|
Name |
Accession |
Description |
Interval |
E-value |
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
4-328 |
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: 536.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 4 IGINGFGRIGRMFARQALVR-KDVKIVAINDPSlDPKYLAYMLRYDSTHGQFNQKISVDGNNLVVNGKKIQLLKESDVKK 82
Cdd:COG0057 5 VAINGFGRIGRLVLRALLERgPDIEVVAINDLG-DAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 83 IKWCDLGVHTVVECSGRFTTLKACQGHLDSGAKKVVISAPSADA-PMFVCGVNLEAYKPGTAIISNASCTTNCLAPLAKV 161
Cdd:COG0057 84 LPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAPVAKV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 162 VHDNFEICEGLMTTVHAATATQKIIDGPSSKlWRDGRSGMTNIIPASTGAAKAVGKVIPDLNGKLTGMAFRVPVPNVSVV 241
Cdd:COG0057 164 LNDAFGIEKGLMTTIHAYTNDQNLLDAPHKD-LRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 242 DLTCRLSKPAKMDDIKKCIKAASKCEMKGILGYVEEEVVSTDFNGSRFASVFDAKACIALNDNFVKLISWYDNETGYSCR 321
Cdd:COG0057 243 DLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGYSNR 322
|
....*..
gi 19922412 322 LLDLVLY 328
Cdd:COG0057 323 MVDLAEY 329
|
|
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
4-332 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 516.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 4 IGINGFGRIGRMFARQALVRKDVKIVAINDPSLDPKYLAYMLRYDSTHGQFNQKISV-DGNNLVVNGKKIQLLKESDVKK 82
Cdd:PLN02272 88 IGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDPAE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 83 IKWCDLGVHTVVECSGRFTTLKACQGHLDSGAKKVVISAPSADAPMFVCGVNLEAYKPGTAIISNASCTTNCLAPLAKVV 162
Cdd:PLN02272 168 IPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLAKVV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 163 HDNFEICEGLMTTVHAATATQKIIDGPSSKLWRDGRSGMTNIIPASTGAAKAVGKVIPDLNGKLTGMAFRVPVPNVSVVD 242
Cdd:PLN02272 248 HEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVD 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 243 LTCRLSKPAKMDDIKKCIKAASKCEMKGILGYVEEEVVSTDFNGSRFASVFDAKACIALNDNFVKLISWYDNETGYSCRL 322
Cdd:PLN02272 328 LTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYSNRV 407
|
330
....*....|
gi 19922412 323 LDLVLYAQLV 332
Cdd:PLN02272 408 LDLIEHMALV 417
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
4-324 |
1.37e-164 |
|
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: 462.13 E-value: 1.37e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 4 IGINGFGRIGRMFARQALVRKD--VKIVAINDPsLDPKYLAYMLRYDSTHGQFNQKISVDGNNLVVNGKK-IQLLKESDV 80
Cdd:TIGR01534 2 VGINGFGRIGRLVLRRILEKPGndLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEvISVFSERDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 81 KKIKWCDLGVHTVVECSGRFTTLKACQGHLDSGAKKVVISAPSADA-PMFVCGVNLEAYKPGTAIISNASCTTNCLAPLA 159
Cdd:TIGR01534 81 SDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLAPLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 160 KVVHDNFEICEGLMTTVHAATATQKIIDGPsSKLWRDGRSGMTNIIPASTGAAKAVGKVIPDLNGKLTGMAFRVPVPNVS 239
Cdd:TIGR01534 161 KVLDEAFGIVSGLMTTVHAYTNDQNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 240 VVDLTCRLSKPAKMDDIKKCIKAASKCEMKGILGYVEEEVVSTDFNGSRFASVFDAKA--CIALNDNFVKLISWYDNETG 317
Cdd:TIGR01534 240 LVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATAtkVTGLGDSLVKVYAWYDNEWG 319
|
....*..
gi 19922412 318 YSCRLLD 324
Cdd:TIGR01534 320 YSNRLVD 326
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
4-326 |
6.53e-111 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 325.73 E-value: 6.53e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 4 IGINGFGRIGRMFARQALVRKDVKIVAINDPSLDPKYLAYMLRYDSTHGQFNQKISVDGNNLVVNGKKIQLLKESDVKKI 83
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 84 KWCDlGVHTVVECSGRFTTLKACQGHLDSGAKKVVISAP--SADAPMFVCGVNLEAYKPGT-AIISNASCTTNCLAPLAK 160
Cdd:NF033735 81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARhRIVTAASCTTNCLAPVVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 161 VVHDNFEICEGLMTTVHAATATQKIIDGPSSKLwRDGRSGMTNIIPASTGAAKAVGKVIPDLNGKLTGMAFRVPVPNVSV 240
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAPHKDL-RRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 241 VDLTCRLSKPAKMDDIKKCIKAASKCEMKGILGYVEEEVVSTDFNGSRFASVFDAKACIALNDNFVKLISWYDNETGYSC 320
Cdd:NF033735 239 TDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYAN 318
|
....*.
