|
Name |
Accession |
Description |
Interval |
E-value |
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
1-331 |
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: 610.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 1 MTIKVGINGFGRIGRIVFRAAQER-SDIEIVAINDLLDAEYMAYMLKYDSTHGRFNGTVEVKDGHLVVNGKTIRVTAEKD 79
Cdd:COG0057 1 MTIRVAINGFGRIGRLVLRALLERgPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 80 PANLKWNEVGVDVVAEATGIFLTDETARKHITAGAKKVVLTGPSKDATPMFVRGANFDKY-AGQDIVSNASCTTNCLAPL 158
Cdd:COG0057 81 PAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDDPTIVYGVNHDDYdADHRIISNASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 159 AKVINDNFGIVEGLMTTVHATTATQKTVDGPsHKDWRGGRGASQNIIPSSTGAAKAVGVVLPELKGKLTGMAFRVPTPNV 238
Cdd:COG0057 161 AKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 239 SVVDLTVRLEKAATYEEIKKAIKDAAEGSMKGVLGYVEDDVVSTDFNGEVLTSVFDAKAGIALNDNFVKLVSWYDNETGY 318
Cdd:COG0057 240 SLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGY 319
|
330
....*....|...
gi 491070598 319 SNKVLDLIAHISK 331
Cdd:COG0057 320 SNRMVDLAEYMAK 332
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
1-331 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 608.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 1 MTIKVGINGFGRIGRIVFRAAQERSDIEIVAINDLLDAEYMAYMLKYDSTHGRFNGTVEVKDGHLVVNGKTIRVTAEKDP 80
Cdd:PRK15425 1 MTIKVGINGFGRIGRIVFRAAQKRSDIEIVAINDLLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 81 ANLKWNEVGVDVVAEATGIFLTDETARKHITAGAKKVVLTGPSKDATPMFVRGANFDKYAGQDIVSNASCTTNCLAPLAK 160
Cdd:PRK15425 81 ANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDNTPMFVKGANFDKYAGQDIVSNASCTTNCLAPLAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 161 VINDNFGIVEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGVVLPELKGKLTGMAFRVPTPNVSV 240
Cdd:PRK15425 161 VINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 241 VDLTVRLEKAATYEEIKKAIKDAAEGSMKGVLGYVEDDVVSTDFNGEVLTSVFDAKAGIALNDNFVKLVSWYDNETGYSN 320
Cdd:PRK15425 241 VDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYSN 320
|
330
....*....|.
gi 491070598 321 KVLDLIAHISK 331
Cdd:PRK15425 321 KVLDLIAHISK 331
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
4-324 |
1.72e-179 |
|
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: 499.11 E-value: 1.72e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 4 KVGINGFGRIGRIVFRAAQER--SDIEIVAINDLLDAEYMAYMLKYDSTHGRFNGTVEVKDGHLVVNGK-TIRVTAEKDP 80
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKpgNDLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKeVISVFSERDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 81 ANLKWNEVGVDVVAEATGIFLTDETARKHITAGAKKVVLTGPSKDATPMFVRGANFDKY-AGQDIVSNASCTTNCLAPLA 159
Cdd:TIGR01534 81 SDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDVKTIVYGVNHDEYdGEERIISNASCTTNCLAPLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 160 KVINDNFGIVEGLMTTVHATTATQKTVDGPsHKDWRGGRGASQNIIPSSTGAAKAVGVVLPELKGKLTGMAFRVPTPNVS 239
Cdd:TIGR01534 161 KVLDEAFGIVSGLMTTVHAYTNDQNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 240 VVDLTVRLEKAATYEEIKKAIKDAAEGSMKGVLGYVEDDVVSTDFNGEVLTSVFDAKAGIA--LNDNFVKLVSWYDNETG 317
Cdd:TIGR01534 240 LVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNEWG 319
|
....*..
gi 491070598 318 YSNKVLD 324
Cdd:TIGR01534 320 YSNRLVD 326
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
150-315 |
2.59e-119 |
|
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: 340.59 E-value: 2.59e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 150 CTTNCLAPLAKVINDNFGIVEGLMTTVHATTATQKTVDGPsHKDWRGGRGASQNIIPSSTGAAKAVGVVLPELKGKLTGM 229
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGP-HKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 230 AFRVPTPNVSVVDLTVRLEKAATYEEIKKAIKDAAEGSMKGVLGYVEDDVVSTDFNGEVLTSVFDAKAGIALNDNFVKLV 309
Cdd:cd18126 80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159
|
....*.
