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Conserved domains on  [gi|338173024|gb|AEI83275|]
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glyceraldehyde-3-phosphate dehydrogenase, partial [Hypogymnia tubulosa]

Protein Classification

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

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

CATH:  3.30.360.10|3.40.50.720
EC:  1.2.1.-
Gene Ontology:  GO:0006006|GO:0006096|GO:0030554|GO:0016620
PubMed:  21895736|25286305
SCOP:  4000077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 4-274 4.50e-166

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: 462.94  E-value: 4.50e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024   4 DVKVVAVNDPfIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFTTTE 83
Cdd:COG0057   27 DIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAELPWGELGVDVVIECTGKFTDRE 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024  84 KAKAHLKGGAKKVVISAPSADA-AMFVMGVNEK*YKSDI*II*NASCT*NCLAPLAKVMHDNFTIIEGLMTTIHSYTA*Q 162
Cdd:COG0057  106 KASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAPVAKVLNDAFGIEKGLMTTIHAYTNDQ 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024 163 KTVDGPSsKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKETMKKA 242
Cdd:COG0057  186 NLLDAPH-KDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVELEKETTVEEVNAALKEA 264

                        250       260       270
                 ....*....|....*....|....*....|..
gi 338173024 243 SEGELKGIMSYSEDALVSTDLNGDNHSCIFDA 274
Cdd:COG0057  265 AEGPLKGILGYTEEPLVSSDFNGDPHSSIFDA 296
 
Name Accession Description Interval E-value
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 4-274 4.50e-166

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: 462.94  E-value: 4.50e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024   4 DVKVVAVNDPfIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFTTTE 83
Cdd:COG0057   27 DIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAELPWGELGVDVVIECTGKFTDRE 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024  84 KAKAHLKGGAKKVVISAPSADA-AMFVMGVNEK*YKSDI*II*NASCT*NCLAPLAKVMHDNFTIIEGLMTTIHSYTA*Q 162
Cdd:COG0057  106 KASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAPVAKVLNDAFGIEKGLMTTIHAYTNDQ 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024 163 KTVDGPSsKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKETMKKA 242
Cdd:COG0057  186 NLLDAPH-KDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVELEKETTVEEVNAALKEA 264

                        250       260       270
                 ....*....|....*....|....*....|..
gi 338173024 243 SEGELKGIMSYSEDALVSTDLNGDNHSCIFDA 274
Cdd:COG0057  265 AEGPLKGILGYTEEPLVSSDFNGDPHSSIFDA 296
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 4-274 3.34e-164

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 461.63  E-value: 3.34e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024   4 DVKVVAVNDPFIEPHYAAYMLKYDSQHGQFKGTIEV-KGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFTTT 82
Cdd:PLN02272 109 DIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDPAEIPWGDFGAEYVVESSGVFTTV 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024  83 EKAKAHLKGGAKKVVISAPSADAAMFVMGVNEK*YKSDI*II*NASCT*NCLAPLAKVMHDNFTIIEGLMTTIHSYTA*Q 162
Cdd:PLN02272 189 EKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQ 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024 163 KTVDGPSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKETMKKA 242
Cdd:PLN02272 269 KTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYA 348

                        250       260       270
                 ....*....|....*....|....*....|..
gi 338173024 243 SEGELKGIMSYSEDALVSTDLNGDNHSCIFDA 274
Cdd:PLN02272 349 SEGPLKGILGYTDEDVVSNDFVGDSRSSIFDA 380
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 4-274 8.56e-139

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: 393.57  E-value: 8.56e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024    4 DVKVVAVNDPfIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFY-TEKDPANIPWKDTGAYYIVESTGVFTTT 82
Cdd:TIGR01534  25 DLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEVISVfSERDPSDLPWKALGVDIVIECTGKFRDK 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024   83 EKAKAHLKGGAKKVVISAPSADAA-MFVMGVNEK*YKSDI*II*NASCT*NCLAPLAKVMHDNFTIIEGLMTTIHSYTA* 161
Cdd:TIGR01534 104 EKLEKHLEAGAKKVLISAPSKGDVkTIVYGVNHDEYDGEERIISNASCTTNCLAPLAKVLDEAFGIVSGLMTTVHAYTND 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024  162 QKTVDGPsSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKETMKK 241
Cdd:TIGR01534 184 QNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNVSLVDLVVNLEKDVTVEEVNAALKE 262