gi 19922412 321 RLLDLV 326
Cdd:NF033735 319 RMVDLA 324
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
150-315 |
8.69e-110 |
|
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: 316.70 E-value: 8.69e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 150 CTTNCLAPLAKVVHDNFEICEGLMTTVHAATATQKIIDGPSsKLWRDGRSGMTNIIPASTGAAKAVGKVIPDLNGKLTGM 229
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 230 AFRVPVPNVSVVDLTCRLSKPAKMDDIKKCIKAASKCEMKGILGYVEEEVVSTDFNGSRFASVFDAKACIALNDNFVKLI 309
Cdd:cd18126 80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159
|
....*.
gi 19922412 310 SWYDNE 315
Cdd:cd18126 160 AWYDNE 165
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
155-312 |
1.97e-83 |
|
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: 249.82 E-value: 1.97e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 155 LAPLAKVVHDNFEICEGLMTTVHAATATQKIIDGPSSKLWRDGRSGMTNIIPASTGAAKAVGKVIPDLNGKLTGMAFRVP 234
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19922412 235 VPNVSVVDLTCRLSKPAKMDDIKKCIKAASKCEMKGILGYVEEEVVSTDFNGSRFASVFDAKACIALNDNFVKLISWY 312
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
4-150 |
3.21e-74 |
|
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: 225.89 E-value: 3.21e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 4 IGINGFGRIGRMFARQALVRKDVKIVAINDPSlDPKYLAYMLRYDSTHGQFNQKISVDGNNLVVNGKKIQLLKESDVKKI 83
Cdd:smart00846 3 VGINGFGRIGRLVLRAALERPDVEVVAINDLT-DPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANL 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19922412 84 KWCDLGVHTVVECSGRFTTLKACQGHLDSGAKKVVISAPSADA-PMFVCGVNLEAYKPGTAIISNASC 150
Cdd:smart00846 82 PWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
4-328 |
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: 536.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 4 IGINGFGRIGRMFARQALVR-KDVKIVAINDPSlDPKYLAYMLRYDSTHGQFNQKISVDGNNLVVNGKKIQLLKESDVKK 82
Cdd:COG0057 5 VAINGFGRIGRLVLRALLERgPDIEVVAINDLG-DAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 83 IKWCDLGVHTVVECSGRFTTLKACQGHLDSGAKKVVISAPSADA-PMFVCGVNLEAYKPGTAIISNASCTTNCLAPLAKV 161
Cdd:COG0057 84 LPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAPVAKV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 162 VHDNFEICEGLMTTVHAATATQKIIDGPSSKlWRDGRSGMTNIIPASTGAAKAVGKVIPDLNGKLTGMAFRVPVPNVSVV 241
Cdd:COG0057 164 LNDAFGIEKGLMTTIHAYTNDQNLLDAPHKD-LRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 242 DLTCRLSKPAKMDDIKKCIKAASKCEMKGILGYVEEEVVSTDFNGSRFASVFDAKACIALNDNFVKLISWYDNETGYSCR 321
Cdd:COG0057 243 DLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGYSNR 322
|
....*..
gi 19922412 322 LLDLVLY 328
Cdd:COG0057 323 MVDLAEY 329
|
|
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
4-332 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 516.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 4 IGINGFGRIGRMFARQALVRKDVKIVAINDPSLDPKYLAYMLRYDSTHGQFNQKISV-DGNNLVVNGKKIQLLKESDVKK 82
Cdd:PLN02272 88 IGINGFGRIGRLVLRIATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDPAE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 83 IKWCDLGVHTVVECSGRFTTLKACQGHLDSGAKKVVISAPSADAPMFVCGVNLEAYKPGTAIISNASCTTNCLAPLAKVV 162
Cdd:PLN02272 168 IPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLAKVV 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 163 HDNFEICEGLMTTVHAATATQKIIDGPSSKLWRDGRSGMTNIIPASTGAAKAVGKVIPDLNGKLTGMAFRVPVPNVSVVD 242
Cdd:PLN02272 248 HEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVD 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 243 LTCRLSKPAKMDDIKKCIKAASKCEMKGILGYVEEEVVSTDFNGSRFASVFDAKACIALNDNFVKLISWYDNETGYSCRL 322
Cdd:PLN02272 328 LTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYSNRV 407
|
330
....*....|
gi 19922412 323 LDLVLYAQLV 332
Cdd:PLN02272 408 LDLIEHMALV 417
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
4-324 |
1.37e-164 |
|
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: 462.13 E-value: 1.37e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 4 IGINGFGRIGRMFARQALVRKD--VKIVAINDPsLDPKYLAYMLRYDSTHGQFNQKISVDGNNLVVNGKK-IQLLKESDV 80
Cdd:TIGR01534 2 VGINGFGRIGRLVLRRILEKPGndLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEvISVFSERDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 81 KKIKWCDLGVHTVVECSGRFTTLKACQGHLDSGAKKVVISAPSADA-PMFVCGVNLEAYKPGTAIISNASCTTNCLAPLA 159
Cdd:TIGR01534 81 SDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDvKTIVYGVNHDEYDGEERIISNASCTTNCLAPLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 160 KVVHDNFEICEGLMTTVHAATATQKIIDGPsSKLWRDGRSGMTNIIPASTGAAKAVGKVIPDLNGKLTGMAFRVPVPNVS 239
Cdd:TIGR01534 161 KVLDEAFGIVSGLMTTVHAYTNDQNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 240 VVDLTCRLSKPAKMDDIKKCIKAASKCEMKGILGYVEEEVVSTDFNGSRFASVFDAKA--CIALNDNFVKLISWYDNETG 317
Cdd:TIGR01534 240 LVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATAtkVTGLGDSLVKVYAWYDNEWG 319
|
....*..
