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Conserved domains on  [gi|1333553996|ref|XP_023505332|]
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glyceraldehyde-3-phosphate dehydrogenase, testis-specific isoform X3 [Equus caballus]

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
 5-309 2.81e-179

glyceraldehyde-3-phosphate dehydrogenase


The actual alignment was detected with superfamily member PLN02272:

Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 501.69  E-value: 2.81e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996   5 VKVVAVNDPFIDPEYMVYMFKYDSTHGRYKGNVE-FKNGRLVVDKQEITVFQCKQPREIPWRSVGSPFVVEATGAYLSLE 83
Cdd:PLN02272  110 IEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINvVDDSTLEINGKQIKVTSKRDPAEIPWGDFGAEYVVESSGVFTTVE 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996  84 ETSSHIEAGAPRVVICAPSPDAPMFVMGVNEKDYNPgSMKIVSNASCTTNCLAPLAKVIHERFGIVEGLMTTVHSYTATQ 163
Cdd:PLN02272  190 KASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKP-NMNIVSNASCTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQ 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 164 KTVDGPSRKAWRDGRGAHQNIIPASTGAAKAVGKVIPSLKGKLTGMAFRVPTPDVSVVDLTCRLAQPAPYSAIKEAIKAA 243
Cdd:PLN02272  269 KTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYA 348

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333553996 244 AKGPLAGILAYTEDEVVSTDFLGDPHSSIFDANASIALNDNFVKLISWYDNEYGYSHRVVDLLRYM 309
Cdd:PLN02272  349 SEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYSNRVLDLIEHM 414
 
Name Accession Description Interval E-value
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 5-309 2.81e-179

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 501.69  E-value: 2.81e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996   5 VKVVAVNDPFIDPEYMVYMFKYDSTHGRYKGNVE-FKNGRLVVDKQEITVFQCKQPREIPWRSVGSPFVVEATGAYLSLE 83
Cdd:PLN02272  110 IEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINvVDDSTLEINGKQIKVTSKRDPAEIPWGDFGAEYVVESSGVFTTVE 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996  84 ETSSHIEAGAPRVVICAPSPDAPMFVMGVNEKDYNPgSMKIVSNASCTTNCLAPLAKVIHERFGIVEGLMTTVHSYTATQ 163
Cdd:PLN02272  190 KASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKP-NMNIVSNASCTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQ 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 164 KTVDGPSRKAWRDGRGAHQNIIPASTGAAKAVGKVIPSLKGKLTGMAFRVPTPDVSVVDLTCRLAQPAPYSAIKEAIKAA 243
Cdd:PLN02272  269 KTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYA 348

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333553996 244 AKGPLAGILAYTEDEVVSTDFLGDPHSSIFDANASIALNDNFVKLISWYDNEYGYSHRVVDLLRYM 309
Cdd:PLN02272  349 SEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYSNRVLDLIEHM 414
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 3-309 6.79e-174

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: 484.51  E-value: 6.79e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996   3 KGVKVVAVNDPfIDPEYMVYMFKYDSTHGRYKGNVEFKNGRLVVDKQEITVFQCKQPREIPWRSVGSPFVVEATGAYLSL 82
Cdd:COG0057    26 PDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAELPWGELGVDVVIECTGKFTDR 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996  83 EETSSHIEAGAPRVVICAPSPDA-PMFVMGVNEKDYNPgSMKIVSNASCTTNCLAPLAKVIHERFGIVEGLMTTVHSYTA 161
Cdd:COG0057   105 EKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDA-DHRIISNASCTTNCLAPVAKVLNDAFGIEKGLMTTIHAYTN 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 162 TQKTVDGPsRKAWRDGRGAHQNIIPASTGAAKAVGKVIPSLKGKLTGMAFRVPTPDVSVVDLTCRLAQPAPYSAIKEAIK 241
Cdd:COG0057   184 DQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVELEKETTVEEVNAALK 262

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333553996 242 AAAKGPLAGILAYTEDEVVSTDFLGDPHSSIFDANASIALNDNFVKLISWYDNEYGYSHRVVDLLRYM 309
Cdd:COG0057   263 EAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGYSNRMVDLAEYM 330
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 5-304 1.30e-147

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: 417.83  E-value: 1.30e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996   5 VKVVAVNDPfIDPEYMVYMFKYDSTHGRYKGNVEFKNGRLVVDKQEIT-VFQCKQPREIPWRSVGSPFVVEATGAYLSLE 83
Cdd:TIGR01534  26 LEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEVIsVFSERDPSDLPWKALGVDIVIECTGKFRDKE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996  84 ETSSHIEAGAPRVVICAPS-PDAPMFVMGVNEKDYNPGSmKIVSNASCTTNCLAPLAKVIHERFGIVEGLMTTVHSYTAT 162
Cdd:TIGR01534 105 KLEKHLEAGAKKVLISAPSkGDVKTIVYGVNHDEYDGEE-RIISNASCTTNCLAPLAKVLDEAFGIVSGLMTTVHAYTND 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 163 QKTVDGPsRKAWRDGRGAHQNIIPASTGAAKAVGKVIPSLKGKLTGMAFRVPTPDVSVVDLTCRLAQPAPYSAIKEAIKA 242
Cdd:TIGR01534 184 QNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNVSLVDLVVNLEKDVTVEEVNAALKE 262

