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Conserved domains on  [gi|2168678143|gb|UHJ15676|]
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glyceraldehyde-3-phosphate dehydrogenase A, partial [Pectobacterium odoriferum]

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 ...
 1-278 0e+00

Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]; Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase is part of the Pathway/BioSystem: Glycolysis


:

Pssm-ID: 439827 [Multi-domain]  Cd Length: 334  Bit Score: 525.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143   1 RAAQER-SDIEIVAINDLLDAEYMAYMLKYDSTHGRFDGTVEVKDGHLVVNGKTIRVTAERDPANLKWNEVNVDVVAEAT 79
Cdd:COG0057    19 RALLERgPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAELPWGELGVDVVIECT 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143  80 GLFLTDETARKHIAAGAKKVVLTGPSKDDTPMFVMGVNHKTY-AGQEIVSNASCTTNCLAPLAKVINDNFGIVEALMTTV 158
Cdd:COG0057    99 GKFTDREKASAHLKAGAKKVLISAPAKGDDPTIVYGVNHDDYdADHRIISNASCTTNCLAPVAKVLNDAFGIEKGLMTTI 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143 159 HATTATQKTVDGPsHKDWRGGRGAAQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTARLEKPASYKEI 238
Cdd:COG0057   179 HAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVELEKETTVEEV 257

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2168678143 239 CAAIKAASEGELKGVLGYTEDEVVSTDFNGEKLTSVFDAK 278
Cdd:COG0057   258 NAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDAL 297
 
Name Accession Description Interval E-value
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-278 0e+00

Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]; Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 439827 [Multi-domain]  Cd Length: 334  Bit Score: 525.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143   1 RAAQER-SDIEIVAINDLLDAEYMAYMLKYDSTHGRFDGTVEVKDGHLVVNGKTIRVTAERDPANLKWNEVNVDVVAEAT 79
Cdd:COG0057    19 RALLERgPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAELPWGELGVDVVIECT 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143  80 GLFLTDETARKHIAAGAKKVVLTGPSKDDTPMFVMGVNHKTY-AGQEIVSNASCTTNCLAPLAKVINDNFGIVEALMTTV 158
Cdd:COG0057    99 GKFTDREKASAHLKAGAKKVLISAPAKGDDPTIVYGVNHDDYdADHRIISNASCTTNCLAPVAKVLNDAFGIEKGLMTTI 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143 159 HATTATQKTVDGPsHKDWRGGRGAAQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTARLEKPASYKEI 238
Cdd:COG0057   179 HAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVELEKETTVEEV 257

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2168678143 239 CAAIKAASEGELKGVLGYTEDEVVSTDFNGEKLTSVFDAK 278
Cdd:COG0057   258 NAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDAL 297
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
1-278 2.58e-177

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 491.56  E-value: 2.58e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143   1 RAAQERSDIEIVAINDLLDAEYMAYMLKYDSTHGRFDGTVEVKDGHLVVNGKTIRVTAERDPANLKWNEVNVDVVAEATG 80
Cdd:PRK15425   19 RAAQKRSDIEIVAINDLLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPANLKWDEVGVDVVAEATG 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143  81 LFLTDETARKHIAAGAKKVVLTGPSKDDTPMFVMGVNHKTYAGQEIVSNASCTTNCLAPLAKVINDNFGIVEALMTTVHA 160
Cdd:PRK15425   99 LFLTDETARKHITAGAKKVVMTGPSKDNTPMFVKGANFDKYAGQDIVSNASCTTNCLAPLAKVINDNFGIIEGLMTTVHA 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143 161 TTATQKTVDGPSHKDWRGGRGAAQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTARLEKPASYKEICA 240
Cdd:PRK15425  179 TTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAATYEQIKA 258

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2168678143 241 AIKAASEGELKGVLGYTEDEVVSTDFNGEKLTSVFDAK 278
Cdd:PRK15425  259 AVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAK 296
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 1-278 5.04e-156

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: 437.48  E-value: 5.04e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143   1 RAAQER--SDIEIVAINDLLDAEYMAYMLKYDSTHGRFDGTVEVKDGHLVVNGK-TIRVTAERDPANLKWNEVNVDVVAE 77
Cdd:TIGR01534  16 RRILEKpgNDLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKeVISVFSERDPSDLPWKALGVDIVIE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143  78 ATGLFLTDETARKHIAAGAKKVVLTGPSKDDTPMFVMGVNHKTYAGQE-IVSNASCTTNCLAPLAKVINDNFGIVEALMT 156
Cdd:TIGR01534  96 CTGKFRDKEKLEKHLEAGAKKVLISAPSKGDVKTIVYGVNHDEYDGEErIISNASCTTNCLAPLAKVLDEAFGIVSGLMT 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143 157 TVHATTATQKTVDGPsHKDWRGGRGAAQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTARLEKPASYK 236
Cdd:TIGR01534 176 TVHAYTNDQNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNVSLVDLVVNLEKDVTVE 254

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2168678143 237 EICAAIKAASEGELKGVLGYTEDEVVSTDFNGEKLTSVFDAK 278
Cdd:TIGR01534 255 EVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDAT 296
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 132-278 3.63e-106

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: 305.15  E-value: 3.63e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143 132 CTTNCLAPLAKVINDNFGIVEALMTTVHATTATQKTVDGPsHKDWRGGRGAAQNIIPSSTGAAKAVGKVIPELNGKLTGM 211
Cdd:cd18126     1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGP-HKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2168678143 212 AFRVPTPNVSVVDLTARLEKPASYKEICAAIKAASEGELKGVLGYTEDEVVSTDFNGEKLTSVFDAK 278
Cdd:cd18126    80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDAT 146
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
1-277 1.83e-96

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 286.44  E-value: 1.83e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143   1 RAAQERSDIEIVAINDLL-DAEYMAYMLKYDSTHGRFDGTVEVKDGHLVVNGKTIRVTAERDPANLKWNEvNVDVVAEAT 79
Cdd:NF033735   15 RALWGRPGLEIVHINDLAgDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDTPWGD-GVDVVIECT 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143  80 GLFLTDETARKHIAAGAKKVVLTGPSKDDTPM-FVMGVNHKTYAGQE--IVSNASCTTNCLAPLAKVINDNFGIVEALMT 156
Cdd:NF033735   94 GKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLnIVYGVNDHLYDPARhrIVTAASCTTNCLAPVVKVIHEKIGIKHGSIT 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143 157 TVHATTATQKTVDGPsHKDWRGGRGAAQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTARLEKPASYK 236
Cdd:NF033735  174 TIHDITNTQTIVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASLTDCVFEVERPTTVE 252

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2168678143 237 EICAAIKAASEGELKGVLGYTEDEVVSTDFNGEKLTSVFDA 277
Cdd:NF033735  253 EVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDA 293
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 137-278 2.29e-82

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: 244.42  E-value: 2.29e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143 137 LAPLAKVINDNFGIVEALMTTVHATTATQKTVDGPSHKDWRGGRGAAQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVP 216
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2168678143 217 TPNVSVVDLTARLEKPASYKEICAAIKAASEGELKGVLGYTEDEVVSTDFNGEKLTSVFDAK 278
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAK 142
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-132 8.14e-73

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: 219.73  E-value: 8.14e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143    1 RAAQERSDIEIVAINDLLDAEYMAYMLKYDSTHGRFDGTVEVKDGHLVVNGKTIRVTAERDPANLKWNEVNVDVVAEATG 80
Cdd:smart00846  17 RAALERPDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANLPWGELGVDIVVECTG 96

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2168678143   81 LFLTDETARKHIAAGAKKVVLTGPSKDDTPMFVMGVNHKTYAGQE-IVSNASC 132
Cdd:smart00846  97 GFTTREKASAHLKAGAKKVIISAPSKDADPTFVYGVNHDEYDGEDhIISNASC 149
 
Name Accession Description Interval E-value
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-278 0e+00

Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism]; Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 439827 [Multi-domain]  Cd Length: 334  Bit Score: 525.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143   1 RAAQER-SDIEIVAINDLLDAEYMAYMLKYDSTHGRFDGTVEVKDGHLVVNGKTIRVTAERDPANLKWNEVNVDVVAEAT 79
Cdd:COG0057    19 RALLERgPDIEVVAINDLGDAETLAHLLKYDSVHGRFPGEVEVEGDSLIVNGKKIKVLAERDPAELPWGELGVDVVIECT 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143  80 GLFLTDETARKHIAAGAKKVVLTGPSKDDTPMFVMGVNHKTY-AGQEIVSNASCTTNCLAPLAKVINDNFGIVEALMTTV 158
Cdd:COG0057    99 GKFTDREKASAHLKAGAKKVLISAPAKGDDPTIVYGVNHDDYdADHRIISNASCTTNCLAPVAKVLNDAFGIEKGLMTTI 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143 159 HATTATQKTVDGPsHKDWRGGRGAAQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTARLEKPASYKEI 238
Cdd:COG0057   179 HAYTNDQNLLDAP-HKDLRRARAAALNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVPTPNVSLVDLTVELEKETTVEEV 257

