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Conserved domains on  [gi|6226817|sp|O14556|]
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RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase, testis-specific; AltName: Full=Spermatogenic cell-specific glyceraldehyde 3-phosphate dehydrogenase 2; Short=GAPDH-2; AltName: Full=Spermatogenic glyceraldehyde-3-phosphate dehydrogenase

Protein Classification

type I glyceraldehyde-3-phosphate dehydrogenase( domain architecture ID 1000016)

type I glyceraldehyde-3-phosphate dehydrogenase is responsible for the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02272 super family cl30355
glyceraldehyde-3-phosphate dehydrogenase
 78-403 0e+00

glyceraldehyde-3-phosphate dehydrogenase


The actual alignment was detected with superfamily member PLN02272:

Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 554.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817    78 VGINGFGRIGRLVLR-ACMEKGVKVVAVNDPFIDPEYMVYMFKYDSTHGRYKGSVE-FRNGQLVVDNHEISVYQCKEPKQ 155
Cdd:PLN02272  88 IGINGFGRIGRLVLRiATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINvVDDSTLEINGKQIKVTSKRDPAE 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   156 IPWRAVGSPYVVESTGVYLSIQAASDHISAGAQRVVISAPSPDAPMFVMGVNENDYNPgSMNIVSNASCTTNCLAPLAKV 235
Cdd:PLN02272 168 IPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKP-NMNIVSNASCTTNCLAPLAKV 246

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   236 IHERFGIVEGLMTTVHSYTATQKTVDGPSRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKLTGMAFRVPTPDVSVV 315
Cdd:PLN02272 247 VHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVV 326

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   316 DLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLGDTHSSIFDAKAGIALNDNFVKLISWYDNEYGYSHR 395
Cdd:PLN02272 327 DLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYSNR 406


                 ....*...
gi 6226817   396 VVDLLRYM 403
Cdd:PLN02272 407 VLDLIEHM 414
 
Name Accession Description Interval E-value
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 78-403 0e+00

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 554.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817    78 VGINGFGRIGRLVLR-ACMEKGVKVVAVNDPFIDPEYMVYMFKYDSTHGRYKGSVE-FRNGQLVVDNHEISVYQCKEPKQ 155
Cdd:PLN02272  88 IGINGFGRIGRLVLRiATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINvVDDSTLEINGKQIKVTSKRDPAE 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   156 IPWRAVGSPYVVESTGVYLSIQAASDHISAGAQRVVISAPSPDAPMFVMGVNENDYNPgSMNIVSNASCTTNCLAPLAKV 235
Cdd:PLN02272 168 IPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKP-NMNIVSNASCTTNCLAPLAKV 246

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   236 IHERFGIVEGLMTTVHSYTATQKTVDGPSRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKLTGMAFRVPTPDVSVV 315
Cdd:PLN02272 247 VHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVV 326

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   316 DLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLGDTHSSIFDAKAGIALNDNFVKLISWYDNEYGYSHR 395
Cdd:PLN02272 327 DLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYSNR 406


                 ....*...
gi 6226817   396 VVDLLRYM 403
Cdd:PLN02272 407 VLDLIEHM 414
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 78-407 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: 553.85  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   78 VGINGFGRIGRLVLRACMEKG--VKVVAVNDPfIDPEYMVYMFKYDSTHGRYKGSVEFRNGQLVVDNHEISVYQCKEPKQ 155
Cdd:COG0057   5 VAINGFGRIGRLVLRALLERGpdIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAE 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817  156 IPWRAVGSPYVVESTGVYLSIQAASDHISAGAQRVVISAPSPDA-PMFVMGVNENDYNPgSMNIVSNASCTTNCLAPLAK 234
Cdd:COG0057  84 LPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDA-DHRIISNASCTTNCLAPVAK 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817  235 VIHERFGIVEGLMTTVHSYTATQKTVDGPsRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKLTGMAFRVPTPDVSV 314
Cdd:COG0057 163 VLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSL 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817  315 VDLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLGDTHSSIFDAKAGIALNDNFVKLISWYDNEYGYSH 394
Cdd:COG0057 242 VDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGYSN 321

                       330
                ....*....|...
gi 6226817  395 RVVDLLRYMFSRD 407
Cdd:COG0057 322 RMVDLAEYMAKLL 334
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 77-398 1.60e-166

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: 469.45  E-value: 1.60e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817     77 TVGINGFGRIGRLVLRACMEKG---VKVVAVNDPfIDPEYMVYMFKYDSTHGRYKGSVEFRNGQLVVDNHE-ISVYQCKE 152
Cdd:TIGR01534   1 KVGINGFGRIGRLVLRRILEKPgndLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEvISVFSERD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817    153 PKQIPWRAVGSPYVVESTGVYLSIQAASDHISAGAQRVVISAPS-PDAPMFVMGVNENDYNPGSmNIVSNASCTTNCLAP 231
Cdd:TIGR01534  80 PSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSkGDVKTIVYGVNHDEYDGEE-RIISNASCTTNCLAP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817    232 LAKVIHERFGIVEGLMTTVHSYTATQKTVDGPsRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKLTGMAFRVPTPD 311
Cdd:TIGR01534 159 LAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPN 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817    312 VSVVDLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLGDTHSSIFDAKAGIA--LNDNFVKLISWYDNE 389
Cdd:TIGR01534 238 VSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNE 317


                  ....*....
gi 6226817    390 YGYSHRVVD 398
Cdd:TIGR01534 318 WGYSNRLVD 326
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 224-389 4.57e-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: 342.90  E-value: 4.57e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817  224 CTTNCLAPLAKVIHERFGIVEGLMTTVHSYTATQKTVDGPSRKaWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKLTGM 303
Cdd:cd18126   1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHKD-LRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817  304 AFRVPTPDVSVVDLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLGDTHSSIFDAKAGIALNDNFVKLI 383
Cdd:cd18126  80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159


                ....*.
gi 6226817  384 SWYDNE 389
Cdd:cd18126 160 AWYDNE 165
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
78-399 2.51e-111