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333553996 243 AAKGPLAGILAYTEDEVVSTDFLGDPHSSIFDANASIA--LNDNFVKLISWYDNEYGYSHRVVD 304
Cdd:TIGR01534 263 ASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNEWGYSNRLVD 326
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 130-295 4.55e-111

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: 319.02  E-value: 4.55e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 130 CTTNCLAPLAKVIHERFGIVEGLMTTVHSYTATQKTVDGPSRKaWRDGRGAHQNIIPASTGAAKAVGKVIPSLKGKLTGM 209
Cdd:cd18126     1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHKD-LRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 210 AFRVPTPDVSVVDLTCRLAQPAPYSAIKEAIKAAAKGPLAGILAYTEDEVVSTDFLGDPHSSIFDANASIALNDNFVKLI 289
Cdd:cd18126    80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159


                  ....*.
gi 1333553996 290 SWYDNE 295
Cdd:cd18126   160 AWYDNE 165
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
4-305 2.27e-94

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 282.59  E-value: 2.27e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996   4 GVKVVAVNDPFIDPEYMVYMFKYDSTHGRYKGNVEFKNGRLVVDKQEITVFQCKQPREIPWrSVGSPFVVEATGAYLSLE 83
Cdd:NF033735   22 GLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDTPW-GDGVDVVIECTGKFKTPE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996  84 ETSSHIEAGAPRVVICAP--SPDAPMFVMGVNEKDYNPGSMKIVSNASCTTNCLAPLAKVIHERFGIVEGLMTTVHSYTA 161
Cdd:NF033735  101 KLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARHRIVTAASCTTNCLAPVVKVIHEKIGIKHGSITTIHDITN 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 162 TQKTVDGPsRKAWRDGRGAHQNIIPASTGAAKAVGKVIPSLKGKLTGMAFRVPTPDVSVVDLTCRLAQPAPYSAIKEAIK 241
Cdd:NF033735  181 TQTIVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASLTDCVFEVERPTTVEEVNALFK 259

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333553996 242 AAAKGPLAGILAYTEDEVVSTDFLGDPHSSIFDANASIALNDNFVKLISWYDNEYGYSHRVVDL 305
Cdd:NF033735  260 AAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYANRMVDL 323
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 135-292 2.41e-83

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


Pssm-ID: 460700  Cd Length: 158  Bit Score: 248.28  E-value: 2.41e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 135 LAPLAKVIHERFGIVEGLMTTVHSYTATQKTVDGPSRKAWRDGRGAHQNIIPASTGAAKAVGKVIPSLKGKLTGMAFRVP 214
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333553996 215 TPDVSVVDLTCRLAQPAPYSAIKEAIKAAAKGPLAGILAYTEDEVVSTDFLGDPHSSIFDANASIALNDNFVKLISWY 292
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-130 1.20e-53

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: 172.35  E-value: 1.20e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996    1 MEKGVKVVAVNDPfIDPEYMVYMFKYDSTHGRYKGNVEFKNGRLVVDKQEITVFQCKQPREIPWRSVGSPFVVEATGAYL 80
Cdd:smart00846  21 ERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANLPWGELGVDIVVECTGGFT 99

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1333553996   81 SLEETSSHIEAGAPRVVICAPSPDA-PMFVMGVNEKDYNPgSMKIVSNASC 130
Cdd:smart00846 100 TREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDG-EDHIISNASC 149
 
Name Accession Description Interval E-value
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 5-309 2.81e-179

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 501.69  E-value: 2.81e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996   5 VKVVAVNDPFIDPEYMVYMFKYDSTHGRYKGNVE-FKNGRLVVDKQEITVFQCKQPREIPWRSVGSPFVVEATGAYLSLE 83
Cdd:PLN02272  110 IEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINvVDDSTLEINGKQIKVTSKRDPAEIPWGDFGAEYVVESSGVFTTVE 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996  84 ETSSHIEAGAPRVVICAPSPDAPMFVMGVNEKDYNPgSMKIVSNASCTTNCLAPLAKVIHERFGIVEGLMTTVHSYTATQ 163
Cdd:PLN02272  190 KASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKP-NMNIVSNASCTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQ 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 164 KTVDGPSRKAWRDGRGAHQNIIPASTGAAKAVGKVIPSLKGKLTGMAFRVPTPDVSVVDLTCRLAQPAPYSAIKEAIKAA 243
Cdd:PLN02272  269 KTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYA 348

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333553996 244 AKGPLAGILAYTEDEVVSTDFLGDPHSSIFDANASIALNDNFVKLISWYDNEYGYSHRVVDLLRYM 309
Cdd:PLN02272  349 SEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAKAGIGLSASFMKLVSWYDNEWGYSNRVLDLIEHM 414
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 3-309 6.79e-174