gi 19922412 318 YSCRLLD 324
Cdd:TIGR01534 320 YSNRLVD 326
|
|
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
4-328 |
3.55e-159 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 448.90 E-value: 3.55e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 4 IGINGFGRIGRMFARQALVRKDVKIVAINDPSLDPKYLAYMLRYDSTHGQFNQKISVDGNNLVVNGKKIQLLKESDVKKI 83
Cdd:PTZ00023 5 LGINGFGRIGRLVFRAALEREDVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKDPAAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 84 KWCDLGVHTVVECSGRFTTLKACQGHLDSGAKKVVISAP-SADAPMFVCGVNLEAYKPGTAIISNASCTTNCLAPLAKVV 162
Cdd:PTZ00023 85 PWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPpKDDTPIYVMGVNHTQYDKSQRIVSNASCTTNCLAPLAKVV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 163 HDNFEICEGLMTTVHAATATQKIIDGPS--SKLWRDGRSGMTNIIPASTGAAKAVGKVIPDLNGKLTGMAFRVPVPNVSV 240
Cdd:PTZ00023 165 NDKFGIVEGLMTTVHASTANQLTVDGPSkgGKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVPDVSV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 241 VDLTCRLSKPAKMDDIKKCIKAASKCEMKGILGYVEEEVVSTDFNGSRFASVFDAKACIALNDNFVKLISWYDNETGYSC 320
Cdd:PTZ00023 245 VDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDNEWGYSN 324
|
....*...
gi 19922412 321 RLLDLVLY 328
Cdd:PTZ00023 325 RLLDLAHY 332
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
4-328 |
9.23e-149 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 422.22 E-value: 9.23e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 4 IGINGFGRIGRMFARQALVRKDVKIVAINDpSLDPKYLAYMLRYDSTHGQFNQKISVDGNNLVVNGKKIQLLKESDVKKI 83
Cdd:PRK15425 5 VGINGFGRIGRIVFRAAQKRSDIEIVAIND-LLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPANL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 84 KWCDLGVHTVVECSGRFTTLKACQGHLDSGAKKVVISAPSAD-APMFVCGVNLEAYKpGTAIISNASCTTNCLAPLAKVV 162
Cdd:PRK15425 84 KWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDnTPMFVKGANFDKYA-GQDIVSNASCTTNCLAPLAKVI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 163 HDNFEICEGLMTTVHAATATQKIIDGPSSKLWRDGRSGMTNIIPASTGAAKAVGKVIPDLNGKLTGMAFRVPVPNVSVVD 242
Cdd:PRK15425 163 NDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 243 LTCRLSKPAKMDDIKKCIKAASKCEMKGILGYVEEEVVSTDFNGSRFASVFDAKACIALNDNFVKLISWYDNETGYSCRL 322
Cdd:PRK15425 243 LTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYSNKV 322
|
....*.
gi 19922412 323 LDLVLY 328
Cdd:PRK15425 323 LDLIAH 328
|
|
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
4-328 |
7.95e-136 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 389.85 E-value: 7.95e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 4 IGINGFGRIGRMFARQALVRKDVKIVAINDPSLDPKYLAYMLRYDSTHGQF--NQKISVDGNNLVVNGKKIQLLKESDVK 81
Cdd:PLN02358 8 IGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWkhHELKVKDDKTLLFGEKPVTVFGIRNPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 82 KIKWCDLGVHTVVECSGRFTTLKACQGHLDSGAKKVVISAPSADAPMFVCGVNLEAYKPGTAIISNASCTTNCLAPLAKV 161
Cdd:PLN02358 88 DIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCTTNCLAPLAKV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 162 VHDNFEICEGLMTTVHAATATQKIIDGPSSKLWRDGRSGMTNIIPASTGAAKAVGKVIPDLNGKLTGMAFRVPVPNVSVV 241
Cdd:PLN02358 168 INDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 242 DLTCRLSKPAKMDDIKKCIKAASKCEMKGILGYVEEEVVSTDFNGSRFASVFDAKACIALNDNFVKLISWYDNETGYSCR 321
Cdd:PLN02358 248 DLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEWGYSSR 327
|
....*..
