|
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: 881.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 1 MAFSCLLRSTPAAPLVEASRSDFSPSPSDRFKVSSVSFNSLKSIFGtSIPTGSSSSQTCSGRSIQPIKATATEMPPTVLK 80
Cdd:PLN02272 1 MAFSSLLRSAATAPAAAARGSDFSSSSSDPSKVSSVGFSSSLSFSG-SSSGASSSLQSCSARSVQPIKATATEAPPAVLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 81 SRADGKTKIGINGFGRIGRLVLRVATFRDDIDVVAVNDPFIDANYMAYMFKYDSTHGVFSGTIKVLDDSNLEINGKQIKI 160
Cdd:PLN02272 80 SSSSGKTKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVVDDSTLEINGKQIKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 161 TSKRDPTEIPWGDFGAEYVVESSGIFTTVEKAAAHMKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMDIVSNASCTTNC 240
Cdd:PLN02272 160 TSKRDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 241 LAPLAKVVHEEFGIIEGLMTTVHATTATQKTVDGPSRKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVP 320
Cdd:PLN02272 240 LAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 321 TPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDDDVVSSDFLGDSRSSIFDAKAGIGLSASFMKLVSWYDN 400
Cdd:PLN02272 320 TPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDN 399
|
410 420
....*....|....*....|..
gi 1334302015 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: 591.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 86 KTKIGINGFGRIGRLVLRVATFR-DDIDVVAVNDPfIDANYMAYMFKYDSTHGVFSGTIKVlDDSNLEINGKQIKITSKR 164
Cdd:COG0057 2 TIRVAINGFGRIGRLVLRALLERgPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEV-EGDSLIVNGKKIKVLAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 165 DPTEIPWGDFGAEYVVESSGIFTTVEKAAAHMKGGAKKVVISAPSADA-PMFVVGVNEKTYKPNMDIVSNASCTTNCLAP 243
Cdd:COG0057 80 DPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 244 LAKVVHEEFGIIEGLMTTVHATTATQKTVDGPsRKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPN 323
Cdd:COG0057 160 VAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 324 VSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDDDVVSSDFLGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWG 403
Cdd:COG0057 239 VSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWG 318
|
330
....*....|...
gi 1334302015 404 YSNRVLDLIEHMA 416
Cdd:COG0057 319 YSNRMVDLAEYMA 331
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
88-410 |
2.27e-175 |
|
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: 492.56 E-value: 2.27e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 88 KIGINGFGRIGRLVLRVATFRDD--IDVVAVNDPfIDANYMAYMFKYDSTHGVFSGTIKVlDDSNLEINGKQ-IKITSKR 164
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKPGndLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTV-DEDGLVVNGKEvISVFSER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 165 DPTEIPWGDFGAEYVVESSGIFTTVEKAAAHMKGGAKKVVISAPSADA-PMFVVGVNEKTYKPNMDIVSNASCTTNCLAP 243
Cdd:TIGR01534 79 DPSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 244 LAKVVHEEFGIIEGLMTTVHATTATQKTVDGPsRKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPN 323
Cdd:TIGR01534 159 LAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 324 VSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDDDVVSSDFLGDSRSSIFDAKAGI--GLSASFMKLVSWYDNE 401
Cdd:TIGR01534 238 VSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKvtGLGDSLVKVYAWYDNE 317
|
....*....
gi 1334302015 402 WGYSNRVLD 410
Cdd:TIGR01534 318 WGYSNRLVD 326
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
89-411 |
1.98e-121 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 355.40 E-value: 1.98e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 89 IGINGFGRIGRLVLRVATFRDDIDVVAVNDPFIDANYMAYMFKYDSTHGVFSGTIKVlDDSNLEINGKQIKITSKRDPTE 168
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTA-EEDSIVIDGKRISFSSNKDIED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 169 IPWGDfGAEYVVESSGIFTTVEKAAAHMKGGAKKVVISAP--SADAPMFVVGVNEKTYKPNMD-IVSNASCTTNCLAPLA 245
Cdd:NF033735 80 TPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARHrIVTAASCTTNCLAPVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 246 KVVHEEFGIIEGLMTTVHATTATQKTVDGPsRKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVS 325
Cdd:NF033735 159 KVIHEKIGIKHGSITTIHDITNTQTIVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNAS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 326 VVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDDDVVSSDFLGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYS 405
Cdd:NF033735 238 LTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYA 317
|
....*.
gi 1334302015 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 |
3.16e-120 |
|
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (1.2.1.12), NADP (1.2.1.13) or either (1.2.1.59). The family corresponds to the ubiquitous NAD+ or NADP+ utilizing type I GAPDH and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose.