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: 484.51  E-value: 6.79e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996   3 KGVKVVAVNDPfIDPEYMVYMFKYDSTHGRYKGNVEFKNGRLVVDKQEITVFQCKQPREIPWRSVGSPFVVEATGAYLSL 82
Cdd:COG0057    26 PDIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAELPWGELGVDVVIECTGKFTDR 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996  83 EETSSHIEAGAPRVVICAPSPDA-PMFVMGVNEKDYNPgSMKIVSNASCTTNCLAPLAKVIHERFGIVEGLMTTVHSYTA 161
Cdd:COG0057   105 EKASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDA-DHRIISNASCTTNCLAPVAKVLNDAFGIEKGLMTTIHAYTN 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 162 TQKTVDGPsRKAWRDGRGAHQNIIPASTGAAKAVGKVIPSLKGKLTGMAFRVPTPDVSVVDLTCRLAQPAPYSAIKEAIK 241
Cdd:COG0057   184 DQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVELEKETTVEEVNAALK 262

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333553996 242 AAAKGPLAGILAYTEDEVVSTDFLGDPHSSIFDANASIALNDNFVKLISWYDNEYGYSHRVVDLLRYM 309
Cdd:COG0057   263 EAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDALQTIVIGGNLVKVLAWYDNEWGYSNRMVDLAEYM 330
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
 3-313 8.05e-150

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 423.86  E-value: 8.05e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996   3 KGVKVVAVNDPFIDPEYMVYMFKYDSTHGRYKGNVEFKNGRLVVDKQEITVFQCKQPREIPWRSVGSPFVVEATGAYLSL 82
Cdd:PTZ00023   25 EDVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKDPAAIPWGKNGVDVVCESTGVFLTK 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996  83 EETSSHIEAGAPRVVICAP-SPDAPMFVMGVNEKDYNPgSMKIVSNASCTTNCLAPLAKVIHERFGIVEGLMTTVHSYTA 161
Cdd:PTZ00023  105 EKAQAHLKGGAKKVIMSAPpKDDTPIYVMGVNHTQYDK-SQRIVSNASCTTNCLAPLAKVVNDKFGIVEGLMTTVHASTA 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 162 TQKTVDGPSR--KAWRDGRGAHQNIIPASTGAAKAVGKVIPSLKGKLTGMAFRVPTPDVSVVDLTCRLAQPAPYSAIKEA 239
Cdd:PTZ00023  184 NQLTVDGPSKggKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVPDVSVVDLTCKLAKPAKYEEIVAA 263

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333553996 240 IKAAAKGPLAGILAYTEDEVVSTDFLGDPHSSIFDANASIALNDNFVKLISWYDNEYGYSHRVVDLLRYMFSRD 313
Cdd:PTZ00023  264 VKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVKAGIALNDTFVKLVSWYDNEWGYSNRLLDLAHYITQKY 337
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 5-304 1.30e-147

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: 417.83  E-value: 1.30e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996   5 VKVVAVNDPfIDPEYMVYMFKYDSTHGRYKGNVEFKNGRLVVDKQEIT-VFQCKQPREIPWRSVGSPFVVEATGAYLSLE 83
Cdd:TIGR01534  26 LEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEVIsVFSERDPSDLPWKALGVDIVIECTGKFRDKE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996  84 ETSSHIEAGAPRVVICAPS-PDAPMFVMGVNEKDYNPGSmKIVSNASCTTNCLAPLAKVIHERFGIVEGLMTTVHSYTAT 162
Cdd:TIGR01534 105 KLEKHLEAGAKKVLISAPSkGDVKTIVYGVNHDEYDGEE-RIISNASCTTNCLAPLAKVLDEAFGIVSGLMTTVHAYTND 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 163 QKTVDGPsRKAWRDGRGAHQNIIPASTGAAKAVGKVIPSLKGKLTGMAFRVPTPDVSVVDLTCRLAQPAPYSAIKEAIKA 242
Cdd:TIGR01534 184 QNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNVSLVDLVVNLEKDVTVEEVNAALKE 262

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333553996 243 AAKGPLAGILAYTEDEVVSTDFLGDPHSSIFDANASIA--LNDNFVKLISWYDNEYGYSHRVVD 304
Cdd:TIGR01534 263 ASEGELKGVLGYTEDELVSSDFIGSPYSSIVDATATKVtgLGDSLVKVYAWYDNEWGYSNRLVD 326
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
 5-309 1.01e-137

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 393.32  E-value: 1.01e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996   5 VKVVAVNDPFIDPEYMVYMFKYDSTHGRYKGN-VEFKNGR-LVVDKQEITVFQCKQPREIPWRSVGSPFVVEATGAYLSL 82
Cdd:PLN02358   30 VELVAVNDPFITTEYMTYMFKYDSVHGQWKHHeLKVKDDKtLLFGEKPVTVFGIRNPEDIPWGEAGADFVVESTGVFTDK 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996  83 EETSSHIEAGAPRVVICAPSPDAPMFVMGVNEKDYNpGSMKIVSNASCTTNCLAPLAKVIHERFGIVEGLMTTVHSYTAT 162
Cdd:PLN02358  110 DKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYK-SDLDIVSNASCTTNCLAPLAKVINDRFGIVEGLMTTVHSITAT 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 163 QKTVDGPSRKAWRDGRGAHQNIIPASTGAAKAVGKVIPSLKGKLTGMAFRVPTPDVSVVDLTCRLAQPAPYSAIKEAIKA 242
Cdd:PLN02358  189 QKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRLEKAATYDEIKKAIKE 268

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333553996 243 AAKGPLAGILAYTEDEVVSTDFLGDPHSSIFDANASIALNDNFVKLISWYDNEYGYSHRVVDLLRYM 309
Cdd:PLN02358  269 ESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEWGYSSRVVDLIVHM 335
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
5-309 3.19e-131

