 SWYDNE 401
Cdd:cd18126 160 AWYDNE 165
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
12-411 |
2.96e-116 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 346.89 E-value: 2.96e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 12 AAPLIEASRSDFSPSPSDRFEVSSIRFNSSKSIFGASVPTGSSSLHTCSGRSIQPIKATATempptVLRSRADGKTKIGI 91
Cdd:PLN02237 6 ASSRIPATTRLPSKASHKRLEVAEFSGLRASSCVTFAKNAREASFFDVVASQLAPKVAGST-----PVRGETVAKLKVAI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 92 NGFGRIGRLVLRVATFRDD--IDVVAVNDPFiDAEYMAYMFRYDSTHGVFNGTIKVLDDSTLEINGKQIKITSKRDPAEI 169
Cdd:PLN02237 81 NGFGRIGRNFLRCWHGRKDspLDVVVVNDSG-GVKNASHLLKYDSMLGTFKADVKIVDDETISVDGKPIKVVSNRDPLKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 170 PWGDFGAEFVVESSGVFTTLEKAAAHKKGGAKKVVISAPS--ADAPMFVVGVNEKTYKPNM-DVVSNASCTTNCLAPLAK 246
Cdd:PLN02237 160 PWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAkgADIPTYVVGVNEDDYDHEVaNIVSNASCTTNCLAPFVK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 247 VVHEEFGILEGLMTTVHATTATQKTVDGpSMKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSV 326
Cdd:PLN02237 240 VLDEEFGIVKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTPNVSV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 327 VDLTCRLEKSA-SYEDVKAAIKYASEGPLMGILGYTDDDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYS 405
Cdd:PLN02237 319 VDLVVNVEKKGiTAEDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVAWYDNEWGYS 398
|
....*.
gi 224101329 406 NRVLDL 411
Cdd:PLN02237 399 QRVVDL 404
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
12-416 |
1.65e-115 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 343.07 E-value: 1.65e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 12 AAPLIEASRSDFSpspsdrfEVSSIRFNSSKSIFGASVPTGSSSLHTCSGRSIQPIKATATEmpptvlrsradGKTKIGI 91
Cdd:PLN03096 4 AKPSLQAGSKGFS-------EFSGLKSSSAVTFGKRSDSLDFVVFATSAVSSSGGARRAVTE-----------AKIKVAI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 92 NGFGRIGRLVLRVATFRDD--IDVVAVNDPFiDAEYMAYMFRYDSTHGVFNGTIKVLDDSTLEINGKQIKITSKRDPAEI 169
Cdd:PLN03096 66 NGFGRIGRNFLRCWHGRKDspLDVVAINDTG-GVKQASHLLKYDSTLGTFDADVKPVGDDAISVDGKVIKVVSDRNPLNL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 170 PWGDFGAEFVVESSGVFTTLEKAAAHKKGGAKKVVISAPS-ADAPMFVVGVNEKTYKPNMDVVSNASCTTNCLAPLAKVV 248
Cdd:PLN03096 145 PWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGkGDIPTYVVGVNADDYKHSDPIISNASCTTNCLAPFVKVL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 249 HEEFGILEGLMTTVHATTATQKTVDGpSMKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVD 328
Cdd:PLN03096 225 DQKFGIIKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 329 LTCRLEKSASYEDVKAAIKYASEGPLMGILGYTDDDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYSNRV 408
Cdd:PLN03096 304 LVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAWYDNEWGYSQRV 383
|
....*...
gi 224101329 409 LDLIEHMA 416
Cdd:PLN03096 384 VDLADIVA 391
|
|
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
88-418 |
4.28e-105 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 314.36 E-value: 4.28e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 88 KIGINGFGRIGRLVLRVATFRDDIDVVAVNDPFIDAEYMAYMFRYDSTHGVFNGTIKVlDDSTLEINGKQIKITSKRDPA 167
Cdd:PRK08955 4 KVGINGFGRIGRLALRAAWDWPELEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTA-EGDAIVINGKRIRTTQNKAIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 168 EIPWGdfGAEFVVESSGVFTTLEKAAAHKKGGAKKVVISAPSADAPMF--VVGVNEKTYKPNMD-VVSNASCTTNCLAPL 244
Cdd:PRK08955 83 DTDWS--GCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLniVMGVNDHLFDPAIHpIVTAASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 245 AKVVHEEFGILEGLMTTVHATTATQKTVDGPSmKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNV 324
Cdd:PRK08955 161 VKVIHEKLGIKHGSMTTIHDLTNTQTILDAPH-KDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLANA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 325 SVVDLTCRLEKSASYEDVKAAIKYASEGPLMGILGYTDDDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGY 404
Cdd:PRK08955 240 SLTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNEWGY 319
|
330
....*....|....