Pssm-ID: 467676 Cd Length: 165 Bit Score: 346.36 E-value: 3.16e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 236 CTTNCLAPLAKVVHEEFGIIEGLMTTVHATTATQKTVDGPSrKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGM 315
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 316 AFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDDDVVSSDFLGDSRSSIFDAKAGIGLSASFMKLV 395
Cdd:cd18126 80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159
|
....*.
gi 1334302015 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 |
2.59e-91 |
|
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. C-terminal domain is a mixed alpha/antiparallel beta fold.
Pssm-ID: 460700 Cd Length: 158 Bit Score: 272.54 E-value: 2.59e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 241 LAPLAKVVHEEFGIIEGLMTTVHATTATQKTVDGPSRKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVP 320
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1334302015 321 TPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDDDVVSSDFLGDSRSSIFDAKAGIGLSASFMKLVSWY 398
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
87-236 |
2.50e-80 |
|
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: 244.00 E-value: 2.50e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 87 TKIGINGFGRIGRLVLRVATFRDDIDVVAVNDPfIDANYMAYMFKYDSTHGVFSGTIKVlDDSNLEINGKQIKITSKRDP 166
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEV-EGDGLVVNGKAIKVFAERDP 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1334302015 167 TEIPWGDFGAEYVVESSGIFTTVEKAAAHMKGGAKKVVISAPSADA-PMFVVGVNEKTYKPNMDIVSNASC 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: 881.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 1 MAFSCLLRSTPAAPLVEASRSDFSPSPSDRFKVSSVSFNSLKSIFGtSIPTGSSSSQTCSGRSIQPIKATATEMPPTVLK 80
Cdd:PLN02272 1 MAFSSLLRSAATAPAAAARGSDFSSSSSDPSKVSSVGFSSSLSFSG-SSSGASSSLQSCSARSVQPIKATATEAPPAVLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 81 SRADGKTKIGINGFGRIGRLVLRVATFRDDIDVVAVNDPFIDANYMAYMFKYDSTHGVFSGTIKVLDDSNLEINGKQIKI 160
Cdd:PLN02272 80 SSSSGKTKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVVDDSTLEINGKQIKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 161 TSKRDPTEIPWGDFGAEYVVESSGIFTTVEKAAAHMKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMDIVSNASCTTNC 240
Cdd:PLN02272 160 TSKRDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNC 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 241 LAPLAKVVHEEFGIIEGLMTTVHATTATQKTVDGPSRKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVP 320
Cdd:PLN02272 240 LAPLAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 321 TPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDDDVVSSDFLGDSRSSIFDAKAGIGLSASFMKLVSWYDN 400
Cdd:PLN02272 320 TPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDN 399
|
410 420
....*....|....*....|..
gi 1334302015 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: 591.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 86 KTKIGINGFGRIGRLVLRVATFR-DDIDVVAVNDPfIDANYMAYMFKYDSTHGVFSGTIKVlDDSNLEINGKQIKITSKR 164
Cdd:COG0057 2 TIRVAINGFGRIGRLVLRALLERgPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEV-EGDSLIVNGKKIKVLAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 165 DPTEIPWGDFGAEYVVESSGIFTTVEKAAAHMKGGAKKVVISAPSADA-PMFVVGVNEKTYKPNMDIVSNASCTTNCLAP 243
Cdd:COG0057 80 DPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 244 LAKVVHEEFGIIEGLMTTVHATTATQKTVDGPsRKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPN 323
Cdd:COG0057 160 VAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 324 VSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDDDVVSSDFLGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWG 403
Cdd:COG0057 239 VSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWG 318
|
330
....*....|...
