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Conserved domains on  [gi|506351262|ref|WP_015870981|]
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glyceraldehyde-3-phosphate dehydrogenase [Edwardsiella ictaluri]

Protein Classification

type I glyceraldehyde-3-phosphate dehydrogenase( domain architecture ID 11414602)

type I glyceraldehyde-3-phosphate dehydrogenase catalyzes the NAD-dependent oxidative phosphorylation of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate

Graphical summary

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List of domain hits

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: 614.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262   1 MTIKVGINGFGRIGRIVFRAAQER-SDIEIVGINDLLDANYMAYMLKYDSTHGRFNGTVEVEEGHLIVNGKKIRVTAERD 79
Cdd:COG0057    1 MTIRVAINGFGRIGRLVLRALLERgPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262  80 PANLKWNEIGVDVVAEATGLFLTDETARKHIAAGAKKVVMTGPSKDATPMFVMGVNHKNY-AGQAIVSNASCTTNCLAPL 158
Cdd:COG0057   81 PAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDDPTIVYGVNHDDYdADHRIISNASCTTNCLAPV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 159 AKVLNDNFGIVEALMTTVHATTATQKTVDGPsMKDWRGGRGASQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNV 238
Cdd:COG0057  161 AKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 239 SVVDLTARLAKPATYQQICEVMKAASEGEMKGVLGYTDEAVVSTDFNGEVCTSVFDADAGISLNDNFVKLVSWYDNETGY 318
Cdd:COG0057  240 SLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGY 319
                        330
                 ....*....|...
gi 506351262 319 SNKVLDLIAHISK 331
Cdd:COG0057  320 SNRMVDLAEYMAK 332
 
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: 614.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262   1 MTIKVGINGFGRIGRIVFRAAQER-SDIEIVGINDLLDANYMAYMLKYDSTHGRFNGTVEVEEGHLIVNGKKIRVTAERD 79
Cdd:COG0057    1 MTIRVAINGFGRIGRLVLRALLERgPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262  80 PANLKWNEIGVDVVAEATGLFLTDETARKHIAAGAKKVVMTGPSKDATPMFVMGVNHKNY-AGQAIVSNASCTTNCLAPL 158
Cdd:COG0057   81 PAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDDPTIVYGVNHDDYdADHRIISNASCTTNCLAPV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 159 AKVLNDNFGIVEALMTTVHATTATQKTVDGPsMKDWRGGRGASQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNV 238
Cdd:COG0057  161 AKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 239 SVVDLTARLAKPATYQQICEVMKAASEGEMKGVLGYTDEAVVSTDFNGEVCTSVFDADAGISLNDNFVKLVSWYDNETGY 318
Cdd:COG0057  240 SLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGY 319
                        330
                 ....*....|...
gi 506351262 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: 578.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262   1 MTIKVGINGFGRIGRIVFRAAQERSDIEIVGINDLLDANYMAYMLKYDSTHGRFNGTVEVEEGHLIVNGKKIRVTAERDP 80
Cdd:PRK15425   1 MTIKVGINGFGRIGRIVFRAAQKRSDIEIVAINDLLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262  81 ANLKWNEIGVDVVAEATGLFLTDETARKHIAAGAKKVVMTGPSKDATPMFVMGVNHKNYAGQAIVSNASCTTNCLAPLAK 160
Cdd:PRK15425  81 ANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDNTPMFVKGANFDKYAGQDIVSNASCTTNCLAPLAK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 161 VLNDNFGIVEALMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSV 240
Cdd:PRK15425 161 VINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 241 VDLTARLAKPATYQQICEVMKAASEGEMKGVLGYTDEAVVSTDFNGEVCTSVFDADAGISLNDNFVKLVSWYDNETGYSN 320
Cdd:PRK15425 241 VDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYSN 320
                        330
                 ....*....|.
gi 506351262 321 KVLDLIAHISK 331
Cdd:PRK15425 321 KVLDLIAHISK 331
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
4-324 3.64e-180

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: 501.04  E-value: 3.64e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262    4 KVGINGFGRIGRIVFRAAQER--SDIEIVGINDLLDANYMAYMLKYDSTHGRFNGTVEVEEGHLIVNGKK-IRVTAERDP 80
Cdd:TIGR01534   1 KVGINGFGRIGRLVLRRILEKpgNDLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEvISVFSERDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262   81 ANLKWNEIGVDVVAEATGLFLTDETARKHIAAGAKKVVMTGPSKDATPMFVMGVNHKNY-AGQAIVSNASCTTNCLAPLA 159
Cdd:TIGR01534  81 SDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDVKTIVYGVNHDEYdGEERIISNASCTTNCLAPLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262  160 KVLNDNFGIVEALMTTVHATTATQKTVDGPsMKDWRGGRGASQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVS 239
Cdd:TIGR01534 161 KVLDEAFGIVSGLMTTVHAYTNDQNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNVS 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262  240 VVDLTARLAKPATYQQICEVMKAASEGEMKGVLGYTDEAVVSTDFNGEVCTSVFDADAGI--SLNDNFVKLVSWYDNETG 317
Cdd:TIGR01534 240 LVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKvtGLGDSLVKVYAWYDNEWG 319

                  ....*..
gi 506351262  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 5.37e-118

C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (1.2.1.12), NADP (1.2.1.13) or either (1.2.1.59). The family corresponds to the ubiquitous NAD+ or NADP+ utilizing type I GAPDH and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose.