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2168678143 239 CAAIKAASEGELKGVLGYTEDEVVSTDFNGEKLTSVFDAK 278
Cdd:COG0057   258 NAALKEAAEGPLKGILGYTEEPLVSSDFNGDPHSSIFDAL 297
gapA PRK15425
glyceraldehyde-3-phosphate dehydrogenase;
1-278 2.58e-177

glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 185323 [Multi-domain]  Cd Length: 331  Bit Score: 491.56  E-value: 2.58e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143   1 RAAQERSDIEIVAINDLLDAEYMAYMLKYDSTHGRFDGTVEVKDGHLVVNGKTIRVTAERDPANLKWNEVNVDVVAEATG 80
Cdd:PRK15425   19 RAAQKRSDIEIVAINDLLDADYMAYMLKYDSTHGRFDGTVEVKDGHLIVNGKKIRVTAERDPANLKWDEVGVDVVAEATG 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143  81 LFLTDETARKHIAAGAKKVVLTGPSKDDTPMFVMGVNHKTYAGQEIVSNASCTTNCLAPLAKVINDNFGIVEALMTTVHA 160
Cdd:PRK15425   99 LFLTDETARKHITAGAKKVVMTGPSKDNTPMFVKGANFDKYAGQDIVSNASCTTNCLAPLAKVINDNFGIIEGLMTTVHA 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143 161 TTATQKTVDGPSHKDWRGGRGAAQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTARLEKPASYKEICA 240
Cdd:PRK15425  179 TTATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTVRLEKAATYEQIKA 258

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2168678143 241 AIKAASEGELKGVLGYTEDEVVSTDFNGEKLTSVFDAK 278
Cdd:PRK15425  259 AVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAK 296
PLN02272 PLN02272
glyceraldehyde-3-phosphate dehydrogenase
 1-278 3.43e-162

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 177912 [Multi-domain]  Cd Length: 421  Bit Score: 457.01  E-value: 3.43e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143   1 RAAQERSDIEIVAIND-LLDAEYMAYMLKYDSTHGRFDGTVEV-KDGHLVVNGKTIRVTAERDPANLKWNEVNVDVVAEA 78
Cdd:PLN02272  102 RIATSRDDIEVVAVNDpFIDAKYMAYMFKYDSTHGNFKGTINVvDDSTLEINGKQIKVTSKRDPAEIPWGDFGAEYVVES 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143  79 TGLFLTDETARKHIAAGAKKVVLTGPSKDdTPMFVMGVNHKTY-AGQEIVSNASCTTNCLAPLAKVINDNFGIVEALMTT 157
Cdd:PLN02272  182 SGVFTTVEKASAHLKGGAKKVVISAPSAD-APMFVVGVNEKTYkPNMNIVSNASCTTNCLAPLAKVVHEEFGILEGLMTT 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143 158 VHATTATQKTVDGPSHKDWRGGRGAAQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTARLEKPASYKE 237
Cdd:PLN02272  261 VHATTATQKTVDGPSMKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSVVDLTCRLEKSASYED 340

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2168678143 238 ICAAIKAASEGELKGVLGYTEDEVVSTDFNGEKLTSVFDAK 278
Cdd:PLN02272  341 VKAAIKYASEGPLKGILGYTDEDVVSNDFVGDSRSSIFDAK 381
GAPDH-I TIGR01534
glyceraldehyde-3-phosphate dehydrogenase, type I; This model represents ...
 1-278 5.04e-156

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: 437.48  E-value: 5.04e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143   1 RAAQER--SDIEIVAINDLLDAEYMAYMLKYDSTHGRFDGTVEVKDGHLVVNGK-TIRVTAERDPANLKWNEVNVDVVAE 77
Cdd:TIGR01534  16 RRILEKpgNDLEVVAINDLTDLEKLAYLLKYDSVHGRFEGEVTVDEDGLVVNGKeVISVFSERDPSDLPWKALGVDIVIE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143  78 ATGLFLTDETARKHIAAGAKKVVLTGPSKDDTPMFVMGVNHKTYAGQE-IVSNASCTTNCLAPLAKVINDNFGIVEALMT 156
Cdd:TIGR01534  96 CTGKFRDKEKLEKHLEAGAKKVLISAPSKGDVKTIVYGVNHDEYDGEErIISNASCTTNCLAPLAKVLDEAFGIVSGLMT 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143 157 TVHATTATQKTVDGPsHKDWRGGRGAAQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTARLEKPASYK 236
Cdd:TIGR01534 176 TVHAYTNDQNLLDGP-HKDLRRARAAALNIIPTSTGAAKAIGKVLPELAGKLTGMAIRVPTPNVSLVDLVVNLEKDVTVE 254