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 329.20  E-value: 2.51e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817    78 VGINGFGRIGRLVLRACMEK-GVKVVAVNDPFIDPEYMVYMFKYDSTHGRYKGSVEFRNGQLVVDNHEISVYQCKEPKQI 156
Cdd:NF033735   1 IGINGFGRIGRLALRALWGRpGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   157 PWRAvGSPYVVESTGVYLSIQAASDHISAGAQRVVISAP--SPDAPMFVMGVNENDYNPGSMNIVSNASCTTNCLAPLAK 234
Cdd:NF033735  81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARHRIVTAASCTTNCLAPVVK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   235 VIHERFGIVEGLMTTVHSYTATQKTVDGPsRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKLTGMAFRVPTPDVSV 314
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   315 VDLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLGDTHSSIFDAKAGIALNDNFVKLISWYDNEYGYSH 394
Cdd:NF033735 239 TDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYAN 318


                 ....*
gi 6226817   395 RVVDL 399
Cdd:NF033735 319 RMVDL 323
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 229-386 1.45e-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: 265.23  E-value: 1.45e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817    229 LAPLAKVIHERFGIVEGLMTTVHSYTATQKTVDGPSRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKLTGMAFRVP 308
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6226817    309 TPDVSVVDLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLGDTHSSIFDAKAGIALNDNFVKLISWY 386
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 78-224 1.75e-68

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: 213.18  E-value: 1.75e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817      78 VGINGFGRIGRLVLRACME-KGVKVVAVNDPfIDPEYMVYMFKYDSTHGRYKGSVEFRNGQLVVDNHEISVYQCKEPKQI 156
Cdd:smart00846   3 VGINGFGRIGRLVLRAALErPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANL 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6226817     157 PWRAVGSPYVVESTGVYLSIQAASDHISAGAQRVVISAPSPDA-PMFVMGVNENDYNPgSMNIVSNASC 224
Cdd:smart00846  82 PWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDG-EDHIISNASC 149
 
Name Accession Description Interval E-value
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 78-403 0e+00

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 554.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817    78 VGINGFGRIGRLVLR-ACMEKGVKVVAVNDPFIDPEYMVYMFKYDSTHGRYKGSVE-FRNGQLVVDNHEISVYQCKEPKQ 155
Cdd:PLN02272  88 IGINGFGRIGRLVLRiATSRDDIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINvVDDSTLEINGKQIKVTSKRDPAE 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   156 IPWRAVGSPYVVESTGVYLSIQAASDHISAGAQRVVISAPSPDAPMFVMGVNENDYNPgSMNIVSNASCTTNCLAPLAKV 235
Cdd:PLN02272 168 IPWGDFGAEYVVESSGVFTTVEKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKP-NMNIVSNASCTTNCLAPLAKV 246

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   236 IHERFGIVEGLMTTVHSYTATQKTVDGPSRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKLTGMAFRVPTPDVSVV 315
Cdd:PLN02272 247 VHEEFGILEGLMTTVHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVV 326

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   316 DLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLGDTHSSIFDAKAGIALNDNFVKLISWYDNEYGYSHR 395
Cdd:PLN02272 327 DLTCRLEKSASYEDVKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYSNR 406


                 ....*...
gi 6226817   396 VVDLLRYM 403
Cdd:PLN02272 407 VLDLIEHM 414
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 78-407 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: 553.85  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   78 VGINGFGRIGRLVLRACMEKG--VKVVAVNDPfIDPEYMVYMFKYDSTHGRYKGSVEFRNGQLVVDNHEISVYQCKEPKQ 155
Cdd:COG0057   5 VAINGFGRIGRLVLRALLERGpdIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAE 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817  156 IPWRAVGSPYVVESTGVYLSIQAASDHISAGAQRVVISAPSPDA-PMFVMGVNENDYNPgSMNIVSNASCTTNCLAPLAK 234
Cdd:COG0057  84 LPWGELGVDVVIECTGKFTDREKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDA-DHRIISNASCTTNCLAPVAK 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817  235 VIHERFGIVEGLMTTVHSYTATQKTVDGPsRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKLTGMAFRVPTPDVSV 314
Cdd:COG0057 163 VLNDAFGIEKGLMTTIHAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSL 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817  315 VDLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLGDTHSSIFDAKAGIALNDNFVKLISWYDNEYGYSH 394
Cdd:COG0057 242 VDLTVELEKETTVEEVNAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGYSN 321

                       330
                ....*....|...
gi 6226817  395 RVVDLLRYMFSRD 407
Cdd:COG0057 322 RMVDLAEYMAKLL 334
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
 78-407 1.86e-168

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 475.09  E-value: 1.86e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817    78 VGINGFGRIGRLVLRACMEKG-VKVVAVNDPFIDPEYMVYMFKYDSTHGRYKGSVEFRNGQLVVDNHEISVYQCKEPKQI 156
Cdd:PTZ00023   5 LGINGFGRIGRLVFRAALEREdVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKDPAAI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   157 PWRAVGSPYVVESTGVYLSIQAASDHISAGAQRVVISAP-SPDAPMFVMGVNENDYNPgSMNIVSNASCTTNCLAPLAKV 235
Cdd:PTZ00023  85 PWGKNGVDVVCESTGVFLTKEKAQAHLKGGAKKVIMSAPpKDDTPIYVMGVNHTQYDK-SQRIVSNASCTTNCLAPLAKV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   236 IHERFGIVEGLMTTVHSYTATQKTVDGPSR--KAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKLTGMAFRVPTPDVS 313
Cdd:PTZ00023 164 VNDKFGIVEGLMTTVHASTANQLTVDGPSKggKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVPDVS 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   314 VVDLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLGDTHSSIFDAKAGIALNDNFVKLISWYDNEYGYS 393
Cdd:PTZ00023 244 VVDLTCKLAKPAKYEEIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDNEWGYS 323

                        330
                 ....*....|....
gi 6226817   394 HRVVDLLRYMFSRD 407
Cdd:PTZ00023 324 NRLLDLAHYITQKY 337
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 77-398 1.60e-166

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: 469.45  E-value: 1.60e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817     77 TVGINGFGRIGRLVLRACMEKG---VKVVAVNDPfIDPEYMVYMFKYDSTHGRYKGSVEFRNGQLVVDNHE-ISVYQCKE 152
Cdd:TIGR01534   1 KVGINGFGRIGRLVLRRILEKPgndLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEvISVFSERD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817    153 PKQIPWRAVGSPYVVESTGVYLSIQAASDHISAGAQRVVISAPS-PDAPMFVMGVNENDYNPGSmNIVSNASCTTNCLAP 231
Cdd:TIGR01534  80 PSDLPWKALGVDIVIECTGKFRDKEKLEKHLEAGAKKVLISAPSkGDVKTIVYGVNHDEYDGEE-RIISNASCTTNCLAP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817    232 LAKVIHERFGIVEGLMTTVHSYTATQKTVDGPsRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKLTGMAFRVPTPD 311
Cdd:TIGR01534 159 LAKVLDEAFGIVSGLMTTVHAYTNDQNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPN 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817    312 VSVVDLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLGDTHSSIFDAKAGIA--LNDNFVKLISWYDNE 389
Cdd:TIGR01534 238 VSLVDLVVNLEKDVTVEEVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNE 317