                         250       260       270
                  ....*....|....*....|....*....|...
gi 338173024  242 ASEGELKGIMSYSEDALVSTDLNGDNHSCIFDA 274
Cdd:TIGR01534 263 ASEGELKGVLGYTEDELVSSDFIGSPYSSIVDA 295
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 129-274 2.78e-101

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: 292.44  E-value: 2.78e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024 129 CT*NCLAPLAKVMHDNFTIIEGLMTTIHSYTA*QKTVDGPSsKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGM 208
Cdd:cd18126    1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338173024 209 SMRVPTSNVSVVDLTCRLEKSVTYDQIKETMKKASEGELKGIMSYSEDALVSTDLNGDNHSCIFDA 274
Cdd:cd18126   80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDA 145
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
1-274 1.63e-86

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 261.02  E-value: 1.63e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024   1 EHGDVKVVAVNDPFIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDtGAYYIVESTGVFT 80
Cdd:NF033735  19 GRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDTPWGD-GVDVVIECTGKFK 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024  81 TTEKAKAHLKGGAKKVVISAP--SADAAMFVMGVNEK*YKSDI-*II*NASCT*NCLAPLAKVMHDNFTIIEGLMTTIHS 157
Cdd:NF033735  98 TPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARhRIVTAASCTTNCLAPVVKVIHEKIGIKHGSITTIHD 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024 158 YTA*QKTVDGPsSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKE 237
Cdd:NF033735 178 ITNTQTIVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASLTDCVFEVERPTTVEEVNA 256

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 338173024 238 TMKKASEGELKGIMSYSEDALVSTDLNGDNHSCIFDA 274
Cdd:NF033735 257 LFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDA 293
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 134-274 1.07e-81

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: 242.50  E-value: 1.07e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024  134 LAPLAKVMHDNFTIIEGLMTTIHSYTA*QKTVDGPSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVP 213
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338173024  214 TSNVSVVDLTCRLEKSVTYDQIKETMKKASEGELKGIMSYSEDALVSTDLNGDNHSCIFDA 274
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDA 141
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-129 7.04e-60

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


Pssm-ID: 214851 [Multi-domain]  Cd Length: 149  Bit Score: 186.99  E-value: 7.04e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024     1 EHGDVKVVAVNDPfIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFT 80
Cdd:smart00846  21 ERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANLPWGELGVDIVVECTGGFT 99

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 338173024    81 TTEKAKAHLKGGAKKVVISAPSADAA-MFVMGVNEK*YKSDI*II*NASC 129
Cdd:smart00846 100 TREKASAHLKAGAKKVIISAPSKDADpTFVYGVNHDEYDGEDHIISNASC 149
 
Name Accession Description Interval E-value
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 4-274 4.50e-166

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: 462.94  E-value: 4.50e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024   4 DVKVVAVNDPfIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFTTTE 83
Cdd:COG0057   27 DIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAELPWGELGVDVVIECTGKFTDRE 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024  84 KAKAHLKGGAKKVVISAPSADA-AMFVMGVNEK*YKSDI*II*NASCT*NCLAPLAKVMHDNFTIIEGLMTTIHSYTA*Q 162
Cdd:COG0057  106 KASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAPVAKVLNDAFGIEKGLMTTIHAYTNDQ 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024 163 KTVDGPSsKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKETMKKA 242
Cdd:COG0057  186 NLLDAPH-KDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVELEKETTVEEVNAALKEA 264

                        250       260       270
                 ....*....|....*....|....*....|..
gi 338173024 243 SEGELKGIMSYSEDALVSTDLNGDNHSCIFDA 274
Cdd:COG0057  265 AEGPLKGILGYTEEPLVSSDFNGDPHSSIFDA 296
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 4-274 3.34e-164

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 461.63  E-value: 3.34e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024   4 DVKVVAVNDPFIEPHYAAYMLKYDSQHGQFKGTIEV-KGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFTTT 82
Cdd:PLN02272 109 DIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDPAEIPWGDFGAEYVVESSGVFTTV 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024  83 EKAKAHLKGGAKKVVISAPSADAAMFVMGVNEK*YKSDI*II*NASCT*NCLAPLAKVMHDNFTIIEGLMTTIHSYTA*Q 162
Cdd:PLN02272 189 EKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQ 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024 163 KTVDGPSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKETMKKA 242
Cdd:PLN02272 269 KTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYA 348