gi 19922412 322 LLDLVLY 328
Cdd:PLN02358 328 VVDLIVH 334
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
4-329 |
1.09e-129 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 374.07 E-value: 1.09e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 4 IGINGFGRIGRMFARQALVRKDVKIVAINdPSLDPKYLAYMLRYDSTHGQFNQKISVDGNNLVVNGKKIQLLKESDVKKI 83
Cdd:PRK07729 5 VAINGFGRIGRMVFRKAIKESAFEIVAIN-ASYPSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDPKEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 84 KWCDLGVHTVVECSGRFTTLKACQGHLDSGAKKVVISAPSADAPM-FVCGVNLEAYKPGT-AIISNASCTTNCLAPLAKV 161
Cdd:PRK07729 84 PWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVtIVVGVNEDQLDIEKhTIISNASCTTNCLAPVVKV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 162 VHDNFEICEGLMTTVHAATATQKIIDGPSSKLwRDGRSGMTNIIPASTGAAKAVGKVIPDLNGKLTGMAFRVPVPNVSVV 241
Cdd:PRK07729 164 LDEQFGIENGLMTTVHAYTNDQKNIDNPHKDL-RRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNVSLV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 242 DLTCRLSKPAKMDDIKKCIKAASKCEMKGILGYVEEEVVSTDFNGSRFASVFDAKACIALNDNFVKLISWYDNETGYSCR 321
Cdd:PRK07729 243 DLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEWGYSCR 322
|
....*...
gi 19922412 322 LLDLVLYA 329
Cdd:PRK07729 323 VVDLVTLV 330
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
4-338 |
5.83e-121 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 352.82 E-value: 5.83e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 4 IGINGFGRIGRM----FARQALVRKDVKIVAINDPSLDPKYLAYMLRYDSTHGQFNQKISV--------DGNNLVVNGKK 71
Cdd:PTZ00434 6 VGINGFGRIGRMvfqaICDQGLIGTEIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVETtksspsvkTDDVLVVNGHR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 72 IQLLK-ESDVKKIKWCDLGVHTVVECSGRFTTLKACQGHLDSGAKKVVISAP-SADAPMFVCGVNLEAYKPGTA-IISNA 148
Cdd:PTZ00434 86 IKCVKaQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPaSGGAKTIVMGVNQHEYSPTEHhVVSNA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 149 SCTTNCLAPLAKV-VHDNFEICEGLMTTVHAATATQKIIDGPSSKLWRDGRSGMTNIIPASTGAAKAVGKVIPDLNGKLT 227
Cdd:PTZ00434 166 SCTTNCLAPIVHVlTKEGFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGKLT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 228 GMAFRVPVPNVSVVDLTCRLSKPAKMDDIKKCIKAASKCEMKGILGYVEEEVVSTDFNGSRFASVFDAKACIALN----D 303
Cdd:PTZ00434 246 GMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKATLQNNlpgeR 325
|
330 340 350
....*....|....*....|....*....|....*
gi 19922412 304 NFVKLISWYDNETGYSCRLLDLVLYAQLVDQCDAK 338
Cdd:PTZ00434 326 RFFKIVSWYDNEWGYSHRVVDLVRYMAAKDAASAK 360
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
1-334 |
7.63e-112 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 328.79 E-value: 7.63e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 1 MSGIGINGFGRIGRMFARQALVRKD--VKIVAINDPSlDPKYLAYMLRYDSTHGQFNQKISVDGNNLVVNGKKIQLLKES 78
Cdd:PRK07403 1 MIRVAINGFGRIGRNFLRCWLGRENsqLELVAINDTS-DPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 79 DVKKIKWCDLGVHTVVECSGRFTTLKACQGHLDSGAKKVVISAP--SADAPMFVCGVNLEAYKPGT-AIISNASCTTNCL 155
Cdd:PRK07403 80 NPLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPgkGEDIGTYVVGVNHHEYDHEDhNIISNASCTTNCL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 156 APLAKVVHDNFEICEGLMTTVHAATATQKIIDGPSSKLwRDGRSGMTNIIPASTGAAKAVGKVIPDLNGKLTGMAFRVPV 235
Cdd:PRK07403 160 APIAKVLHDNFGIIKGTMTTTHSYTGDQRILDASHRDL-RRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 236 PNVSVVDLTCRLSKPAKMDDIKKCIKAASKCEMKGILGYVEEEVVSTDFNGSRFASVFDAKACIALNDNFVKLISWYDNE 315
Cdd:PRK07403 239 PNVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYDNE 318
|
330
....*....|....*....