Pssm-ID: 467676  Cd Length: 165  Bit Score: 337.12  E-value: 5.37e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 150 CTTNCLAPLAKVLNDNFGIVEALMTTVHATTATQKTVDGPSmKDWRGGRGASQNIIPSSTGAAKAVGKVIPELNGKLTGM 229
Cdd:cd18126    1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 230 AFRVPTPNVSVVDLTARLAKPATYQQICEVMKAASEGEMKGVLGYTDEAVVSTDFNGEVCTSVFDADAGISLNDNFVKLV 309
Cdd:cd18126   80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159

                 ....*.
gi 506351262 310 SWYDNE 315
Cdd:cd18126  160 AWYDNE 165
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
5-325 1.24e-115

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 337.29  E-value: 1.24e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262   5 VGINGFGRIGRIVFRAAQERSDIEIVGINDLL-DANYMAYMLKYDSTHGRFNGTVEVEEGHLIVNGKKIRVTAERDPANL 83
Cdd:NF033735   1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAgDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262  84 KWNEiGVDVVAEATGLFLTDETARKHIAAGAKKVVMTGPSKDATPM-FVMGVNHKNYAGQA--IVSNASCTTNCLAPLAK 160
Cdd:NF033735  81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLnIVYGVNDHLYDPARhrIVTAASCTTNCLAPVVK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 161 VLNDNFGIVEALMTTVHATTATQKTVDGPSmKDWRGGRGASQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSV 240
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAPH-KDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 241 VDLTARLAKPATYQQICEVMKAASEGEMKGVLGYTDEAVVSTDFNGEVCTSVFDADAGISLNDNFVKLVSWYDNETGYSN 320
Cdd:NF033735 239 TDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYAN 318

                 ....*
gi 506351262 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 1.43e-88

Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. C-terminal domain is a mixed alpha/antiparallel beta fold.


Pssm-ID: 460700  Cd Length: 158  Bit Score: 262.14  E-value: 1.43e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262  155 LAPLAKVLNDNFGIVEALMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVP 234
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506351262  235 TPNVSVVDLTARLAKPATYQQICEVMKAASEGEMKGVLGYTDEAVVSTDFNGEVCTSVFDADAGISLNDNFVKLVSWY 312
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
3-150 1.24e-87

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: 259.41  E-value: 1.24e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262     3 IKVGINGFGRIGRIVFRAAQERSDIEIVGINDLLDANYMAYMLKYDSTHGRFNGTVEVEEGHLIVNGKKIRVTAERDPAN 82
Cdd:smart00846   1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPAN 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506351262    83 LKWNEIGVDVVAEATGLFLTDETARKHIAAGAKKVVMTGPSKDATPMFVMGVNHKNYAG-QAIVSNASC 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: 614.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262   1 MTIKVGINGFGRIGRIVFRAAQER-SDIEIVGINDLLDANYMAYMLKYDSTHGRFNGTVEVEEGHLIVNGKKIRVTAERD 79
Cdd:COG0057    1 MTIRVAINGFGRIGRLVLRALLERgPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262  80 PANLKWNEIGVDVVAEATGLFLTDETARKHIAAGAKKVVMTGPSKDATPMFVMGVNHKNY-AGQAIVSNASCTTNCLAPL 158
Cdd:COG0057   81 PAELPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDDPTIVYGVNHDDYdADHRIISNASCTTNCLAPV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 159 AKVLNDNFGIVEALMTTVHATTATQKTVDGPsMKDWRGGRGASQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNV 238
Cdd:COG0057  161 AKVLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 239 SVVDLTARLAKPATYQQICEVMKAASEGEMKGVLGYTDEAVVSTDFNGEVCTSVFDADAGISLNDNFVKLVSWYDNETGY 318
Cdd:COG0057  240 SLVDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGY 319
                        330
                 ....*....|...
gi 506351262 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: 578.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262   1 MTIKVGINGFGRIGRIVFRAAQERSDIEIVGINDLLDANYMAYMLKYDSTHGRFNGTVEVEEGHLIVNGKKIRVTAERDP 80
Cdd:PRK15425   1 MTIKVGINGFGRIGRIVFRAAQKRSDIEIVAINDLLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262  81 ANLKWNEIGVDVVAEATGLFLTDETARKHIAAGAKKVVMTGPSKDATPMFVMGVNHKNYAGQAIVSNASCTTNCLAPLAK 160
Cdd:PRK15425  81 ANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDNTPMFVKGANFDKYAGQDIVSNASCTTNCLAPLAK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 161 VLNDNFGIVEALMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSV 240
Cdd:PRK15425 161 VINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 241 VDLTARLAKPATYQQICEVMKAASEGEMKGVLGYTDEAVVSTDFNGEVCTSVFDADAGISLNDNFVKLVSWYDNETGYSN 320
Cdd:PRK15425 241 VDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYSN 320
                        330
                 ....*....|.
gi 506351262 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: 544.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262   3 IKVGINGFGRIGRIVFRAAQERSDIEIVGIND-LLDANYMAYMLKYDSTHGRFNGTVEV-EEGHLIVNGKKIRVTAERDP 80
Cdd:PLN02272  86 TKIGINGFGRIGRLVLRIATSRDDIEVVAVNDpFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDP 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262  81 ANLKWNEIGVDVVAEATGLFLTDETARKHIAAGAKKVVMTGPSKDAtPMFVMGVNHKNY-AGQAIVSNASCTTNCLAPLA 159
Cdd:PLN02272 166 AEIPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADA-PMFVVGVNEKTYkPNMNIVSNASCTTNCLAPLA 244
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 160 KVLNDNFGIVEALMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVS 239
Cdd:PLN02272 245 KVVHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVS 324
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 240 VVDLTARLAKPATYQQICEVMKAASEGEMKGVLGYTDEAVVSTDFNGEVCTSVFDADAGISLNDNFVKLVSWYDNETGYS 319
Cdd:PLN02272 325 VVDLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYS 404
                        330
                 ....*....|.
gi 506351262 320 NKVLDLIAHIS 330
Cdd:PLN02272 405 NRVLDLIEHMA 415
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
4-324 3.64e-180

