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Conserved domains on  [gi|672216968|gb|AIJ02563|]
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glyceraldehyde-3-phosphate dehydrogenase, partial [Sulcaria badia]

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 ...
 5-273 2.66e-168

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: 468.72  E-value: 2.66e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968   5 DVKVVAVNDPfIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFTTTE 84
Cdd:COG0057   27 DIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAELPWGELGVDVVIECTGKFTDRE 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968  85 KAKAHLKGGAKKVVISAPSADA-AMFVMGVNEKEYKSDIEVISNASCTTNCLAPLAKVMHDNYTIIEGLMTTIHSYTATQ 163
Cdd:COG0057  106 KASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAPVAKVLNDAFGIEKGLMTTIHAYTNDQ 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968 164 KTVDGPSsKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKETMKKA 243
Cdd:COG0057  186 NLLDAPH-KDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVELEKETTVEEVNAALKEA 264

                        250       260       270
                 ....*....|....*....|....*....|
gi 672216968 244 SEGELKGILSYSEDALVSTDLNGDNHSCIF 273
Cdd:COG0057  265 AEGPLKGILGYTEEPLVSSDFNGDPHSSIF 294
 
Name Accession Description Interval E-value
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 5-273 2.66e-168

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: 468.72  E-value: 2.66e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968   5 DVKVVAVNDPfIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFTTTE 84
Cdd:COG0057   27 DIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAELPWGELGVDVVIECTGKFTDRE 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968  85 KAKAHLKGGAKKVVISAPSADA-AMFVMGVNEKEYKSDIEVISNASCTTNCLAPLAKVMHDNYTIIEGLMTTIHSYTATQ 163
Cdd:COG0057  106 KASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAPVAKVLNDAFGIEKGLMTTIHAYTNDQ 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968 164 KTVDGPSsKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKETMKKA 243
Cdd:COG0057  186 NLLDAPH-KDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVELEKETTVEEVNAALKEA 264

                        250       260       270
                 ....*....|....*....|....*....|
gi 672216968 244 SEGELKGILSYSEDALVSTDLNGDNHSCIF 273
Cdd:COG0057  265 AEGPLKGILGYTEEPLVSSDFNGDPHSSIF 294
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 5-273 3.19e-165

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 464.33  E-value: 3.19e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968   5 DVKVVAVNDPFIEPHYAAYMLKYDSQHGQFKGTIEV-KGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFTTT 83
Cdd:PLN02272 109 DIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDPAEIPWGDFGAEYVVESSGVFTTV 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968  84 EKAKAHLKGGAKKVVISAPSADAAMFVMGVNEKEYKSDIEVISNASCTTNCLAPLAKVMHDNYTIIEGLMTTIHSYTATQ 163
Cdd:PLN02272 189 EKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQ 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968 164 KTVDGPSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKETMKKA 243
Cdd:PLN02272 269 KTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYA 348

                        250       260       270
                 ....*....|....*....|....*....|
gi 672216968 244 SEGELKGILSYSEDALVSTDLNGDNHSCIF 273
Cdd:PLN02272 349 SEGPLKGILGYTDEDVVSNDFVGDSRSSIF 378
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 5-273 1.43e-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: 395.49  E-value: 1.43e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968    5 DVKVVAVNDPfIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFY-TEKDPANIPWKDTGAYYIVESTGVFTTT 83
Cdd:TIGR01534  25 DLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEVISVfSERDPSDLPWKALGVDIVIECTGKFRDK 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968   84 EKAKAHLKGGAKKVVISAPSADAA-MFVMGVNEKEYKSDIEVISNASCTTNCLAPLAKVMHDNYTIIEGLMTTIHSYTAT 162
Cdd:TIGR01534 104 EKLEKHLEAGAKKVLISAPSKGDVkTIVYGVNHDEYDGEERIISNASCTTNCLAPLAKVLDEAFGIVSGLMTTVHAYTND 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968  163 QKTVDGPsSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKETMKK 242
Cdd:TIGR01534 184 QNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNVSLVDLVVNLEKDVTVEEVNAALKE 262