gi 1334302015 404 YSNRVLDLIEHMA 416
Cdd:COG0057 319 YSNRMVDLAEYMA 331
|
|
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
87-415 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 509.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 87 TKIGINGFGRIGRLVLRVATFRDDIDVVAVNDPFIDANYMAYMFKYDSTHGVFSGTIKVLDDSnLEINGKQIKITSKRDP 166
Cdd:PTZ00023 3 VKLGINGFGRIGRLVFRAALEREDVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGF-LMIGSKKVHVFFEKDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 167 TEIPWGDFGAEYVVESSGIFTTVEKAAAHMKGGAKKVVISAP-SADAPMFVVGVNEKTYKPNMDIVSNASCTTNCLAPLA 245
Cdd:PTZ00023 82 AAIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPpKDDTPIYVMGVNHTQYDKSQRIVSNASCTTNCLAPLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 246 KVVHEEFGIIEGLMTTVHATTATQKTVDGPSR--KDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPN 323
Cdd:PTZ00023 162 KVVNDKFGIVEGLMTTVHASTANQLTVDGPSKggKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVPD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 324 VSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDDDVVSSDFLGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWG 403
Cdd:PTZ00023 242 VSVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDNEWG 321
|
330
....*....|..
gi 1334302015 404 YSNRVLDLIEHM 415
Cdd:PTZ00023 322 YSNRLLDLAHYI 333
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
88-410 |
2.27e-175 |
|
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: 492.56 E-value: 2.27e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 88 KIGINGFGRIGRLVLRVATFRDD--IDVVAVNDPfIDANYMAYMFKYDSTHGVFSGTIKVlDDSNLEINGKQ-IKITSKR 164
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKPGndLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTV-DEDGLVVNGKEvISVFSER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 165 DPTEIPWGDFGAEYVVESSGIFTTVEKAAAHMKGGAKKVVISAPSADA-PMFVVGVNEKTYKPNMDIVSNASCTTNCLAP 243
Cdd:TIGR01534 79 DPSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 244 LAKVVHEEFGIIEGLMTTVHATTATQKTVDGPsRKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPN 323
Cdd:TIGR01534 159 LAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 324 VSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDDDVVSSDFLGDSRSSIFDAKAGI--GLSASFMKLVSWYDNE 401
Cdd:TIGR01534 238 VSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKvtGLGDSLVKVYAWYDNE 317
|
....*....
gi 1334302015 402 WGYSNRVLD 410
Cdd:TIGR01534 318 WGYSNRLVD 326
|
|
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
83-416 |
3.85e-173 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 487.69 E-value: 3.85e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 83 ADGKTKIGINGFGRIGRLVLRVATFRDDIDVVAVNDPFIDANYMAYMFKYDSTHGVFS-GTIKVLDDSNLEINGKQIKIT 161
Cdd:PLN02358 2 ADKKIRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKhHELKVKDDKTLLFGEKPVTVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 162 SKRDPTEIPWGDFGAEYVVESSGIFTTVEKAAAHMKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMDIVSNASCTTNCL 241
Cdd:PLN02358 82 GIRNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCTTNCL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 242 APLAKVVHEEFGIIEGLMTTVHATTATQKTVDGPSRKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPT 321
Cdd:PLN02358 162 APLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 322 PNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDDDVVSSDFLGDSRSSIFDAKAGIGLSASFMKLVSWYDNE 401
Cdd:PLN02358 242 VDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNE 321
|
330
....*....|....*
gi 1334302015 402 WGYSNRVLDLIEHMA 416
Cdd:PLN02358 322 WGYSSRVVDLIVHMS 336
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
88-416 |
2.57e-163 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 462.28 E-value: 2.57e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 88 KIGINGFGRIGRLVLRVATFRDDIDVVAVNDpFIDANYMAYMFKYDSTHGVFSGTIKVlDDSNLEINGKQIKITSKRDPT 167
Cdd:PRK15425 4 KVGINGFGRIGRIVFRAAQKRSDIEIVAIND-LLDADYMAYMLKYDSTHGRFDGTVEV-KDGHLIVNGKKIRVTAERDPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 168 EIPWGDFGAEYVVESSGIFTTVEKAAAHMKGGAKKVVISAPSAD-APMFVVGVNEKTYKpNMDIVSNASCTTNCLAPLAK 246
Cdd:PRK15425 82 NLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDnTPMFVKGANFDKYA-GQDIVSNASCTTNCLAPLAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 247 VVHEEFGIIEGLMTTVHATTATQKTVDGPSRKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSV 326
Cdd:PRK15425 161 VINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 327 VDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDDDVVSSDFLGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYSN 406
Cdd:PRK15425 241 VDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYSN 320
|
330
....*....|
gi 1334302015 407 RVLDLIEHMA 416
Cdd:PRK15425 321 KVLDLIAHIS 330
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