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: 501.04  E-value: 3.64e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262    4 KVGINGFGRIGRIVFRAAQER--SDIEIVGINDLLDANYMAYMLKYDSTHGRFNGTVEVEEGHLIVNGKK-IRVTAERDP 80
Cdd:TIGR01534   1 KVGINGFGRIGRLVLRRILEKpgNDLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEvISVFSERDP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262   81 ANLKWNEIGVDVVAEATGLFLTDETARKHIAAGAKKVVMTGPSKDATPMFVMGVNHKNY-AGQAIVSNASCTTNCLAPLA 159
Cdd:TIGR01534  81 SDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSKGDVKTIVYGVNHDEYdGEERIISNASCTTNCLAPLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262  160 KVLNDNFGIVEALMTTVHATTATQKTVDGPsMKDWRGGRGASQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVS 239
Cdd:TIGR01534 161 KVLDEAFGIVSGLMTTVHAYTNDQNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNVS 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262  240 VVDLTARLAKPATYQQICEVMKAASEGEMKGVLGYTDEAVVSTDFNGEVCTSVFDADAGI--SLNDNFVKLVSWYDNETG 317
Cdd:TIGR01534 240 LVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKvtGLGDSLVKVYAWYDNEWG 319

                  ....*..
gi 506351262  318 YSNKVLD 324
Cdd:TIGR01534 320 YSNRLVD 326
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
1-331 2.95e-177

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 493.97  E-value: 2.95e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262   1 MTIKVGINGFGRIGRIVFRAAQERSDIEIVGIND-LLDANYMAYMLKYDSTHGRFNGTVEVEEGHLIVNGKKIRVTAERD 79
Cdd:PTZ00023   1 MVVKLGINGFGRIGRLVFRAALEREDVEVVAINDpFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262  80 PANLKWNEIGVDVVAEATGLFLTDETARKHIAAGAKKVVMTGPSKDATPMFVMGVNHKNY-AGQAIVSNASCTTNCLAPL 158
Cdd:PTZ00023  81 PAAIPWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPPKDDTPIYVMGVNHTQYdKSQRIVSNASCTTNCLAPL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 159 AKVLNDNFGIVEALMTTVHATTATQKTVDGPSM--KDWRGGRGASQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTP 236
Cdd:PTZ00023 161 AKVVNDKFGIVEGLMTTVHASTANQLTVDGPSKggKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 237 NVSVVDLTARLAKPATYQQICEVMKAASEGEMKGVLGYTDEAVVSTDFNGEVCTSVFDADAGISLNDNFVKLVSWYDNET 316
Cdd:PTZ00023 241 DVSVVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDNEW 320
                        330
                 ....*....|....*
gi 506351262 317 GYSNKVLDLIAHISK 331
Cdd:PTZ00023 321 GYSNRLLDLAHYITQ 335
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
1-331 1.32e-147

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 419.14  E-value: 1.32e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262   1 MTIKVGINGFGRIGRIVFRAAQERSDIEIVGINDLLDANYMAYMLKYDSTHGRFNGTVEVEEGHLIVNGKKIRVTAERDP 80
Cdd:PRK07729   1 MKTKVAINGFGRIGRMVFRKAIKESAFEIVAINASYPSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262  81 ANLKWNEIGVDVVAEATGLFLTDETARKHIAAGAKKVVMTGPSKDATPMFVMGVNHKNYAGQ--AIVSNASCTTNCLAPL 158
Cdd:PRK07729  81 KELPWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVTIVVGVNEDQLDIEkhTIISNASCTTNCLAPV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 159 AKVLNDNFGIVEALMTTVHATTATQKTVDGPSmKDWRGGRGASQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNV 238
Cdd:PRK07729 161 VKVLDEQFGIENGLMTTVHAYTNDQKNIDNPH-KDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 239 SVVDLTARLAKPATYQQICEVMKAASEGEMKGVLGYTDEAVVSTDFNGEVCTSVFDADAGISLNDNFVKLVSWYDNETGY 318
Cdd:PRK07729 240 SLVDLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEWGY 319
                        330
                 ....*....|...
gi 506351262 319 SNKVLDLIAHISK 331
Cdd:PRK07729 320 SCRVVDLVTLVAD 332
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
3-331 1.90e-142