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 376.38  E-value: 3.19e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996   5 VKVVAVNDpFIDPEYMVYMFKYDSTHGRYKGNVEFKNGRLVVDKQEITVFQCKQPREIPWRSVGSPFVVEATGAYLSLEE 84
Cdd:PRK15425   27 IEIVAIND-LLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPANLKWDEVGVDVVAEATGLFLTDET 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996  85 TSSHIEAGAPRVVICAPSPD-APMFVMGVNEKDYnpGSMKIVSNASCTTNCLAPLAKVIHERFGIVEGLMTTVHSYTATQ 163
Cdd:PRK15425  106 ARKHITAGAKKVVMTGPSKDnTPMFVKGANFDKY--AGQDIVSNASCTTNCLAPLAKVINDNFGIIEGLMTTVHATTATQ 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 164 KTVDGPSRKAWRDGRGAHQNIIPASTGAAKAVGKVIPSLKGKLTGMAFRVPTPDVSVVDLTCRLAQPAPYSAIKEAIKAA 243
Cdd:PRK15425  184 KTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAATYEQIKAAVKAA 263

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333553996 244 AKGPLAGILAYTEDEVVSTDFLGDPHSSIFDANASIALNDNFVKLISWYDNEYGYSHRVVDLLRYM 309
Cdd:PRK15425  264 AEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIALNDNFVKLVSWYDNETGYSNKVLDLIAHI 329
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 5-313 2.96e-121

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 352.44  E-value: 2.96e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996   5 VKVVAVNDPFIDPEYMVYMFKYDSTHGRYKGNVEF--------KNGRLVVDKQEITVFQCKQ-PREIPWRSVGSPFVVEA 75
Cdd:PTZ00434   32 IDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVETtksspsvkTDDVLVVNGHRIKCVKAQRnPADLPWGKLGVDYVIES 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996  76 TGAYLSLEETSSHIEAGAPRVVICAP-SPDAPMFVMGVNEKDYNPGSMKIVSNASCTTNCLAPLAKVI-HERFGIVEGLM 153
Cdd:PTZ00434  112 TGLFTDKLAAEGHLKGGAKKVVISAPaSGGAKTIVMGVNQHEYSPTEHHVVSNASCTTNCLAPIVHVLtKEGFGIETGLM 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 154 TTVHSYTATQKTVDGPSRKAWRDGRGAHQNIIPASTGAAKAVGKVIPSLKGKLTGMAFRVPTPDVSVVDLTCRLAQPAPY 233
Cdd:PTZ00434  192 TTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGKLTGMSFRVPTPDVSVVDLTFRATRDTSI 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 234 SAIKEAIKAAAKGPLAGILAYTEDEVVSTDFLGDPHSSIFDANASIALN----DNFVKLISWYDNEYGYSHRVVDLLRYM 309
Cdd:PTZ00434  272 QEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSKATLQNNlpgeRRFFKIVSWYDNEWGYSHRVVDLVRYM 351


                  ....
gi 1333553996 310 FSRD 313
Cdd:PTZ00434  352 AAKD 355
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-312 1.12e-120

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 350.19  E-value: 1.12e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996   1 MEKGVKVVAVNDPFiDPEYMVYMFKYDSTHGRYKGNVEFKNGRLVVDKQEITVFQCKQPREIPWRSVGSPFVVEATGAYL 80
Cdd:PRK07729   23 KESAFEIVAINASY-PSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDPKELPWTDLGIDIVIEATGKFN 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996  81 SLEETSSHIEAGAPRVVICAPSPDAPM-FVMGVNEKDYNPGSMKIVSNASCTTNCLAPLAKVIHERFGIVEGLMTTVHSY 159
Cdd:PRK07729  102 SKEKAILHVEAGAKKVILTAPGKNEDVtIVVGVNEDQLDIEKHTIISNASCTTNCLAPVVKVLDEQFGIENGLMTTVHAY 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 160 TATQKTVDGPsRKAWRDGRGAHQNIIPASTGAAKAVGKVIPSLKGKLTGMAFRVPTPDVSVVDLTCRLAQPAPYSAIKEA 239
Cdd:PRK07729  182 TNDQKNIDNP-HKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNVSLVDLVVDVKRDVTVEEINEA 260

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333553996 240 IKAAAKGPLAGILAYTEDEVVSTDFLGDPHSSIFDANASIALNDNFVKLISWYDNEYGYSHRVVDLLRYMFSR 312
Cdd:PRK07729  261 FKTAANGALKGILEFSEEPLVSIDFNTNTHSAIIDGLSTMVMGDRKVKVLAWYDNEWGYSCRVVDLVTLVADE 333
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 130-295 4.55e-111

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: 319.02  E-value: 4.55e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 130 CTTNCLAPLAKVIHERFGIVEGLMTTVHSYTATQKTVDGPSRKaWRDGRGAHQNIIPASTGAAKAVGKVIPSLKGKLTGM 209
Cdd:cd18126     1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPHKD-LRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 210 AFRVPTPDVSVVDLTCRLAQPAPYSAIKEAIKAAAKGPLAGILAYTEDEVVSTDFLGDPHSSIFDANASIALNDNFVKLI 289
Cdd:cd18126    80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDATATIVLGGNLVKVV 159


                  ....*.
gi 1333553996 290 SWYDNE 295
Cdd:cd18126   160 AWYDNE 165
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
4-305 8.92e-101

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 299.51  E-value: 8.92e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996   4 GVKVVAVNDPFiDPEYMVYMFKYDSTHGRYKGNVEFKNGRLVVDKQEITVFQCKQPREIPWRSVGSPFVVEATGAYLSLE 83
Cdd:PRK07403   27 QLELVAINDTS-DPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDRNPLNLPWKEWGIDLIIESTGVFVTKE 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996  84 ETSSHIEAGAPRVVICAP--SPDAPMFVMGVNEKDYNPGSMKIVSNASCTTNCLAPLAKVIHERFGIVEGLMTTVHSYTA 161
Cdd:PRK07403  106 GASKHIQAGAKKVLITAPgkGEDIGTYVVGVNHHEYDHEDHNIISNASCTTNCLAPIAKVLHDNFGIIKGTMTTTHSYTG 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 162 TQKTVDGpSRKAWRDGRGAHQNIIPASTGAAKAVGKVIPSLKGKLTGMAFRVPTPDVSVVDLTCRLAQPAPYSAIKEAIK 241
Cdd:PRK07403  186 DQRILDA-SHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTPNVSVVDLVVQVEKRTITEQVNEVLK 264

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333553996 242 AAAKGPLAGILAYTEDEVVSTDFLGDPHSSIFDANASIALNDNFVKLISWYDNEYGYSHRVVDL 305
Cdd:PRK07403  265 DASEGPLKGILEYSDLPLVSSDYRGTDASSIVDASLTMVMGGDMVKVIAWYDNEWGYSQRVVDL 328
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
4-305 2.27e-94

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 282.59  E-value: 2.27e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996   4 GVKVVAVNDPFIDPEYMVYMFKYDSTHGRYKGNVEFKNGRLVVDKQEITVFQCKQPREIPWrSVGSPFVVEATGAYLSLE 83
Cdd:NF033735   22 GLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDTPW-GDGVDVVIECTGKFKTPE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996  84 ETSSHIEAGAPRVVICAP--SPDAPMFVMGVNEKDYNPGSMKIVSNASCTTNCLAPLAKVIHERFGIVEGLMTTVHSYTA 161
Cdd:NF033735  101 KLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARHRIVTAASCTTNCLAPVVKVIHEKIGIKHGSITTIHDITN 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 162 TQKTVDGPsRKAWRDGRGAHQNIIPASTGAAKAVGKVIPSLKGKLTGMAFRVPTPDVSVVDLTCRLAQPAPYSAIKEAIK 241
Cdd:NF033735  181 TQTIVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASLTDCVFEVERPTTVEEVNALFK 259

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333553996 242 AAAKGPLAGILAYTEDEVVSTDFLGDPHSSIFDANASIALNDNFVKLISWYDNEYGYSHRVVDL 305
Cdd:NF033735  260 AAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDALSTMVVNGTQVKIYAWYDNEWGYANRMVDL 323
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
 5-305 1.44e-89

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 274.09  E-value: 1.44e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996   5 VKVVAVNDPFiDPEYMVYMFKYDSTHGRYKGNVEF-KNGRLVVDKQEITVFQCKQPREIPWRSVGSPFVVEATGAYLSLE 83
Cdd:PLN02237  102 LDVVVVNDSG-GVKNASHLLKYDSMLGTFKADVKIvDDETISVDGKPIKVVSNRDPLKLPWAELGIDIVIEGTGVFVDGP 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996  84 ETSSHIEAGAPRVVICAPSP--DAPMFVMGVNEKDYNPGSMKIVSNASCTTNCLAPLAKVIHERFGIVEGLMTTVHSYTA 161
Cdd:PLN02237  181 GAGKHIQAGAKKVIITAPAKgaDIPTYVVGVNEDDYDHEVANIVSNASCTTNCLAPFVKVLDEEFGIVKGTMTTTHSYTG 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 162 TQKTVDGpSRKAWRDGRGAHQNIIPASTGAAKAVGKVIPSLKGKLTGMAFRVPTPDVSVVDLTCRLAQPAPYSAIKEAI- 240
Cdd:PLN02237  261 DQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTPNVSVVDLVVNVEKKGITAEDVNAAf 339

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333553996 241 KAAAKGPLAGILAYTEDEVVSTDFLGDPHSSIFDANASIALNDNFVKLISWYDNEYGYSHRVVDL 305
Cdd:PLN02237  340 RKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDASLTMVMGDDMVKVVAWYDNEWGYSQRVVDL 404
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
 7-305 8.59e-89

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 270.65  E-value: 8.59e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996   7 VVAVNDPFiDPEYMVYMFKYDSTHGRYKGNVEFK-NGRLVVDKQEITVFQCKQPREIPWRSVGSPFVVEATGAYLSLEET 85
Cdd:PLN03096   89 VVAINDTG-GVKQASHLLKYDSTLGTFDADVKPVgDDAISVDGKVIKVVSDRNPLNLPWGELGIDLVIEGTGVFVDREGA 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996  86 SSHIEAGAPRVVICAPSP-DAPMFVMGVNEKDYNPgSMKIVSNASCTTNCLAPLAKVIHERFGIVEGLMTTVHSYTATQK 164
Cdd:PLN03096  168 GKHIQAGAKKVLITAPGKgDIPTYVVGVNADDYKH-SDPIISNASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQR 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 165 TVDGpSRKAWRDGRGAHQNIIPASTGAAKAVGKVIPSLKGKLTGMAFRVPTPDVSVVDLTCRLAQPAPYSAIKEAIKAAA 244
Cdd:PLN03096  247 LLDA-SHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQVEKKTFAEEVNAAFRDAA 325