gi 19922412 316 TGYSCRLLDLvlyAQLVDQ 334
Cdd:PRK07403 319 WGYSQRVVDL---AELVAR 334
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
4-326 |
6.53e-111 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 325.73 E-value: 6.53e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 4 IGINGFGRIGRMFARQALVRKDVKIVAINDPSLDPKYLAYMLRYDSTHGQFNQKISVDGNNLVVNGKKIQLLKESDVKKI 83
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 84 KWCDlGVHTVVECSGRFTTLKACQGHLDSGAKKVVISAP--SADAPMFVCGVNLEAYKPGT-AIISNASCTTNCLAPLAK 160
Cdd:NF033735 81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARhRIVTAASCTTNCLAPVVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 161 VVHDNFEICEGLMTTVHAATATQKIIDGPSSKLwRDGRSGMTNIIPASTGAAKAVGKVIPDLNGKLTGMAFRVPVPNVSV 240
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAPHKDL-RRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 241 VDLTCRLSKPAKMDDIKKCIKAASKCEMKGILGYVEEEVVSTDFNGSRFASVFDAKACIALNDNFVKLISWYDNETGYSC 320
Cdd:NF033735 239 TDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYAN 318
|
....*.
gi 19922412 321 RLLDLV 326
Cdd:NF033735 319 RMVDLA 324
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
150-315 |
8.69e-110 |
|
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: 316.70 E-value: 8.69e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 150 CTTNCLAPLAKVVHDNFEICEGLMTTVHAATATQKIIDGPSsKLWRDGRSGMTNIIPASTGAAKAVGKVIPDLNGKLTGM 229
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 230 AFRVPVPNVSVVDLTCRLSKPAKMDDIKKCIKAASKCEMKGILGYVEEEVVSTDFNGSRFASVFDAKACIALNDNFVKLI 309
Cdd:cd18126 80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159
|
....*.
gi 19922412 310 SWYDNE 315
Cdd:cd18126 160 AWYDNE 165
|
|
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
4-333 |
8.21e-100 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 297.80 E-value: 8.21e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 4 IGINGFGRIGRMFARQALVRKDVKIVAINDPSLDPKYLAYMLRYDSTHGQFNQKISVDGNNLVVNGKKIQLLKESDVKKI 83
Cdd:PRK08955 5 VGINGFGRIGRLALRAAWDWPELEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKAIADT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 84 KW--CDLgvhtVVECSGRFTTLKACQGHLDSGAKKVVISAPSADAPMF--VCGVNLEAYKPGT-AIISNASCTTNCLAPL 158
Cdd:PRK08955 85 DWsgCDV----VIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLniVMGVNDHLFDPAIhPIVTAASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 159 AKVVHDNFEICEGLMTTVHAATATQKIIDGPSSKLWRDGRSGMTnIIPASTGAAKAVGKVIPDLNGKLTGMAFRVPVPNV 238
Cdd:PRK08955 161 VKVIHEKLGIKHGSMTTIHDLTNTQTILDAPHKDLRRARACGMS-LIPTTTGSATAITEIFPELKGKLNGHAVRVPLANA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 239 SVVDLTCRLSKPAKMDDIKKCIKAASKCEMKGILGYVEEEVVSTDFNGSRFASVFDAKACIALNDNFVKLISWYDNETGY 318
Cdd:PRK08955 240 SLTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNEWGY 319
|
330
....*....|....*
gi 19922412 319 SCRLLDLVLYAQLVD 333
Cdd:PRK08955 320 ANRTAELARKVGLAD 334
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
4-325 |
6.61e-96 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 289.91 E-value: 6.61e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 4 IGINGFGRIGRMFARQALVRKD--VKIVAINDpSLDPKYLAYMLRYDSTHGQFNQKISVDGNN-LVVNGKKIQLLKESDV 80
Cdd:PLN03096 63 VAINGFGRIGRNFLRCWHGRKDspLDVVAIND-TGGVKQASHLLKYDSTLGTFDADVKPVGDDaISVDGKVIKVVSDRNP 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 81 KKIKWCDLGVHTVVECSGRFTTLKACQGHLDSGAKKVVISAPS-ADAPMFVCGVNLEAYKPGTAIISNASCTTNCLAPLA 159
Cdd:PLN03096 142 LNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGkGDIPTYVVGVNADDYKHSDPIISNASCTTNCLAPFV 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 160 KVVHDNFEICEGLMTTVHAATATQKIIDGPSSKLwRDGRSGMTNIIPASTGAAKAVGKVIPDLNGKLTGMAFRVPVPNVS 239
Cdd:PLN03096 222 KVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDL-RRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVS 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 240 VVDLTCRLSKPAKMDDIKKCIKAASKCEMKGILGYVEEEVVSTDFNGSRFASVFDAKACIALNDNFVKLISWYDNETGYS 319
Cdd:PLN03096 301 VVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAWYDNEWGYS 380
|
....*.