                         250       260       270
                  ....*....|....*....|....*....|.
gi 672216968  243 ASEGELKGILSYSEDALVSTDLNGDNHSCIF 273
Cdd:TIGR01534 263 ASEGELKGVLGYTEDELVSSDFIGSPYSSIV 293
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 130-273 4.01e-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: 292.05  E-value: 4.01e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968 130 CTTNCLAPLAKVMHDNYTIIEGLMTTIHSYTATQKTVDGPSsKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGM 209
Cdd:cd18126    1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672216968 210 SMRVPTSNVSVVDLTCRLEKSVTYDQIKETMKKASEGELKGILSYSEDALVSTDLNGDNHSCIF 273
Cdd:cd18126   80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIF 143
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
2-272 7.75e-87

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 261.79  E-value: 7.75e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968   2 EHGDVKVVAVNDPFIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDtGAYYIVESTGVFT 81
Cdd:NF033735  19 GRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDTPWGD-GVDVVIECTGKFK 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968  82 TTEKAKAHLKGGAKKVVISAP--SADAAMFVMGVNEKEYKSDIE-VISNASCTTNCLAPLAKVMHDNYTIIEGLMTTIHS 158
Cdd:NF033735  98 TPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARHrIVTAASCTTNCLAPVVKVIHEKIGIKHGSITTIHD 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968 159 YTATQKTVDGPsSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKE 238
Cdd:NF033735 178 ITNTQTIVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASLTDCVFEVERPTTVEEVNA 256

                        250       260       270
                 ....*....|....*....|....*....|....
gi 672216968 239 TMKKASEGELKGILSYSEDALVSTDLNGDNHSCI 272
Cdd:NF033735 257 LFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSI 290
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 135-273 3.78e-80

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: 238.65  E-value: 3.78e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968  135 LAPLAKVMHDNYTIIEGLMTTIHSYTATQKTVDGPSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVP 214
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 672216968  215 TSNVSVVDLTCRLEKSVTYDQIKETMKKASEGELKGILSYSEDALVSTDLNGDNHSCIF 273
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIF 139
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-130 1.90e-61

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


Pssm-ID: 214851 [Multi-domain]  Cd Length: 149  Bit Score: 190.84  E-value: 1.90e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968     1 VEHGDVKVVAVNDPfIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVF 80
Cdd:smart00846  20 LERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANLPWGELGVDIVVECTGGF 98

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 672216968    81 TTTEKAKAHLKGGAKKVVISAPSADAA-MFVMGVNEKEYKSDIEVISNASC 130
Cdd:smart00846  99 TTREKASAHLKAGAKKVIISAPSKDADpTFVYGVNHDEYDGEDHIISNASC 149
 
Name Accession Description Interval E-value
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 5-273 2.66e-168

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: 468.72  E-value: 2.66e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968   5 DVKVVAVNDPfIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFTTTE 84
Cdd:COG0057   27 DIEVVAINDL-GDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAELPWGELGVDVVIECTGKFTDRE 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968  85 KAKAHLKGGAKKVVISAPSADA-AMFVMGVNEKEYKSDIEVISNASCTTNCLAPLAKVMHDNYTIIEGLMTTIHSYTATQ 163
Cdd:COG0057  106 KASAHLKAGAKKVLISAPAKGDdPTIVYGVNHDDYDADHRIISNASCTTNCLAPVAKVLNDAFGIEKGLMTTIHAYTNDQ 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968 164 KTVDGPSsKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKETMKKA 243
Cdd:COG0057  186 NLLDAPH-KDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVELEKETTVEEVNAALKEA 264

                        250       260       270
                 ....*....|....*....|....*....|
gi 672216968 244 SEGELKGILSYSEDALVSTDLNGDNHSCIF 273
Cdd:COG0057  265 AEGPLKGILGYTEEPLVSSDFNGDPHSSIF 294
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 5-273 3.19e-165

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 464.33  E-value: 3.19e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968   5 DVKVVAVNDPFIEPHYAAYMLKYDSQHGQFKGTIEV-KGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFTTT 83
Cdd:PLN02272 109 DIEVVAVNDPFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDPAEIPWGDFGAEYVVESSGVFTTV 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968  84 EKAKAHLKGGAKKVVISAPSADAAMFVMGVNEKEYKSDIEVISNASCTTNCLAPLAKVMHDNYTIIEGLMTTIHSYTATQ 163
Cdd:PLN02272 189 EKASAHLKGGAKKVVISAPSADAPMFVVGVNEKTYKPNMNIVSNASCTTNCLAPLAKVVHEEFGILEGLMTTVHATTATQ 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968 164 KTVDGPSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKETMKKA 243
Cdd:PLN02272 269 KTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRLEKSASYEDVKAAIKYA 348

                        250       260       270
                 ....*....|....*....|....*....|
gi 672216968 244 SEGELKGILSYSEDALVSTDLNGDNHSCIF 273
Cdd:PLN02272 349 SEGPLKGILGYTDEDVVSNDFVGDSRSSIF 378
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 5-273 1.43e-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: 395.49  E-value: 1.43e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968    5 DVKVVAVNDPfIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFY-TEKDPANIPWKDTGAYYIVESTGVFTTT 83
Cdd:TIGR01534  25 DLEVVAINDL-TDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKEVISVfSERDPSDLPWKALGVDIVIECTGKFRDK 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968   84 EKAKAHLKGGAKKVVISAPSADAA-MFVMGVNEKEYKSDIEVISNASCTTNCLAPLAKVMHDNYTIIEGLMTTIHSYTAT 162
Cdd:TIGR01534 104 EKLEKHLEAGAKKVLISAPSKGDVkTIVYGVNHDEYDGEERIISNASCTTNCLAPLAKVLDEAFGIVSGLMTTVHAYTND 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968  163 QKTVDGPsSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKETMKK 242
Cdd:TIGR01534 184 QNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNVSLVDLVVNLEKDVTVEEVNAALKE 262

                         250       260       270
                  ....*....|....*....|....*....|.
gi 672216968  243 ASEGELKGILSYSEDALVSTDLNGDNHSCIF 273
Cdd:TIGR01534 263 ASEGELKGVLGYTEDELVSSDFIGSPYSSIV 293
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
 2-273 9.69e-130

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 371.09  E-value: 9.69e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968   2 EHGDVKVVAVNDPFIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFT 81
Cdd:PTZ00023  23 EREDVEVVAINDPFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKDPAAIPWGKNGVDVVCESTGVFL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968  82 TTEKAKAHLKGGAKKVVISAPSADAA-MFVMGVNEKEYKSDIEVISNASCTTNCLAPLAKVMHDNYTIIEGLMTTIHSYT 160
Cdd:PTZ00023 103 TKEKAQAHLKGGAKKVIMSAPPKDDTpIYVMGVNHTQYDKSQRIVSNASCTTNCLAPLAKVVNDKFGIVEGLMTTVHAST 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968 161 ATQKTVDGPS--SKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKE 238
Cdd:PTZ00023 183 ANQLTVDGPSkgGKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVPDVSVVDLTCKLAKPAKYEEIVA 262

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 672216968 239 TMKKASEGELKGILSYSEDALVSTDLNGDNHSCIF 273
Cdd:PTZ00023 263 AVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIF 297
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
 1-273 2.58e-127