gi 491070598 310 SWYDNE 315
Cdd:cd18126 160 AWYDNE 165
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
5-325 |
3.75e-115 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 336.14 E-value: 3.75e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 5 VGINGFGRIGRIVFRAAQERSDIEIVAINDLL-DAEYMAYMLKYDSTHGRFNGTVEVKDGHLVVNGKTIRVTAEKDPANL 83
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAgDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 84 KWNEvGVDVVAEATGIFLTDETARKHITAGAKKVVLTGPSKDATPM-FVRGANFDKY--AGQDIVSNASCTTNCLAPLAK 160
Cdd:NF033735 81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLnIVYGVNDHLYdpARHRIVTAASCTTNCLAPVVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 161 VINDNFGIVEGLMTTVHATTATQKTVDGPsHKDWRGGRGASQNIIPSSTGAAKAVGVVLPELKGKLTGMAFRVPTPNVSV 240
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 241 VDLTVRLEKAATYEEIKKAIKDAAEGSMKGVLGYVEDDVVSTDFNGEVLTSVFDAKAGIALNDNFVKLVSWYDNETGYSN 320
Cdd:NF033735 239 TDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYAN 318
|
....*
gi 491070598 321 KVLDL 325
Cdd:NF033735 319 RMVDL 323
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
155-312 |
1.41e-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: 267.54 E-value: 1.41e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 155 LAPLAKVINDNFGIVEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGVVLPELKGKLTGMAFRVP 234
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491070598 235 TPNVSVVDLTVRLEKAATYEEIKKAIKDAAEGSMKGVLGYVEDDVVSTDFNGEVLTSVFDAKAGIALNDNFVKLVSWY 312
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-150 |
1.35e-84 |
|
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: 251.70 E-value: 1.35e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 3 IKVGINGFGRIGRIVFRAAQERSDIEIVAINDLLDAEYMAYMLKYDSTHGRFNGTVEVKDGHLVVNGKTIRVTAEKDPAN 82
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPAN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491070598 83 LKWNEVGVDVVAEATGIFLTDETARKHITAGAKKVVLTGPSKDATPMFVRGANFDKYAGQD-IVSNASC 150
Cdd:smart00846 81 LPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDADPTFVYGVNHDEYDGEDhIISNASC 149
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GapA |
COG0057 |
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ... |
1-331 |
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: 610.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 1 MTIKVGINGFGRIGRIVFRAAQER-SDIEIVAINDLLDAEYMAYMLKYDSTHGRFNGTVEVKDGHLVVNGKTIRVTAEKD 79
Cdd:COG0057 1 MTIRVAINGFGRIGRLVLRALLERgPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 80 PANLKWNEVGVDVVAEATGIFLTDETARKHITAGAKKVVLTGPSKDATPMFVRGANFDKY-AGQDIVSNASCTTNCLAPL 158
Cdd:COG0057 81 PAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDDPTIVYGVNHDDYdADHRIISNASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 159 AKVINDNFGIVEGLMTTVHATTATQKTVDGPsHKDWRGGRGASQNIIPSSTGAAKAVGVVLPELKGKLTGMAFRVPTPNV 238
Cdd:COG0057 161 AKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 239 SVVDLTVRLEKAATYEEIKKAIKDAAEGSMKGVLGYVEDDVVSTDFNGEVLTSVFDAKAGIALNDNFVKLVSWYDNETGY 318
Cdd:COG0057 240 SLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGY 319
|
330
....*....|...
gi 491070598 319 SNKVLDLIAHISK 331
Cdd:COG0057 320 SNRMVDLAEYMAK 332
|
|
| gapA |
PRK15425 |
glyceraldehyde-3-phosphate dehydrogenase; |
1-331 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 185323 [Multi-domain] Cd Length: 331 Bit Score: 608.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 1 MTIKVGINGFGRIGRIVFRAAQERSDIEIVAINDLLDAEYMAYMLKYDSTHGRFNGTVEVKDGHLVVNGKTIRVTAEKDP 80
Cdd:PRK15425 1 MTIKVGINGFGRIGRIVFRAAQKRSDIEIVAINDLLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 81 ANLKWNEVGVDVVAEATGIFLTDETARKHITAGAKKVVLTGPSKDATPMFVRGANFDKYAGQDIVSNASCTTNCLAPLAK 160
Cdd:PRK15425 81 ANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDNTPMFVKGANFDKYAGQDIVSNASCTTNCLAPLAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 161 VINDNFGIVEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGVVLPELKGKLTGMAFRVPTPNVSV 240
Cdd:PRK15425 161 VINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 241 VDLTVRLEKAATYEEIKKAIKDAAEGSMKGVLGYVEDDVVSTDFNGEVLTSVFDAKAGIALNDNFVKLVSWYDNETGYSN 320
Cdd:PRK15425 241 VDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYSN 320
|
330
....*....|.
gi 491070598 321 KVLDLIAHISK 331
Cdd:PRK15425 321 KVLDLIAHISK 331
|
|
| PLN02272 |
PLN02272 |
glyceraldehyde-3-phosphate dehydrogenase |
3-330 |
0e+00 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 177912 [Multi-domain] Cd Length: 421 Bit Score: 546.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 3 IKVGINGFGRIGRIVFRAAQERSDIEIVAIND-LLDAEYMAYMLKYDSTHGRFNGTVEV-KDGHLVVNGKTIRVTAEKDP 80
Cdd:PLN02272 86 TKIGINGFGRIGRLVLRIATSRDDIEVVAVNDpFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDP 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 81 ANLKWNEVGVDVVAEATGIFLTDETARKHITAGAKKVVLTGPSKDAtPMFVRGANFDKY-AGQDIVSNASCTTNCLAPLA 159
Cdd:PLN02272 166 AEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADA-PMFVVGVNEKTYkPNMNIVSNASCTTNCLAPLA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 160 KVINDNFGIVEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGVVLPELKGKLTGMAFRVPTPNVS 239
Cdd:PLN02272 245 KVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVS 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 240 VVDLTVRLEKAATYEEIKKAIKDAAEGSMKGVLGYVEDDVVSTDFNGEVLTSVFDAKAGIALNDNFVKLVSWYDNETGYS 319
Cdd:PLN02272 325 VVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYS 404
|
330
....*....|.