                  ....*....
gi 6226817    390 YGYSHRVVD 398
Cdd:TIGR01534 318 WGYSNRLVD 326
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
 74-403 1.59e-150

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 429.53  E-value: 1.59e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817    74 RELTVGINGFGRIGRLVLRACMEKG-VKVVAVNDPFIDPEYMVYMFKYDSTHGRYK-GSVEFRNGQ-LVVDNHEISVYQC 150
Cdd:PLN02358   4 KKIRIGINGFGRIGRLVARVVLQRDdVELVAVNDPFITTEYMTYMFKYDSVHGQWKhHELKVKDDKtLLFGEKPVTVFGI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   151 KEPKQIPWRAVGSPYVVESTGVYLSIQAASDHISAGAQRVVISAPSPDAPMFVMGVNENDYNpGSMNIVSNASCTTNCLA 230
Cdd:PLN02358  84 RNPEDIPWGEAGADFVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYK-SDLDIVSNASCTTNCLA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   231 PLAKVIHERFGIVEGLMTTVHSYTATQKTVDGPSRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKLTGMAFRVPTP 310
Cdd:PLN02358 163 PLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTV 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   311 DVSVVDLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLGDTHSSIFDAKAGIALNDNFVKLISWYDNEY 390
Cdd:PLN02358 243 DVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEW 322

                        330
                 ....*....|...
gi 6226817   391 GYSHRVVDLLRYM 403
Cdd:PLN02358 323 GYSSRVVDLIVHM 335
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
76-403 3.63e-149

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 426.07  E-value: 3.63e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817    76 LTVGINGFGRIGRLVLRACMEKG-VKVVAVNDpFIDPEYMVYMFKYDSTHGRYKGSVEFRNGQLVVDNHEISVYQCKEPK 154
Cdd:PRK15425   3 IKVGINGFGRIGRIVFRAAQKRSdIEIVAIND-LLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   155 QIPWRAVGSPYVVESTGVYLSIQAASDHISAGAQRVVISAPSPD-APMFVMGVNENDYnpGSMNIVSNASCTTNCLAPLA 233
Cdd:PRK15425  82 NLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMTGPSKDnTPMFVKGANFDKY--AGQDIVSNASCTTNCLAPLA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   234 KVIHERFGIVEGLMTTVHSYTATQKTVDGPSRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKLTGMAFRVPTPDVS 313
Cdd:PRK15425 160 KVINDNFGIIEGLMTTVHATTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   314 VVDLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLGDTHSSIFDAKAGIALNDNFVKLISWYDNEYGYS 393
Cdd:PRK15425 240 VVDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYS 319

                        330
                 ....*....|
gi 6226817   394 HRVVDLLRYM 403
Cdd:PRK15425 320 NKVLDLIAHI 329
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 76-407 2.74e-140

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 404.44  E-value: 2.74e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817    76 LTVGINGFGRIGRLVLRACMEKG-----VKVVAVNDPFIDPEYMVYMFKYDSTHGRYKGSVEF--------RNGQLVVDN 142
Cdd:PTZ00434   4 IKVGINGFGRIGRMVFQAICDQGligteIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVETtksspsvkTDDVLVVNG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   143 HEI-SVYQCKEPKQIPWRAVGSPYVVESTGVYLSIQAASDHISAGAQRVVISAP-SPDAPMFVMGVNENDYNPGSMNIVS 220
Cdd:PTZ00434  84 HRIkCVKAQRNPADLPWGKLGVDYVIESTGLFTDKLAAEGHLKGGAKKVVISAPaSGGAKTIVMGVNQHEYSPTEHHVVS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   221 NASCTTNCLAPLAKVI-HERFGIVEGLMTTVHSYTATQKTVDGPSRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGK 299
Cdd:PTZ00434 164 NASCTTNCLAPIVHVLtKEGFGIETGLMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGK 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   300 LTGMAFRVPTPDVSVVDLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLGDTHSSIFDAKAGIALN--- 376
Cdd:PTZ00434 244 LTGMSFRVPTPDVSVVDLTFRATRDTSIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKATLQNNlpg 323

                        330       340       350
                 ....*....|....*....|....*....|..
gi 6226817   377 -DNFVKLISWYDNEYGYSHRVVDLLRYMFSRD 407
Cdd:PTZ00434 324 eRRFFKIVSWYDNEWGYSHRVVDLVRYMAAKD 355
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 78-406 1.92e-132

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 383.70  E-value: 1.92e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817    78 VGINGFGRIGRLVLR-ACMEKGVKVVAVNDPFiDPEYMVYMFKYDSTHGRYKGSVEFRNGQLVVDNHEISVYQCKEPKQI 156
Cdd:PRK07729   5 VAINGFGRIGRMVFRkAIKESAFEIVAINASY-PSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDPKEL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   157 PWRAVGSPYVVESTGVYLSIQAASDHISAGAQRVVISAPSPDAPM-FVMGVNENDYNPGSMNIVSNASCTTNCLAPLAKV 235
Cdd:PRK07729  84 PWTDLGIDIVIEATGKFNSKEKAILHVEAGAKKVILTAPGKNEDVtIVVGVNEDQLDIEKHTIISNASCTTNCLAPVVKV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   236 IHERFGIVEGLMTTVHSYTATQKTVDGPsRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKLTGMAFRVPTPDVSVV 315
Cdd:PRK07729 164 LDEQFGIENGLMTTVHAYTNDQKNIDNP-HKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNVSLV 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   316 DLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLGDTHSSIFDAKAGIALNDNFVKLISWYDNEYGYSHR 395
Cdd:PRK07729 243 DLVVDVKRDVTVEEINEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEWGYSCR 322