gi 19922412 320 CRLLDL 325
Cdd:PLN03096 381 QRVVDL 386
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
4-327 |
7.07e-91 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 275.01 E-value: 7.07e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 4 IGINGFGRIGRMFARqALV----RKDVKIVAINDPSlDPKYLAYMLRYDSTHGQFNQKISVDGNNLVVNGKKIQLLKESD 79
Cdd:PRK13535 4 VAINGFGRIGRNVLR-ALYesgrRAEITVVAINELA-DAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHERD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 80 VKKIKWCDLGVHTVVECSGRFTTLKACQGHLDSGAKKVVISAPSA---DAPMfVCGVNLEAYKPGTAIISNASCTTNCLA 156
Cdd:PRK13535 82 IASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSndlDATV-VYGVNHDQLRAEHRIVSNASCTTNCII 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 157 PLAKVVHDNFEICEGLMTTVHAATATQKIIDGPSSKLwRDGRSGMTNIIPASTGAAKAVGKVIPDLNGKLTGMAFRVPVP 236
Cdd:PRK13535 161 PVIKLLDDAFGIESGTVTTIHSAMNDQQVIDAYHPDL-RRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPTI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 237 NVSVVDLTCRLSKPAKMDDIKKCIKAASKCEMKGILGYVEEEVVSTDFNGSRFASVFDAKACIALNDNFVKLISWYDNET 316
Cdd:PRK13535 240 NVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNEW 319
|
330
....*....|.
gi 19922412 317 GYSCRLLDLVL 327
Cdd:PRK13535 320 GFANRMLDTTL 330
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
4-325 |
3.40e-90 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 277.17 E-value: 3.40e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 4 IGINGFGRIGRMFARQALVRKD--VKIVAINDpSLDPKYLAYMLRYDSTHGQFNQKIS-VDGNNLVVNGKKIQLLKESDV 80
Cdd:PLN02237 78 VAINGFGRIGRNFLRCWHGRKDspLDVVVVND-SGGVKNASHLLKYDSMLGTFKADVKiVDDETISVDGKPIKVVSNRDP 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 81 KKIKWCDLGVHTVVECSGRFTTLKACQGHLDSGAKKVVISAPS--ADAPMFVCGVNLEAYKPGTA-IISNASCTTNCLAP 157
Cdd:PLN02237 157 LKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAkgADIPTYVVGVNEDDYDHEVAnIVSNASCTTNCLAP 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 158 LAKVVHDNFEICEGLMTTVHAATATQKIIDGPSSKLwRDGRSGMTNIIPASTGAAKAVGKVIPDLNGKLTGMAFRVPVPN 237
Cdd:PLN02237 237 FVKVLDEEFGIVKGTMTTTHSYTGDQRLLDASHRDL-RRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTPN 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 238 VSVVDLTCRLSKPA-KMDDIKKCIKAASKCEMKGILGYVEEEVVSTDFNGSRFASVFDAKACIALNDNFVKLISWYDNET 316
Cdd:PLN02237 316 VSVVDLVVNVEKKGiTAEDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVAWYDNEW 395
|
....*....
gi 19922412 317 GYSCRLLDL 325
Cdd:PLN02237 396 GYSQRVVDL 404
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
150-315 |
5.93e-84 |
|
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (1.2.1.12), NADP (1.2.1.13) or either (1.2.1.59). GADPH family members include the ubiquitous NAD+ or NADP+ utilizing type I, type II NADP+ utilizing mainly from archaea, and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose.
Pssm-ID: 467673 Cd Length: 164 Bit Score: 251.38 E-value: 5.93e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 150 CTTNCLAPLAKVVHDNFEICEGLMTTVHAATATQKIIDGPSSKLWRDGRSGMTNIIPASTGAAKAVGKVIPDLNGKLTGM 229
Cdd:cd18123 1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 230 AFRVPVPNVSVVDLTCRLSKPAKMDDIKKCIKAASkcEMKGILGYVEEEVVSTDFNGSRFASVFDAKACIALNDNFVKLI 309
Cdd:cd18123 81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAP--EGKGRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLM 158
|
....*.
gi 19922412 310 SWYDNE 315
Cdd:cd18123 159 QWYDNE 164
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
155-312 |
1.97e-83 |
|
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: 249.82 E-value: 1.97e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 155 LAPLAKVVHDNFEICEGLMTTVHAATATQKIIDGPSSKLWRDGRSGMTNIIPASTGAAKAVGKVIPDLNGKLTGMAFRVP 234
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19922412 235 VPNVSVVDLTCRLSKPAKMDDIKKCIKAASKCEMKGILGYVEEEVVSTDFNGSRFASVFDAKACIALNDNFVKLISWY 312
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| GAPDH_I_N |
cd05214 |
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
4-149 |
6.18e-80 |
|
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; GAPDH plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (EC 1.2.1.12), NADP (EC 1.2.1.13) or either (EC 1.2.1.59). The family corresponds to the ubiquitous NAD+ or NADP+ utilizing type I GAPDH and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose.