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333553996 245 KGPLAGILAYTEDEVVSTDFLGDPHSSIFDANASIALNDNFVKLISWYDNEYGYSHRVVDL 305
Cdd:PLN03096  326 EKELKGILAVCDEPLVSVDFRCSDVSSTIDSSLTMVMGDDMVKVVAWYDNEWGYSQRVVDL 386
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 135-292 2.41e-83

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


Pssm-ID: 460700  Cd Length: 158  Bit Score: 248.28  E-value: 2.41e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 135 LAPLAKVIHERFGIVEGLMTTVHSYTATQKTVDGPSRKAWRDGRGAHQNIIPASTGAAKAVGKVIPSLKGKLTGMAFRVP 214
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333553996 215 TPDVSVVDLTCRLAQPAPYSAIKEAIKAAAKGPLAGILAYTEDEVVSTDFLGDPHSSIFDANASIALNDNFVKLISWY 292
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAKETIVVNGNFVKVVAWY 158
PRK08955 PRK08955
glyceraldehyde-3-phosphate dehydrogenase; Validated
 5-307 7.87e-81

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 169599 [Multi-domain]  Cd Length: 334  Bit Score: 248.49  E-value: 7.87e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996   5 VKVVAVNDPFIDPEYMVYMFKYDSTHGRYKGNVEFKNGRLVVDKQEITVFQCKQPREIPWRsvGSPFVVEATGAYLSLEE 84
Cdd:PRK08955   27 LEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKAIADTDWS--GCDVVIEASGVMKTKAL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996  85 TSSHIEAGAPRVVICAP--SPDAPMFVMGVNEKDYNPGSMKIVSNASCTTNCLAPLAKVIHERFGIVEGLMTTVHSYTAT 162
Cdd:PRK08955  105 LQAYLDQGVKRVVVTAPvkEEGVLNIVMGVNDHLFDPAIHPIVTAASCTTNCLAPVVKVIHEKLGIKHGSMTTIHDLTNT 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 163 QKTVDGPsRKAWRDGRGAHQNIIPASTGAAKAVGKVIPSLKGKLTGMAFRVPTPDVSVVDLTCRLAQPAPYSAIKEAIKA 242
Cdd:PRK08955  185 QTILDAP-HKDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLANASLTDCVFEVERDTTVEEVNALLKE 263

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333553996 243 AAKGPLAGILAYTEDEVVSTDFLGDPHSSIFDANASIALNDNFVKLISWYDNEYGYSHRVVDLLR 307
Cdd:PRK08955  264 AAEGELKGILGYEERPLVSIDYKTDPRSSIVDALSTMVVNGTQVKLYAWYDNEWGYANRTAELAR 328
E4PD_g-proteo TIGR01532
erythrose-4-phosphate dehydrogenase; This model represents the small clade of dehydrogenases ...
 4-304 1.53e-76

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: 237.10  E-value: 1.53e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996   4 GVKVVAVNDpFIDPEYMVYMFKYDSTHGRYKGNVEFKNGRLVVDKQEITVFQCKQPREIPWRSVGSPFVVEATGAYLSLE 83
Cdd:TIGR01532  26 EITVVAINE-LADAAGMAHLLKYDTSHGRFAWEVRQDRDQLFVGDDAIRVLHERSLQSLPWRELGVDLVLDCTGVYGSRE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996  84 ETSSHIEAGAPRVVICAPSP---DAPMfVMGVNEKDYNpGSMKIVSNASCTTNCLAPLAKVIHERFGIVEGLMTTVHSYT 160
Cdd:TIGR01532 105 HGEAHIAAGAKKVLFSHPGAsdlDATI-VYGVNQDQLR-AEHRIVSNASCTTNCIVPVIKLLDDAYGIESGTITTIHSAM 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 161 ATQKTVDGpSRKAWRDGRGAHQNIIPASTGAAKAVGKVIPSLKGKLTGMAFRVPTPDVSVVDLTCRLAQPAPYSAIKEAI 240
Cdd:TIGR01532 183 NDQQVIDA-YHPDLRRTRAASQSIIPVDTKLAAGIERFFPQFNDRFEAIAVRVPTVNVTAIDLSVTVKKPVKANEVNLLL 261

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333553996 241 KAAAKGPLAGILAYTEDEVVSTDFLGDPHSSIFDANASIALNDNFVKLISWYDNEYGYSHRVVD 304
Cdd:TIGR01532 262 QKAAQGALRGIVDYTELPLVSVDFNHDPHSAIVDGTQTRVSGAHLVKTLVWCDNEWGFANRMLD 325
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 130-295 1.41e-75