gi 224101329 405 SNRVLDLIEHMALV 418
Cdd:PRK08955 320 ANRTAELARKVGLA 333
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
88-416 |
6.73e-93 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 283.10 E-value: 6.73e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 88 KIGINGFGRIGRLVLRvATF----RDDIDVVAVNDpFIDAEYMAYMFRYDSTHGVFNGTIKvLDDSTLEINGKQIKITSK 163
Cdd:PRK13535 3 RVAINGFGRIGRNVLR-ALYesgrRAEITVVAINE-LADAEGMAHLLKYDTSHGRFAWDVR-QERDQLFVGDDAIRLLHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 164 RDPAEIPWGDFGAEFVVESSGVFTTLEKAAAHKKGGAKKVVISAPSA---DAPMfVVGVNEKTYKPNMDVVSNASCTTNC 240
Cdd:PRK13535 80 RDIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSndlDATV-VYGVNHDQLRAEHRIVSNASCTTNC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 241 LAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGpSMKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVP 320
Cdd:PRK13535 159 IIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 321 TPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLMGILGYTDDDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDN 400
Cdd:PRK13535 238 TINVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDN 317
|
330
....*....|....*.
gi 224101329 401 EWGYSNRVLDLIEHMA 416
Cdd:PRK13535 318 EWGFANRMLDTTLAMA 333
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
241-398 |
4.01e-88 |
|
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: 264.45 E-value: 4.01e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 241 LAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVP 320
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 224101329 321 TPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLMGILGYTDDDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWY 398
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
93-416 |
2.39e-85 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 268.33 E-value: 2.39e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 93 GFGRIGRLV---------------LRVATFRDDIDVvavndpfiDAEYMAYMFRYDSTHGVFNGTIKV-LDDSTLEINGK 156
Cdd:PRK08289 134 GFGRIGRLLarlliektgggnglrLRAIVVRKGSEG--------DLEKRASLLRRDSVHGPFNGTITVdEENNAIIANGN 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 157 QIKITSKRDPAEIPWGDFGAE--FVVESSGVFTTLEKAAAH-KKGGAKKVVISAPS-ADAPMFVVGVNEKTYKPNMDVVS 232
Cdd:PRK08289 206 YIQVIYANSPEEVDYTAYGINnaLVVDNTGKWRDEEGLSQHlKSKGVAKVLLTAPGkGDIKNIVHGVNHSDITDEDKIVS 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 233 NASCTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDwRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKL 312
Cdd:PRK08289 286 AASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKGD-RRGRSAPLNMVITETGAAKAVAKALPELAGKL 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 313 TGMAFRVPTPNVSVVDLTCRLEKSASYEDVKAAIK-YASEGPLMGILGYTDD-DVVSNDFVGDSRSSIFDAKAGIgLSAS 390
Cdd:PRK08289 365 TGNAIRVPTPNVSMAILNLNLEKETSREELNEYLRqMSLHSPLQNQIDYTDStEVVSSDFVGSRHAGVVDSQATI-VNGN 443
|
330 340
....*....|....*....|....*.
gi 224101329 391 FMKLVSWYDNEWGYSNRVLDLIEHMA 416
Cdd:PRK08289 444 RAVLYVWYDNEFGYSCQVVRVMEQMA 469
|
|
| GAPDH_I_N |
cd05214 |
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
87-235 |
2.52e-85 |
|
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: 257.32 E-value: 2.52e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 87 TKIGINGFGRIGRLVLRVATFRDDIDVVAVNDPFiDAEYMAYMFRYDSTHGVFNGTIKVlDDSTLEINGKQIKITSKRDP 166
Cdd:cd05214 1 IKVGINGFGRIGRLVFRAALERDDIEVVAINDLT-DDETLAYLLKYDSVHGRFDGEVEV-DDDALIVNGKKIKVFAERDP 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 167 AEIPWGDFGAEFVVESSGVFTTLEKAAAHKKGGAKKVVISAPSAD-APMFVVGVNEKTYKPNMDVVSNAS 235
Cdd:cd05214 79 AELPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDADDKIISNAS 148
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
236-401 |
1.91e-81 |
|
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: 247.53 E-value: 1.91e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 236 CTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGM 315
Cdd:cd18123 1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 316 AFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPlmGILGYTDDDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLV 395
Cdd:cd18123 81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEGK--GRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLM 158
|
....*.
