|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
2-333 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 620.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 2 GKIKIGINGFGRIGRLVARVALQSEDVELVAVNDPFITTDYMTYMFKYDTVHGHWKhSDITLKDSKTLLFGDKPVTVFGI 81
Cdd:PLN02272 84 GKTKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFK-GTINVVDDSTLEINGKQIKVTSK 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 82 RNPEEIPWGEAGAEYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEDKYTSDVNIVSNASCTTNCLAP 161
Cdd:PLN02272 163 RDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAP 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 162 LAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSAKDWRGGRAASFNIIPSSTGAAKAVGKVLPDLNGKLTGMSFRVPTVD 241
Cdd:PLN02272 243 LAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPN 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 242 VSVVDLTVRIEKGASYEDIKKAIKAASEGPLKGIMGYVEEDLVSTDFLGDSRSSIFDAKAGIALNDHFVKLVSWYDNEWG 321
Cdd:PLN02272 323 VSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWG 402
|
330
....*....|..
gi 162460999 322 YSNRVVDLIRHM 333
Cdd:PLN02272 403 YSNRVLDLIEHM 414
|
|
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
3-333 |
0e+00 |
|
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]; Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 439827 [Multi-domain] Cd Length: 334 Bit Score: 569.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 3 KIKIGINGFGRIGRLVARVALQS-EDVELVAVNDPfITTDYMTYMFKYDTVHGHWKHsDITLKDSkTLLFGDKPVTVFGI 81
Cdd:COG0057 2 TIRVAINGFGRIGRLVLRALLERgPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPG-EVEVEGD-SLIVNGKKIKVLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 82 RNPEEIPWGEAGAEYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDA-PMFVVGVNEDKYTSDVNIVSNASCTTNCLA 160
Cdd:COG0057 79 RDPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 161 PLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPsAKDWRGGRAASFNIIPSSTGAAKAVGKVLPDLNGKLTGMSFRVPTV 240
Cdd:COG0057 159 PVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 241 DVSVVDLTVRIEKGASYEDIKKAIKAASEGPLKGIMGYVEEDLVSTDFLGDSRSSIFDAKAGIALNDHFVKLVSWYDNEW 320
Cdd:COG0057 238 NVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEW 317
|
330
....*....|...
gi 162460999 321 GYSNRVVDLIRHM 333
Cdd:COG0057 318 GYSNRMVDLAEYM 330
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
5-328 |
9.73e-170 |
|
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: 474.84 E-value: 9.73e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 5 KIGINGFGRIGRLVARVALQSED--VELVAVNDPfITTDYMTYMFKYDTVHGHWKHSdITLKDsKTLLFGDKPVT-VFGI 81
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKPGndLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGE-VTVDE-DGLVVNGKEVIsVFSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 82 RNPEEIPWGEAGAEYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDA-PMFVVGVNEDKYTSDVNIVSNASCTTNCLA 160
Cdd:TIGR01534 78 RDPSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 161 PLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSaKDWRGGRAASFNIIPSSTGAAKAVGKVLPDLNGKLTGMSFRVPTV 240
Cdd:TIGR01534 158 PLAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPH-KDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 241 DVSVVDLTVRIEKGASYEDIKKAIKAASEGPLKGIMGYVEEDLVSTDFLGDSRSSIFDAKAGIA--LNDHFVKLVSWYDN 318
Cdd:TIGR01534 237 NVSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDN 316
|
330
....*....|
gi 162460999 319 EWGYSNRVVD 328
Cdd:TIGR01534 317 EWGYSNRLVD 326
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
154-319 |
2.09e-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: 343.67 E-value: 2.09e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 154 CTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSaKDWRGGRAASFNIIPSSTGAAKAVGKVLPDLNGKLTGM 233
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 234 SFRVPTVDVSVVDLTVRIEKGASYEDIKKAIKAASEGPLKGIMGYVEEDLVSTDFLGDSRSSIFDAKAGIALNDHFVKLV 313
Cdd:cd18126 80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159
|
....*.
gi 162460999 314 SWYDNE 319
Cdd:cd18126 160 AWYDNE 165
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
6-329 |
3.84e-118 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 343.84 E-value: 3.84e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 6 IGINGFGRIGRLVARVALQSEDVELVAVNDPFITTDYMTYMFKYDTVHGHWKHSdiTLKDSKTLLFGDKPVTVFGIRNPE 85
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAE--VTAEEDSIVIDGKRISFSSNKDIE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 86 EIPWGEaGAEYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMF--VVGVNEDKYTSDV-NIVSNASCTTNCLAPL 162
Cdd:NF033735 79 DTPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLniVYGVNDHLYDPARhRIVTAASCTTNCLAPV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 163 AKVIHDNFGIVEGLMTTVHAITATQKTVDGPsAKDWRGGRAASFNIIPSSTGAAKAVGKVLPDLNGKLTGMSFRVPTVDV 242
Cdd:NF033735 158 VKVIHEKIGIKHGSITTIHDITNTQTIVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 243 SVVDLTVRIEKGASYEDIKKAIKAASEGPLKGIMGYVEEDLVSTDFLGDSRSSIFDAKAGIALNDHFVKLVSWYDNEWGY 322
Cdd:NF033735 237 SLTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGY 316
|
....*..
gi 162460999 323 SNRVVDL 329
Cdd:NF033735 317 ANRMVDL 323
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
159-316 |
5.22e-90 |
|
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. C-terminal domain is a mixed alpha/antiparallel beta fold.