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 365.20  E-value: 2.58e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968   1 VEHGDVKVVAVNDPFIEPHYAAYMLKYDSQHGQFK-GTIEVKGSDLVVNGQT-VKFYTEKDPANIPWKDTGAYYIVESTG 78
Cdd:PLN02358  25 LQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKhHELKVKDDKTLLFGEKpVTVFGIRNPEDIPWGEAGADFVVESTG 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968  79 VFTTTEKAKAHLKGGAKKVVISAPSADAAMFVMGVNEKEYKSDIEVISNASCTTNCLAPLAKVMHDNYTIIEGLMTTIHS 158
Cdd:PLN02358 105 VFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCTTNCLAPLAKVINDRFGIVEGLMTTVHS 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968 159 YTATQKTVDGPSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKE 238
Cdd:PLN02358 185 ITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRLEKAATYDEIKK 264

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 672216968 239 TMKKASEGELKGILSYSEDALVSTDLNGDNHSCIF 273
Cdd:PLN02358 265 AIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIF 299
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
2-273 4.41e-116

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 336.32  E-value: 4.41e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968   2 EHGDVKVVAVNDpFIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFT 81
Cdd:PRK15425  23 KRSDIEIVAIND-LLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPANLKWDEVGVDVVAEATGLFL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968  82 TTEKAKAHLKGGAKKVVISAPSAD-AAMFVMGVNEKEYKSDiEVISNASCTTNCLAPLAKVMHDNYTIIEGLMTTIHSYT 160
Cdd:PRK15425 102 TDETARKHITAGAKKVVMTGPSKDnTPMFVKGANFDKYAGQ-DIVSNASCTTNCLAPLAKVINDNFGIIEGLMTTVHATT 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968 161 ATQKTVDGPSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKETM 240
Cdd:PRK15425 181 ATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAATYEQIKAAV 260

                        250       260       270
                 ....*....|....*....|....*....|...
gi 672216968 241 KKASEGELKGILSYSEDALVSTDLNGDNHSCIF 273
Cdd:PRK15425 261 KAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVF 293
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-272 2.69e-108

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 317.06  E-value: 2.69e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968   1 VEHGDVKVVAVNDPFiEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVF 80
Cdd:PRK07729  22 IKESAFEIVAINASY-PSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDPKELPWTDLGIDIVIEATGKF 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968  81 TTTEKAKAHLKGGAKKVVISAPSADA-AMFVMGVNEKEYKSDIE-VISNASCTTNCLAPLAKVMHDNYTIIEGLMTTIHS 158
Cdd:PRK07729 101 NSKEKAILHVEAGAKKVILTAPGKNEdVTIVVGVNEDQLDIEKHtIISNASCTTNCLAPVVKVLDEQFGIENGLMTTVHA 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968 159 YTATQKTVDGPSsKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKE 238
Cdd:PRK07729 181 YTNDQKNIDNPH-KDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNVSLVDLVVDVKRDVTVEEINE 259

                        250       260       270
                 ....*....|....*....|....*....|....
gi 672216968 239 TMKKASEGELKGILSYSEDALVSTDLNGDNHSCI 272
Cdd:PRK07729 260 AFKTAANGALKGILEFSEEPLVSIDFNTNTHSAI 293
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 5-273 2.92e-107

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 315.07  E-value: 2.92e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968   5 DVKVVAVNDPFIEPHYAAYMLKYDSQHGQFKGTIE-------VKGSD-LVVNGQTVK-FYTEKDPANIPWKDTGAYYIVE 75
Cdd:PTZ00434  31 EIDVVAVVDMSTNAEYFAYQMKYDTVHGRPKYTVEttksspsVKTDDvLVVNGHRIKcVKAQRNPADLPWGKLGVDYVIE 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968  76 STGVFTTTEKAKAHLKGGAKKVVISAP-SADAAMFVMGVNEKEYK-SDIEVISNASCTTNCLAPLAKVM-HDNYTIIEGL 152
Cdd:PTZ00434 111 STGLFTDKLAAEGHLKGGAKKVVISAPaSGGAKTIVMGVNQHEYSpTEHHVVSNASCTTNCLAPIVHVLtKEGFGIETGL 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968 153 MTTIHSYTATQKTVDGPSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVT 232
Cdd:PTZ00434 191 MTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGKLTGMSFRVPTPDVSVVDLTFRATRDTS 270