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 406.03  E-value: 1.90e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262   3 IKVGINGFGRIGRIVFRAAQERSDIEIVGIND-LLDANYMAYMLKYDSTHGRF--NGTVEVEEGHLIVNGKKIRVTAERD 79
Cdd:PLN02358   6 IRIGINGFGRIGRLVARVVLQRDDVELVAVNDpFITTEYMTYMFKYDSVHGQWkhHELKVKDDKTLLFGEKPVTVFGIRN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262  80 PANLKWNEIGVDVVAEATGLFLTDETARKHIAAGAKKVVMTGPSKDAtPMFVMGVNHKNYAGQA-IVSNASCTTNCLAPL 158
Cdd:PLN02358  86 PEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDA-PMFVVGVNEHEYKSDLdIVSNASCTTNCLAPL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 159 AKVLNDNFGIVEALMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNV 238
Cdd:PLN02358 165 AKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDV 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 239 SVVDLTARLAKPATYQQICEVMKAASEGEMKGVLGYTDEAVVSTDFNGEVCTSVFDADAGISLNDNFVKLVSWYDNETGY 318
Cdd:PLN02358 245 SVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEWGY 324
                        330
                 ....*....|...
gi 506351262 319 SNKVLDLIAHISK 331
Cdd:PLN02358 325 SSRVVDLIVHMSK 337
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
1-330 3.34e-134

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 385.95  E-value: 3.34e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262   1 MTIKVGINGFGRIGRIVFRAAQER----SDIEIVGINDL-LDANYMAYMLKYDSTHGRFNGTVEVEEGH--------LIV 67
Cdd:PTZ00434   2 APIKVGINGFGRIGRMVFQAICDQgligTEIDVVAVVDMsTNAEYFAYQMKYDTVHGRPKYTVETTKSSpsvktddvLVV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262  68 NGKKIR-VTAERDPANLKWNEIGVDVVAEATGLFLTDETARKHIAAGAKKVVMTGPSKDATPMFVMGVNHKNYAGQA--I 144
Cdd:PTZ00434  82 NGHRIKcVKAQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPASGGAKTIVMGVNQHEYSPTEhhV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 145 VSNASCTTNCLAPLAKVL-NDNFGIVEALMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVIPELN 223
Cdd:PTZ00434 162 VSNASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTK 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 224 GKLTGMAFRVPTPNVSVVDLTARLAKPATYQQICEVMKAASEGEMKGVLGYTDEAVVSTDFNGEVCTSVFDADAGISLN- 302
Cdd:PTZ00434 242 GKLTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKATLQNNl 321
                        330       340       350
                 ....*....|....*....|....*....|.
gi 506351262 303 ---DNFVKLVSWYDNETGYSNKVLDLIAHIS 330
Cdd:PTZ00434 322 pgeRRFFKIVSWYDNEWGYSHRVVDLVRYMA 352
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
2-325 5.01e-127

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 366.92  E-value: 5.01e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262   2 TIKVGINGFGRIGRIVFRA--AQERSDIEIVGINDLLDANYMAYMLKYDSTHGRFNGTVEVEEGHLIVNGKKIRVTAERD 79
Cdd:PRK07403   1 MIRVAINGFGRIGRNFLRCwlGRENSQLELVAINDTSDPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDRN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262  80 PANLKWNEIGVDVVAEATGLFLTDETARKHIAAGAKKVVMTGPSKDATP-MFVMGVNHKNYAGQ--AIVSNASCTTNCLA 156
Cdd:PRK07403  81 PLNLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPGKGEDIgTYVVGVNHHEYDHEdhNIISNASCTTNCLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 157 PLAKVLNDNFGIVEALMTTVHATTATQKTVDGpSMKDWRGGRGASQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTP 236
Cdd:PRK07403 161 PIAKVLHDNFGIIKGTMTTTHSYTGDQRILDA-SHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTP 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 237 NVSVVDLTARLAKPATYQQICEVMKAASEGEMKGVLGYTDEAVVSTDFNGEVCTSVFDADAGISLNDNFVKLVSWYDNET 316
Cdd:PRK07403 240 NVSVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYDNEW 319

                 ....*....
gi 506351262 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 5.37e-118

C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar proteins; Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. It has been implicated in varied activities including regulating mRNA stability, the regulation of gene expression, induction of apoptosis, intracellular membrane trafficking, iron uptake and transport (via secreted GAPDH), heme metabolism, the maintenance of genomic integrity, and nuclear tRNA export. GAPDH proteins contains an N-terminal NAD(P)-binding domain and a C-terminal catalytic domain. The primarily N-terminal NAD(P)-binding domain contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft. Phosphatidyl-serine, RNA, and glutathione binding sites have been identified in the N-terminus. Different forms of GAPDH exist which utilize NAD (1.2.1.12), NADP (1.2.1.13) or either (1.2.1.59). The family corresponds to the ubiquitous NAD+ or NADP+ utilizing type I GAPDH and a small clade of dehydrogenases, called erythrose-4-phosphate dehydrogenase (E4PDH) proteins, which utilize NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose.