                        250       260       270
                 ....*....|....*....|....*....|..
gi 338173024 243 SEGELKGIMSYSEDALVSTDLNGDNHSCIFDA 274
Cdd:PLN02272 349 SEGPLKGILGYTDEDVVSNDFVGDSRSSIFDA 380
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 4-274 8.56e-139

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: 393.57  E-value: 8.56e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024    4 DVKVVAVNDPfIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFY-TEKDPANIPWKDTGAYYIVESTGVFTTT 82
Cdd:TIGR01534  25 DLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEVISVfSERDPSDLPWKALGVDIVIECTGKFRDK 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024   83 EKAKAHLKGGAKKVVISAPSADAA-MFVMGVNEK*YKSDI*II*NASCT*NCLAPLAKVMHDNFTIIEGLMTTIHSYTA* 161
Cdd:TIGR01534 104 EKLEKHLEAGAKKVLISAPSKGDVkTIVYGVNHDEYDGEERIISNASCTTNCLAPLAKVLDEAFGIVSGLMTTVHAYTND 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024  162 QKTVDGPsSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKETMKK 241
Cdd:TIGR01534 184 QNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNVSLVDLVVNLEKDVTVEEVNAALKE 262

                         250       260       270
                  ....*....|....*....|....*....|...
gi 338173024  242 ASEGELKGIMSYSEDALVSTDLNGDNHSCIFDA 274
Cdd:TIGR01534 263 ASEGELKGVLGYTEDELVSSDFIGSPYSSIVDA 295
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
 1-273 2.50e-129

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 370.32  E-value: 2.50e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024   1 EHGDVKVVAVNDPFIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFT 80
Cdd:PTZ00023  23 EREDVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKDPAAIPWGKNGVDVVCESTGVFL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024  81 TTEKAKAHLKGGAKKVVISAPSADAA-MFVMGVNEK*YKSDI*II*NASCT*NCLAPLAKVMHDNFTIIEGLMTTIHSYT 159
Cdd:PTZ00023 103 TKEKAQAHLKGGAKKVIMSAPPKDDTpIYVMGVNHTQYDKSQRIVSNASCTTNCLAPLAKVVNDKFGIVEGLMTTVHAST 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024 160 A*QKTVDGPS--SKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKE 237
Cdd:PTZ00023 183 ANQLTVDGPSkgGKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVPDVSVVDLTCKLAKPAKYEEIVA 262

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 338173024 238 TMKKASEGELKGIMSYSEDALVSTDLNGDNHSCIFD 273
Cdd:PTZ00023 263 AVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFD 298
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
 1-274 6.31e-126

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 361.73  E-value: 6.31e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024   1 EHGDVKVVAVNDPFIEPHYAAYMLKYDSQHGQFK-GTIEVKGSDLVVNGQT-VKFYTEKDPANIPWKDTGAYYIVESTGV 78
Cdd:PLN02358  26 QRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKhHELKVKDDKTLLFGEKpVTVFGIRNPEDIPWGEAGADFVVESTGV 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024  79 FTTTEKAKAHLKGGAKKVVISAPSADAAMFVMGVNEK*YKSDI*II*NASCT*NCLAPLAKVMHDNFTIIEGLMTTIHSY 158
Cdd:PLN02358 106 FTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCTTNCLAPLAKVINDRFGIVEGLMTTVHSI 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024 159 TA*QKTVDGPSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKET 238
Cdd:PLN02358 186 TATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRLEKAATYDEIKKA 265

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 338173024 239 MKKASEGELKGIMSYSEDALVSTDLNGDNHSCIFDA 274
Cdd:PLN02358 266 IKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDA 301
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
1-274 8.63e-116

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 335.55  E-value: 8.63e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024   1 EHGDVKVVAVNDpFIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFT 80
Cdd:PRK15425  23 KRSDIEIVAIND-LLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPANLKWDEVGVDVVAEATGLFL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024  81 TTEKAKAHLKGGAKKVVISAPSAD-AAMFVMGVNEK*YKSDi*II*NASCT*NCLAPLAKVMHDNFTIIEGLMTTIHSYT 159
Cdd:PRK15425 102 TDETARKHITAGAKKVVMTGPSKDnTPMFVKGANFDKYAGQ-DIVSNASCTTNCLAPLAKVINDNFGIIEGLMTTVHATT 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024 160 A*QKTVDGPSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKETM 239
Cdd:PRK15425 181 ATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAATYEQIKAAV 260