86-416 |
1.76e-145 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 417.60 E-value: 1.76e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 86 KTKIGINGFGRIGRLVLRVATFRDDIDVVAVNDPFiDANYMAYMFKYDSTHGVFSGTIKVLDDSnLEINGKQIKITSKRD 165
Cdd:PRK07729 2 KTKVAINGFGRIGRMVFRKAIKESAFEIVAINASY-PSETLAHLIKYDTVHGKFDGTVEAFEDH-LLVDGKKIRLLNNRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 166 PTEIPWGDFGAEYVVESSGIFTTVEKAAAHMKGGAKKVVISAPSADAPM-FVVGVNEKTYKPNMD-IVSNASCTTNCLAP 243
Cdd:PRK07729 80 PKELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVtIVVGVNEDQLDIEKHtIISNASCTTNCLAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 244 LAKVVHEEFGIIEGLMTTVHATTATQKTVDGPsRKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPN 323
Cdd:PRK07729 160 VVKVLDEQFGIENGLMTTVHAYTNDQKNIDNP-HKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 324 VSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDDDVVSSDFLGDSRSSIFDakagiGLSASFM-----KLVSWY 398
Cdd:PRK07729 239 VSLVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIID-----GLSTMVMgdrkvKVLAWY 313
|
330
....*....|....*...
gi 1334302015 399 DNEWGYSNRVLDLIEHMA 416
Cdd:PRK07729 314 DNEWGYSCRVVDLVTLVA 331
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
88-416 |
4.60e-144 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 414.84 E-value: 4.60e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 88 KIGINGFGRIGRLVLRVATFRD----DIDVVAVNDPFIDANYMAYMFKYDSTHGVFSGTIK-------VLDDSNLEINGK 156
Cdd:PTZ00434 5 KVGINGFGRIGRMVFQAICDQGligtEIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVEttksspsVKTDDVLVVNGH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 157 QIK-ITSKRDPTEIPWGDFGAEYVVESSGIFTTVEKAAAHMKGGAKKVVISAP-SADAPMFVVGVNEKTYKP-NMDIVSN 233
Cdd:PTZ00434 85 RIKcVKAQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPaSGGAKTIVMGVNQHEYSPtEHHVVSN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 234 ASCTTNCLAPLAKV-VHEEFGIIEGLMTTVHATTATQKTVDGPSRKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKL 312
Cdd:PTZ00434 165 ASCTTNCLAPIVHVlTKEGFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGKL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 313 TGMAFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDDDVVSSDFLGDSRSSIFDAKA----GIGLS 388
Cdd:PTZ00434 245 TGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKAtlqnNLPGE 324
|
330 340
....*....|....*....|....*...
gi 1334302015 389 ASFMKLVSWYDNEWGYSNRVLDLIEHMA 416
Cdd:PTZ00434 325 RRFFKIVSWYDNEWGYSHRVVDLVRYMA 352
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
87-416 |
1.74e-122 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 358.84 E-value: 1.74e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 87 TKIGINGFGRIGRLVLRVATFRDD--IDVVAVNDPfIDANYMAYMFKYDSTHGVFSGTIKVlDDSNLEINGKQIKITSKR 164
Cdd:PRK07403 2 IRVAINGFGRIGRNFLRCWLGRENsqLELVAINDT-SDPRTNAHLLKYDSMLGKLNADISA-DENSITVNGKTIKCVSDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 165 DPTEIPWGDFGAEYVVESSGIFTTVEKAAAHMKGGAKKVVISAP--SADAPMFVVGVNEKTYKPNM-DIVSNASCTTNCL 241
Cdd:PRK07403 80 NPLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPgkGEDIGTYVVGVNHHEYDHEDhNIISNASCTTNCL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 242 APLAKVVHEEFGIIEGLMTTVHATTATQKTVDGpSRKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPT 321
Cdd:PRK07403 160 APIAKVLHDNFGIIKGTMTTTHSYTGDQRILDA-SHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 322 PNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDDDVVSSDFLGDSRSSIFDAKAGIGLSASFMKLVSWYDNE 401
Cdd:PRK07403 239 PNVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYDNE 318
|
330
....*....|....*
gi 1334302015 402 WGYSNRVLDLIEHMA 416
Cdd:PRK07403 319 WGYSQRVVDLAELVA 333
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
89-411 |
1.98e-121 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 355.40 E-value: 1.98e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 89 IGINGFGRIGRLVLRVATFRDDIDVVAVNDPFIDANYMAYMFKYDSTHGVFSGTIKVlDDSNLEINGKQIKITSKRDPTE 168
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTA-EEDSIVIDGKRISFSSNKDIED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 169 IPWGDfGAEYVVESSGIFTTVEKAAAHMKGGAKKVVISAP--SADAPMFVVGVNEKTYKPNMD-IVSNASCTTNCLAPLA 245
Cdd:NF033735 80 TPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARHrIVTAASCTTNCLAPVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 246 KVVHEEFGIIEGLMTTVHATTATQKTVDGPsRKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVS 325
Cdd:NF033735 159 KVIHEKIGIKHGSITTIHDITNTQTIVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNAS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 326 VVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDDDVVSSDFLGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYS 405
Cdd:NF033735 238 LTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYA 317
|
....*.