Pssm-ID: 460700 Cd Length: 158 Bit Score: 266.00 E-value: 5.22e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 159 LAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSAKDWRGGRAASFNIIPSSTGAAKAVGKVLPDLNGKLTGMSFRVP 238
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162460999 239 TVDVSVVDLTVRIEKGASYEDIKKAIKAASEGPLKGIMGYVEEDLVSTDFLGDSRSSIFDAKAGIALNDHFVKLVSWY 316
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
4-154 |
1.42e-71 |
|
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: 218.96 E-value: 1.42e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 4 IKIGINGFGRIGRLVARVALQSEDVELVAVNDPfITTDYMTYMFKYDTVHGHWKHsDITLKDSkTLLFGDKPVTVFGIRN 83
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPG-TVEVEGD-GLVVNGKAIKVFAERD 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162460999 84 PEEIPWGEAGAEYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDA-PMFVVGVNEDKYTSDVNIVSNASC 154
Cdd:smart00846 78 PANLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
2-333 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 620.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 2 GKIKIGINGFGRIGRLVARVALQSEDVELVAVNDPFITTDYMTYMFKYDTVHGHWKhSDITLKDSKTLLFGDKPVTVFGI 81
Cdd:PLN02272 84 GKTKIGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFK-GTINVVDDSTLEINGKQIKVTSK 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 82 RNPEEIPWGEAGAEYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEDKYTSDVNIVSNASCTTNCLAP 161
Cdd:PLN02272 163 RDPAEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAP 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 162 LAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSAKDWRGGRAASFNIIPSSTGAAKAVGKVLPDLNGKLTGMSFRVPTVD 241
Cdd:PLN02272 243 LAKVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPN 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 242 VSVVDLTVRIEKGASYEDIKKAIKAASEGPLKGIMGYVEEDLVSTDFLGDSRSSIFDAKAGIALNDHFVKLVSWYDNEWG 321
Cdd:PLN02272 323 VSVVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWG 402
|
330
....*....|..
gi 162460999 322 YSNRVVDLIRHM 333
Cdd:PLN02272 403 YSNRVLDLIEHM 414
|
|
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
3-336 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 579.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 3 KIKIGINGFGRIGRLVARVALQSEDVELVAVNDPFITTDYMTYMFKYDTVHGHWKHSDITLKDSKTLLFGDKPVTVFGIR 82
Cdd:PLN02358 5 KIRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKHHELKVKDDKTLLFGEKPVTVFGIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 83 NPEEIPWGEAGAEYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEDKYTSDVNIVSNASCTTNCLAPL 162
Cdd:PLN02358 85 NPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCTTNCLAPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 163 AKVIHDNFGIVEGLMTTVHAITATQKTVDGPSAKDWRGGRAASFNIIPSSTGAAKAVGKVLPDLNGKLTGMSFRVPTVDV 242
Cdd:PLN02358 165 AKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 243 SVVDLTVRIEKGASYEDIKKAIKAASEGPLKGIMGYVEEDLVSTDFLGDSRSSIFDAKAGIALNDHFVKLVSWYDNEWGY 322
Cdd:PLN02358 245 SVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEWGY 324
|
330
....*....|....
gi 162460999 323 SNRVVDLIRHMFKS 336
Cdd:PLN02358 325 SSRVVDLIVHMSKA 338
|
|
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
3-333 |
0e+00 |
|
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]; Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 439827 [Multi-domain] Cd Length: 334 Bit Score: 569.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 3 KIKIGINGFGRIGRLVARVALQS-EDVELVAVNDPfITTDYMTYMFKYDTVHGHWKHsDITLKDSkTLLFGDKPVTVFGI 81
Cdd:COG0057 2 TIRVAINGFGRIGRLVLRALLERgPDIEVVAINDL-GDAETLAHLLKYDSVHGRFPG-EVEVEGD-SLIVNGKKIKVLAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 82 RNPEEIPWGEAGAEYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDA-PMFVVGVNEDKYTSDVNIVSNASCTTNCLA 160
Cdd:COG0057 79 RDPAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 161 PLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPsAKDWRGGRAASFNIIPSSTGAAKAVGKVLPDLNGKLTGMSFRVPTV 240
Cdd:COG0057 159 PVAKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 241 DVSVVDLTVRIEKGASYEDIKKAIKAASEGPLKGIMGYVEEDLVSTDFLGDSRSSIFDAKAGIALNDHFVKLVSWYDNEW 320
Cdd:COG0057 238 NVSLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEW 317
|
330
....*....|...
gi 162460999 321 GYSNRVVDLIRHM 333
Cdd:COG0057 318 GYSNRMVDLAEYM 330
|
|
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
4-337 |
3.28e-178 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 496.66 E-value: 3.28e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 4 IKIGINGFGRIGRLVARVALQSEDVELVAVNDPFITTDYMTYMFKYDTVHGHWKhSDITLKDSKtLLFGDKPVTVFGIRN 83
Cdd:PTZ00023 3 VKLGINGFGRIGRLVFRAALEREDVEVVAINDPFMTLDYMCYLLKYDSVHGSLP-AEVSVTDGF-LMIGSKKVHVFFEKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 84 PEEIPWGEAGAEYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKD-APMFVVGVNEDKYTSDVNIVSNASCTTNCLAPL 162
Cdd:PTZ00023 81 PAAIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKDdTPIYVMGVNHTQYDKSQRIVSNASCTTNCLAPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 163 AKVIHDNFGIVEGLMTTVHAITATQKTVDGPS--AKDWRGGRAASFNIIPSSTGAAKAVGKVLPDLNGKLTGMSFRVPTV 240
Cdd:PTZ00023 161 AKVVNDKFGIVEGLMTTVHASTANQLTVDGPSkgGKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 241 DVSVVDLTVRIEKGASYEDIKKAIKAASEGPLKGIMGYVEEDLVSTDFLGDSRSSIFDAKAGIALNDHFVKLVSWYDNEW 320
Cdd:PTZ00023 241 DVSVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDNEW 320
|
330
....*....|....*..