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 338173024 240 KKASEGELKGIMSYSEDALVSTDLNGDNHSCIFDA 274
Cdd:PRK15425 261 KAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDA 295
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-273 5.04e-107

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 313.60  E-value: 5.04e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024   1 EHGDVKVVAVNDPFiEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFT 80
Cdd:PRK07729  23 KESAFEIVAINASY-PSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDPKELPWTDLGIDIVIEATGKFN 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024  81 TTEKAKAHLKGGAKKVVISAPSADA-AMFVMGVNEK*YKSDI-*II*NASCT*NCLAPLAKVMHDNFTIIEGLMTTIHSY 158
Cdd:PRK07729 102 SKEKAILHVEAGAKKVILTAPGKNEdVTIVVGVNEDQLDIEKhTIISNASCTTNCLAPVVKVLDEQFGIENGLMTTVHAY 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024 159 TA*QKTVDGPSsKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKET 238
Cdd:PRK07729 182 TNDQKNIDNPH-KDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNVSLVDLVVDVKRDVTVEEINEA 260

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 338173024 239 MKKASEGELKGIMSYSEDALVSTDLNGDNHSCIFD 273
Cdd:PRK07729 261 FKTAANGALKGILEFSEEPLVSIDFNTNTHSAIID 295
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 4-274 4.13e-105

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 309.68  E-value: 4.13e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024   4 DVKVVAVNDPFIEPHYAAYMLKYDSQHGQFKGTIE-------VKGSD-LVVNGQTVK-FYTEKDPANIPWKDTGAYYIVE 74
Cdd:PTZ00434  31 EIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVEttksspsVKTDDvLVVNGHRIKcVKAQRNPADLPWGKLGVDYVIE 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024  75 STGVFTTTEKAKAHLKGGAKKVVISAP-SADAAMFVMGVNEK*YK-SDI*II*NASCT*NCLAPLAKVM-HDNFTIIEGL 151
Cdd:PTZ00434 111 STGLFTDKLAAEGHLKGGAKKVVISAPaSGGAKTIVMGVNQHEYSpTEHHVVSNASCTTNCLAPIVHVLtKEGFGIETGL 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024 152 MTTIHSYTA*QKTVDGPSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVT 231
Cdd:PTZ00434 191 MTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGKLTGMSFRVPTPDVSVVDLTFRATRDTS 270

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 338173024 232 YDQIKETMKKASEGELKGIMSYSEDALVSTDLNGDNHSCIFDA 274
Cdd:PTZ00434 271 IQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDS 313
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 129-274 2.78e-101

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: 292.44  E-value: 2.78e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024 129 CT*NCLAPLAKVMHDNFTIIEGLMTTIHSYTA*QKTVDGPSsKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGM 208
Cdd:cd18126    1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338173024 209 SMRVPTSNVSVVDLTCRLEKSVTYDQIKETMKKASEGELKGIMSYSEDALVSTDLNGDNHSCIFDA 274
Cdd:cd18126   80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDA 145
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
1-274 1.43e-100

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 297.20  E-value: 1.43e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024   1 EHGDVKVVAVNDPfIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFT 80
Cdd:PRK07403  24 ENSQLELVAINDT-SDPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDRNPLNLPWKEWGIDLIIESTGVFV 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024  81 TTEKAKAHLKGGAKKVVISAP--SADAAMFVMGVNEK*YKSDI-*II*NASCT*NCLAPLAKVMHDNFTIIEGLMTTIHS 157
Cdd:PRK07403 103 TKEGASKHIQAGAKKVLITAPgkGEDIGTYVVGVNHHEYDHEDhNIISNASCTTNCLAPIAKVLHDNFGIIKGTMTTTHS 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024 158 YTA*QKTVDGpSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKE 237
Cdd:PRK07403 183 YTGDQRILDA-SHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTPNVSVVDLVVQVEKRTITEQVNE 261

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 338173024 238 TMKKASEGELKGIMSYSEDALVSTDLNGDNHSCIFDA 274
Cdd:PRK07403 262 VLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDA 298
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
1-274 1.63e-86