                        330
                 ....*....|.
gi 6226817   396 VVDLLRYMFSR 406
Cdd:PRK07729 323 VVDLVTLVADE 333
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 224-389 4.57e-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: 342.90  E-value: 4.57e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817  224 CTTNCLAPLAKVIHERFGIVEGLMTTVHSYTATQKTVDGPSRKaWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKLTGM 303
Cdd:cd18126   1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHKD-LRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817  304 AFRVPTPDVSVVDLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLGDTHSSIFDAKAGIALNDNFVKLI 383
Cdd:cd18126  80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159


                ....*.
gi 6226817  384 SWYDNE 389
Cdd:cd18126 160 AWYDNE 165
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
78-399 4.53e-114

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 336.88  E-value: 4.53e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817    78 VGINGFGRIGRLVLRACMEK---GVKVVAVNDPFiDPEYMVYMFKYDSTHGRYKGSVEFRNGQLVVDNHEISVYQCKEPK 154
Cdd:PRK07403   4 VAINGFGRIGRNFLRCWLGRensQLELVAINDTS-DPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDRNPL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   155 QIPWRAVGSPYVVESTGVYLSIQAASDHISAGAQRVVISAP--SPDAPMFVMGVNENDYNPGSMNIVSNASCTTNCLAPL 232
Cdd:PRK07403  83 NLPWKEWGIDLIIESTGVFVTKEGASKHIQAGAKKVLITAPgkGEDIGTYVVGVNHHEYDHEDHNIISNASCTTNCLAPI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   233 AKVIHERFGIVEGLMTTVHSYTATQKTVDGpSRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKLTGMAFRVPTPDV 312
Cdd:PRK07403 163 AKVLHDNFGIIKGTMTTTHSYTGDQRILDA-SHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTPNV 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   313 SVVDLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLGDTHSSIFDAKAGIALNDNFVKLISWYDNEYGY 392
Cdd:PRK07403 242 SVVDLVVQVEKRTITEQVNEVLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYDNEWGY 321


                 ....*..
gi 6226817   393 SHRVVDL 399
Cdd:PRK07403 322 SQRVVDL 328
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
78-399 2.51e-111

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 329.20  E-value: 2.51e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817    78 VGINGFGRIGRLVLRACMEK-GVKVVAVNDPFIDPEYMVYMFKYDSTHGRYKGSVEFRNGQLVVDNHEISVYQCKEPKQI 156
Cdd:NF033735   1 IGINGFGRIGRLALRALWGRpGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   157 PWRAvGSPYVVESTGVYLSIQAASDHISAGAQRVVISAP--SPDAPMFVMGVNENDYNPGSMNIVSNASCTTNCLAPLAK 234
Cdd:NF033735  81 PWGD-GVDVVIECTGKFKTPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARHRIVTAASCTTNCLAPVVK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   235 VIHERFGIVEGLMTTVHSYTATQKTVDGPsRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKLTGMAFRVPTPDVSV 314
Cdd:NF033735 160 VIHEKIGIKHGSITTIHDITNTQTIVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   315 VDLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLGDTHSSIFDAKAGIALNDNFVKLISWYDNEYGYSH 394
Cdd:NF033735 239 TDCVFEVERPTTVEEVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYAN 318


                 ....*
gi 6226817   395 RVVDL 399
Cdd:NF033735 319 RMVDL 323
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
 68-399 1.05e-102

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 311.45  E-value: 1.05e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817    68 KMVSVAReLTVGINGFGRIGRLVLRACMEKG---VKVVAVNDPFiDPEYMVYMFKYDSTHGRYKGSVEFRNGQLV-VDNH 143
Cdd:PLN02237  69 RGETVAK-LKVAINGFGRIGRNFLRCWHGRKdspLDVVVVNDSG-GVKNASHLLKYDSMLGTFKADVKIVDDETIsVDGK 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   144 EISVYQCKEPKQIPWRAVGSPYVVESTGVYLSIQAASDHISAGAQRVVISAPSP--DAPMFVMGVNENDYNPGSMNIVSN 221
Cdd:PLN02237 147 PIKVVSNRDPLKLPWAELGIDIVIEGTGVFVDGPGAGKHIQAGAKKVIITAPAKgaDIPTYVVGVNEDDYDHEVANIVSN 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   222 ASCTTNCLAPLAKVIHERFGIVEGLMTTVHSYTATQKTVDGpSRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKLT 301
Cdd:PLN02237 227 ASCTTNCLAPFVKVLDEEFGIVKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLN 305

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   302 GMAFRVPTPDVSVVDLTCRLAQPAPYSA-IKEAVKAAAKGPMAGILAYTEDEVVSTDFLGDTHSSIFDAKAGIALNDNFV 380
Cdd:PLN02237 306 GIALRVPTPNVSVVDLVVNVEKKGITAEdVNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMV 385

                        330
                 ....*....|....*....
gi 6226817   381 KLISWYDNEYGYSHRVVDL 399
Cdd:PLN02237 386 KVVAWYDNEWGYSQRVVDL 404
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
 75-399 5.37e-98

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 298.00  E-value: 5.37e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817    75 ELTVGINGFGRIGRLVLRACMEKG---VKVVAVNDPFiDPEYMVYMFKYDSTHGRYKGSVEFR-NGQLVVDNHEISVYQC 150
Cdd:PLN03096  60 KIKVAINGFGRIGRNFLRCWHGRKdspLDVVAINDTG-GVKQASHLLKYDSTLGTFDADVKPVgDDAISVDGKVIKVVSD 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   151 KEPKQIPWRAVGSPYVVESTGVYLSIQAASDHISAGAQRVVISAPSP-DAPMFVMGVNENDYNPgSMNIVSNASCTTNCL 229
Cdd:PLN03096 139 RNPLNLPWGELGIDLVIEGTGVFVDREGAGKHIQAGAKKVLITAPGKgDIPTYVVGVNADDYKH-SDPIISNASCTTNCL 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   230 APLAKVIHERFGIVEGLMTTVHSYTATQKTVDGpSRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKLTGMAFRVPT 309
Cdd:PLN03096 218 APFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPT 296

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   310 PDVSVVDLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLGDTHSSIFDAKAGIALNDNFVKLISWYDNE 389
Cdd:PLN03096 297 PNVSVVDLVVQVEKKTFAEEVNAAFRDAAEKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAWYDNE 376

                        330
                 ....*....|
gi 6226817   390 YGYSHRVVDL 399
Cdd:PLN03096 377 WGYSQRVVDL 386
PRK08955 PRK08955
glyceraldehyde-3-phosphate dehydrogenase; Validated
 78-401 1.88e-96