gi 491070598 320 NKVLDLIAHIS 330
Cdd:PLN02272 405 NRVLDLIEHMA 415
|
|
| GAPDH-I |
TIGR01534 |
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ... |
4-324 |
1.72e-179 |
|
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: 499.11 E-value: 1.72e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 4 KVGINGFGRIGRIVFRAAQER--SDIEIVAINDLLDAEYMAYMLKYDSTHGRFNGTVEVKDGHLVVNGK-TIRVTAEKDP 80
Cdd:TIGR01534 1 KVGINGFGRIGRLVLRRILEKpgNDLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKeVISVFSERDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 81 ANLKWNEVGVDVVAEATGIFLTDETARKHITAGAKKVVLTGPSKDATPMFVRGANFDKY-AGQDIVSNASCTTNCLAPLA 159
Cdd:TIGR01534 81 SDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDVKTIVYGVNHDEYdGEERIISNASCTTNCLAPLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 160 KVINDNFGIVEGLMTTVHATTATQKTVDGPsHKDWRGGRGASQNIIPSSTGAAKAVGVVLPELKGKLTGMAFRVPTPNVS 239
Cdd:TIGR01534 161 KVLDEAFGIVSGLMTTVHAYTNDQNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 240 VVDLTVRLEKAATYEEIKKAIKDAAEGSMKGVLGYVEDDVVSTDFNGEVLTSVFDAKAGIA--LNDNFVKLVSWYDNETG 317
Cdd:TIGR01534 240 LVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNEWG 319
|
....*..
gi 491070598 318 YSNKVLD 324
Cdd:TIGR01534 320 YSNRLVD 326
|
|
| PTZ00023 |
PTZ00023 |
glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-331 |
2.06e-174 |
|
glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173322 [Multi-domain] Cd Length: 337 Bit Score: 487.03 E-value: 2.06e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 1 MTIKVGINGFGRIGRIVFRAAQERSDIEIVAIND-LLDAEYMAYMLKYDSTHGRFNGTVEVKDGHLVVNGKTIRVTAEKD 79
Cdd:PTZ00023 1 MVVKLGINGFGRIGRLVFRAALEREDVEVVAINDpFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 80 PANLKWNEVGVDVVAEATGIFLTDETARKHITAGAKKVVLTGPSKDATPMFVRGANFDKY-AGQDIVSNASCTTNCLAPL 158
Cdd:PTZ00023 81 PAAIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKDDTPIYVMGVNHTQYdKSQRIVSNASCTTNCLAPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 159 AKVINDNFGIVEGLMTTVHATTATQKTVDGPSH--KDWRGGRGASQNIIPSSTGAAKAVGVVLPELKGKLTGMAFRVPTP 236
Cdd:PTZ00023 161 AKVVNDKFGIVEGLMTTVHASTANQLTVDGPSKggKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 237 NVSVVDLTVRLEKAATYEEIKKAIKDAAEGSMKGVLGYVEDDVVSTDFNGEVLTSVFDAKAGIALNDNFVKLVSWYDNET 316
Cdd:PTZ00023 241 DVSVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDNEW 320
|
330
....*....|....*
gi 491070598 317 GYSNKVLDLIAHISK 331
Cdd:PTZ00023 321 GYSNRLLDLAHYITQ 335
|
|
| PRK07729 |
PRK07729 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-331 |
5.83e-149 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 236079 [Multi-domain] Cd Length: 343 Bit Score: 422.61 E-value: 5.83e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 1 MTIKVGINGFGRIGRIVFRAAQERSDIEIVAINDLLDAEYMAYMLKYDSTHGRFNGTVEVKDGHLVVNGKTIRVTAEKDP 80
Cdd:PRK07729 1 MKTKVAINGFGRIGRMVFRKAIKESAFEIVAINASYPSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 81 ANLKWNEVGVDVVAEATGIFLTDETARKHITAGAKKVVLTGPSKDATPMFVRGANFDKYAGQ--DIVSNASCTTNCLAPL 158
Cdd:PRK07729 81 KELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVTIVVGVNEDQLDIEkhTIISNASCTTNCLAPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 159 AKVINDNFGIVEGLMTTVHATTATQKTVDGPsHKDWRGGRGASQNIIPSSTGAAKAVGVVLPELKGKLTGMAFRVPTPNV 238
Cdd:PRK07729 161 VKVLDEQFGIENGLMTTVHAYTNDQKNIDNP-HKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 239 SVVDLTVRLEKAATYEEIKKAIKDAAEGSMKGVLGYVEDDVVSTDFNGEVLTSVFDAKAGIALNDNFVKLVSWYDNETGY 318
Cdd:PRK07729 240 SLVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEWGY 319
|
330
....*....|...
gi 491070598 319 SNKVLDLIAHISK 331
Cdd:PRK07729 320 SCRVVDLVTLVAD 332
|
|
| PLN02358 |
PLN02358 |
glyceraldehyde-3-phosphate dehydrogenase |
3-331 |
1.54e-148 |
|
glyceraldehyde-3-phosphate dehydrogenase
Pssm-ID: 165999 [Multi-domain] Cd Length: 338 Bit Score: 421.44 E-value: 1.54e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 3 IKVGINGFGRIGRIVFRAAQERSDIEIVAIND-LLDAEYMAYMLKYDSTHGRF-NGTVEVKDGHLVVNG-KTIRVTAEKD 79
Cdd:PLN02358 6 IRIGINGFGRIGRLVARVVLQRDDVELVAVNDpFITTEYMTYMFKYDSVHGQWkHHELKVKDDKTLLFGeKPVTVFGIRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 80 PANLKWNEVGVDVVAEATGIFLTDETARKHITAGAKKVVLTGPSKDAtPMFVRGANFDKYAGQ-DIVSNASCTTNCLAPL 158
Cdd:PLN02358 86 PEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDA-PMFVVGVNEHEYKSDlDIVSNASCTTNCLAPL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 159 AKVINDNFGIVEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGVVLPELKGKLTGMAFRVPTPNV 238
Cdd:PLN02358 165 AKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 239 SVVDLTVRLEKAATYEEIKKAIKDAAEGSMKGVLGYVEDDVVSTDFNGEVLTSVFDAKAGIALNDNFVKLVSWYDNETGY 318
Cdd:PLN02358 245 SVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEWGY 324
|
330
....*....|...