gi 1334302015 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 |
3.16e-120 |
|
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (1.2.1.12), NADP (1.2.1.13) or either (1.2.1.59). The family corresponds to the ubiquitous NAD+ or NADP+ utilizing type I GAPDH and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose.
Pssm-ID: 467676 Cd Length: 165 Bit Score: 346.36 E-value: 3.16e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 236 CTTNCLAPLAKVVHEEFGIIEGLMTTVHATTATQKTVDGPSrKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGM 315
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 316 AFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDDDVVSSDFLGDSRSSIFDAKAGIGLSASFMKLV 395
Cdd:cd18126 80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159
|
....*.
gi 1334302015 396 SWYDNE 401
Cdd:cd18126 160 AWYDNE 165
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
80-416 |
1.69e-117 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 348.07 E-value: 1.69e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 80 KSRADGKTKIGINGFGRIGRLVLRVATFRDD--IDVVAVNDPFiDANYMAYMFKYDSTHGVFSGTIKVLDDSNLEINGKQ 157
Cdd:PLN03096 54 RAVTEAKIKVAINGFGRIGRNFLRCWHGRKDspLDVVAINDTG-GVKQASHLLKYDSTLGTFDADVKPVGDDAISVDGKV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 158 IKITSKRDPTEIPWGDFGAEYVVESSGIFTTVEKAAAHMKGGAKKVVISAPS-ADAPMFVVGVNEKTYKPNMDIVSNASC 236
Cdd:PLN03096 133 IKVVSDRNPLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGkGDIPTYVVGVNADDYKHSDPIISNASC 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 237 TTNCLAPLAKVVHEEFGIIEGLMTTVHATTATQKTVDGpSRKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMA 316
Cdd:PLN03096 213 TTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 317 FRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDDDVVSSDFLGDSRSSIFDAKAGIGLSASFMKLVS 396
Cdd:PLN03096 292 LRVPTPNVSVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVA 371
|
330 340
....*....|....*....|
gi 1334302015 397 WYDNEWGYSNRVLDLIEHMA 416
Cdd:PLN03096 372 WYDNEWGYSQRVVDLADIVA 391
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
25-411 |
1.02e-116 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 348.04 E-value: 1.02e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 25 PSPSDRFKVSSVSFNSLK--SIFGTSIPTGSSSSQTCSGRSIQPIKATATempptVLKSRADGKTKIGINGFGRIGRLVL 102
Cdd:PLN02237 17 PSKASHKRLEVAEFSGLRasSCVTFAKNAREASFFDVVASQLAPKVAGST-----PVRGETVAKLKVAINGFGRIGRNFL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 103 RVATFRDD--IDVVAVNDPFiDANYMAYMFKYDSTHGVFSGTIKVLDDSNLEINGKQIKITSKRDPTEIPWGDFGAEYVV 180
Cdd:PLN02237 92 RCWHGRKDspLDVVVVNDSG-GVKNASHLLKYDSMLGTFKADVKIVDDETISVDGKPIKVVSNRDPLKLPWAELGIDIVI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 181 ESSGIFTTVEKAAAHMKGGAKKVVISAPS--ADAPMFVVGVNEKTYKPNM-DIVSNASCTTNCLAPLAKVVHEEFGIIEG 257
Cdd:PLN02237 171 EGTGVFVDGPGAGKHIQAGAKKVIITAPAkgADIPTYVVGVNEDDYDHEVaNIVSNASCTTNCLAPFVKVLDEEFGIVKG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 258 LMTTVHATTATQKTVDGpSRKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRLEKSA 337