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 169599 [Multi-domain]  Cd Length: 334  Bit Score: 291.63  E-value: 1.88e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817    78 VGINGFGRIGRLVLRACME-KGVKVVAVNDPFIDPEYMVYMFKYDSTHGRYKGSVEFRNGQLVVDNHEISVYQCKEPKQI 156
Cdd:PRK08955   5 VGINGFGRIGRLALRAAWDwPELEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKAIADT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   157 PWRavGSPYVVESTGVYLSIQAASDHISAGAQRVVISAP--SPDAPMFVMGVNENDYNPGSMNIVSNASCTTNCLAPLAK 234
Cdd:PRK08955  85 DWS--GCDVVIEASGVMKTKALLQAYLDQGVKRVVVTAPvkEEGVLNIVMGVNDHLFDPAIHPIVTAASCTTNCLAPVVK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   235 VIHERFGIVEGLMTTVHSYTATQKTVDGPsRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKLTGMAFRVPTPDVSV 314
Cdd:PRK08955 163 VIHEKLGIKHGSMTTIHDLTNTQTILDAP-HKDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLANASL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   315 VDLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLGDTHSSIFDAKAGIALNDNFVKLISWYDNEYGYSH 394
Cdd:PRK08955 242 TDCVFEVERDTTVEEVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNEWGYAN 321


                 ....*..
gi 6226817   395 RVVDLLR 401
Cdd:PRK08955 322 RTAELAR 328
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 229-386 1.45e-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: 265.23  E-value: 1.45e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817    229 LAPLAKVIHERFGIVEGLMTTVHSYTATQKTVDGPSRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKLTGMAFRVP 308
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6226817    309 TPDVSVVDLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLGDTHSSIFDAKAGIALNDNFVKLISWY 386
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
 76-403 1.49e-88

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 271.55  E-value: 1.49e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817    76 LTVGINGFGRIGRLVLRACMEKG----VKVVAVNDpFIDPEYMVYMFKYDSTHGRYKGSVEFRNGQLVVDNHEISVYQCK 151
Cdd:PRK13535   2 IRVAINGFGRIGRNVLRALYESGrraeITVVAINE-LADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   152 EPKQIPWRAVGSPYVVESTGVYLSIQAASDHISAGAQRVVISAPSP---DAPMfVMGVNENDYNPGSmNIVSNASCTTNC 228
Cdd:PRK13535  81 DIASLPWRELGVDVVLDCTGVYGSREDGEAHIAAGAKKVLFSHPGSndlDATV-VYGVNHDQLRAEH-RIVSNASCTTNC 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   229 LAPLAKVIHERFGIVEGLMTTVHSYTATQKTVDGpSRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKLTGMAFRVP 308
Cdd:PRK13535 159 IIPVIKLLDDAFGIESGTVTTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVP 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   309 TPDVSVVDLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLGDTHSSIFDAKAGIALNDNFVKLISWYDN 388
Cdd:PRK13535 238 TINVTAIDLSVTVKKPVKVNEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDN 317

                        330
                 ....*....|....*
gi 6226817   389 EYGYSHRVVDLLRYM 403
Cdd:PRK13535 318 EWGFANRMLDTTLAM 332
E4PD_g-proteo TIGR01532
erythrose-4-phosphate dehydrogenase; This model represents the small clade of dehydrogenases ...
 78-398 3.30e-88

erythrose-4-phosphate dehydrogenase; This model represents the small clade of dehydrogenases in gamma-proteobacteria 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. This enzyme activity appears to have evolved from glyceraldehyde-3-phosphate dehydrogenase, whose substrate differs only in the lack of one carbon relative to E4P. Accordingly, this model is very close to the corresponding models for GAPDH, and those sequences which hit above trusted here invariably hit between trusted and noise to the GAPDH model (TIGR01534). Similarly, it may be found that there are species outside of the gamma proteobacteria which synthesize pyridoxine and have more than one aparrent GAPDH gene of which one may have E4PD activity - this may necessitate a readjustment of these models. Alternatively, some of the GAPDH enzymes may prove to be bifunctional in certain species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]


Pssm-ID: 130595  Cd Length: 325  Bit Score: 270.23  E-value: 3.30e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817     78 VGINGFGRIGRLVLRACMEKG----VKVVAVNDpFIDPEYMVYMFKYDSTHGRYKGSVEFRNGQLVVDNHEISVYQCKEP 153
Cdd:TIGR01532   2 VAINGFGRIGRNVLRALYESGrraeITVVAINE-LADAAGMAHLLKYDTSHGRFAWEVRQDRDQLFVGDDAIRVLHERSL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817    154 KQIPWRAVGSPYVVESTGVYLSIQAASDHISAGAQRVVISAPSP---DAPMfVMGVNENDYNpGSMNIVSNASCTTNCLA 230
Cdd:TIGR01532  81 QSLPWRELGVDLVLDCTGVYGSREHGEAHIAAGAKKVLFSHPGAsdlDATI-VYGVNQDQLR-AEHRIVSNASCTTNCIV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817    231 PLAKVIHERFGIVEGLMTTVHSYTATQKTVDGpSRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKLTGMAFRVPTP 310
Cdd:TIGR01532 159 PVIKLLDDAYGIESGTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLAAGIERFFPQFNDRFEAIAVRVPTV 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817    311 DVSVVDLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLGDTHSSIFDAKAGIALNDNFVKLISWYDNEY 390
Cdd:TIGR01532 238 NVTAIDLSVTVKKPVKANEVNLLLQKAAQGALRGIVDYTELPLVSVDFNHDPHSAIVDGTQTRVSGAHLVKTLVWCDNEW 317


                  ....*...
gi 6226817    391 GYSHRVVD 398
Cdd:TIGR01532 318 GFANRMLD 325
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 224-389 1.36e-81

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: 247.53  E-value: 1.36e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817  224 CTTNCLAPLAKVIHERFGIVEGLMTTVHSYTATQKTVDGPSRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKLTGM 303
Cdd:cd18123   1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817  304 AFRVPTPDVSVVDLTCRLAQPAPYSAIKEAVKAAAKGPmaGILAYTEDEVVSTDFLGDTHSSIFDAKAGIALNDNFVKLI 383
Cdd:cd18123  81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEGK--GRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLM 158


                ....*.
gi 6226817  384 SWYDNE 389
Cdd:cd18123 159 QWYDNE 164
PRK08289 PRK08289
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
 82-403 8.23e-78