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 672216968 233 YDQIKETMKKASEGELKGILSYSEDALVSTDLNGDNHSCIF 273
Cdd:PTZ00434 271 IQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIY 311
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
2-272 1.43e-101

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 299.51  E-value: 1.43e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968   2 EHGDVKVVAVNDPfIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFT 81
Cdd:PRK07403  24 ENSQLELVAINDT-SDPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDRNPLNLPWKEWGIDLIIESTGVFV 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968  82 TTEKAKAHLKGGAKKVVISAP--SADAAMFVMGVNEKEYKSDI-EVISNASCTTNCLAPLAKVMHDNYTIIEGLMTTIHS 158
Cdd:PRK07403 103 TKEGASKHIQAGAKKVLITAPgkGEDIGTYVVGVNHHEYDHEDhNIISNASCTTNCLAPIAKVLHDNFGIIKGTMTTTHS 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968 159 YTATQKTVDGpSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKE 238
Cdd:PRK07403 183 YTGDQRILDA-SHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTPNVSVVDLVVQVEKRTITEQVNE 261

                        250       260       270
                 ....*....|....*....|....*....|....
gi 672216968 239 TMKKASEGELKGILSYSEDALVSTDLNGDNHSCI 272
Cdd:PRK07403 262 VLKDASEGPLKGILEYSDLPLVSSDYRGTDASSI 295
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 130-273 4.01e-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: 292.05  E-value: 4.01e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968 130 CTTNCLAPLAKVMHDNYTIIEGLMTTIHSYTATQKTVDGPSsKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGM 209
Cdd:cd18126    1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGPH-KDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672216968 210 SMRVPTSNVSVVDLTCRLEKSVTYDQIKETMKKASEGELKGILSYSEDALVSTDLNGDNHSCIF 273
Cdd:cd18126   80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIF 143
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
2-272 7.75e-87

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 261.79  E-value: 7.75e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968   2 EHGDVKVVAVNDPFIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDtGAYYIVESTGVFT 81
Cdd:NF033735  19 GRPGLEIVHINDLAGDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDTPWGD-GVDVVIECTGKFK 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968  82 TTEKAKAHLKGGAKKVVISAP--SADAAMFVMGVNEKEYKSDIE-VISNASCTTNCLAPLAKVMHDNYTIIEGLMTTIHS 158
Cdd:NF033735  98 TPEKLQPYFDQGVKKVVVSAPvkEEGVLNIVYGVNDHLYDPARHrIVTAASCTTNCLAPVVKVIHEKIGIKHGSITTIHD 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968 159 YTATQKTVDGPsSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKE 238
Cdd:NF033735 178 ITNTQTIVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASLTDCVFEVERPTTVEEVNA 256

                        250       260       270
                 ....*....|....*....|....*....|....
gi 672216968 239 TMKKASEGELKGILSYSEDALVSTDLNGDNHSCI 272
Cdd:NF033735 257 LFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSI 290
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
 8-271 3.13e-83

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 254.86  E-value: 3.13e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968   8 VVAVNDPFiEPHYAAYMLKYDSQHGQFKGTIEVKGSD-LVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFTTTEKA 86
Cdd:PLN03096  89 VVAINDTG-GVKQASHLLKYDSTLGTFDADVKPVGDDaISVDGKVIKVVSDRNPLNLPWGELGIDLVIEGTGVFVDREGA 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968  87 KAHLKGGAKKVVISAPS-ADAAMFVMGVNEKEYKSDIEVISNASCTTNCLAPLAKVMHDNYTIIEGLMTTIHSYTATQKT 165
Cdd:PLN03096 168 GKHIQAGAKKVLITAPGkGDIPTYVVGVNADDYKHSDPIISNASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRL 247