gi 491070598 319 SNKVLDLIAHISK 331
Cdd:PLN02358 325 SSRVVDLIVHMSK 337
|
|
| PTZ00434 |
PTZ00434 |
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional |
1-330 |
6.64e-133 |
|
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
Pssm-ID: 185614 [Multi-domain] Cd Length: 361 Bit Score: 382.48 E-value: 6.64e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 1 MTIKVGINGFGRIGRIVFRAAQER----SDIEIVAINDL-LDAEYMAYMLKYDSTHGRFNGTVEV--------KDGHLVV 67
Cdd:PTZ00434 2 APIKVGINGFGRIGRMVFQAICDQgligTEIDVVAVVDMsTNAEYFAYQMKYDTVHGRPKYTVETtksspsvkTDDVLVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 68 NGKTIR-VTAEKDPANLKWNEVGVDVVAEATGIFLTDETARKHITAGAKKVVLTGPSKDATPMFVRGANFDKYAGQD--I 144
Cdd:PTZ00434 82 NGHRIKcVKAQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPASGGAKTIVMGVNQHEYSPTEhhV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 145 VSNASCTTNCLAPLAKVI-NDNFGIVEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGVVLPELK 223
Cdd:PTZ00434 162 VSNASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 224 GKLTGMAFRVPTPNVSVVDLTVRLEKAATYEEIKKAIKDAAEGSMKGVLGYVEDDVVSTDFNGEVLTSVFDAKAGIALN- 302
Cdd:PTZ00434 242 GKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKATLQNNl 321
|
330 340 350
....*....|....*....|....*....|.
gi 491070598 303 ---DNFVKLVSWYDNETGYSNKVLDLIAHIS 330
Cdd:PTZ00434 322 pgeRRFFKIVSWYDNEWGYSHRVVDLVRYMA 352
|
|
| PRK07403 |
PRK07403 |
type I glyceraldehyde-3-phosphate dehydrogenase; |
2-325 |
4.12e-126 |
|
type I glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 180962 [Multi-domain] Cd Length: 337 Bit Score: 364.61 E-value: 4.12e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 2 TIKVGINGFGRIGRIVFRA--AQERSDIEIVAINDLLDAEYMAYMLKYDSTHGRFNGTVEVKDGHLVVNGKTIRVTAEKD 79
Cdd:PRK07403 1 MIRVAINGFGRIGRNFLRCwlGRENSQLELVAINDTSDPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 80 PANLKWNEVGVDVVAEATGIFLTDETARKHITAGAKKVVLTGPSKDATP-MFVRGANFDKYAGQD--IVSNASCTTNCLA 156
Cdd:PRK07403 81 PLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPGKGEDIgTYVVGVNHHEYDHEDhnIISNASCTTNCLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 157 PLAKVINDNFGIVEGLMTTVHATTATQKTVDGpSHKDWRGGRGASQNIIPSSTGAAKAVGVVLPELKGKLTGMAFRVPTP 236
Cdd:PRK07403 161 PIAKVLHDNFGIIKGTMTTTHSYTGDQRILDA-SHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 237 NVSVVDLTVRLEKAATYEEIKKAIKDAAEGSMKGVLGYVEDDVVSTDFNGEVLTSVFDAKAGIALNDNFVKLVSWYDNET 316
Cdd:PRK07403 240 NVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYDNEW 319
|
....*....
gi 491070598 317 GYSNKVLDL 325
Cdd:PRK07403 320 GYSQRVVDL 328
|
|
| GAPDH_I_C |
cd18126 |
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ... |
150-315 |
2.59e-119 |
|
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: 340.59 E-value: 2.59e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 150 CTTNCLAPLAKVINDNFGIVEGLMTTVHATTATQKTVDGPsHKDWRGGRGASQNIIPSSTGAAKAVGVVLPELKGKLTGM 229
Cdd:cd18126 1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGP-HKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 230 AFRVPTPNVSVVDLTVRLEKAATYEEIKKAIKDAAEGSMKGVLGYVEDDVVSTDFNGEVLTSVFDAKAGIALNDNFVKLV 309
Cdd:cd18126 80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159
|
....*.