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 236219 [Multi-domain]  Cd Length: 477  Bit Score: 248.30  E-value: 8.23e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817    82 GFGRIGRLVLRACMEKGVK--------VVAVNDPFIDPEYMVYMFKYDSTHGRYKGSVEF--RNGQLVVDNHEISVYQCK 151
Cdd:PRK08289 134 GFGRIGRLLARLLIEKTGGgnglrlraIVVRKGSEGDLEKRASLLRRDSVHGPFNGTITVdeENNAIIANGNYIQVIYAN 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   152 EPKQIPWRAVG--SPYVVESTGVYLSIQAASDHI-SAGAQRVVISAPSP-DAPMFVMGVNENDYNPgSMNIVSNASCTTN 227
Cdd:PRK08289 214 SPEEVDYTAYGinNALVVDNTGKWRDEEGLSQHLkSKGVAKVLLTAPGKgDIKNIVHGVNHSDITD-EDKIVSAASCTTN 292

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   228 CLAPLAKVIHERFGIVEGLMTTVHSYTATQKTVDGpSRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKLTGMAFRV 307
Cdd:PRK08289 293 AITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDN-YHKGDRRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNAIRV 371

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   308 PTPDVSVVDLTCRLAQPAPYSAIKEAVKAAA-KGPMAGILAYTED-EVVSTDFLGDTHSSIFDAKAGIALNDNFVkLISW 385
Cdd:PRK08289 372 PTPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQIDYTDStEVVSSDFVGSRHAGVVDSQATIVNGNRAV-LYVW 450

                        330
                 ....*....|....*...
gi 6226817   386 YDNEYGYSHRVVDLLRYM 403
Cdd:PRK08289 451 YDNEFGYSCQVVRVMEQM 468
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 78-223 1.35e-77

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: 237.29  E-value: 1.35e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   78 VGINGFGRIGRLVLRACMEK-GVKVVAVNDPFiDPEYMVYMFKYDSTHGRYKGSVEFRNGQLVVDNHEISVYQCKEPKQI 156
Cdd:cd05214   3 VGINGFGRIGRLVFRAALERdDIEVVAINDLT-DDETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAEL 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6226817  157 PWRAVGSPYVVESTGVYLSIQAASDHISAGAQRVVISAPSPD-APMFVMGVNENDYNPgSMNIVSNAS 223
Cdd:cd05214  82 PWGELGVDIVIESTGVFTTKEKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDA-DDKIISNAS 148
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 78-224 1.75e-68

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: 213.18  E-value: 1.75e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817      78 VGINGFGRIGRLVLRACME-KGVKVVAVNDPfIDPEYMVYMFKYDSTHGRYKGSVEFRNGQLVVDNHEISVYQCKEPKQI 156
Cdd:smart00846   3 VGINGFGRIGRLVLRAALErPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANL 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6226817     157 PWRAVGSPYVVESTGVYLSIQAASDHISAGAQRVVISAPSPDA-PMFVMGVNENDYNPgSMNIVSNASC 224
Cdd:smart00846  82 PWGELGVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDG-EDHIISNASC 149
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
 76-407 5.25e-50

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 171.98  E-value: 5.25e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817    76 LTVGINGFGRIGRLVLRACM-EKGVKVVAVNDPFIDPEYMVYMFKYDSTHGRYKG-SVEFRNGQLVVDN-HEISVYQCKE 152
Cdd:PTZ00353   3 ITVGINGFGPVGKAVLFASLtDPLVTVVAVNDASVSIAYIAYVLEQESPLSAPDGaSIRVVGEQIVLNGtQKIRVSAKHD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   153 PKQIPWRAVGSPYVVESTGVYLSIQAASDHISAGAQRVVISAPSPDAPMFVMGVNENDYNpGSMNIVSNASCTTNCLAPL 232
Cdd:PTZ00353  83 LVEIAWRDYGVQYVVECTGLYSTRSRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDERLS-ASLPVCCAGAPIAVALAPV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   233 AKVIHERFGIVEGLMTTVHSyTATQKTVDGPSRKA--WRDGRGAHQNIIPASTGAAKAVTKVIPELKGKLTGMAFRVPTP 310
Cdd:PTZ00353 162 IRALHEVYGVEECSYTAIHG-MQPQEPIAARSKNSqdWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVK 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   311 DVSVVDLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLGDThSSIFDAKAGIALNDNFV-KLISWYDNE 389
Cdd:PTZ00353 241 KGCAIDMLVRTKQPVSKEVVDSALAEAASDRLNGVLCISKRDMISVDCIPNG-KLCYDATSSSSSREGEVhKMVLWFDVE 319

                        330
                 ....*....|....*...
gi 6226817   390 YGYSHRVVDLLRYMFSRD 407
Cdd:PTZ00353 320 CYYAARLLSLVKQLHQIH 337
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 78-175 1.48e-48

Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric NAD-binding enzyme involved in glycolysis and glyconeogenesis. N-terminal domain is a Rossmann NAD(P) binding fold.


Pssm-ID: 459648 [Multi-domain]  Cd Length: 101  Bit Score: 160.35  E-value: 1.48e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817     78 VGINGFGRIGRLVLRACME-KGVKVVAVNDpFIDPEYMVYMFKYDSTHGRYKGSVEFRNGQLVVDNHEISVYQCKEPKQI 156
Cdd:pfam00044   3 VGINGFGRIGRLVLRAALErPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAEL 81

                          90
                  ....*....|....*....
gi 6226817    157 PWRAVGSPYVVESTGVYLS 175
Cdd:pfam00044  82 PWGDLGVDVVIESTGVFTT 100
GAPDH_N_E4PDH cd17892
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 78-223 1.70e-47

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


Pssm-ID: 467615 [Multi-domain]  Cd Length: 169  Bit Score: 159.74  E-value: 1.70e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   78 VGINGFGRIGRLVLRACMEKG----VKVVAVNDPfIDPEYMVYMFKYDSTHGRYKGSVEFRNGQLVVDNHEISVYQCKEP 153
Cdd:cd17892   3 VAINGYGRIGRNVLRALYESGrraeFQVVAINEL-ADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPDP 81

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6226817  154 KQIPWRAVGSPYVVESTGVYLSIQAASDHISAGAQRVVISAPSP---DAPMfVMGVNENDYNPgSMNIVSNAS 223
Cdd:cd17892  82 ENLPWRELGIDLVLECTGVFGSREDAERHLAAGAKKVLFSHPASndvDATI-VYGINQDLLRA-EHRIVSNAS 152
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 224-389 1.92e-45