gi 162460999 321 GYSNRVVDLIRHMFKSQ 337
Cdd:PTZ00023 321 GYSNRLLDLAHYITQKY 337
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
5-328 |
9.73e-170 |
|
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: 474.84 E-value: 9.73e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 5 KIGINGFGRIGRLVARVALQSED--VELVAVNDPfITTDYMTYMFKYDTVHGHWKHSdITLKDsKTLLFGDKPVT-VFGI 81
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKPGndLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGE-VTVDE-DGLVVNGKEVIsVFSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 82 RNPEEIPWGEAGAEYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDA-PMFVVGVNEDKYTSDVNIVSNASCTTNCLA 160
Cdd:TIGR01534 78 RDPSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 161 PLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSaKDWRGGRAASFNIIPSSTGAAKAVGKVLPDLNGKLTGMSFRVPTV 240
Cdd:TIGR01534 158 PLAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGPH-KDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 241 DVSVVDLTVRIEKGASYEDIKKAIKAASEGPLKGIMGYVEEDLVSTDFLGDSRSSIFDAKAGIA--LNDHFVKLVSWYDN 318
Cdd:TIGR01534 237 NVSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDN 316
|
330
....*....|
gi 162460999 319 EWGYSNRVVD 328
Cdd:TIGR01534 317 EWGYSNRLVD 326
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
4-335 |
4.80e-149 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 422.61 E-value: 4.80e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 4 IKIGINGFGRIGRLVARVALQSEDVELVAVNDpFITTDYMTYMFKYDTVHGHWKHSdITLKDSKTLLFGDKpVTVFGIRN 83
Cdd:PRK15425 3 IKVGINGFGRIGRIVFRAAQKRSDIEIVAIND-LLDADYMAYMLKYDSTHGRFDGT-VEVKDGHLIVNGKK-IRVTAERD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 84 PEEIPWGEAGAEYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKD-APMFVVGVNEDKYTSDvNIVSNASCTTNCLAPL 162
Cdd:PRK15425 80 PANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDnTPMFVKGANFDKYAGQ-DIVSNASCTTNCLAPL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 163 AKVIHDNFGIVEGLMTTVHAITATQKTVDGPSAKDWRGGRAASFNIIPSSTGAAKAVGKVLPDLNGKLTGMSFRVPTVDV 242
Cdd:PRK15425 159 AKVINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 243 SVVDLTVRIEKGASYEDIKKAIKAASEGPLKGIMGYVEEDLVSTDFLGDSRSSIFDAKAGIALNDHFVKLVSWYDNEWGY 322
Cdd:PRK15425 239 SVVDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGY 318
|
330
....*....|...
gi 162460999 323 SNRVVDLIRHMFK 335
Cdd:PRK15425 319 SNKVLDLIAHISK 331
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
1-333 |
1.61e-146 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 417.53 E-value: 1.61e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 1 MGKIKIGINGFGRIGRLVARV----ALQSEDVELVAVNDPFITTDYMTYMFKYDTVHGHWKHSDITLKDSKTLLFGDKPV 76
Cdd:PTZ00434 1 MAPIKVGINGFGRIGRMVFQAicdqGLIGTEIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVETTKSSPSVKTDDVLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 77 T-------VFGIRNPEEIPWGEAGAEYVVESTGVFTDKDKAAAHLKGGAKKVVISAP-SKDAPMFVVGVNEDKYT-SDVN 147
Cdd:PTZ00434 81 VnghrikcVKAQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPaSGGAKTIVMGVNQHEYSpTEHH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 148 IVSNASCTTNCLAPLAKVI-HDNFGIVEGLMTTVHAITATQKTVDGPSAKDWRGGRAASFNIIPSSTGAAKAVGKVLPDL 226
Cdd:PTZ00434 161 VVSNASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPST 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 227 NGKLTGMSFRVPTVDVSVVDLTVRIEKGASYEDIKKAIKAASEGPLKGIMGYVEEDLVSTDFLGDSRSSIFDAKAGIALN 306
Cdd:PTZ00434 241 KGKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKATLQNN 320
|
330 340 350
....*....|....*....|....*....|.