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 261.02  E-value: 1.63e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024   1 EHGDVKVVAVNDPFIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDtGAYYIVESTGVFT 80
Cdd:NF033735  19 GRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDTPWGD-GVDVVIECTGKFK 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024  81 TTEKAKAHLKGGAKKVVISAP--SADAAMFVMGVNEK*YKSDI-*II*NASCT*NCLAPLAKVMHDNFTIIEGLMTTIHS 157
Cdd:NF033735  98 TPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARhRIVTAASCTTNCLAPVVKVIHEKIGIKHGSITTIHD 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024 158 YTA*QKTVDGPsSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKE 237
Cdd:NF033735 178 ITNTQTIVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASLTDCVFEVERPTTVEEVNA 256

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 338173024 238 TMKKASEGELKGIMSYSEDALVSTDLNGDNHSCIFDA 274
Cdd:NF033735 257 LFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDA 293
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
 7-274 8.33e-83

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 253.70  E-value: 8.33e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024   7 VVAVNDPFiEPHYAAYMLKYDSQHGQFKGTIEVKGSD-LVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFTTTEKA 85
Cdd:PLN03096  89 VVAINDTG-GVKQASHLLKYDSTLGTFDADVKPVGDDaISVDGKVIKVVSDRNPLNLPWGELGIDLVIEGTGVFVDREGA 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024  86 KAHLKGGAKKVVISAPS-ADAAMFVMGVNEK*YKSDI*II*NASCT*NCLAPLAKVMHDNFTIIEGLMTTIHSYTA*QKT 164
Cdd:PLN03096 168 GKHIQAGAKKVLITAPGkGDIPTYVVGVNADDYKHSDPIISNASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRL 247

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024 165 VDGpSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKETMKKASE 244
Cdd:PLN03096 248 LDA-SHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQVEKKTFAEEVNAAFRDAAE 326

                        250       260       270
                 ....*....|....*....|....*....|
gi 338173024 245 GELKGIMSYSEDALVSTDLNGDNHSCIFDA 274
Cdd:PLN03096 327 KELKGILAVCDEPLVSVDFRCSDVSSTIDS 356
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 134-274 1.07e-81

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: 242.50  E-value: 1.07e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024  134 LAPLAKVMHDNFTIIEGLMTTIHSYTA*QKTVDGPSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVP 213
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 338173024  214 TSNVSVVDLTCRLEKSVTYDQIKETMKKASEGELKGIMSYSEDALVSTDLNGDNHSCIFDA 274
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDA 141
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
 5-274 6.49e-80

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 247.89  E-value: 6.49e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024   5 VKVVAVNDPF-IEPhyAAYMLKYDSQHGQFKGTIE-VKGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFTTT 82
Cdd:PLN02237 102 LDVVVVNDSGgVKN--ASHLLKYDSMLGTFKADVKiVDDETISVDGKPIKVVSNRDPLKLPWAELGIDIVIEGTGVFVDG 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024  83 EKAKAHLKGGAKKVVISAPS--ADAAMFVMGVNEK*YKSDI*-II*NASCT*NCLAPLAKVMHDNFTIIEGLMTTIHSYT 159
Cdd:PLN02237 180 PGAGKHIQAGAKKVIITAPAkgADIPTYVVGVNEDDYDHEVAnIVSNASCTTNCLAPFVKVLDEEFGIVKGTMTTTHSYT 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024 160 A*QKTVDGpSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKS-VTYDQIKET 238
Cdd:PLN02237 260 GDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTPNVSVVDLVVNVEKKgITAEDVNAA 338

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 338173024 239 MKKASEGELKGIMSYSEDALVSTDLNGDNHSCIFDA 274
Cdd:PLN02237 339 FRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDA 374
PRK08955 PRK08955
glyceraldehyde-3-phosphate dehydrogenase; Validated
 4-274 1.05e-75

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 169599 [Multi-domain]  Cd Length: 334  Bit Score: 233.47  E-value: 1.05e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024   4 DVKVVAVNDPFIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWkdTGAYYIVESTGVFTTTE 83
Cdd:PRK08955  26 ELEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKAIADTDW--SGCDVVIEASGVMKTKA 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024  84 KAKAHLKGGAKKVVISAPSAD--AAMFVMGVNEK*YKSDI-*II*NASCT*NCLAPLAKVMHDNFTIIEGLMTTIHSYTA 160
Cdd:PRK08955 104 LLQAYLDQGVKRVVVTAPVKEegVLNIVMGVNDHLFDPAIhPIVTAASCTTNCLAPVVKVIHEKLGIKHGSMTTIHDLTN 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024 161 *QKTVDGPsSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKETMK 240
Cdd:PRK08955 184 TQTILDAP-HKDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLANASLTDCVFEVERDTTVEEVNALLK 262