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968 166 VDGpSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKETMKKASE 245
Cdd:PLN03096 248 LDA-SHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQVEKKTFAEEVNAAFRDAAE 326

                        250       260
                 ....*....|....*....|....*.
gi 672216968 246 GELKGILSYSEDALVSTDLNGDNHSC 271
Cdd:PLN03096 327 KELKGILAVCDEPLVSVDFRCSDVSS 352
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
 6-263 1.24e-80

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 249.82  E-value: 1.24e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968   6 VKVVAVNDPF-IEPhyAAYMLKYDSQHGQFKGTIE-VKGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFTTT 83
Cdd:PLN02237 102 LDVVVVNDSGgVKN--ASHLLKYDSMLGTFKADVKiVDDETISVDGKPIKVVSNRDPLKLPWAELGIDIVIEGTGVFVDG 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968  84 EKAKAHLKGGAKKVVISAPS--ADAAMFVMGVNEKEYKSDI-EVISNASCTTNCLAPLAKVMHDNYTIIEGLMTTIHSYT 160
Cdd:PLN02237 180 PGAGKHIQAGAKKVIITAPAkgADIPTYVVGVNEDDYDHEVaNIVSNASCTTNCLAPFVKVLDEEFGIVKGTMTTTHSYT 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968 161 ATQKTVDGpSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKS-VTYDQIKET 239
Cdd:PLN02237 260 GDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTPNVSVVDLVVNVEKKgITAEDVNAA 338

                        250       260
                 ....*....|....*....|....
gi 672216968 240 MKKASEGELKGILSYSEDALVSTD 263
Cdd:PLN02237 339 FRKAADGPLKGILAVCDVPLVSVD 362
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 135-273 3.78e-80

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: 238.65  E-value: 3.78e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968  135 LAPLAKVMHDNYTIIEGLMTTIHSYTATQKTVDGPSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVP 214
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 672216968  215 TSNVSVVDLTCRLEKSVTYDQIKETMKKASEGELKGILSYSEDALVSTDLNGDNHSCIF 273
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIF 139
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
 3-272 1.27e-75

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 233.41  E-value: 1.27e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968   3 HGDVKVVAVNDpFIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFTT 82
Cdd:PRK13535  26 RAEITVVAINE-LADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHERDIASLPWRELGVDVVLDCTGVYGS 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968  83 TEKAKAHLKGGAKKVVISAPSA---DAAMfVMGVNEKEYKSDIEVISNASCTTNCLAPLAKVMHDNYTIIEGLMTTIHSY 159
Cdd:PRK13535 105 REDGEAHIAAGAKKVLFSHPGSndlDATV-VYGVNHDQLRAEHRIVSNASCTTNCIIPVIKLLDDAFGIESGTVTTIHSA 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968 160 TATQKTVDGPSSkDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKET 239
Cdd:PRK13535 184 MNDQQVIDAYHP-DLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPTINVTAIDLSVTVKKPVKVNEVNQL 262

                        250       260       270
                 ....*....|....*....|....*....|...
gi 672216968 240 MKKASEGELKGILSYSEDALVSTDLNGDNHSCI 272
Cdd:PRK13535 263 LQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAI 295
PRK08955 PRK08955
glyceraldehyde-3-phosphate dehydrogenase; Validated
 5-272 3.31e-75

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 169599 [Multi-domain]  Cd Length: 334  Bit Score: 232.31  E-value: 3.31e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968   5 DVKVVAVNDPFIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWkdTGAYYIVESTGVFTTTE 84
Cdd:PRK08955  26 ELEFVQINDPAGDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKAIADTDW--SGCDVVIEASGVMKTKA 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968  85 KAKAHLKGGAKKVVISAPSAD--AAMFVMGVNEKEYKSDI-EVISNASCTTNCLAPLAKVMHDNYTIIEGLMTTIHSYTA 161
Cdd:PRK08955 104 LLQAYLDQGVKRVVVTAPVKEegVLNIVMGVNDHLFDPAIhPIVTAASCTTNCLAPVVKVIHEKLGIKHGSMTTIHDLTN 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968 162 TQKTVDGPsSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKETMK 241
Cdd:PRK08955 184 TQTILDAP-HKDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLANASLTDCVFEVERDTTVEEVNALLK 262