Pssm-ID: 467676  Cd Length: 165  Bit Score: 337.12  E-value: 5.37e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 150 CTTNCLAPLAKVLNDNFGIVEALMTTVHATTATQKTVDGPSmKDWRGGRGASQNIIPSSTGAAKAVGKVIPELNGKLTGM 229
Cdd:cd18126    1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 230 AFRVPTPNVSVVDLTARLAKPATYQQICEVMKAASEGEMKGVLGYTDEAVVSTDFNGEVCTSVFDADAGISLNDNFVKLV 309
Cdd:cd18126   80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159

                 ....*.
gi 506351262 310 SWYDNE 315
Cdd:cd18126  160 AWYDNE 165
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
5-325 1.24e-115

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 337.29  E-value: 1.24e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262   5 VGINGFGRIGRIVFRAAQERSDIEIVGINDLL-DANYMAYMLKYDSTHGRFNGTVEVEEGHLIVNGKKIRVTAERDPANL 83
Cdd:NF033735   1 IGINGFGRIGRLALRALWGRPGLEIVHINDLAgDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262  84 KWNEiGVDVVAEATGLFLTDETARKHIAAGAKKVVMTGPSKDATPM-FVMGVNHKNYAGQA--IVSNASCTTNCLAPLAK 160
Cdd:NF033735  81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLnIVYGVNDHLYDPARhrIVTAASCTTNCLAPVVK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 161 VLNDNFGIVEALMTTVHATTATQKTVDGPSmKDWRGGRGASQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSV 240
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAPH-KDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 241 VDLTARLAKPATYQQICEVMKAASEGEMKGVLGYTDEAVVSTDFNGEVCTSVFDADAGISLNDNFVKLVSWYDNETGYSN 320
Cdd:NF033735 239 TDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYAN 318

                 ....*
gi 506351262 321 KVLDL 325
Cdd:NF033735 319 RMVDL 323
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
3-325 1.48e-110

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 326.89  E-value: 1.48e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262   3 IKVGINGFGRIGRIVFRAAQERSD--IEIVGINDLLDANYMAYMLKYDSTHGRFNGTVEVE-EGHLIVNGKKIRVTAERD 79
Cdd:PLN03096  61 IKVAINGFGRIGRNFLRCWHGRKDspLDVVAINDTGGVKQASHLLKYDSTLGTFDADVKPVgDDAISVDGKVIKVVSDRN 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262  80 PANLKWNEIGVDVVAEATGLFLTDETARKHIAAGAKKVVMTGPSKDATPMFVMGVNHKNYA-GQAIVSNASCTTNCLAPL 158
Cdd:PLN03096 141 PLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKGDIPTYVVGVNADDYKhSDPIISNASCTTNCLAPF 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 159 AKVLNDNFGIVEALMTTVHATTATQKTVDGpSMKDWRGGRGASQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNV 238
Cdd:PLN03096 221 VKVLDQKFGIIKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNV 299
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 239 SVVDLTARLAKPATYQQICEVMKAASEGEMKGVLGYTDEAVVSTDFNGEVCTSVFDADAGISLNDNFVKLVSWYDNETGY 318
Cdd:PLN03096 300 SVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAWYDNEWGY 379

                 ....*..
gi 506351262 319 SNKVLDL 325
Cdd:PLN03096 380 SQRVVDL 386
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
3-329 4.31e-107

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 319.92  E-value: 4.31e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262   3 IKVGINGFGRIGRIVFRAAQERSD--IEIVGINDLLDANYMAYMLKYDSTHGRFNGTVEVEEGHLI-VNGKKIRVTAERD 79
Cdd:PLN02237  76 LKVAINGFGRIGRNFLRCWHGRKDspLDVVVVNDSGGVKNASHLLKYDSMLGTFKADVKIVDDETIsVDGKPIKVVSNRD 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262  80 PANLKWNEIGVDVVAEATGLFLTDETARKHIAAGAKKVVMTGPSKDA-TPMFVMGVNHKNYAGQA--IVSNASCTTNCLA 156
Cdd:PLN02237 156 PLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAKGAdIPTYVVGVNEDDYDHEVanIVSNASCTTNCLA 235
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 157 PLAKVLNDNFGIVEALMTTVHATTATQKTVDGpSMKDWRGGRGASQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTP 236
Cdd:PLN02237 236 PFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTP 314
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 237 NVSVVDLTARLAKPA-TYQQICEVMKAASEGEMKGVLGYTDEAVVSTDFNGEVCTSVFDADAGISLNDNFVKLVSWYDNE 315
Cdd:PLN02237 315 NVSVVDLVVNVEKKGiTAEDVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVAWYDNE 394
                        330
                 ....*....|....
gi 506351262 316 TGYSNKVLDLiAHI 329
Cdd:PLN02237 395 WGYSQRVVDL-AHL 407
PRK08955 PRK08955
glyceraldehyde-3-phosphate dehydrogenase; Validated
1-326 2.05e-106