gi 162460999 307 ----DHFVKLVSWYDNEWGYSNRVVDLIRHM 333
Cdd:PTZ00434 321 lpgeRRFFKIVSWYDNEWGYSHRVVDLVRYM 351
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
3-332 |
9.93e-131 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 376.77 E-value: 9.93e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 3 KIKIGINGFGRIGRLVARVALQSEDVELVAVNDPFiTTDYMTYMFKYDTVHGHWKHSDITLKDSktLLFGDKPVTVFGIR 82
Cdd:PRK07729 2 KTKVAINGFGRIGRMVFRKAIKESAFEIVAINASY-PSETLAHLIKYDTVHGKFDGTVEAFEDH--LLVDGKKIRLLNNR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 83 NPEEIPWGEAGAEYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPM-FVVGVNEDKYTSDVN-IVSNASCTTNCLA 160
Cdd:PRK07729 79 DPKELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVtIVVGVNEDQLDIEKHtIISNASCTTNCLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 161 PLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSaKDWRGGRAASFNIIPSSTGAAKAVGKVLPDLNGKLTGMSFRVPTV 240
Cdd:PRK07729 159 PVVKVLDEQFGIENGLMTTVHAYTNDQKNIDNPH-KDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 241 DVSVVDLTVRIEKGASYEDIKKAIKAASEGPLKGIMGYVEEDLVSTDFLGDSRSSIFDAKAGIALNDHFVKLVSWYDNEW 320
Cdd:PRK07729 238 NVSLVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEW 317
|
330
....*....|..
gi 162460999 321 GYSNRVVDLIRH 332
Cdd:PRK07729 318 GYSCRVVDLVTL 329
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
154-319 |
2.09e-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: 343.67 E-value: 2.09e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 154 CTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSaKDWRGGRAASFNIIPSSTGAAKAVGKVLPDLNGKLTGM 233
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 234 SFRVPTVDVSVVDLTVRIEKGASYEDIKKAIKAASEGPLKGIMGYVEEDLVSTDFLGDSRSSIFDAKAGIALNDHFVKLV 313
Cdd:cd18126 80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159
|
....*.
gi 162460999 314 SWYDNE 319
Cdd:cd18126 160 AWYDNE 165
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
6-329 |
3.84e-118 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 343.84 E-value: 3.84e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 6 IGINGFGRIGRLVARVALQSEDVELVAVNDPFITTDYMTYMFKYDTVHGHWKHSdiTLKDSKTLLFGDKPVTVFGIRNPE 85
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAE--VTAEEDSIVIDGKRISFSSNKDIE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 86 EIPWGEaGAEYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMF--VVGVNEDKYTSDV-NIVSNASCTTNCLAPL 162
Cdd:NF033735 79 DTPWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLniVYGVNDHLYDPARhRIVTAASCTTNCLAPV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 163 AKVIHDNFGIVEGLMTTVHAITATQKTVDGPsAKDWRGGRAASFNIIPSSTGAAKAVGKVLPDLNGKLTGMSFRVPTVDV 242
Cdd:NF033735 158 VKVIHEKIGIKHGSITTIHDITNTQTIVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 243 SVVDLTVRIEKGASYEDIKKAIKAASEGPLKGIMGYVEEDLVSTDFLGDSRSSIFDAKAGIALNDHFVKLVSWYDNEWGY 322
Cdd:NF033735 237 SLTDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGY 316
|
....*..
gi 162460999 323 SNRVVDL 329
Cdd:NF033735 317 ANRMVDL 323
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
4-329 |
8.01e-118 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 343.81 E-value: 8.01e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 4 IKIGINGFGRIGRLVARVALQSED--VELVAVNDpfiTTDYMT--YMFKYDTVHGHWkHSDITLKDSKTLLFGdKPVTVF 79
Cdd:PRK07403 2 IRVAINGFGRIGRNFLRCWLGRENsqLELVAIND---TSDPRTnaHLLKYDSMLGKL-NADISADENSITVNG-KTIKCV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 80 GIRNPEEIPWGEAGAEYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSK--DAPMFVVGVNEDKYTSDV-NIVSNASCTT 156
Cdd:PRK07403 77 SDRNPLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPGKgeDIGTYVVGVNHHEYDHEDhNIISNASCTT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 157 NCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGpSAKDWRGGRAASFNIIPSSTGAAKAVGKVLPDLNGKLTGMSFR 236
Cdd:PRK07403 157 NCLAPIAKVLHDNFGIIKGTMTTTHSYTGDQRILDA-SHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 237 VPTVDVSVVDLTVRIEKGASYEDIKKAIKAASEGPLKGIMGYVEEDLVSTDFLGDSRSSIFDAKAGIALNDHFVKLVSWY 316
Cdd:PRK07403 236 VPTPNVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWY 315
|
330
....*....|...
gi 162460999 317 DNEWGYSNRVVDL 329
Cdd:PRK07403 316 DNEWGYSQRVVDL 328
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
3-329 |
8.21e-110 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 326.86 E-value: 8.21e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 3 KIKIGINGFGRIGRLVARVALQSED--VELVAVNDPFITTDyMTYMFKYDTVHGHWKhSDITLKDSKTLLFGDKPVTVFG 80
Cdd:PLN02237 75 KLKVAINGFGRIGRNFLRCWHGRKDspLDVVVVNDSGGVKN-ASHLLKYDSMLGTFK-ADVKIVDDETISVDGKPIKVVS 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 81 IRNPEEIPWGEAGAEYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSK--DAPMFVVGVNEDKYTSDV-NIVSNASCTTN 157
Cdd:PLN02237 153 NRDPLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAKgaDIPTYVVGVNEDDYDHEVaNIVSNASCTTN 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 158 CLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGpSAKDWRGGRAASFNIIPSSTGAAKAVGKVLPDLNGKLTGMSFRV 237
Cdd:PLN02237 233 CLAPFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRV 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 238 PTVDVSVVDLTVRIEK-GASYEDIKKAIKAASEGPLKGIMGYVEEDLVSTDFLGDSRSSIFDAKAGIALNDHFVKLVSWY 316
Cdd:PLN02237 312 PTPNVSVVDLVVNVEKkGITAEDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVAWY 391
|
330
....*....|...