gi 491070598 310 SWYDNE 315
Cdd:cd18126 160 AWYDNE 165
|
|
| PLN03096 |
PLN03096 |
glyceraldehyde-3-phosphate dehydrogenase A; Provisional |
3-325 |
1.23e-117 |
|
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
Pssm-ID: 215572 [Multi-domain] Cd Length: 395 Bit Score: 344.99 E-value: 1.23e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 3 IKVGINGFGRIGRIVFRAAQERSD--IEIVAINDLLDAEYMAYMLKYDSTHGRFNGTVE-VKDGHLVVNGKTIRVTAEKD 79
Cdd:PLN03096 61 IKVAINGFGRIGRNFLRCWHGRKDspLDVVAINDTGGVKQASHLLKYDSTLGTFDADVKpVGDDAISVDGKVIKVVSDRN 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 80 PANLKWNEVGVDVVAEATGIFLTDETARKHITAGAKKVVLTGPSKDATPMFVRGANFDKYAGQD-IVSNASCTTNCLAPL 158
Cdd:PLN03096 141 PLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKGDIPTYVVGVNADDYKHSDpIISNASCTTNCLAPF 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 159 AKVINDNFGIVEGLMTTVHATTATQKTVDGpSHKDWRGGRGASQNIIPSSTGAAKAVGVVLPELKGKLTGMAFRVPTPNV 238
Cdd:PLN03096 221 VKVLDQKFGIIKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNV 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 239 SVVDLTVRLEKAATYEEIKKAIKDAAEGSMKGVLGYVEDDVVSTDFNGEVLTSVFDAKAGIALNDNFVKLVSWYDNETGY 318
Cdd:PLN03096 300 SVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAWYDNEWGY 379
|
....*..
gi 491070598 319 SNKVLDL 325
Cdd:PLN03096 380 SQRVVDL 386
|
|
| G3PDH_Arsen |
NF033735 |
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase; |
5-325 |
3.75e-115 |
|
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 468158 [Multi-domain] Cd Length: 324 Bit Score: 336.14 E-value: 3.75e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 5 VGINGFGRIGRIVFRAAQERSDIEIVAINDLL-DAEYMAYMLKYDSTHGRFNGTVEVKDGHLVVNGKTIRVTAEKDPANL 83
Cdd:NF033735 1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAgDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 84 KWNEvGVDVVAEATGIFLTDETARKHITAGAKKVVLTGPSKDATPM-FVRGANFDKY--AGQDIVSNASCTTNCLAPLAK 160
Cdd:NF033735 81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLnIVYGVNDHLYdpARHRIVTAASCTTNCLAPVVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 161 VINDNFGIVEGLMTTVHATTATQKTVDGPsHKDWRGGRGASQNIIPSSTGAAKAVGVVLPELKGKLTGMAFRVPTPNVSV 240
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 241 VDLTVRLEKAATYEEIKKAIKDAAEGSMKGVLGYVEDDVVSTDFNGEVLTSVFDAKAGIALNDNFVKLVSWYDNETGYSN 320
Cdd:NF033735 239 TDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYAN 318
|
....*
gi 491070598 321 KVLDL 325
Cdd:NF033735 319 RMVDL 323
|
|
| PLN02237 |
PLN02237 |
glyceraldehyde-3-phosphate dehydrogenase B |
3-329 |
8.76e-113 |
|
glyceraldehyde-3-phosphate dehydrogenase B
Pssm-ID: 215131 [Multi-domain] Cd Length: 442 Bit Score: 334.18 E-value: 8.76e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 3 IKVGINGFGRIGRIVFRAAQERSD--IEIVAINDLLDAEYMAYMLKYDSTHGRFNGTVEVKDGHLV-VNGKTIRVTAEKD 79
Cdd:PLN02237 76 LKVAINGFGRIGRNFLRCWHGRKDspLDVVVVNDSGGVKNASHLLKYDSMLGTFKADVKIVDDETIsVDGKPIKVVSNRD 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 80 PANLKWNEVGVDVVAEATGIFLTDETARKHITAGAKKVVLTGPSKDA-TPMFVRGANFDKYAGQ--DIVSNASCTTNCLA 156
Cdd:PLN02237 156 PLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAKGAdIPTYVVGVNEDDYDHEvaNIVSNASCTTNCLA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 157 PLAKVINDNFGIVEGLMTTVHATTATQKTVDGpSHKDWRGGRGASQNIIPSSTGAAKAVGVVLPELKGKLTGMAFRVPTP 236
Cdd:PLN02237 236 PFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 237 NVSVVDLTVRLEKAA-TYEEIKKAIKDAAEGSMKGVLGYVEDDVVSTDFNGEVLTSVFDAKAGIALNDNFVKLVSWYDNE 315
Cdd:PLN02237 315 NVSVVDLVVNVEKKGiTAEDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVAWYDNE 394
|
330
....*....|....
gi 491070598 316 TGYSNKVLDLiAHI 329
Cdd:PLN02237 395 WGYSQRVVDL-AHL 407
|
|
| PRK08955 |
PRK08955 |
glyceraldehyde-3-phosphate dehydrogenase; Validated |
1-326 |
1.17e-107 |
|
glyceraldehyde-3-phosphate dehydrogenase; Validated
Pssm-ID: 169599 [Multi-domain] Cd Length: 334 Bit Score: 317.44 E-value: 1.17e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 1 MTIKVGINGFGRIGRIVFRAAQERSDIEIVAINDLL-DAEYMAYMLKYDSTHGRFNGTVEVKDGHLVVNGKTIRVTAEKD 79
Cdd:PRK08955 1 MTIKVGINGFGRIGRLALRAAWDWPELEFVQINDPAgDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 80 PANLKWNevGVDVVAEATGIFLTDETARKHITAGAKKVVLTGPSKDATPM-FVRGAN---FDKyAGQDIVSNASCTTNCL 155
Cdd:PRK08955 81 IADTDWS--GCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLnIVMGVNdhlFDP-AIHPIVTAASCTTNCL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 156 APLAKVINDNFGIVEGLMTTVHATTATQKTVDGPsHKDWRGGRGASQNIIPSSTGAAKAVGVVLPELKGKLTGMAFRVPT 235
Cdd:PRK08955 158 APVVKVIHEKLGIKHGSMTTIHDLTNTQTILDAP-HKDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 236 PNVSVVDLTVRLEKAATYEEIKKAIKDAAEGSMKGVLGYVEDDVVSTDFNGEVLTSVFDAKAGIALNDNFVKLVSWYDNE 315
Cdd:PRK08955 237 ANASLTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNE 316
|
330
....*....|.