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 169599 [Multi-domain]  Cd Length: 334  Bit Score: 314.36  E-value: 2.05e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262   1 MTIKVGINGFGRIGRIVFRAAQERSDIEIVGINDLL-DANYMAYMLKYDSTHGRFNGTVEVEEGHLIVNGKKIRVTAERD 79
Cdd:PRK08955   1 MTIKVGINGFGRIGRLALRAAWDWPELEFVQINDPAgDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262  80 PANLKWNeiGVDVVAEATGLFLTDETARKHIAAGAKKVVMTGPSKDATPM-FVMGVNHK--NYAGQAIVSNASCTTNCLA 156
Cdd:PRK08955  81 IADTDWS--GCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLnIVMGVNDHlfDPAIHPIVTAASCTTNCLA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 157 PLAKVLNDNFGIVEALMTTVHATTATQKTVDGPSmKDWRGGRGASQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTP 236
Cdd:PRK08955 159 PVVKVIHEKLGIKHGSMTTIHDLTNTQTILDAPH-KDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLA 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 237 NVSVVDLTARLAKPATYQQICEVMKAASEGEMKGVLGYTDEAVVSTDFNGEVCTSVFDADAGISLNDNFVKLVSWYDNET 316
Cdd:PRK08955 238 NASLTDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNEW 317
                        330
                 ....*....|
gi 506351262 317 GYSNKVLDLI 326
Cdd:PRK08955 318 GYANRTAELA 327
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
2-324 8.22e-102

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 302.75  E-value: 8.22e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262   2 TIKVGINGFGRIGRIVFRAAQE---RSDIEIVGINDLLDANYMAYMLKYDSTHGRFNGTVEVEEGHLIVNGKKIRVTAER 78
Cdd:PRK13535   1 TIRVAINGFGRIGRNVLRALYEsgrRAEITVVAINELADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262  79 DPANLKWNEIGVDVVAEATGLFLTDETARKHIAAGAKKVVMTGPSK---DATpmFVMGVNHKNY-AGQAIVSNASCTTNC 154
Cdd:PRK13535  81 DIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSndlDAT--VVYGVNHDQLrAEHRIVSNASCTTNC 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 155 LAPLAKVLNDNFGIVEALMTTVHATTATQKTVDGpSMKDWRGGRGASQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVP 234
Cdd:PRK13535 159 IIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVP 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 235 TPNVSVVDLTARLAKPATYQQICEVMKAASEGEMKGVLGYTDEAVVSTDFNGEVCTSVFDADAGISLNDNFVKLVSWYDN 314
Cdd:PRK13535 238 TINVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDN 317
                        330
                 ....*....|
gi 506351262 315 ETGYSNKVLD 324
Cdd:PRK13535 318 EWGFANRMLD 327
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
3-149 2.70e-93

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: 274.27  E-value: 2.70e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262   3 IKVGINGFGRIGRIVFRAAQERSDIEIVGINDLLDANYMAYMLKYDSTHGRFNGTVEVEEGHLIVNGKKIRVTAERDPAN 82
Cdd:cd05214    1 IKVGINGFGRIGRLVFRAALERDDIEVVAINDLTDDETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAE 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506351262  83 LKWNEIGVDVVAEATGLFLTDETARKHIAAGAKKVVMTGPSKDATPMFVMGVNHKNY-AGQAIVSNAS 149
Cdd:cd05214   81 LPWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDDDPTIVMGVNHDKYdADDKIISNAS 148
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
155-312 1.43e-88

Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. C-terminal domain is a mixed alpha/antiparallel beta fold.


Pssm-ID: 460700  Cd Length: 158  Bit Score: 262.14  E-value: 1.43e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262  155 LAPLAKVLNDNFGIVEALMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVP 234
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 506351262  235 TPNVSVVDLTARLAKPATYQQICEVMKAASEGEMKGVLGYTDEAVVSTDFNGEVCTSVFDADAGISLNDNFVKLVSWY 312
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
3-150 1.24e-87

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: 259.41  E-value: 1.24e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262     3 IKVGINGFGRIGRIVFRAAQERSDIEIVGINDLLDANYMAYMLKYDSTHGRFNGTVEVEEGHLIVNGKKIRVTAERDPAN 82
Cdd:smart00846   1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPAN 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 506351262    83 LKWNEIGVDVVAEATGLFLTDETARKHIAAGAKKVVMTGPSKDATPMFVMGVNHKNYAG-QAIVSNASC 150
Cdd:smart00846  81 LPWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDADPTFVYGVNHDEYDGeDHIISNASC 149
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
150-315 1.28e-86