gi 162460999 317 DNEWGYSNRVVDL 329
Cdd:PLN02237 392 DNEWGYSQRVVDL 404
|
|
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
3-331 |
3.75e-108 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 318.98 E-value: 3.75e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 3 KIKIGINGFGRIGRLVARVALQSEDVELVAVNDPFITTDYMTYMFKYDTVHGHWKHSDITlkDSKTLLFGDKPVTVFGIR 82
Cdd:PRK08955 2 TIKVGINGFGRIGRLALRAAWDWPELEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTA--EGDAIVINGKRIRTTQNK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 83 NPEEIPWgeAGAEYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMF--VVGVNEDKYTSDVN-IVSNASCTTNCL 159
Cdd:PRK08955 80 AIADTDW--SGCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLniVMGVNDHLFDPAIHpIVTAASCTTNCL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 160 APLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSaKDWRGGRAASFNIIPSSTGAAKAVGKVLPDLNGKLTGMSFRVPT 239
Cdd:PRK08955 158 APVVKVIHEKLGIKHGSMTTIHDLTNTQTILDAPH-KDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 240 VDVSVVDLTVRIEKGASYEDIKKAIKAASEGPLKGIMGYVEEDLVSTDFLGDSRSSIFDAKAGIALNDHFVKLVSWYDNE 319
Cdd:PRK08955 237 ANASLTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNE 316
|
330
....*....|..
gi 162460999 320 WGYSNRVVDLIR 331
Cdd:PRK08955 317 WGYANRTAELAR 328
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
3-329 |
1.41e-107 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 319.57 E-value: 1.41e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 3 KIKIGINGFGRIGRLVARV--ALQSEDVELVAVNDPFiTTDYMTYMFKYDTVHGHWKhSDITLKDSKTLLFGDKPVTVFG 80
Cdd:PLN03096 60 KIKVAINGFGRIGRNFLRCwhGRKDSPLDVVAINDTG-GVKQASHLLKYDSTLGTFD-ADVKPVGDDAISVDGKVIKVVS 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 81 IRNPEEIPWGEAGAEYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSK-DAPMFVVGVNEDKYTSDVNIVSNASCTTNCL 159
Cdd:PLN03096 138 DRNPLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKgDIPTYVVGVNADDYKHSDPIISNASCTTNCL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 160 APLAKVIHDNFGIVEGLMTTVHAITATQKTVDGpSAKDWRGGRAASFNIIPSSTGAAKAVGKVLPDLNGKLTGMSFRVPT 239
Cdd:PLN03096 218 APFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPT 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 240 VDVSVVDLTVRIEKGASYEDIKKAIKAASEGPLKGIMGYVEEDLVSTDFLGDSRSSIFDAKAGIALNDHFVKLVSWYDNE 319
Cdd:PLN03096 297 PNVSVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAWYDNE 376
|
330
....*....|
gi 162460999 320 WGYSNRVVDL 329
Cdd:PLN03096 377 WGYSQRVVDL 386
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
4-337 |
4.83e-95 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 285.41 E-value: 4.83e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 4 IKIGINGFGRIGRLVARVALQS---EDVELVAVNDpFITTDYMTYMFKYDTVHGHWkHSDITLkDSKTLLFGDKPVTVFG 80
Cdd:PRK13535 2 IRVAINGFGRIGRNVLRALYESgrrAEITVVAINE-LADAEGMAHLLKYDTSHGRF-AWDVRQ-ERDQLFVGDDAIRLLH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 81 IRNPEEIPWGEAGAEYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSK---DAPMfVVGVNEDKYTSDVNIVSNASCTTN 157
Cdd:PRK13535 79 ERDIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSndlDATV-VYGVNHDQLRAEHRIVSNASCTTN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 158 CLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGpSAKDWRGGRAASFNIIPSSTGAAKAVGKVLPDLNGKLTGMSFRV 237
Cdd:PRK13535 158 CIIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 238 PTVDVSVVDLTVRIEKGASYEDIKKAIKAASEGPLKGIMGYVEEDLVSTDFLGDSRSSIFDAKAGIALNDHFVKLVSWYD 317
Cdd:PRK13535 237 PTINVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCD 316
|
330 340
....*....|....*....|
gi 162460999 318 NEWGYSNRVVDLIRHMFKSQ 337
Cdd:PRK13535 317 NEWGFANRMLDTTLAMAAAG 336
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
159-316 |
5.22e-90 |
|
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. C-terminal domain is a mixed alpha/antiparallel beta fold.
Pssm-ID: 460700 Cd Length: 158 Bit Score: 266.00 E-value: 5.22e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 159 LAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSAKDWRGGRAASFNIIPSSTGAAKAVGKVLPDLNGKLTGMSFRVP 238
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162460999 239 TVDVSVVDLTVRIEKGASYEDIKKAIKAASEGPLKGIMGYVEEDLVSTDFLGDSRSSIFDAKAGIALNDHFVKLVSWY 316
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
154-319 |
1.16e-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: 250.23 E-value: 1.16e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 154 CTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSAKDWRGGRAASFNIIPSSTGAAKAVGKVLPDLNGKLTGM 233
Cdd:cd18123 1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 234 SFRVPTVDVSVVDLTVRIEKGASYEDIKKAIKAASEGplKGIMGYVEEDLVSTDFLGDSRSSIFDAKAGIALNDHFVKLV 313
Cdd:cd18123 81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLM 158
|
....*.