Cdd:PLN02237 251 TMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTPNVSVVDLVVNVEKKG 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1334302015 338 -SYEDVKAAIKYASEGPLKGILGYTDDDVVSSDFLGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYSNRVLDL 411
Cdd:PLN02237 330 iTAEDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVAWYDNEWGYSQRVVDL 404
|
|
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
88-418 |
5.62e-107 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 318.98 E-value: 5.62e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 88 KIGINGFGRIGRLVLRVATFRDDIDVVAVNDPFIDANYMAYMFKYDSTHGVFSGTIKVlDDSNLEINGKQIKITSKRDPT 167
Cdd:PRK08955 4 KVGINGFGRIGRLALRAAWDWPELEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTA-EGDAIVINGKRIRTTQNKAIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 168 EIPWGdfGAEYVVESSGIFTTVEKAAAHMKGGAKKVVISAPSADAPMF--VVGVNEKTYKPNMD-IVSNASCTTNCLAPL 244
Cdd:PRK08955 83 DTDWS--GCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLniVMGVNDHLFDPAIHpIVTAASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 245 AKVVHEEFGIIEGLMTTVHATTATQKTVDGPsRKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNV 324
Cdd:PRK08955 161 VKVIHEKLGIKHGSMTTIHDLTNTQTILDAP-HKDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLANA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 325 SVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDDDVVSSDFLGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGY 404
Cdd:PRK08955 240 SLTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNEWGY 319
|
330
....*....|....
gi 1334302015 405 SNRVLDLIEHMALV 418
Cdd:PRK08955 320 ANRTAELARKVGLA 333
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
88-416 |
3.70e-94 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 286.57 E-value: 3.70e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 88 KIGINGFGRIGRLVLRvATF----RDDIDVVAVNDpFIDANYMAYMFKYDSTHGVFSGTIKvLDDSNLEINGKQIKITSK 163
Cdd:PRK13535 3 RVAINGFGRIGRNVLR-ALYesgrRAEITVVAINE-LADAEGMAHLLKYDTSHGRFAWDVR-QERDQLFVGDDAIRLLHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 164 RDPTEIPWGDFGAEYVVESSGIFTTVEKAAAHMKGGAKKVVISAPSA---DAPMfVVGVNEKTYKPNMDIVSNASCTTNC 240
Cdd:PRK13535 80 RDIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSndlDATV-VYGVNHDQLRAEHRIVSNASCTTNC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 241 LAPLAKVVHEEFGIIEGLMTTVHATTATQKTVDGpSRKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVP 320
Cdd:PRK13535 159 IIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 321 TPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDDDVVSSDFLGDSRSSIFDAKAGIGLSASFMKLVSWYDN 400
Cdd:PRK13535 238 TINVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDN 317
|
330
....*....|....*.
gi 1334302015 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 |
2.59e-91 |
|
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. C-terminal domain is a mixed alpha/antiparallel beta fold.