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: 229.04  E-value: 1.41e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 130 CTTNCLAPLAKVIHERFGIVEGLMTTVHSYTATQKTVDGPSRKAWRDGRGAHQNIIPASTGAAKAVGKVIPSLKGKLTGM 209
Cdd:cd18123     1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 210 AFRVPTPDVSVVDLTCRLAQPAPYSAIKEAIKAAAKGPlaGILAYTEDEVVSTDFLGDPHSSIFDANASIALNDNFVKLI 289
Cdd:cd18123    81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEGK--GRLGYTEAEDVSSDFRGDIFESVFDAESIIAVNDNEVKLM 158


                  ....*.
gi 1333553996 290 SWYDNE 295
Cdd:cd18123   159 QWYDNE 164
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
 5-309 1.66e-74

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 232.25  E-value: 1.66e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996   5 VKVVAVNDpFIDPEYMVYMFKYDSTHGRYKGNVEFKNGRLVVDKQEITVFQCKQPREIPWRSVGSPFVVEATGAYLSLEE 84
Cdd:PRK13535   29 ITVVAINE-LADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHERDIASLPWRELGVDVVLDCTGVYGSRED 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996  85 TSSHIEAGAPRVVICAPSP---DAPMfVMGVNEKDYNPGSmKIVSNASCTTNCLAPLAKVIHERFGIVEGLMTTVHSYTA 161
Cdd:PRK13535  108 GEAHIAAGAKKVLFSHPGSndlDATV-VYGVNHDQLRAEH-RIVSNASCTTNCIIPVIKLLDDAFGIESGTVTTIHSAMN 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 162 TQKTVDGpSRKAWRDGRGAHQNIIPASTGAAKAVGKVIPSLKGKLTGMAFRVPTPDVSVVDLTCRLAQPAPYSAIKEAIK 241
Cdd:PRK13535  186 DQQVIDA-YHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPTINVTAIDLSVTVKKPVKVNEVNQLLQ 264

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333553996 242 AAAKGPLAGILAYTEDEVVSTDFLGDPHSSIFDANASIALNDNFVKLISWYDNEYGYSHRVVDLLRYM 309
Cdd:PRK13535  265 KAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVDGTQTRVSGAHLIKTLVWCDNEWGFANRMLDTTLAM 332
PRK08289 PRK08289
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
 25-309 1.23e-71

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 236219 [Multi-domain]  Cd Length: 477  Bit Score: 229.04  E-value: 1.23e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996  25 KYDSTHGRYKGNVEF--KNGRLVVDKQEITVFQCKQPREIPWRSVG--SPFVVEATGAYLSLEETSSHIEA-GAPRVVIC 99
Cdd:PRK08289  179 RRDSVHGPFNGTITVdeENNAIIANGNYIQVIYANSPEEVDYTAYGinNALVVDNTGKWRDEEGLSQHLKSkGVAKVLLT 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 100 APSP-DAPMFVMGVNEKDYNPgSMKIVSNASCTTNCLAPLAKVIHERFGIVEGLMTTVHSYTATQKTVDGpSRKAWRDGR 178
Cdd:PRK08289  259 APGKgDIKNIVHGVNHSDITD-EDKIVSAASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDN-YHKGDRRGR 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 179 GAHQNIIPASTGAAKAVGKVIPSLKGKLTGMAFRVPTPDVSVVDLTCRLAQPAPY-SAIKEAIKAAAKGPLAGILAYTED 257
Cdd:PRK08289  337 SAPLNMVITETGAAKAVAKALPELAGKLTGNAIRVPTPNVSMAILNLNLEKETSReELNEYLRQMSLHSPLQNQIDYTDS 416

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1333553996 258 -EVVSTDFLGDPHSSIFDANASIALNDNFVkLISWYDNEYGYSHRVVDLLRYM 309
Cdd:PRK08289  417 tEVVSSDFVGSRHAGVVDSQATIVNGNRAV-LYVWYDNEFGYSCQVVRVMEQM 468
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 3-129 1.72e-58

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: 185.29  E-value: 1.72e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996   3 KGVKVVAVNDPFiDPEYMVYMFKYDSTHGRYKGNVEFKNGRLVVDKQEITVFQCKQPREIPWRSVGSPFVVEATGAYLSL 82
Cdd:cd05214    23 DDIEVVAINDLT-DDETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAELPWGELGVDIVIESTGVFTTK 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1333553996  83 EETSSHIEAGAPRVVICAPSPD-APMFVMGVNEKDYNPgSMKIVSNAS 129
Cdd:cd05214   102 EKASAHLKAGAKKVIISAPAKDdDPTIVMGVNHDKYDA-DDKIISNAS 148
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-130 1.20e-53

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: 172.35  E-value: 1.20e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996    1 MEKGVKVVAVNDPfIDPEYMVYMFKYDSTHGRYKGNVEFKNGRLVVDKQEITVFQCKQPREIPWRSVGSPFVVEATGAYL 80
Cdd:smart00846  21 ERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANLPWGELGVDIVVECTGGFT 99

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1333553996   81 SLEETSSHIEAGAPRVVICAPSPDA-PMFVMGVNEKDYNPgSMKIVSNASC 130
Cdd:smart00846 100 TREKASAHLKAGAKKVIISAPSKDAdPTFVYGVNHDEYDG-EDHIISNASC 149
GAPDH_C_E4PDH cd23937
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 130-295 4.12e-41