gi 224101329 396 SWYDNE 401
Cdd:cd18123 159 QWYDNE 164
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
87-236 |
3.84e-79 |
|
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: 240.92 E-value: 3.84e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 87 TKIGINGFGRIGRLVLRVATFRDDIDVVAVNDPfIDAEYMAYMFRYDSTHGVFNGTIKVlDDSTLEINGKQIKITSKRDP 166
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEV-EGDGLVVNGKAIKVFAERDP 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 224101329 167 AEIPWGDFGAEFVVESSGVFTTLEKAAAHKKGGAKKVVISAPSADA-PMFVVGVNEKTYKPNMDVVSNASC 236
Cdd:smart00846 79 ANLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
89-415 |
1.08e-60 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 200.49 E-value: 1.08e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 89 IGINGFGRIGRLVLRVATFRDDIDVVAVNDPFIDAEYMAYMFRYDSTHGVFNGT-IKVLDDSTLEINGKQIKITSKRDPA 167
Cdd:PTZ00353 5 VGINGFGPVGKAVLFASLTDPLVTVVAVNDASVSIAYIAYVLEQESPLSAPDGAsIRVVGEQIVLNGTQKIRVSAKHDLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 168 EIPWGDFGAEFVVESSGVFTTLEKAAAHKKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMDVVSNASCTTNCLAPLAKV 247
Cdd:PTZ00353 85 EIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDERLSASLPVCCAGAPIAVALAPVIRA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 248 VHEEFGILEGLMTTVHATTATQKT-VDGPSMKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSV 326
Cdd:PTZ00353 165 LHEVYGVEECSYTAIHGMQPQEPIaARSKNSQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVKKGCA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 327 VDLTCRLEKSASYEDVKAAIKYASEGPLMGILGYTDDDVVSNDFVGDSRsSIFDAKAGIGLS-ASFMKLVSWYDNEWGYS 405
Cdd:PTZ00353 245 IDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCIPNGK-LCYDATSSSSSReGEVHKMVLWFDVECYYA 323
|
330
....*....|
gi 224101329 406 NRVLDLIEHM 415
Cdd:PTZ00353 324 ARLLSLVKQL 333
|
|
| Gp_dh_N |
pfam00044 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
87-188 |
6.58e-51 |
|
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: 166.51 E-value: 6.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 87 TKIGINGFGRIGRLVLRVATFRDDIDVVAVNDpFIDAEYMAYMFRYDSTHGVFNGTIKVlDDSTLEINGKQIKITSKRDP 166
Cdd:pfam00044 1 VKVGINGFGRIGRLVLRAALERPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEA-EEDGLVVNGKKIKVFAERDP 78
|
90 100
....*....|....*....|..
gi 224101329 167 AEIPWGDFGAEFVVESSGVFTT 188
Cdd:pfam00044 79 AELPWGDLGVDVVIESTGVFTT 100
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
236-401 |
1.04e-45 |
|
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: 155.37 E-value: 1.04e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 236 CTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWrgGRGAAQNIIPSSTGAAKAVGKVLPELN--GKLT 313
Cdd:cd18122 1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIGkpIKVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 314 GMAFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLMGILGYTDDDVVSNDFVGDSRSSIFDAKAGIGLSASFMK 393
Cdd:cd18122 79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLK 158
|
....*...