Pssm-ID: 460700 Cd Length: 158 Bit Score: 272.54 E-value: 2.59e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 241 LAPLAKVVHEEFGIIEGLMTTVHATTATQKTVDGPSRKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVP 320
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1334302015 321 TPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDDDVVSSDFLGDSRSSIFDAKAGIGLSASFMKLVSWY 398
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| GAPDH_I_N |
cd05214 |
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
87-235 |
3.57e-86 |
|
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: 259.63 E-value: 3.57e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 87 TKIGINGFGRIGRLVLRVATFRDDIDVVAVNDPFiDANYMAYMFKYDSTHGVFSGTIKVlDDSNLEINGKQIKITSKRDP 166
Cdd:cd05214 1 IKVGINGFGRIGRLVFRAALERDDIEVVAINDLT-DDETLAYLLKYDSVHGRFDGEVEV-DDDALIVNGKKIKVFAERDP 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 167 TEIPWGDFGAEYVVESSGIFTTVEKAAAHMKGGAKKVVISAPSAD-APMFVVGVNEKTYKPNMDIVSNAS 235
Cdd:cd05214 79 AELPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDADDKIISNAS 148
|
|
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
93-416 |
2.46e-85 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 268.33 E-value: 2.46e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 93 GFGRIGRLV---------------LRVATFRD--DIDVVAvndpfidanyMAYMFKYDSTHGVFSGTIKVLDDSN-LEIN 154
Cdd:PRK08289 134 GFGRIGRLLarlliektgggnglrLRAIVVRKgsEGDLEK----------RASLLRRDSVHGPFNGTITVDEENNaIIAN 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 155 GKQIKITSKRDPTEIPWGDFGAE--YVVESSGIFTTVEKAAAHMKG-GAKKVVISAPS-ADAPMFVVGVNEKTYKPNMDI 230
Cdd:PRK08289 204 GNYIQVIYANSPEEVDYTAYGINnaLVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGkGDIKNIVHGVNHSDITDEDKI 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 231 VSNASCTTNCLAPLAKVVHEEFGIIEGLMTTVHATTATQKTVDGPSRKDwRGGRGAAQNIIPSSTGAAKAVGKVLPELNG 310
Cdd:PRK08289 284 VSAASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKGD-RRGRSAPLNMVITETGAAKAVAKALPELAG 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 311 KLTGMAFRVPTPNVSVVDLTCRLEKSASYEDVKAAIK-YASEGPLKGILGYTDD-DVVSSDFLGDSRSSIFDAKAGIgLS 388
Cdd:PRK08289 363 KLTGNAIRVPTPNVSMAILNLNLEKETSREELNEYLRqMSLHSPLQNQIDYTDStEVVSSDFVGSRHAGVVDSQATI-VN 441
|
330 340
....*....|....*....|....*...
gi 1334302015 389 ASFMKLVSWYDNEWGYSNRVLDLIEHMA 416
Cdd:PRK08289 442 GNRAVLYVWYDNEFGYSCQVVRVMEQMA 469
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
236-401 |
2.45e-83 |
|
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: 252.54 E-value: 2.45e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 236 CTTNCLAPLAKVVHEEFGIIEGLMTTVHATTATQKTVDGPSRKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGM 315
Cdd:cd18123 1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 316 AFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYASEGplKGILGYTDDDVVSSDFLGDSRSSIFDAKAGIGLSASFMKLV 395
Cdd:cd18123 81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLM 158
|
....*.
gi 1334302015 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 |
2.50e-80 |
|
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: 244.00 E-value: 2.50e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 87 TKIGINGFGRIGRLVLRVATFRDDIDVVAVNDPfIDANYMAYMFKYDSTHGVFSGTIKVlDDSNLEINGKQIKITSKRDP 166
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEV-EGDGLVVNGKAIKVFAERDP 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1334302015 167 TEIPWGDFGAEYVVESSGIFTTVEKAAAHMKGGAKKVVISAPSADA-PMFVVGVNEKTYKPNMDIVSNASC 236
Cdd:smart00846 79 ANLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
89-415 |
8.84e-63 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 205.88 E-value: 8.84e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 89 IGINGFGRIGRLVLRVATFRDDIDVVAVNDPFIDANYMAYMFKYDSTHGVFSGT-IKVLDDSnLEINGKQ-IKITSKRDP 166
Cdd:PTZ00353 5 VGINGFGPVGKAVLFASLTDPLVTVVAVNDASVSIAYIAYVLEQESPLSAPDGAsIRVVGEQ-IVLNGTQkIRVSAKHDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 167 TEIPWGDFGAEYVVESSGIFTTVEKAAAHMKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMDIVSNASCTTNCLAPLAK 246
Cdd:PTZ00353 84 VEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDERLSASLPVCCAGAPIAVALAPVIR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 247 VVHEEFGIIEGLMTTVHATTAtQKTVDGPSR--KDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNV 324
Cdd:PTZ00353 164 ALHEVYGVEECSYTAIHGMQP-QEPIAARSKnsQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVKKG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 325 SVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDDDVVSSDFLGDSRsSIFDAKAGIGLS-ASFMKLVSWYDNEWG 403
Cdd:PTZ00353 243 CAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCIPNGK-LCYDATSSSSSReGEVHKMVLWFDVECY 321
|
330
....*....|..