                        250       260       270
                 ....*....|....*....|....*....|.
gi 672216968 242 KASEGELKGILSYSEDALVSTDLNGDNHSCI 272
Cdd:PRK08955 263 EAAEGELKGILGYEERPLVSIDYKTDPRSSI 293
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 1-129 4.10e-69

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: 210.71  E-value: 4.10e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968   1 VEHGDVKVVAVNDPFIePHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVF 80
Cdd:cd05214   20 LERDDIEVVAINDLTD-DETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAELPWGELGVDIVIESTGVF 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 672216968  81 TTTEKAKAHLKGGAKKVVISAPSADAA-MFVMGVNEKEYKSDIEVISNAS 129
Cdd:cd05214   99 TTKEKASAHLKAGAKKVIISAPAKDDDpTIVMGVNHDKYDADDKIISNAS 148
PRK08289 PRK08289
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
 22-273 2.52e-66

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 236219 [Multi-domain]  Cd Length: 477  Bit Score: 213.63  E-value: 2.52e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968  22 AYMLKYDSQHGQFKGTIEV--KGSDLVVNGQTVKFYTEKDPANIpwkDTGAYYI-----VESTGVFTTTEKAKAHLKG-G 93
Cdd:PRK08289 175 ASLLRRDSVHGPFNGTITVdeENNAIIANGNYIQVIYANSPEEV---DYTAYGInnalvVDNTGKWRDEEGLSQHLKSkG 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968  94 AKKVVISAPS-ADAAMFVMGVNEKEYKSDIEVISNASCTTNCLAPLAKVMHDNYTIIEGLMTTIHSYTATQKTVDGPSSK 172
Cdd:PRK08289 252 VAKVLLTAPGkGDIKNIVHGVNHSDITDEDKIVSAASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDNYHKG 331

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968 173 DwRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKETMKKAS-EGELKGI 251
Cdd:PRK08289 332 D-RRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNAIRVPTPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQNQ 410

                        250       260
                 ....*....|....*....|...
gi 672216968 252 LSYSEDA-LVSTDLNGDNHSCIF 273
Cdd:PRK08289 411 IDYTDSTeVVSSDFVGSRHAGVV 433
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 130-273 4.94e-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: 203.23  E-value: 4.94e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968 130 CTTNCLAPLAKVMHDNYTIIEGLMTTIHSYTATQKTVDGPSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGM 209
Cdd:cd18123    1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672216968 210 SMRVPTSNVSVVDLTCRLEKSVTYDQIKETMKKASEGelKGILSYSEDALVSTDLNGDNHSCIF 273
Cdd:cd18123   81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIFESVF 142
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-130 1.90e-61

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


Pssm-ID: 214851 [Multi-domain]  Cd Length: 149  Bit Score: 190.84  E-value: 1.90e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968     1 VEHGDVKVVAVNDPfIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVF 80
Cdd:smart00846  20 LERPDVEVVAINDL-TDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANLPWGELGVDIVVECTGGF 98

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 672216968    81 TTTEKAKAHLKGGAKKVVISAPSADAA-MFVMGVNEKEYKSDIEVISNASC 130
Cdd:smart00846  99 TTREKASAHLKAGAKKVIISAPSKDADpTFVYGVNHDEYDGEDHIISNASC 149
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
 6-271 2.93e-48