gi 162460999 314 SWYDNE 319
Cdd:cd18123 159 QWYDNE 164
|
|
| GAPDH_I_N |
cd05214 |
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
4-153 |
5.12e-82 |
|
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: 246.15 E-value: 5.12e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 4 IKIGINGFGRIGRLVARVALQSEDVELVAVNDPFITtDYMTYMFKYDTVHGHWKHsDITLKDSKtLLFGDKPVTVFGIRN 83
Cdd:cd05214 1 IKVGINGFGRIGRLVFRAALERDDIEVVAINDLTDD-ETLAYLLKYDSVHGRFDG-EVEVDDDA-LIVNGKKIKVFAERD 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 162460999 84 PEEIPWGEAGAEYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKD-APMFVVGVNEDKYTSDVNIVSNAS 153
Cdd:cd05214 78 PAELPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDADDKIISNAS 148
|
|
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
10-333 |
2.20e-80 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 252.54 E-value: 2.20e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 10 GFGRIGRLVARVALQ----SEDVELVAV-------NDpfitTDYMTYMFKYDTVHGHWKHSDITLKDSKTLLFGDKPVTV 78
Cdd:PRK08289 134 GFGRIGRLLARLLIEktggGNGLRLRAIvvrkgseGD----LEKRASLLRRDSVHGPFNGTITVDEENNAIIANGNYIQV 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 79 FGIRNPEEIPWGEAGAE--YVVESTGVFTDKDKAAAHLKG-GAKKVVISAPSK-DAPMFVVGVNEDKYTSDVNIVSNASC 154
Cdd:PRK08289 210 IYANSPEEVDYTAYGINnaLVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGKgDIKNIVHGVNHSDITDEDKIVSAASC 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 155 TTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSAKDwRGGRAASFNIIPSSTGAAKAVGKVLPDLNGKLTGMS 234
Cdd:PRK08289 290 TTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKGD-RRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNA 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 235 FRVPTVDVSVVDLTVRIEKGASYEDIKKAIKAAS-EGPLKGIMGYVEE-DLVSTDFLGDSRSSIFDAKAGIALNDHFVkL 312
Cdd:PRK08289 369 IRVPTPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQIDYTDStEVVSSDFVGSRHAGVVDSQATIVNGNRAV-L 447
|
330 340
....*....|....*....|.
gi 162460999 313 VSWYDNEWGYSNRVVDLIRHM 333
Cdd:PRK08289 448 YVWYDNEFGYSCQVVRVMEQM 468
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
4-154 |
1.42e-71 |
|
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: 218.96 E-value: 1.42e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 4 IKIGINGFGRIGRLVARVALQSEDVELVAVNDPfITTDYMTYMFKYDTVHGHWKHsDITLKDSkTLLFGDKPVTVFGIRN 83
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPG-TVEVEGD-GLVVNGKAIKVFAERD 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162460999 84 PEEIPWGEAGAEYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDA-PMFVVGVNEDKYTSDVNIVSNASC 154
Cdd:smart00846 78 PANLPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
4-333 |
2.18e-61 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 199.33 E-value: 2.18e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 4 IKIGINGFGRIGRLVARVALQSEDVELVAVNDPFITTDYMTYMFKYDTVHGHWKHSDITLKDSKTLLFGDKPVTVFGIRN 83
Cdd:PTZ00353 3 ITVGINGFGPVGKAVLFASLTDPLVTVVAVNDASVSIAYIAYVLEQESPLSAPDGASIRVVGEQIVLNGTQKIRVSAKHD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 84 PEEIPWGEAGAEYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEDKYTSDVNIVSNASCTTNCLAPLA 163
Cdd:PTZ00353 83 LVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDERLSASLPVCCAGAPIAVALAPVI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 164 KVIHDNFGIVEGLMTTVHAITAtQKTVDGPSA--KDWRGGRAASFNIIPSSTGAAKAVGKVLPDLNGKLTGMSFRVPTVD 241
Cdd:PTZ00353 163 RALHEVYGVEECSYTAIHGMQP-QEPIAARSKnsQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 242 VSVVDLTVRIEKGASYEDIKKAIKAASEGPLKGIMGYVEEDLVSTDFLGDSRsSIFDAKAGIALNDHFV-KLVSWYDNEW 320
Cdd:PTZ00353 242 GCAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCIPNGK-LCYDATSSSSSREGEVhKMVLWFDVEC 320
|
330
....*....|...
gi 162460999 321 GYSNRVVDLIRHM 333
Cdd:PTZ00353 321 YYAARLLSLVKQL 333
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
154-319 |
7.46e-49 |
|
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: 161.43 E-value: 7.46e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 154 CTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGpSAKDWRGGRAASFNIIPSSTGAAKAVGKVLPDLNGKLTGM 233
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 234 SFRVPTVDVSVVDLTVRIEKGASYEDIKKAIKAASEGPLKGIMGYVEEDLVSTDFLGDSRSSIFDAKAGIALNDHFVKLV 313
Cdd:cd23937 80 AVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLL 159
|
....*.
gi 162460999 314 SWYDNE 319
Cdd:cd23937 160 VWCDNE 165
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
154-319 |
8.54e-47 |
|
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) superfamily of proteins; GAPDH-like C-terminal catalytic domains are typically associated with a classic N-terminal Rossmann fold NAD(P)-binding domain. This superfamily includes the C-terminal domains of glyceraldehyde-3-phosphate dehydrogenase (GAPDH), N-acetyl-gamma-glutamyl-phosphate reductase (AGPR), aspartate beta-semialdehyde dehydrogenase (ASADH), acetaldehyde dehydrogenase (ALDH) and USG-1 homolog proteins.