Pssm-ID: 467614 [Multi-domain] Cd Length: 164 Bit Score: 240.76 E-value: 6.18e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 4 IGINGFGRIGRMFARQALVRKDVKIVAINDPSlDPKYLAYMLRYDSTHGQFNQKISVDGNNLVVNGKKIQLLKESDVKKI 83
Cdd:cd05214 3 VGINGFGRIGRLVFRAALERDDIEVVAINDLT-DDETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAEL 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19922412 84 KWCDLGVHTVVECSGRFTTLKACQGHLDSGAKKVVISAPSAD-APMFVCGVNLEAYKPGTAIISNAS 149
Cdd:cd05214 82 PWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDADDKIISNAS 148
|
|
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
8-328 |
2.00e-78 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 247.53 E-value: 2.00e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 8 GFGRIGRMFARQaLVRKDVK--------IVAINDPSLDPKYLAYMLRYDSTHGQFNQKISVDGNN--LVVNGKKIQLLKE 77
Cdd:PRK08289 134 GFGRIGRLLARL-LIEKTGGgnglrlraIVVRKGSEGDLEKRASLLRRDSVHGPFNGTITVDEENnaIIANGNYIQVIYA 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 78 SDVKKIKWCDLGVHT--VVECSGRFTTLKACQGHLDS-GAKKVVISAPS-ADAPMFVCGVNLEAYKPGTAIISNASCTTN 153
Cdd:PRK08289 213 NSPEEVDYTAYGINNalVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGkGDIKNIVHGVNHSDITDEDKIVSAASCTTN 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 154 CLAPLAKVVHDNFEICEGLMTTVHAATATQKIIDGPSSKlWRDGRSGMTNIIPASTGAAKAVGKVIPDLNGKLTGMAFRV 233
Cdd:PRK08289 293 AITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKG-DRRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNAIRV 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 234 PVPNVSVVDLTCRLSKPAKMDDIKKCIKAAS-KCEMKGILGYVEE-EVVSTDFNGSRFASVFDAKACIALNDNFVkLISW 311
Cdd:PRK08289 372 PTPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQIDYTDStEVVSSDFVGSRHAGVVDSQATIVNGNRAV-LYVW 450
|
330
....*....|....*..
gi 19922412 312 YDNETGYSCRLLDLVLY 328
Cdd:PRK08289 451 YDNEFGYSCQVVRVMEQ 467
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
4-150 |
3.21e-74 |
|
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: 225.89 E-value: 3.21e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 4 IGINGFGRIGRMFARQALVRKDVKIVAINDPSlDPKYLAYMLRYDSTHGQFNQKISVDGNNLVVNGKKIQLLKESDVKKI 83
Cdd:smart00846 3 VGINGFGRIGRLVLRAALERPDVEVVAINDLT-DPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANL 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19922412 84 KWCDLGVHTVVECSGRFTTLKACQGHLDSGAKKVVISAPSADA-PMFVCGVNLEAYKPGTAIISNASC 150
Cdd:smart00846 82 PWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDGEDHIISNASC 149
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
4-338 |
1.46e-57 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 189.70 E-value: 1.46e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 4 IGINGFGRIGRMFARQALVRKDVKIVAINDPSLDPKYLAYMLRYDSTHGQFNQ-KISVDGNNLVVNG-KKIQLLKESDVK 81
Cdd:PTZ00353 5 VGINGFGPVGKAVLFASLTDPLVTVVAVNDASVSIAYIAYVLEQESPLSAPDGaSIRVVGEQIVLNGtQKIRVSAKHDLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 82 KIKWCDLGVHTVVECSGRFTTLKACQGHLDSGAKKVVISAPSADAPMFVCGVNLEAYKPGTAIISNASCTTNCLAPLAKV 161
Cdd:PTZ00353 85 EIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDERLSASLPVCCAGAPIAVALAPVIRA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 162 VHDNFEICEGLMTTVHaATATQKIIDGPS--SKLWRDGRSGMTNIIPASTGAAKAVGKVIPDLNGKLTGMAFRVPVPNVS 239
Cdd:PTZ00353 165 LHEVYGVEECSYTAIH-GMQPQEPIAARSknSQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVKKGC 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 240 VVDLTCRLSKPAKMDDIKKCIKAASKCEMKGILGYVEEEVVSTDFNGSRfASVFDAKACIALNDNFV-KLISWYDNETGY 318
Cdd:PTZ00353 244 AIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCIPNG-KLCYDATSSSSSREGEVhKMVLWFDVECYY 322
|
330 340
....*....|....*....|
gi 19922412 319 SCRLLDLVlyaQLVDQCDAK 338
Cdd:PTZ00353 323 AARLLSLV---KQLHQIHAP 339
|
|
| Gp_dh_N |
pfam00044 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
4-102 |
6.88e-48 |
|
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: 156.49 E-value: 6.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 4 IGINGFGRIGRMFARQALVRKDVKIVAINDpSLDPKYLAYMLRYDSTHGQFNQKISVDGNNLVVNGKKIQLLKESDVKKI 83
Cdd:pfam00044 3 VGINGFGRIGRLVLRAALERPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAEL 81
|
90
....*....|....*....