gi 491070598 316 TGYSNKVLDLI 326
Cdd:PRK08955 317 WGYANRTAELA 327
|
|
| PRK13535 |
PRK13535 |
erythrose 4-phosphate dehydrogenase; Provisional |
2-324 |
3.84e-104 |
|
erythrose 4-phosphate dehydrogenase; Provisional
Pssm-ID: 184122 [Multi-domain] Cd Length: 336 Bit Score: 308.52 E-value: 3.84e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 2 TIKVGINGFGRIGRIVFRAAQE---RSDIEIVAINDLLDAEYMAYMLKYDSTHGRFNGTVEVKDGHLVVNGKTIRVTAEK 78
Cdd:PRK13535 1 TIRVAINGFGRIGRNVLRALYEsgrRAEITVVAINELADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 79 DPANLKWNEVGVDVVAEATGIFLTDETARKHITAGAKKVVLTGPSK---DATpmFVRGANFDKYAGQD-IVSNASCTTNC 154
Cdd:PRK13535 81 DIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSndlDAT--VVYGVNHDQLRAEHrIVSNASCTTNC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 155 LAPLAKVINDNFGIVEGLMTTVHATTATQKTVDGpSHKDWRGGRGASQNIIPSSTGAAKAVGVVLPELKGKLTGMAFRVP 234
Cdd:PRK13535 159 IIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 235 TPNVSVVDLTVRLEKAATYEEIKKAIKDAAEGSMKGVLGYVEDDVVSTDFNGEVLTSVFDAKAGIALNDNFVKLVSWYDN 314
Cdd:PRK13535 238 TINVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDN 317
|
330
....*....|
gi 491070598 315 ETGYSNKVLD 324
Cdd:PRK13535 318 EWGFANRMLD 327
|
|
| Gp_dh_C |
pfam02800 |
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ... |
155-312 |
1.41e-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: 267.54 E-value: 1.41e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 155 LAPLAKVINDNFGIVEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGVVLPELKGKLTGMAFRVP 234
Cdd:pfam02800 1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491070598 235 TPNVSVVDLTVRLEKAATYEEIKKAIKDAAEGSMKGVLGYVEDDVVSTDFNGEVLTSVFDAKAGIALNDNFVKLVSWY 312
Cdd:pfam02800 81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
|
|
| GAPDH_I_N |
cd05214 |
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
3-149 |
1.05e-89 |
|
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: 265.41 E-value: 1.05e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 3 IKVGINGFGRIGRIVFRAAQERSDIEIVAINDLLDAEYMAYMLKYDSTHGRFNGTVEVKDGHLVVNGKTIRVTAEKDPAN 82
Cdd:cd05214 1 IKVGINGFGRIGRLVFRAALERDDIEVVAINDLTDDETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491070598 83 LKWNEVGVDVVAEATGIFLTDETARKHITAGAKKVVLTGPSKDATPMFVRGANFDKY-AGQDIVSNAS 149
Cdd:cd05214 81 LPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDDDPTIVMGVNHDKYdADDKIISNAS 148
|
|
| GAPDH_C |
cd18123 |
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ... |
150-315 |
4.14e-89 |
|
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: 264.09 E-value: 4.14e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 150 CTTNCLAPLAKVINDNFGIVEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGVVLPELKGKLTGM 229
Cdd:cd18123 1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 230 AFRVPTPNVSVVDLTVRLEKAATYEEIKKAIKDAAEGsmKGVLGYVEDDVVSTDFNGEVLTSVFDAKAGIALNDNFVKLV 309
Cdd:cd18123 81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLM 158
|
....*.
gi 491070598 310 SWYDNE 315
Cdd:cd18123 159 QWYDNE 164
|
|
| PRK08289 |
PRK08289 |
glyceraldehyde-3-phosphate dehydrogenase; Reviewed |
9-331 |
2.60e-85 |
|
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
Pssm-ID: 236219 [Multi-domain] Cd Length: 477 Bit Score: 264.86 E-value: 2.60e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 9 GFGRIGRIVFRAAQERS----DIEIVAI-------NDLldaEYMAYMLKYDSTHGRFNGTVEVKDGH--LVVNGKTIRVT 75
Cdd:PRK08289 134 GFGRIGRLLARLLIEKTgggnGLRLRAIvvrkgseGDL---EKRASLLRRDSVHGPFNGTITVDEENnaIIANGNYIQVI 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 76 AEKDPANLKWNEVGVD--VVAEATGIFLTDETARKHITA-GAKKVVLTGPSKDATPMFVRGANFDKYAGQD-IVSNASCT 151
Cdd:PRK08289 211 YANSPEEVDYTAYGINnaLVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGKGDIKNIVHGVNHSDITDEDkIVSAASCT 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 152 TNCLAPLAKVINDNFGIVEGLMTTVHATTATQKTVDGpSHKDWRGGRGASQNIIPSSTGAAKAVGVVLPELKGKLTGMAF 231
Cdd:PRK08289 291 TNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDN-YHKGDRRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNAI 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 232 RVPTPNVSVVDLTVRLEKAATYEEIKKAIKDAA-EGSMKGVLGYVED-DVVSTDFNGEVLTSVFDAKAGIALNDNFVkLV 309
Cdd:PRK08289 370 RVPTPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQIDYTDStEVVSSDFVGSRHAGVVDSQATIVNGNRAV-LY 448
|
330 340
....*....|....*....|..