Pssm-ID: 467672 [Multi-domain] Cd Length: 166 Bit Score: 156.14 E-value: 8.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 154 CTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSAKDWrgGRAASFNIIPSSTGAAKAVGKVLPDLN--GKLT 231
Cdd:cd18122 1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIGkpIKVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 232 GMSFRVPTVDVSVVDLTVRIEKGASYEDIKKAIKAASEGPLKGIMGYVEEDLVSTDFLGDSRSSIFDAKAGIALNDHFVK 311
Cdd:cd18122 79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLK 158
|
....*...
gi 162460999 312 LVSWYDNE 319
Cdd:cd18122 159 VFSAVDNE 166
|
|
| Gp_dh_N |
pfam00044 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
4-107 |
4.93e-43 |
|
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: 144.17 E-value: 4.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 4 IKIGINGFGRIGRLVARVALQSEDVELVAVNDpFITTDYMTYMFKYDTVHGHWKHsDITLKDsKTLLFGDKPVTVFGIRN 83
Cdd:pfam00044 1 VKVGINGFGRIGRLVLRAALERPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPG-EVEAEE-DGLVVNGKKIKVFAERD 77
|
90 100
....*....|....*....|....
gi 162460999 84 PEEIPWGEAGAEYVVESTGVFTDK 107
Cdd:pfam00044 78 PAELPWGDLGVDVVIESTGVFTTK 101
|
|
| GAPDH_N_E4PDH |
cd17892 |
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
4-153 |
2.64e-36 |
|
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: 128.92 E-value: 2.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 4 IKIGINGFGRIGRLVARvAL----QSEDVELVAVNDPfITTDYMTYMFKYDTVHGHWkHSDITLKDSKTLLFGDKpVTVF 79
Cdd:cd17892 1 YRVAINGYGRIGRNVLR-ALyesgRRAEFQVVAINEL-ADAETIAHLTKYDTTHGRF-PGEVRVENDQLFVNGDK-IRVL 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162460999 80 GIRNPEEIPWGEAGAEYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSK---DAPMfVVGVNEDKYTSDVNIVSNAS 153
Cdd:cd17892 77 HEPDPENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASndvDATI-VYGINQDLLRAEHRIVSNAS 152
|
|
| GAPDH-like_N |
cd05192 |
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ... |
4-158 |
6.98e-15 |
|
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: 69.69 E-value: 6.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 4 IKIGINGFGRIGRLVARVALQSEDVELVAVNDpfiTTDYmtymfkydtvhghwkhsditlkdsktllfgdkpvtvfgirn 83
Cdd:cd05192 1 IRVAINGFGRIGRIVFRAIADQDDLDVVAIND---RRDV----------------------------------------- 36
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162460999 84 peeipwgeagaeyVVESTGVFTDKDKAAAHLKGGAKKVVISAPSK-DAPMFVVGVNEDKYTSDVNIVSNASCTTNC 158
Cdd:cd05192 37 -------------VIECTGSFTDDDNAEKHIKAGGKKAVITAPEKgDIPTIVVVLNELAKSAGATVVSNANETSYS 99
|
|
| MviM |
COG0673 |
Predicted dehydrogenase [General function prediction only]; |
1-36 |
4.03e-05 |
|
Predicted dehydrogenase [General function prediction only];
Pssm-ID: 440437 [Multi-domain] Cd Length: 295 Bit Score: 44.53 E-value: 4.03e-05
10 20 30
....*....|....*....|....*....|....*.
gi 162460999 1 MGKIKIGINGFGRIGRLVARVALQSEDVELVAVNDP 36
Cdd:COG0673 1 MDKLRVGIIGAGGIGRAHAPALAALPGVELVAVADR 36
|
|
| meso-DAPDH_N |
cd02270 |
N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and ... |
4-33 |
4.82e-05 |
|
N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and similar proteins; Meso-DAPDH (EC 1.4.1.16), also called diaminopimelate dehydrogenase, or meso-DAP dehydrogenase, probably plays a role in lysine biosynthesis. It catalyzes the reversible NADP(H)-dependent reductive amination of L-2-amino-6-oxopimelate, the acyclic form of L-tetrahydrodipicolinate, to generate the meso compound, D,L-2,6-diaminopimelate. DAPDH is a homodimer which is highly specific for meso-DAP and NADP(+) as substrates. Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.
Pssm-ID: 467610 [Multi-domain] Cd Length: 151 Bit Score: 42.94 E-value: 4.82e-05
10 20 30
....*....|....*....|....*....|
gi 162460999 4 IKIGINGFGRIGRLVARVALQSEDVELVAV 33
Cdd:cd02270 1 IRVAIVGYGNLGRGVEEAIQANPDMELVGV 30
|
|
| DapB_N |
pfam01113 |
Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the ... |
4-33 |
8.04e-05 |
|
Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the alpha,beta-unsaturated cyclic imine, dihydro-dipicolinate. This reaction is the second committed step in the biosynthesis of L-lysine and its precursor meso-diaminopimelate, which are critical for both protein and cell wall biosynthesis. The N-terminal domain of DapB binds the dinucleotide NADPH.