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: 257.55  E-value: 1.28e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 150 CTTNCLAPLAKVLNDNFGIVEALMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVIPELNGKLTGM 229
Cdd:cd18123    1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 230 AFRVPTPNVSVVDLTARLAKPATYQQICEVMKAASEGemKGVLGYTDEAVVSTDFNGEVCTSVFDADAGISLNDNFVKLV 309
Cdd:cd18123   81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLM 158

                 ....*.
gi 506351262 310 SWYDNE 315
Cdd:cd18123  159 QWYDNE 164
PRK08289 PRK08289
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
9-331 1.00e-80

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 236219 [Multi-domain]  Cd Length: 477  Bit Score: 253.31  E-value: 1.00e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262   9 GFGRIGRIVFRAAQERSDIE-------IV----GINDLLDanyMAYMLKYDSTHGRFNGTVEVEEGH--LIVNGKKIRVT 75
Cdd:PRK08289 134 GFGRIGRLLARLLIEKTGGGnglrlraIVvrkgSEGDLEK---RASLLRRDSVHGPFNGTITVDEENnaIIANGNYIQVI 210
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262  76 AERDPANLKWNEIGVD--VVAEATGLFLTDETARKHIAA-GAKKVVMTGPSKDATPMFVMGVNHKNYAGQ-AIVSNASCT 151
Cdd:PRK08289 211 YANSPEEVDYTAYGINnaLVVDNTGKWRDEEGLSQHLKSkGVAKVLLTAPGKGDIKNIVHGVNHSDITDEdKIVSAASCT 290
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 152 TNCLAPLAKVLNDNFGIVEALMTTVHATTATQKTVDGPSMKDwRGGRGASQNIIPSSTGAAKAVGKVIPELNGKLTGMAF 231
Cdd:PRK08289 291 TNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKGD-RRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNAI 369
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 232 RVPTPNVSVVDLTARLAKPATYQQICEVMKAAS-EGEMKGVLGYTDEA-VVSTDFNGEVCTSVFDADAGISLNDNFVkLV 309
Cdd:PRK08289 370 RVPTPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQIDYTDSTeVVSSDFVGSRHAGVVDSQATIVNGNRAV-LY 448
                        330       340
                 ....*....|....*....|..
gi 506351262 310 SWYDNETGYSNKVLDLIAHISK 331
Cdd:PRK08289 449 VWYDNEFGYSCQVVRVMEQMAG 470
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
3-102 4.52e-61

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: 190.01  E-value: 4.52e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262    3 IKVGINGFGRIGRIVFRAAQERSDIEIVGINDLLDANYMAYMLKYDSTHGRFNGTVEVEEGHLIVNGKKIRVTAERDPAN 82
Cdd:pfam00044   1 VKVGINGFGRIGRLVLRAALERPDIEVVAINDLTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAE 80
                          90       100
                  ....*....|....*....|
gi 506351262   83 LKWNEIGVDVVAEATGLFLT 102
Cdd:pfam00044  81 LPWGDLGVDVVIESTGVFTT 100
GAPDH_N_E4PDH cd17892
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
3-149 2.24e-55

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: 177.84  E-value: 2.24e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262   3 IKVGINGFGRIGRIVFRAAQE---RSDIEIVGINDLLDANYMAYMLKYDSTHGRFNGTVEVEEGHLIVNGKKIRVTAERD 79
Cdd:cd17892    1 YRVAINGYGRIGRNVLRALYEsgrRAEFQVVAINELADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPD 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506351262  80 PANLKWNEIGVDVVAEATGLFLTDETARKHIAAGAKKVVMTGPSK---DATpmFVMGVNHKNYAGQA-IVSNAS 149
Cdd:cd17892   81 PENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASndvDAT--IVYGINQDLLRAEHrIVSNAS 152
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
1-326 3.67e-54

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 180.46  E-value: 3.67e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262   1 MTIKVGINGFGRIGRIVFRAAQERSDIEIVGINDL-LDANYMAYMLKYDSTHGRFNGT-VEVEEGHLIVNG-KKIRVTAE 77
Cdd:PTZ00353   1 LPITVGINGFGPVGKAVLFASLTDPLVTVVAVNDAsVSIAYIAYVLEQESPLSAPDGAsIRVVGEQIVLNGtQKIRVSAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262  78 RDPANLKWNEIGVDVVAEATGLFLTDETARKHIAAGAKKVVMTGPSKDAtPMFVMGVNHKNY-AGQAIVSNASCTTNCLA 156
Cdd:PTZ00353  81 HDLVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSADA-PTVMAGSNDERLsASLPVCCAGAPIAVALA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 157 PLAKVLNDNFGIVEALMTTVHATTAtQKTVDGPSM--KDWRGGRGASQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVP 234
Cdd:PTZ00353 160 PVIRALHEVYGVEECSYTAIHGMQP-QEPIAARSKnsQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVP 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 235 TPNVSVVDLTARLAKPATYQQICEVMKAASEGEMKGVLGYTDEAVVSTDF--NGEVCtsvFDADAGISLNDNFV-KLVSW 311
Cdd:PTZ00353 239 VKKGCAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCipNGKLC---YDATSSSSSREGEVhKMVLW 315
                        330
                 ....*....|....*
gi 506351262 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 3.28e-51