gi 491070598 310 SWYDNETGYSNKVLDLIAHISK 331
Cdd:PRK08289 449 VWYDNEFGYSCQVVRVMEQMAG 470
|
|
| Gp_dh_N |
smart00846 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-150 |
1.35e-84 |
|
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: 251.70 E-value: 1.35e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 3 IKVGINGFGRIGRIVFRAAQERSDIEIVAINDLLDAEYMAYMLKYDSTHGRFNGTVEVKDGHLVVNGKTIRVTAEKDPAN 82
Cdd:smart00846 1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPAN 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491070598 83 LKWNEVGVDVVAEATGIFLTDETARKHITAGAKKVVLTGPSKDATPMFVRGANFDKYAGQD-IVSNASC 150
Cdd:smart00846 81 LPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDADPTFVYGVNHDEYDGEDhIISNASC 149
|
|
| Gp_dh_N |
pfam00044 |
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ... |
3-102 |
6.24e-60 |
|
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: 187.31 E-value: 6.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 3 IKVGINGFGRIGRIVFRAAQERSDIEIVAINDLLDAEYMAYMLKYDSTHGRFNGTVEVKDGHLVVNGKTIRVTAEKDPAN 82
Cdd:pfam00044 1 VKVGINGFGRIGRLVLRAALERPDIEVVAINDLTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAE 80
|
90 100
....*....|....*....|
gi 491070598 83 LKWNEVGVDVVAEATGIFLT 102
Cdd:pfam00044 81 LPWGDLGVDVVIESTGVFTT 100
|
|
| PTZ00353 |
PTZ00353 |
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional |
1-326 |
2.62e-55 |
|
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 173546 [Multi-domain] Cd Length: 342 Bit Score: 183.54 E-value: 2.62e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 1 MTIKVGINGFGRIGRIVFRAAQERSDIEIVAINDL-LDAEYMAYMLKYDSTHGRFNGT-VEVKDGHLVVNG-KTIRVTAE 77
Cdd:PTZ00353 1 LPITVGINGFGPVGKAVLFASLTDPLVTVVAVNDAsVSIAYIAYVLEQESPLSAPDGAsIRVVGEQIVLNGtQKIRVSAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 78 KDPANLKWNEVGVDVVAEATGIFLTDETARKHITAGAKKVVLTGPSKDAtPMFVRGANFDKY-AGQDIVSNASCTTNCLA 156
Cdd:PTZ00353 81 HDLVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSADA-PTVMAGSNDERLsASLPVCCAGAPIAVALA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 157 PLAKVINDNFGIVEGLMTTVHATTAtQKTVDGPSH--KDWRGGRGASQNIIPSSTGAAKAVGVVLPELKGKLTGMAFRVP 234
Cdd:PTZ00353 160 PVIRALHEVYGVEECSYTAIHGMQP-QEPIAARSKnsQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 235 TPNVSVVDLTVRLEKAATYEEIKKAIKDAAEGSMKGVLGYVEDDVVSTDF--NGEVltsVFDAKAGIALNDNFV-KLVSW 311
Cdd:PTZ00353 239 VKKGCAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCipNGKL---CYDATSSSSSREGEVhKMVLW 315
|
330
....*....|....*
gi 491070598 312 YDNETGYSNKVLDLI 326
Cdd:PTZ00353 316 FDVECYYAARLLSLV 330
|
|
| GAPDH_like_C |
cd18122 |
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ... |
150-315 |
3.58e-53 |
|
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: 172.32 E-value: 3.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 150 CTTNCLAPLAKVINDNFGIVEGLMTTVHATTATQKTVDGPSHKDWrgGRGASQNIIPSSTGAAKAVGVVLPEL--KGKLT 227
Cdd:cd18122 1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIgkPIKVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 228 GMAFRVPTPNVSVVDLTVRLEKAATYEEIKKAIKDAAEGSMKGVLGYVEDDVVSTDFNGEVLTSVFDAKAGIALNDNFVK 307
Cdd:cd18122 79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLK 158
|
....*...
gi 491070598 308 LVSWYDNE 315
Cdd:cd18122 159 VFSAVDNE 166
|
|
| GAPDH_N_E4PDH |
cd17892 |
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
3-149 |
5.81e-53 |
|
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: 171.68 E-value: 5.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 3 IKVGINGFGRIGRIVFRAAQE---RSDIEIVAINDLLDAEYMAYMLKYDSTHGRFNGTVEVKDGHLVVNGKTIRVTAEKD 79
Cdd:cd17892 1 YRVAINGYGRIGRNVLRALYEsgrRAEFQVVAINELADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491070598 80 PANLKWNEVGVDVVAEATGIFLTDETARKHITAGAKKVVLTGPSK---DATpmFVRGANFDKYAGQD-IVSNAS 149
Cdd:cd17892 81 PENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASndvDAT--IVYGINQDLLRAEHrIVSNAS 152
|
|
| GAPDH_C_E4PDH |
cd23937 |
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ... |
150-315 |
3.32e-48 |
|
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar proteins; D-erythrose-4-phosphate dehydrogenase (E4PDH; EC 1.2.1.72), also called E4P dehydrogenase, catalyzes the NAD-dependent conversion of D-erythrose 4-phosphate (E4P) to 4-phosphoerythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose. This enzyme activity appears to have evolved from glyceraldehyde-3-phosphate dehydrogenase (GADPH), whose substrate differs only in the lack of one carbon relative to E4P. E4PDH proteins contain an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal GADPH-like catalytic domain and are members of the GAPDH superfamily of proteins.