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 163.12  E-value: 2.93e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968   6 VKVVAVNDPFIEPHYAAYMLKYDSQHGQFKGT-IEVKGSDLVVNGQTVKFYTEK-DPANIPWKDTGAYYIVESTGVFTTT 83
Cdd:PTZ00353  27 VTVVAVNDASVSIAYIAYVLEQESPLSAPDGAsIRVVGEQIVLNGTQKIRVSAKhDLVEIAWRDYGVQYVVECTGLYSTR 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968  84 EKAKAHLKGGAKKVVISAPSADAAMFVMGVNEKEYKSDIEVISNASCTTNCLAPLAKVMHDNYTIIEGLMTTIHSyTATQ 163
Cdd:PTZ00353 107 SRCWGHVTGGAKGVFVAGQSADAPTVMAGSNDERLSASLPVCCAGAPIAVALAPVIRALHEVYGVEECSYTAIHG-MQPQ 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968 164 KTVDGPS--SKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGMSMRVPTSNVSVVDLTCRLEKSVTYDQIKETMK 241
Cdd:PTZ00353 186 EPIAARSknSQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVKKGCAIDMLVRTKQPVSKEVVDSALA 265

                        250       260       270
                 ....*....|....*....|....*....|
gi 672216968 242 KASEGELKGILSYSEDALVSTDLNGDNHSC 271
Cdd:PTZ00353 266 EAASDRLNGVLCISKRDMISVDCIPNGKLC 295
GAPDH_C_E4PDH cd23937
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 130-273 7.37e-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: 143.71  E-value: 7.37e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968 130 CTTNCLAPLAKVMHDNYTIIEGLMTTIHSYTATQKTVDGpSSKDWRGGRTAAQNIIPSSTGAAKAVGKVIPSLNGKLTGM 209
Cdd:cd23937    1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAI 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672216968 210 SMRVPTSNVSVVDLTCRLEKSVTYDQIKETMKKASEGELKGILSYSEDALVSTDLNGDNHSCIF 273
Cdd:cd23937   80 AVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIV 143
GAPDH_N_E4PDH cd17892
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 5-129 1.84e-36

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: 127.38  E-value: 1.84e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968   5 DVKVVAVNDPfIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFTTTE 84
Cdd:cd17892   27 EFQVVAINEL-ADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPDPENLPWRELGIDLVLECTGVFGSRE 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 672216968  85 KAKAHLKGGAKKVVISAPSA---DAAMfVMGVNEKEYKSDIEVISNAS 129
Cdd:cd17892  106 DAERHLAAGAKKVLFSHPASndvDATI-VYGINQDLLRAEHRIVSNAS 152
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 130-273 3.64e-35

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: 124.17  E-value: 3.64e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968 130 CTTNCLAPLAKVMHDNYTIIEGLMTTIHSYTATQKTVDGPSSKDWrgGRTAAQNIIPSSTGAAKAVGKVIPSLN--GKLT 207
Cdd:cd18122    1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIGkpIKVD 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672216968 208 GMSMRVPTSNVSVVDLTCRLEKSVTYDQIKETMKKASEGELKGILSYSEDALVSTDLNGDNHSCIF 273
Cdd:cd18122   79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPV 144
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 2-82 2.14e-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: 119.90  E-value: 2.14e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672216968    2 EHGDVKVVAVNDpFIEPHYAAYMLKYDSQHGQFKGTIEVKGSDLVVNGQTVKFYTEKDPANIPWKDTGAYYIVESTGVFT 81
Cdd:pfam00044  21 ERPDIEVVAIND-LTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAELPWGDLGVDVVIESTGVFT 99


                  .
gi 672216968   82 T 82
Cdd:pfam00044 100 T 100
GAPDH-like_N cd05192
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ...
 72-134 7.46e-07

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: 46.96  E-value: 7.46e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672216968  72 YIVESTGVFTTTEKAKAHLKGGAKKVVISAPSADAAMF-VMGVNEKEYKSDIEVISNASCTTNC 134
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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