gi 224101329 394 LVSWYDNE 401
Cdd:cd18122 159 VFSAVDNE 166
|
|
| GAPDH_N_E4PDH |
cd17892 |
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
88-235 |
1.13e-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: 155.50 E-value: 1.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 88 KIGINGFGRIGRLVLRV---ATFRDDIDVVAVNDPfIDAEYMAYMFRYDSTHGVFNGTIKVlDDSTLEINGKQIKITSKR 164
Cdd:cd17892 2 RVAINGYGRIGRNVLRAlyeSGRRAEFQVVAINEL-ADAETIAHLTKYDTTHGRFPGEVRV-ENDQLFVNGDKIRVLHEP 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224101329 165 DPAEIPWGDFGAEFVVESSGVFTTLEKAAAHKKGGAKKVVISAPSA---DAPMfVVGVNEKTYKPNMDVVSNAS 235
Cdd:cd17892 80 DPENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASndvDATI-VYGINQDLLRAEHRIVSNAS 152
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
236-401 |
4.02e-45 |
|
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: 154.11 E-value: 4.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 236 CTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGpSMKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGM 315
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 316 AFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLMGILGYTDDDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLV 395
Cdd:cd23937 80 AVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLL 159
|
....*.
gi 224101329 396 SWYDNE 401
Cdd:cd23937 160 VWCDNE 165
|
|
| GAPDH-like_N |
cd05192 |
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ... |
88-240 |
1.96e-13 |
|
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: 66.22 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 224101329 88 KIGINGFGRIGRLVLRVATFRDDIDVVAVNDpfidaeymaymfrydsthgvfngtikvlddsTLEIngkqikitskrdpa 167
Cdd:cd05192 2 RVAINGFGRIGRIVFRAIADQDDLDVVAIND-------------------------------RRDV-------------- 36
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90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224101329 168 eipwgdfgaefVVESSGVFTTLEKAAAHKKGGAKKVVISAPS-ADAPMFVVGVNEKTYKPNMDVVSNASCTTNC 240
Cdd:cd05192 37 -----------VIECTGSFTDDDNAEKHIKAGGKKAVITAPEkGDIPTIVVVLNELAKSAGATVVSNANETSYS 99
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| 2-Hacid_dh_8 |
cd12167 |
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ... |
67-129 |
7.69e-05 |
|
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.
Pssm-ID: 240644 [Multi-domain] Cd Length: 330 Bit Score: 44.47 E-value: 7.69e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 224101329 67 IKATATEMPPTVLRSRADGKTKIGINGFGRIGRLVLR-VATFRDDidvVAVNDPFIDAEYMAYM 129
Cdd:cd12167 131 YRAGRDWGWPTRRGGRGLYGRTVGIVGFGRIGRAVVElLRPFGLR---VLVYDPYLPAAEAAAL 191
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| CtBP_dh |
cd05299 |
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ... |
82-131 |
7.87e-04 |
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C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related repressor; The transcriptional corepressor CtBP is a dehydrogenase with sequence and structural similarity to the d2-hydroxyacid dehydrogenase family. CtBP was initially identified as a protein that bound the PXDLS sequence at the adenovirus E1A C terminus, causing the loss of CR-1-mediated transactivation. CtBP binds NAD(H) within a deep cleft, undergoes a conformational change upon NAD binding, and has NAD-dependent dehydrogenase activity.
Pssm-ID: 240624 [Multi-domain] Cd Length: 312 Bit Score: 41.35 E-value: 7.87e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 224101329 82 RADGKTkIGINGFGRIGRLV-LRVATFrdDIDVVAvNDPFIDAEYMAYMFR 131
Cdd:cd05299 139 RLRGLT-LGLVGFGRIGRAVaKRAKAF--GFRVIA-YDPYVPDGVAALGGV 185
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| PGDH_like_2 |
cd12172 |
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ... |
85-125 |
5.45e-03 |
|
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Many, not all, members of this family are dimeric.
Pssm-ID: 240649 [Multi-domain] Cd Length: 306 Bit Score: 38.62 E-value: 5.45e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 224101329 85 GKTkIGINGFGRIGRLVLRVAT-FrdDIDVVAvNDPFIDAEY 125
Cdd:cd12172 142 GKT-LGIIGLGRIGKAVARRLSgF--GMKVLA-YDPYPDEEF 179
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| PGDH_4 |
cd12173 |
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ... |
85-124 |
8.96e-03 |
|
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases. PGDH in E. coli and Mycobacterium tuberculosis form tetramers, with subunits containing a Rossmann-fold NAD binding domain. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence.
Pssm-ID: 240650 [Multi-domain] Cd Length: 304 Bit Score: 37.78 E-value: 8.96e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 224101329 85 GKTkIGINGFGRIGRLVLRVA-TFrdDIDVVAvNDPFIDAE 124
Cdd:cd12173 138 GKT-LGIVGLGRIGREVARRArAF--GMKVLA-YDPYISAE 174
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