Pssm-ID: 467686 Cd Length: 165 Bit Score: 159.50 E-value: 3.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 150 CTTNCLAPLAKVINDNFGIVEGLMTTVHATTATQKTVDGpSHKDWRGGRGASQNIIPSSTGAAKAVGVVLPELKGKLTGM 229
Cdd:cd23937 1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 230 AFRVPTPNVSVVDLTVRLEKAATYEEIKKAIKDAAEGSMKGVLGYVEDDVVSTDFNGEVLTSVFDAKAGIALNDNFVKLV 309
Cdd:cd23937 80 AVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLL 159
|
....*.
gi 491070598 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 ... |
3-154 |
6.64e-20 |
|
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: 83.56 E-value: 6.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 3 IKVGINGFGRIGRIVFRAAQERSDIEIVAINDLLDaeymaymlkydsthgrfngtvevkdghlvvngktirvtaekdpan 82
Cdd:cd05192 1 IRVAINGFGRIGRIVFRAIADQDDLDVVAINDRRD--------------------------------------------- 35
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491070598 83 lkwnevgvdVVAEATGIFLTDETARKHITAGAKKVVLTGPSKDATPMFVRG-ANFDKYAGQDIVSNASCTTNC 154
Cdd:cd05192 36 ---------VVIECTGSFTDDDNAEKHIKAGGKKAVITAPEKGDIPTIVVVlNELAKSAGATVVSNANETSYS 99
|
|
| PRK04207 |
PRK04207 |
type II glyceraldehyde-3-phosphate dehydrogenase; |
3-261 |
1.08e-05 |
|
type II glyceraldehyde-3-phosphate dehydrogenase;
Pssm-ID: 179786 [Multi-domain] Cd Length: 341 Bit Score: 46.36 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 3 IKVGINGFGRIGRIVFRAAQERSDIEIVAINDLlDAEYMAYMLK------Y---DSTHGRFngtvevKDGHLVVNGkTIR 73
Cdd:PRK04207 2 IKVGVNGYGTIGKRVADAVAAQPDMELVGVAKT-KPDYEARVAVekgyplYvadPEREKAF------EEAGIPVAG-TIE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 74 VTAEKdpanlkwnevgVDVVAEAT--GI-----FLTDETARKHITAGAKKVVLTGPSkdatpmFVRGANFDKYAGQDIVS 146
Cdd:PRK04207 74 DLLEK-----------ADIVVDATpgGVgaknkELYEKAGVKAIFQGGEKAEVAGVS------FNALANYEEALGKDYVR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491070598 147 NASCTTNCLAPLAKVINDNFGIVEglmttVHATTATQKTVDGPSHkdwrggRGASQNIIPSSTGA----AKAVGVVLPEL 222
Cdd:PRK04207 137 VVSCNTTGLCRTLCALDRAFGVKK-----VRATLVRRAADPKEVK------RGPINAIVPDPVTVpshhGPDVKTVLPDL 205
|
250 260 270
....*....|....*....|....*....|....*....
gi 491070598 223 kgKLTGMAFRVPTPNVSVVDLTVRLEKAATYEEIKKAIK 261
Cdd:PRK04207 206 --DITTMAVKVPTTLMHMHSVNVELKKPVTKEEVLEALE 242
|
|
| MviM |
COG0673 |
Predicted dehydrogenase [General function prediction only]; |
1-35 |
2.43e-03 |
|
Predicted dehydrogenase [General function prediction only];
Pssm-ID: 440437 [Multi-domain] Cd Length: 295 Bit Score: 39.14 E-value: 2.43e-03
10 20 30
....*....|....*....|....*....|....*
gi 491070598 1 MTIKVGINGFGRIGRIVFRAAQERSDIEIVAINDL 35
Cdd:COG0673 2 DKLRVGIIGAGGIGRAHAPALAALPGVELVAVADR 36
|
|
| meso-DAPDH_N |
cd02270 |
N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and ... |
3-32 |
3.85e-03 |
|
N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and similar proteins; Meso-DAPDH (EC 1.4.1.16), also called diaminopimelate dehydrogenase, or meso-DAP dehydrogenase, probably plays a role in lysine biosynthesis. It catalyzes the reversible NADP(H)-dependent reductive amination of L-2-amino-6-oxopimelate, the acyclic form of L-tetrahydrodipicolinate, to generate the meso compound, D,L-2,6-diaminopimelate. DAPDH is a homodimer which is highly specific for meso-DAP and NADP(+) as substrates. Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.
Pssm-ID: 467610 [Multi-domain] Cd Length: 151 Bit Score: 37.17 E-value: 3.85e-03
10 20 30
....*....|....*....|....*....|
gi 491070598 3 IKVGINGFGRIGRIVFRAAQERSDIEIVAI 32
Cdd:cd02270 1 IRVAIVGYGNLGRGVEEAIQANPDMELVGV 30
|
|
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