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: 154.60  E-value: 1.92e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817  224 CTTNCLAPLAKVIHERFGIVEGLMTTVHSYTATQKTVDGPSRKAWrdGRGAHQNIIPASTGAAKAVTKVIPEL--KGKLT 301
Cdd:cd18122   1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIgkPIKVD 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817  302 GMAFRVPTPDVSVVDLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLGDTHSSIFDAKAGIALNDNFVK 381
Cdd:cd18122  79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLK 158


                ....*...
gi 6226817  382 LISWYDNE 389
Cdd:cd18122 159 VFSAVDNE 166
GAPDH_C_E4PDH cd23937
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 224-389 1.08e-42

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


Pssm-ID: 467686  Cd Length: 165  Bit Score: 147.18  E-value: 1.08e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817  224 CTTNCLAPLAKVIHERFGIVEGLMTTVHSYTATQKTVDGpSRKAWRDGRGAHQNIIPASTGAAKAVTKVIPELKGKLTGM 303
Cdd:cd23937   1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817  304 AFRVPTPDVSVVDLTCRLAQPAPYSAIKEAVKAAAKGPMAGILAYTEDEVVSTDFLGDTHSSIFDAKAGIALNDNFVKLI 383
Cdd:cd23937  80 AVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLL 159


                ....*.
gi 6226817  384 SWYDNE 389
Cdd:cd23937 160 VWCDNE 165
GAPDH-like_N cd05192
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ...
 78-228 7.99e-08

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: 50.04  E-value: 7.99e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6226817   78 VGINGFGRIGRLVLRACMEK-GVKVVAVNDPfidpeymvymfkydsthgrykgsvefrngqlvvdnheisvyqckepkqi 156
Cdd:cd05192   3 VAINGFGRIGRIVFRAIADQdDLDVVAINDR------------------------------------------------- 33

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6226817  157 pwravgSPYVVESTGVYLSIQAASDHISAGAQRVVISAPSP-DAPMFVMGVNENDYNPGSmNIVSNASCTTNC 228
Cdd:cd05192  34 ------RDVVIECTGSFTDDDNAEKHIKAGGKKAVITAPEKgDIPTIVVVLNELAKSAGA-TVVSNANETSYS 99
LDH_like cd01619
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
 74-122 2.31e-05

D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-HicDH is a NAD-dependent member of the hydroxycarboxylate dehydrogenase family, and shares the Rossmann fold typical of many NAD binding proteins. D-HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. Similar to the structurally distinct L-HicDH, D-HicDH exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. (R)-2-hydroxyglutarate dehydrogenase (HGDH) catalyzes the NAD-dependent reduction of 2-oxoglutarate to (R)-2-hydroxyglutarate. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240620 [Multi-domain]  Cd Length: 323  Bit Score: 46.14  E-value: 2.31e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 6226817   74 RELTVGINGFGRIGRLVLRACMEKGVKVVAVnDPFIDPEYMVYMFKYDS 122
Cdd:cd01619 142 EDQTVGVVGTGKIGRAVAQRAKGFGMKVIAY-DPFRNPELEDKGVKYVS 189
PGDH_like_2 cd12172
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
 77-113 5.40e-05

Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Many, not all, members of this family are dimeric.


Pssm-ID: 240649 [Multi-domain]  Cd Length: 306  Bit Score: 44.79  E-value: 5.40e-05
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 6226817   77 TVGINGFGRIGRLVLRACMEKGVKVVAvNDPFIDPEY 113
Cdd:cd12172 144 TLGIIGLGRIGKAVARRLSGFGMKVLA-YDPYPDEEF 179
CtBP_dh cd05299
C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related ...
 74-118 1.05e-04

C-terminal binding protein (CtBP), D-isomer-specific 2-hydroxyacid dehydrogenases related repressor; The transcriptional corepressor CtBP is a dehydrogenase with sequence and structural similarity to the d2-hydroxyacid dehydrogenase family. CtBP was initially identified as a protein that bound the PXDLS sequence at the adenovirus E1A C terminus, causing the loss of CR-1-mediated transactivation. CtBP binds NAD(H) within a deep cleft, undergoes a conformational change upon NAD binding, and has NAD-dependent dehydrogenase activity.


Pssm-ID: 240624 [Multi-domain]  Cd Length: 312  Bit Score: 44.04  E-value: 1.05e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 6226817   74 RELTVGINGFGRIGRLVlracMEK----GVKVVAvNDPFIDPEYMVYMF 118
Cdd:cd05299 141 RGLTLGLVGFGRIGRAV----AKRakafGFRVIA-YDPYVPDGVAALGG 184
2-Hacid_dh_10 cd12171
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 74-112 2.52e-04

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240648 [Multi-domain]  Cd Length: 310  Bit Score: 42.53  E-value: 2.52e-04
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 6226817   74 RELTVGINGFGRIGRLVLRACMEKGVKVVAVnDPFIDPE 112
Cdd:cd12171 146 RGKTVGIVGFGAIGRRVAKRLKAFGAEVLVY-DPYVDPE 183
PGDH_4 cd12173
Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate ...
 72-112 2.62e-04

Phosphoglycerate dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases. PGDH in E. coli and Mycobacterium tuberculosis form tetramers, with subunits containing a Rossmann-fold NAD binding domain. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence.


Pssm-ID: 240650 [Multi-domain]  Cd Length: 304  Bit Score: 42.40  E-value: 2.62e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 6226817   72 VAREL---TVGINGFGRIGRLVLRACMEKGVKVVAvNDPFIDPE 112
Cdd:cd12173 132 MGVELrgkTLGIVGLGRIGREVARRARAFGMKVLA-YDPYISAE 174
PGDH_like_3 cd12174
Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; ...
 68-112 4.31e-04

Putative D-3-Phosphoglycerate Dehydrogenases, NAD-binding and catalytic domains; Phosphoglycerate dehydrogenases (PGDHs) catalyze the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDHs come in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily, which also include groups such as L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. Many, not all, members of this family are dimeric.