gi 1334302015 404 YSNRVLDLIEHM 415
Cdd:PTZ00353 322 YAARLLSLVKQL 333
|
|
| Gp_dh_N |
pfam00044 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
87-188 |
4.62e-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: 166.89 E-value: 4.62e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 87 TKIGINGFGRIGRLVLRVATFRDDIDVVAVNDpFIDANYMAYMFKYDSTHGVFSGTIKVlDDSNLEINGKQIKITSKRDP 166
Cdd:pfam00044 1 VKVGINGFGRIGRLVLRAALERPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEA-EEDGLVVNGKKIKVFAERDP 78
|
90 100
....*....|....*....|..
gi 1334302015 167 TEIPWGDFGAEYVVESSGIFTT 188
Cdd:pfam00044 79 AELPWGDLGVDVVIESTGVFTT 100
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
236-401 |
8.76e-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: 158.45 E-value: 8.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 236 CTTNCLAPLAKVVHEEFGIIEGLMTTVHATTATQKTVDGPSRKDWrgGRGAAQNIIPSSTGAAKAVGKVLPELN--GKLT 313
Cdd:cd18122 1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIGkpIKVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 314 GMAFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDDDVVSSDFLGDSRSSIFDAKAGIGLSASFMK 393
Cdd:cd18122 79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLK 158
|
....*...
gi 1334302015 394 LVSWYDNE 401
Cdd:cd18122 159 VFSAVDNE 166
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
236-401 |
2.61e-46 |
|
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: 157.19 E-value: 2.61e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 236 CTTNCLAPLAKVVHEEFGIIEGLMTTVHATTATQKTVDGpSRKDWRGGRGAAQNIIPSSTGAAKAVGKVLPELNGKLTGM 315
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 316 AFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDDDVVSSDFLGDSRSSIFDAKAGIGLSASFMKLV 395
Cdd:cd23937 80 AVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLL 159
|
....*.
gi 1334302015 396 SWYDNE 401
Cdd:cd23937 160 VWCDNE 165
|
|
| GAPDH_N_E4PDH |
cd17892 |
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
88-235 |
2.36e-44 |
|
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: 152.04 E-value: 2.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334302015 88 KIGINGFGRIGRLVLRV---ATFRDDIDVVAVNDPfIDANYMAYMFKYDSTHGVFSGTIKVLDDSnLEINGKQIKITSKR 164
Cdd:cd17892 2 RVAINGYGRIGRNVLRAlyeSGRRAEFQVVAINEL-ADAETIAHLTKYDTTHGRFPGEVRVENDQ-LFVNGDKIRVLHEP 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1334302015 165 DPTEIPWGDFGAEYVVESSGIFTTVEKAAAHMKGGAKKVVISAPSA---DAPMfVVGVNEKTYKPNMDIVSNAS 235
Cdd:cd17892 80 DPENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASndvDATI-VYGINQDLLRAEHRIVSNAS 152
|
|
| GAPDH-like_N |
cd05192 |
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ... |
88-240 |
2.65e-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: 65.84 E-value: 2.65e-13
10 20 30 40 50 60 70 80
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gi 1334302015 88 KIGINGFGRIGRLVLRVATFRDDIDVVAVNDpfidanymaymfkydsthgvfsgtikvlddsnleingkqikitsKRDpt 167
Cdd:cd05192 2 RVAINGFGRIGRIVFRAIADQDDLDVVAIND--------------------------------------------RRD-- 35
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90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1334302015 168 eipwgdfgaeYVVESSGIFTTVEKAAAHMKGGAKKVVISAPS-ADAPMFVVGVNEKTYKPNMDIVSNASCTTNC 240
Cdd:cd05192 36 ----------VVIECTGSFTDDDNAEKHIKAGGKKAVITAPEkGDIPTIVVVLNELAKSAGATVVSNANETSYS 99
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| 2-Hacid_dh_8 |
cd12167 |
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ... |
67-129 |
1.38e-03 |
|
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: 40.62 E-value: 1.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1334302015 67 IKATATEMPPTVLKSRADGKTKIGINGFGRIGRLVLR-VATFRDDidvVAVNDPFIDANYMAYM 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 ... |
82-130 |
1.94e-03 |
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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: 39.81 E-value: 1.94e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1334302015 82 RADGKTkIGINGFGRIGRLV-LRVATFrdDIDVVAvNDPFIDANYMAYMF 130
Cdd:cd05299 139 RLRGLT-LGLVGFGRIGRAVaKRAKAF--GFRVIA-YDPYVPDGVAALGG 184
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