                        250       260       270
                 ....*....|....*....|....*....|....
gi 338173024 241 KASEGELKGIMSYSEDALVSTDLNGDNHSCIFDA 274
Cdd:PRK08955 263 EAAEGELKGILGYEERPLVSIDYKTDPRSSIVDA 296
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
 2-273 7.46e-74

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 228.79  E-value: 7.46e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024   2 HGDVKVVAVNDpFIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFTT 81
Cdd:PRK13535  26 RAEITVVAINE-LADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHERDIASLPWRELGVDVVLDCTGVYGS 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024  82 TEKAKAHLKGGAKKVVISAPSA---DAAMfVMGVNEK*YKSDI*II*NASCT*NCLAPLAKVMHDNFTIIEGLMTTIHSY 158
Cdd:PRK13535 105 REDGEAHIAAGAKKVLFSHPGSndlDATV-VYGVNHDQLRAEHRIVSNASCTTNCIIPVIKLLDDAFGIESGTVTTIHSA 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024 159 TA*QKTVDGPSSkDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKET 238
Cdd:PRK13535 184 MNDQQVIDAYHP-DLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPTINVTAIDLSVTVKKPVKVNEVNQL 262

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 338173024 239 MKKASEGELKGIMSYSEDALVSTDLNGDNHSCIFD 273
Cdd:PRK13535 263 LQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVD 297
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 1-128 2.29e-67

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: 206.48  E-value: 2.29e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024   1 EHGDVKVVAVNDPFIePHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFT 80
Cdd:cd05214   21 ERDDIEVVAINDLTD-DETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAELPWGELGVDIVIESTGVFT 99

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 338173024  81 TTEKAKAHLKGGAKKVVISAPSADAA-MFVMGVNEK*YKSDI*II*NAS 128
Cdd:cd05214  100 TKEKASAHLKAGAKKVIISAPAKDDDpTIVMGVNHDKYDADDKIISNAS 148
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 129-274 2.93e-66

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: 203.62  E-value: 2.93e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024 129 CT*NCLAPLAKVMHDNFTIIEGLMTTIHSYTA*QKTVDGPSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGM 208
Cdd:cd18123    1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338173024 209 SMRVPTSNVSVVDLTCRLEKSVTYDQIKETMKKASEGelKGIMSYSEDALVSTDLNGDNHSCIFDA 274
Cdd:cd18123   81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIFESVFDA 144
PRK08289 PRK08289
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
 21-274 8.72e-66

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 236219 [Multi-domain]  Cd Length: 477  Bit Score: 212.48  E-value: 8.72e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024  21 AYMLKYDSQHGQFKGTIEV--KGSDLVVNGQTVKFYTEKDPANIpwkDTGAYYI-----VESTGVFTTTEKAKAHLKG-G 92
Cdd:PRK08289 175 ASLLRRDSVHGPFNGTITVdeENNAIIANGNYIQVIYANSPEEV---DYTAYGInnalvVDNTGKWRDEEGLSQHLKSkG 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024  93 AKKVVISAPS-ADAAMFVMGVNEK*YKSDI*II*NASCT*NCLAPLAKVMHDNFTIIEGLMTTIHSYTA*QKTVDGPSSK 171
Cdd:PRK08289 252 VAKVLLTAPGkGDIKNIVHGVNHSDITDEDKIVSAASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKG 331

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024 172 DwRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKETMKKAS-EGELKGI 250
Cdd:PRK08289 332 D-RRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNAIRVPTPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQ 410

                        250       260
                 ....*....|....*....|....*
gi 338173024 251 MSYSEDA-LVSTDLNGDNHSCIFDA 274
Cdd:PRK08289 411 IDYTDSTeVVSSDFVGSRHAGVVDS 435
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-129 7.04e-60