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: 167.31  E-value: 3.28e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 150 CTTNCLAPLAKVLNDNFGIVEALMTTVHATTATQKTVDGPSMKDWrgGRGASQNIIPSSTGAAKAVGKVIPELN--GKLT 227
Cdd:cd18122    1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIGkpIKVD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 228 GMAFRVPTPNVSVVDLTARLAKPATYQQICEVMKAASEGEMKGVLGYTDEAVVSTDFNGEVCTSVFDADAGISLNDNFVK 307
Cdd:cd18122   79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLK 158

                 ....*...
gi 506351262 308 LVSWYDNE 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 3.62e-45

C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar proteins; D-erythrose-4-phosphate dehydrogenase (E4PDH; EC 1.2.1.72), also called E4P dehydrogenase, catalyzes the NAD-dependent conversion of D-erythrose 4-phosphate (E4P) to 4-phosphoerythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose. This enzyme activity appears to have evolved from glyceraldehyde-3-phosphate dehydrogenase (GADPH), whose substrate differs only in the lack of one carbon relative to E4P. E4PDH proteins contain an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal GADPH-like catalytic domain and are members of the GAPDH superfamily of proteins.


Pssm-ID: 467686  Cd Length: 165  Bit Score: 151.41  E-value: 3.62e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 150 CTTNCLAPLAKVLNDNFGIVEALMTTVHATTATQKTVDGpSMKDWRGGRGASQNIIPSSTGAAKAVGKVIPELNGKLTGM 229
Cdd:cd23937    1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262 230 AFRVPTPNVSVVDLTARLAKPATYQQICEVMKAASEGEMKGVLGYTDEAVVSTDFNGEVCTSVFDADAGISLNDNFVKLV 309
Cdd:cd23937   80 AVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLL 159

                 ....*.
gi 506351262 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 1.31e-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: 85.10  E-value: 1.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506351262   3 IKVGINGFGRIGRIVFRAAQERSDIEIVGINDLLdanymaymlkydsthgrfngtveveeghlivngkkirvtaerdpan 82
Cdd:cd05192    1 IRVAINGFGRIGRIVFRAIADQDDLDVVAINDRR---------------------------------------------- 34
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 506351262  83 lkwneigvDVVAEATGLFLTDETARKHIAAGAKKVVMTGPSKDATPMFVMGVNH-KNYAGQAIVSNASCTTNC 154
Cdd:cd05192   35 --------DVVIECTGSFTDDDNAEKHIKAGGKKAVITAPEKGDIPTIVVVLNElAKSAGATVVSNANETSYS 99
meso-DAPDH_N cd02270
N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and ...
3-32 9.82e-04

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: 39.09  E-value: 9.82e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 506351262   3 IKVGINGFGRIGRIVFRAAQERSDIEIVGI 32
Cdd:cd02270    1 IRVAIVGYGNLGRGVEEAIQANPDMELVGV 30
PRK04207 PRK04207
type II glyceraldehyde-3-phosphate dehydrogenase;
3-46 2.07e-03

type II glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 179786 [Multi-domain]  Cd Length: 341  Bit Score: 39.43  E-value: 2.07e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 506351262   3 IKVGINGFGRIGRIVFRAAQERSDIEIVGINDlLDANYMAYMLK 46
Cdd:PRK04207   2 IKVGVNGYGTIGKRVADAVAAQPDMELVGVAK-TKPDYEARVAV 44
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-35 4.43e-03

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 38.37  E-value: 4.43e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 506351262   1 MTIKVGINGFGRIGRIVFRAAQERSDIEIVGINDL 35
Cdd:COG0673    2 DKLRVGIIGAGGIGRAHAPALAALPGVELVAVADR 36
DHDPR_N cd02274
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; ...
3-31 7.87e-03

N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; DHDPR (EC 1.17.1.8), also called 4-hydroxy-tetrahydrodipicolinate reductase, or HTPA reductase, is a product of an essential gene referred to as dapB. It catalyzes the NAD(P)H-dependent reduction of 2,3-dihydrodipicolinate (DHDP) to 2,3,4,5-tetrahydrodipicolinate (THDP). DHDPR could also function as a dehydratase in addition to the role of a nucleotide dependent reductase. DHDPR is a component of the biosynthetic pathway that generates meso-diaminopimelate, a component of bacterial cell walls, and the amino acid L-lysine in various bacteria, archaea, cyanobacteria and higher plants. The enzyme is a homotetramer where each monomer is composed of two domains, an N-terminal NAD(P)-binding domain which forms a Rossmann fold, and a C-terminal substrate-binding domain that forms an open, mixed alpha-beta sandwich.


Pssm-ID: 467611 [Multi-domain]  Cd Length: 139  Bit Score: 36.38  E-value: 7.87e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 506351262   3 IKVGINGF-GRIGRIVFRAAQERSDIEIVG 31
Cdd:cd02274    1 IKVAVAGAtGRMGRELVKAILEAPDLELVG 30
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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