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: 140.63  E-value: 4.12e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 130 CTTNCLAPLAKVIHERFGIVEGLMTTVHSYTATQKTVDGpSRKAWRDGRGAHQNIIPASTGAAKAVGKVIPSLKGKLTGM 209
Cdd:cd23937     1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 210 AFRVPTPDVSVVDLTCRLAQPAPYSAIKEAIKAAAKGPLAGILAYTEDEVVSTDFLGDPHSSIFDANASIALNDNFVKLI 289
Cdd:cd23937    80 AVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDGTQTRVSGKRLVKLL 159


                  ....*.
gi 1333553996 290 SWYDNE 295
Cdd:cd23937   160 VWCDNE 165
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 130-295 2.98e-39

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: 135.72  E-value: 2.98e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 130 CTTNCLAPLAKVIHERFGIVEGLMTTVHSYTATQKTVDGPSRKAWrdGRGAHQNIIPASTGAAKAVGKVIPSL--KGKLT 207
Cdd:cd18122     1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIgkPIKVD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 208 GMAFRVPTPDVSVVDLTCRLAQPAPYSAIKEAIKAAAKGPLAGILAYTEDEVVSTDFLGDPHSSIFDANASIALNDNFVK 287
Cdd:cd18122    79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQREFAFDDNKLK 158


                  ....*...
gi 1333553996 288 LISWYDNE 295
Cdd:cd18122   159 VFSAVDNE 166
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
 5-313 6.22e-39

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 140.01  E-value: 6.22e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996   5 VKVVAVNDPFIDPEYMVYMFKYDSTHGRYKGNVEFKNGRLVV--DKQEITVFQCKQPREIPWRSVGSPFVVEATGAYLSL 82
Cdd:PTZ00353   27 VTVVAVNDASVSIAYIAYVLEQESPLSAPDGASIRVVGEQIVlnGTQKIRVSAKHDLVEIAWRDYGVQYVVECTGLYSTR 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996  83 EETSSHIEAGAPRVVICAPSPDAPMFVMGVNEKDYNpGSMKIVSNASCTTNCLAPLAKVIHERFGIVEGLMTTVHSyTAT 162
Cdd:PTZ00353  107 SRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDERLS-ASLPVCCAGAPIAVALAPVIRALHEVYGVEECSYTAIHG-MQP 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996 163 QKTVDGPSRKA--WRDGRGAHQNIIPASTGAAKAVGKVIPSLKGKLTGMAFRVPTPDVSVVDLTCRLAQPAPYSAIKEAI 240
Cdd:PTZ00353  185 QEPIAARSKNSqdWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVKKGCAIDMLVRTKQPVSKEVVDSAL 264

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333553996 241 KAAAKGPLAGILAYTEDEVVSTDFLGDpHSSIFDANASIALNDNFV-KLISWYDNEYGYSHRVVDLLRYMFSRD 313
Cdd:PTZ00353  265 AEAASDRLNGVLCISKRDMISVDCIPN-GKLCYDATSSSSSREGEVhKMVLWFDVECYYAARLLSLVKQLHQIH 337
GAPDH_N_E4PDH cd17892
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 3-129 2.61e-34

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: 123.15  E-value: 2.61e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333553996   3 KGVKVVAVNDPfIDPEYMVYMFKYDSTHGRYKGNVEFKNGRLVVDKQEITVFQCKQPREIPWRSVGSPFVVEATGAYLSL 82
Cdd:cd17892    26 AEFQVVAINEL-ADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPDPENLPWRELGIDLVLECTGVFGSR 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1333553996  83 EETSSHIEAGAPRVVICAPSP---DAPMfVMGVNEKDYNPgSMKIVSNAS 129
Cdd:cd17892   105 EDAERHLAAGAKKVLFSHPASndvDATI-VYGINQDLLRA-EHRIVSNAS 152
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 3-81 4.54e-32

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: 114.89  E-value: 4.54e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333553996   3 KGVKVVAVNDpFIDPEYMVYMFKYDSTHGRYKGNVEFKNGRLVVDKQEITVFQCKQPREIPWRSVGSPFVVEATGAYLS 81
Cdd:pfam00044  23 PDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAELPWGDLGVDVVIESTGVFTT 100
GAPDH-like_N cd05192
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ...
 72-134 1.00e-03

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: 38.10  E-value: 1.00e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333553996  72 VVEATGAYLSLEETSSHIEAGAPRVVICAPSP-DAPMFVMGVNEKDYNPGSmKIVSNASCTTNC 134
Cdd:cd05192    37 VIECTGSFTDDDNAEKHIKAGGKKAVITAPEKgDIPTIVVVLNELAKSAGA-TVVSNANETSYS 99
Asd COG0136
Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; ...
 90-148 5.44e-03

Aspartate-semialdehyde dehydrogenase [Amino acid transport and metabolism]; Aspartate-semialdehyde dehydrogenase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439906 [Multi-domain]  Cd Length: 333  Bit Score: 38.09  E-value: 5.44e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333553996  90 EAGAprVVICAPS-----PDAPMFVMGVNE---KDYNPGsmKIVSNASCTTNCLAPLAKVIHERFGI 148
Cdd:COG0136    84 AAGA--VVIDNSSafrmdPDVPLVVPEVNPealADHLPK--GIIANPNCSTIQMLVALKPLHDAAGI 146
 
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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