Pssm-ID: 240651 [Multi-domain]  Cd Length: 305  Bit Score: 41.78  E-value: 4.31e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 6226817   68 KMVSVAREL---TVGINGFGRIGRLVLRACMEKGVKVVAVnDPFIDPE 112
Cdd:cd12174 125 KKQFVGTELrgkTLGVIGLGNIGRLVANAALALGMKVIGY-DPYLSVE 171
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
 73-112 6.82e-04

Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; Phosphoglycerate dehydrogenase or related dehydrogenase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 439881 [Multi-domain]  Cd Length: 314  Bit Score: 41.33  E-value: 6.82e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 6226817   73 ARELTVGINGFGRIGRLVLRACMEKGVKVVAVnDPFIDPE 112
Cdd:COG0111 138 LRGKTVGIVGLGRIGRAVARRLRAFGMRVLAY-DPSPKPE 176
2-Hacid_dh_8 cd12167
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 74-112 1.60e-03

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240644 [Multi-domain]  Cd Length: 330  Bit Score: 40.24  E-value: 1.60e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 6226817   74 RELTVGINGFGRIGRLVLRACMEKGVKVVaVNDPFIDPE 112
Cdd:cd12167 149 YGRTVGIVGFGRIGRAVVELLRPFGLRVL-VYDPYLPAA 186
LDH cd12186
D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding ...
 74-122 2.00e-03

D-Lactate dehydrogenase and D-2-Hydroxyisocaproic acid dehydrogenase (D-HicDH), NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenases family. LDH is homologous to D-2-hydroxyisocaproic acid dehydrogenase(D-HicDH) and shares the 2 domain structure of formate dehydrogenase. D-HicDH is a NAD-dependent member of the hydroxycarboxylate dehydrogenase family, and shares the Rossmann fold typical of many NAD binding proteins. HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. D-HicDH, like the structurally distinct L-HicDH, exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240662  Cd Length: 329  Bit Score: 39.83  E-value: 2.00e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 6226817   74 RELTVGINGFGRIGRLVLRACMEKGVKVVAVnDPFIDPEYMVYMFKYDS 122
Cdd:cd12186 144 RDLTVGIIGTGRIGSAAAKIFKGFGAKVIAY-DPYPNPELEKFLLYYDS 191
PGDH_2 cd05303
Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate ...
 68-116 2.54e-03

Phosphoglycerate dehydrogenase (PGDH) NAD-binding and catalytic domains; Phosphoglycerate dehydrogenase (PGDH) catalyzes the initial step in the biosynthesis of L-serine from D-3-phosphoglycerate. PGDH comes in 3 distinct structural forms, with this first group being related to 2-hydroxy acid dehydrogenases, sharing structural similarity to formate and glycerate dehydrogenases. PGDH in E. coli and Mycobacterium tuberculosis form tetramers, with subunits containing a Rossmann-fold NAD binding domain. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine Hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence.


Pssm-ID: 240628 [Multi-domain]  Cd Length: 301  Bit Score: 39.44  E-value: 2.54e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 6226817   68 KMVSVAREL---TVGINGFGRIGRLVLRACMEKGVKVVAvNDPFIDPEYMVY 116
Cdd:cd05303 129 KKKYKGIELrgkTLGIIGFGRIGREVAKIARALGMNVIA-YDPYPKDEQAVE 179
2-Hacid_dh_C pfam02826
D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted ...
 74-112 4.63e-03

D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; This domain is inserted into the catalytic domain, the large dehydrogenase and D-lactate dehydrogenase families in SCOP. N-terminal portion of which is represented by family pfam00389.


Pssm-ID: 427007 [Multi-domain]  Cd Length: 178  Bit Score: 37.86  E-value: 4.63e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 6226817     74 RELTVGINGFGRIGRLVLRACMEKGVKVVAVnDPFIDPE 112
Cdd:pfam02826  35 SGKTVGIIGLGRIGRAVAKRLKAFGMKVIAY-DRYPKPE 72
ErythrP_dh cd12158
D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; ...
 74-108 5.42e-03

D-Erythronate-4-Phosphate Dehydrogenase NAD-binding and catalytic domains; D-Erythronate-4-phosphate Dehydrogenase (E. coli gene PdxB), a D-specific 2-hydroxyacid dehydrogenase family member, catalyzes the NAD-dependent oxidation of erythronate-4-phosphate, which is followed by transamination to form 4-hydroxy-L-threonine-4-phosphate within the de novo biosynthesis pathway of vitamin B6. D-Erythronate-4-phosphate dehydrogenase has the common architecture shared with D-isomer specific 2-hydroxyacid dehydrogenases but contains an additional C-terminal dimerization domain in addition to an NAD-binding domain and the "lid" domain. The lid domain corresponds to the catalytic domain of phosphoglycerate dehydrogenase and other proteins of the D-isomer specific 2-hydroxyacid dehydrogenase family, which include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence.


Pssm-ID: 240635 [Multi-domain]  Cd Length: 343  Bit Score: 38.67  E-value: 5.42e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 6226817   74 RELTVGINGFGRIGRLVLRACMEKGVKVVaVNDPF 108
Cdd:cd12158 114 KGKTVGIVGVGNVGSRLARRLEALGMNVL-LCDPP 147
LDH_like_2 cd12183
D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate ...
 77-120 9.16e-03

D-Lactate and related Dehydrogenases, NAD-binding and catalytic domains; D-Lactate dehydrogenase (LDH) catalyzes the interconversion of pyruvate and lactate, and is a member of the 2-hydroxyacid dehydrogenase family. LDH is homologous to D-2-hydroxyisocaproic acid dehydrogenase (D-HicDH) and shares the 2-domain structure of formate dehydrogenase. D-2-hydroxyisocaproate dehydrogenase-like (HicDH) proteins are NAD-dependent members of the hydroxycarboxylate dehydrogenase family, and share the Rossmann fold typical of many NAD binding proteins. HicDH from Lactobacillus casei forms a monomer and catalyzes the reaction R-CO-COO(-) + NADH + H+ to R-COH-COO(-) + NAD+. D-HicDH, like the structurally distinct L-HicDH, exhibits low side-chain R specificity, accepting a wide range of 2-oxocarboxylic acid side chains. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain.


Pssm-ID: 240659  Cd Length: 328  Bit Score: 37.81  E-value: 9.16e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 6226817   77 TVGINGFGRIGRLVLRACMEKGVKVVAvNDPFIDPEYMVYMFKY 120
Cdd:cd12183 146 TVGVIGTGKIGQAFARILKGFGCRVLA-YDPYPNPELAKLGVEY 188
 
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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