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


Pssm-ID: 214851 [Multi-domain]  Cd Length: 149  Bit Score: 186.99  E-value: 7.04e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024     1 EHGDVKVVAVNDPfIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFT 80
Cdd:smart00846  21 ERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANLPWGELGVDIVVECTGGFT 99

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 338173024    81 TTEKAKAHLKGGAKKVVISAPSADAA-MFVMGVNEK*YKSDI*II*NASC 129
Cdd:smart00846 100 TREKASAHLKAGAKKVIISAPSKDADpTFVYGVNHDEYDGEDHIISNASC 149
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
 5-274 6.58e-47

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 159.66  E-value: 6.58e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024   5 VKVVAVNDPFIEPHYAAYMLKYDSQHGQFKGT-IEVKGSDLVVNGQTVKFYTEK-DPANIPWKDTGAYYIVESTGVFTTT 82
Cdd:PTZ00353  27 VTVVAVNDASVSIAYIAYVLEQESPLSAPDGAsIRVVGEQIVLNGTQKIRVSAKhDLVEIAWRDYGVQYVVECTGLYSTR 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024  83 EKAKAHLKGGAKKVVISAPSADAAMFVMGVNEK*YKSDI*II*NASCT*NCLAPLAKVMHDNFTIIEGLMTTIHSyTA*Q 162
Cdd:PTZ00353 107 SRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDERLSASLPVCCAGAPIAVALAPVIRALHEVYGVEECSYTAIHG-MQPQ 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024 163 KTVDGPS--SKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKETMK 240
Cdd:PTZ00353 186 EPIAARSknSQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVKKGCAIDMLVRTKQPVSKEVVDSALA 265

                        250       260       270
                 ....*....|....*....|....*....|....
gi 338173024 241 KASEGELKGIMSYSEDALVSTDLNGDNHSCiFDA 274
Cdd:PTZ00353 266 EAASDRLNGVLCISKRDMISVDCIPNGKLC-YDA 298
GAPDH_C_E4PDH cd23937
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 129-274 3.13e-43

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: 144.86  E-value: 3.13e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024 129 CT*NCLAPLAKVMHDNFTIIEGLMTTIHSYTA*QKTVDGpSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGM 208
Cdd:cd23937    1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAI 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 338173024 209 SMRVPTSNVSVVDLTCRLEKSVTYDQIKETMKKASEGELKGIMSYSEDALVSTDLNGDNHSCIFDA 274
Cdd:cd23937   80 AVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDG 145
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 129-274 6.39e-36

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: 126.09  E-value: 6.39e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024 129 CT*NCLAPLAKVMHDNFTIIEGLMTTIHSYTA*QKTVDGPSSKDWrgGRTAAQNIIPSSTGAAKAVGKVIPSLN--GKLT 206
Cdd:cd18122    1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIGkpIKVD 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 338173024 207 GMSMRVPTSNVSVVDLTCRLEKSVTYDQIKETMKKASEGELKGIMSYSEDALVSTDLNGDNHSCIFDA 274
Cdd:cd18122   79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGR 146
GAPDH_N_E4PDH cd17892
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 4-128 3.88e-35

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: 123.92  E-value: 3.88e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024   4 DVKVVAVNDPfIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFTTTE 83
Cdd:cd17892   27 EFQVVAINEL-ADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPDPENLPWRELGIDLVLECTGVFGSRE 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 338173024  84 KAKAHLKGGAKKVVISAPSA---DAAMfVMGVNEK*YKSDI*II*NAS 128
Cdd:cd17892  106 DAERHLAAGAKKVLFSHPASndvDATI-VYGINQDLLRAEHRIVSNAS 152
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-81 2.66e-34

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: 119.51  E-value: 2.66e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 338173024    1 EHGDVKVVAVNDpFIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFT 80
Cdd:pfam00044  21 ERPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAELPWGDLGVDVVIESTGVFT 99


                  .
gi 338173024   81 T 81
Cdd:pfam00044 100 T 100
GAPDH-like_N cd05192
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ...
 71-133 1.62e-05

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: 43.11  E-value: 1.62e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 338173024  71 YIVESTGVFTTTEKAKAHLKGGAKKVVISAPSADAAMF-VMGVNEK*YKSDI*II*NASCT*NC 133
Cdd:cd05192   36 VVIECTGSFTDDDNAEKHIKAGGKKAVITAPEKGDIPTiVVVLNELAKSAGATVVSNANETSYS 99
 
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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