gi 19922412 84 KWCDLGVHTVVECSGRFTT 102
Cdd:pfam00044 82 PWGDLGVDVVIESTGVFTT 100
|
|
| GAPDH_N_E4PDH |
cd17892 |
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
4-149 |
1.63e-47 |
|
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: 158.20 E-value: 1.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 4 IGINGFGRIGRMFARqAL----VRKDVKIVAINDPSlDPKYLAYMLRYDSTHGQFNQKISVDGNNLVVNGKKIQLLKESD 79
Cdd:cd17892 3 VAINGYGRIGRNVLR-ALyesgRRAEFQVVAINELA-DAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19922412 80 VKKIKWCDLGVHTVVECSGRFTTLKACQGHLDSGAKKVVISAPSA---DAPMfVCGVNLEAYKPGTAIISNAS 149
Cdd:cd17892 81 PENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASndvDATI-VYGINQDLLRAEHRIVSNAS 152
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
150-315 |
3.45e-42 |
|
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: 144.20 E-value: 3.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 150 CTTNCLAPLAKVVHDNFEICEGLMTTVHAATATQKIIDGPSSKLWRDGRSgmTNIIPASTGAAKAVGKVIPDLN--GKLT 227
Cdd:cd18122 1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSEVRAII--PNIPKNETKHAPETGKVLGEIGkpIKVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 228 GMAFRVPVPNVSVVDLTCRLSKPAKMDDIKKCIKAASKCEMKGILGYVEEEVVSTDFNGSRFASVFDAKACIALNDNFVK 307
Cdd:cd18122 79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLK 158
|
....*...
gi 19922412 308 LISWYDNE 315
Cdd:cd18122 159 VFSAVDNE 166
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
150-315 |
4.80e-42 |
|
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: 143.71 E-value: 4.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 150 CTTNCLAPLAKVVHDNFEICEGLMTTVHAATATQKIIDGPSSKLwRDGRSGMTNIIPASTGAAKAVGKVIPDLNGKLTGM 229
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDAYHPDL-RRTRAASQSIIPVDTKLARGIERILPHLAGRFEAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 230 AFRVPVPNVSVVDLTCRLSKPAKMDDIKKCIKAASKCEMKGILGYVEEEVVSTDFNGSRFASVFDAKACIALNDNFVKLI 309
Cdd:cd23937 80 AVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLL 159
|
....*.
gi 19922412 310 SWYDNE 315
Cdd:cd23937 160 VWCDNE 165
|
|
| GAPDH-like_N |
cd05192 |
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ... |
4-154 |
1.04e-11 |
|
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: 60.83 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19922412 4 IGINGFGRIGRMFARQALVRKDVKIVAINDpsldpkylaymlrydsthgqfnqkisvdgnnlvvngkkiqllkESDVkki 83
Cdd:cd05192 3 VAINGFGRIGRIVFRAIADQDDLDVVAIND-------------------------------------------RRDV--- 36
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19922412 84 kwcdlgvhtVVECSGRFTTLKACQGHLDSGAKKVVISAPS-ADAPMFVCGVNLEAYKPGTAIISNASCTTNC 154
Cdd:cd05192 37 ---------VIECTGSFTDDDNAEKHIKAGGKKAVITAPEkGDIPTIVVVLNELAKSAGATVVSNANETSYS 99
|
|
| MviM |
COG0673 |
Predicted dehydrogenase [General function prediction only]; |
3-37 |
8.00e-03 |
|
Predicted dehydrogenase [General function prediction only];
Pssm-ID: 440437 [Multi-domain] Cd Length: 295 Bit Score: 37.60 E-value: 8.00e-03
10 20 30
....*....|....*....|....*....|....*
gi 19922412 3 GIGINGFGRIGRMFARQALVRKDVKIVAINDPSLD 37
Cdd:COG0673 5 RVGIIGAGGIGRAHAPALAALPGVELVAVADRDPE 39
|
|
| |