Pssm-ID: 460069 [Multi-domain] Cd Length: 121 Bit Score: 41.45 E-value: 8.04e-05
10 20 30
....*....|....*....|....*....|.
gi 162460999 4 IKIGINGF-GRIGRLVARVALQSEDVELVAV 33
Cdd:pfam01113 1 IKIAVAGAsGRMGRELIKAVLEAPDLELVAA 31
|
|
| DHDPR_N |
cd02274 |
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; ... |
4-35 |
1.94e-04 |
|
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; DHDPR (EC 1.17.1.8), also called 4-hydroxy-tetrahydrodipicolinate reductase, or HTPA reductase, is a product of an essential gene referred to as dapB. It catalyzes the NAD(P)H-dependent reduction of 2,3-dihydrodipicolinate (DHDP) to 2,3,4,5-tetrahydrodipicolinate (THDP). DHDPR could also function as a dehydratase in addition to the role of a nucleotide dependent reductase. DHDPR is a component of the biosynthetic pathway that generates meso-diaminopimelate, a component of bacterial cell walls, and the amino acid L-lysine in various bacteria, archaea, cyanobacteria and higher plants. The enzyme is a homotetramer where each monomer is composed of two domains, an N-terminal NAD(P)-binding domain which forms a Rossmann fold, and a C-terminal substrate-binding domain that forms an open, mixed alpha-beta sandwich.
Pssm-ID: 467611 [Multi-domain] Cd Length: 139 Bit Score: 41.01 E-value: 1.94e-04
10 20 30
....*....|....*....|....*....|...
gi 162460999 4 IKIGINGF-GRIGRLVARVALQSEDVELVAVND 35
Cdd:cd02274 1 IKVAVAGAtGRMGRELVKAILEAPDLELVGAVD 33
|
|
| ASADH_C_arch_fung_like |
cd18130 |
C-terminal catalytic domain of fungal/archaeal aspartate beta-semialdehyde dehydrogenase ... |
154-273 |
2.43e-04 |
|
C-terminal catalytic domain of fungal/archaeal aspartate beta-semialdehyde dehydrogenase (ASADH) and similar proteins; The family corresponds to a new branch of aspartate beta-semialdehyde dehydrogenase (ASADH) enzymes that has a similar overall fold and domain organization but share very little sequence homology with the typical bacterial ASADHs. They are mainly from archaea and fungi. ASADH (EC 1.2.1.11), also called ASA dehydrogenase (ASD), or aspartate-beta-semialdehyde dehydrogenase, catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate, which is the second step of the aspartate biosynthetic pathway. ASA can either be further reduced to homoserine, which leads to methionine, threonine, or isoleucine, or it can be condensed with pyruvate and cyclized into dihydrodipicolinate, and then converted into diaminopimelate, a component of bacterial cell walls, and finally decarboxylated to produce lysine. ASADH contains an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins. This family also includes NADP-dependent malonyl-CoA reductase (MCR, EC 1.2.1.75), which catalyzes the reduction of malonyl-CoA to malonate semialdehyde, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutyrate cycles. It can also use succinyl-CoA and succinate semialdehyde as substrates but at a lower rate than malonyl-CoA.
Pssm-ID: 467680 [Multi-domain] Cd Length: 180 Bit Score: 41.45 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 154 CTTNCLAPLAKVIHDNFGIVEGLMTTVHAIT-ATQKTVDGPSAKDwrggraasfNIIPSSTGAAKAV----GKVLPDLNG 228
Cdd:cd18130 1 CSTAGLALPLKPLHDFFGIEAVIVTTMQAISgAGYPGVPSLDILD---------NVIPYIGGEEEKIesetKKILGTLNE 71
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 162460999 229 --------KLTGMSFRVPTVDVSVVDLTVRIEKGASYEDIKKAIKAASEGPLK 273
Cdd:cd18130 72 dkiepadfKVSATCNRVPVIDGHTESVSVKFKERPDPEEVKEALENYEPEPQV 124
|
|
| PRK04207 |
PRK04207 |
type II glyceraldehyde-3-phosphate dehydrogenase; |
3-46 |
7.87e-04 |
|
type II glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 179786 [Multi-domain] Cd Length: 341 Bit Score: 40.97 E-value: 7.87e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 162460999 3 KIKIGINGFGRIGRLVAR-VALQsEDVELVAVNDpfITTDYMTYM 46
Cdd:PRK04207 1 MIKVGVNGYGTIGKRVADaVAAQ-PDMELVGVAK--TKPDYEARV 42
|
|
| Asd |
COG0136 |
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ... |
67-172 |
2.20e-03 |
|
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; Aspartate-semialdehyde dehydrogenase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439906 [Multi-domain] Cd Length: 333 Bit Score: 39.24 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162460999 67 KTLLFGDKPVTVfgiRNPEEIPWgeAGAEYVVESTGVFTDKD---KAAAHlkgGAkkVVISAPS-----KDAPMFVVGVN 138
Cdd:COG0136 41 KTVSFGGKELTV---EDATDFDF--SGVDIALFSAGGSVSKEyapKAAAA---GA--VVIDNSSafrmdPDVPLVVPEVN 110
|
90 100 110
....*....|....*....|....*....|....*..
gi 162460999 139 ED---KYTSDvNIVSNASCTTNCLAPLAKVIHDNFGI 172
Cdd:COG0136 111 PEalaDHLPK-GIIANPNCSTIQMLVALKPLHDAAGI 146
|
|
| |