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2168678143 237 EICAAIKAASEGELKGVLGYTEDEVVSTDFNGEKLTSVFDAK 278
Cdd:TIGR01534 255 EVNAALKEASEGELKGVLGYTEDELVSSDFIGSPYSSIVDAT 296
PTZ00023 PTZ00023
glyceraldehyde-3-phosphate dehydrogenase; Provisional
 1-278 1.35e-145

glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173322 [Multi-domain]  Cd Length: 337  Bit Score: 411.54  E-value: 1.35e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143   1 RAAQERSDIEIVAIND-LLDAEYMAYMLKYDSTHGRFDGTVEVKDGHLVVNGKTIRVTAERDPANLKWNEVNVDVVAEAT 79
Cdd:PTZ00023   19 RAALEREDVEVVAINDpFMTLDYMCYLLKYDSVHGSLPAEVSVTDGFLMIGSKKVHVFFEKDPAAIPWGKNGVDVVCEST 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143  80 GLFLTDETARKHIAAGAKKVVLTGPSKDDTPMFVMGVNHKTY-AGQEIVSNASCTTNCLAPLAKVINDNFGIVEALMTTV 158
Cdd:PTZ00023   99 GVFLTKEKAQAHLKGGAKKVIMSAPPKDDTPIYVMGVNHTQYdKSQRIVSNASCTTNCLAPLAKVVNDKFGIVEGLMTTV 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143 159 HATTATQKTVDGPSH--KDWRGGRGAAQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTARLEKPASYK 236
Cdd:PTZ00023  179 HASTANQLTVDGPSKggKDWRAGRCAGVNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPVPDVSVVDLTCKLAKPAKYE 258

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2168678143 237 EICAAIKAASEGELKGVLGYTEDEVVSTDFNGEKLTSVFDAK 278
Cdd:PTZ00023  259 EIVAAVKKAAEGPLKGILGYTDDEVVSSDFVHDKRSSIFDVK 300
PRK07729 PRK07729
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-276 3.54e-121

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 236079 [Multi-domain]  Cd Length: 343  Bit Score: 349.81  E-value: 3.54e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143   1 RAAQERSDIEIVAINDLLDAEYMAYMLKYDSTHGRFDGTVEVKDGHLVVNGKTIRVTAERDPANLKWNEVNVDVVAEATG 80
Cdd:PRK07729   19 RKAIKESAFEIVAINASYPSETLAHLIKYDTVHGKFDGTVEAFEDHLLVDGKKIRLLNNRDPKELPWTDLGIDIVIEATG 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143  81 LFLTDETARKHIAAGAKKVVLTGPSKDDTPMFVMGVNHKTYAGQE--IVSNASCTTNCLAPLAKVINDNFGIVEALMTTV 158
Cdd:PRK07729   99 KFNSKEKAILHVEAGAKKVILTAPGKNEDVTIVVGVNEDQLDIEKhtIISNASCTTNCLAPVVKVLDEQFGIENGLMTTV 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143 159 HATTATQKTVDGPsHKDWRGGRGAAQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTARLEKPASYKEI 238
Cdd:PRK07729  179 HAYTNDQKNIDNP-HKDLRRARACGQSIIPTTTGAAKALAKVLPHLNGKLHGMALRVPTPNVSLVDLVVDVKRDVTVEEI 257

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2168678143 239 CAAIKAASEGELKGVLGYTEDEVVSTDFNGEKLTSVFD 276
Cdd:PRK07729  258 NEAFKTAANGALKGILEFSEEPLVSIDFNTNTHSAIID 295
PLN02358 PLN02358
glyceraldehyde-3-phosphate dehydrogenase
 1-278 7.68e-115

glyceraldehyde-3-phosphate dehydrogenase


Pssm-ID: 165999 [Multi-domain]  Cd Length: 338  Bit Score: 333.61  E-value: 7.68e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143   1 RAAQERSDIEIVAIND-LLDAEYMAYMLKYDSTHGRFD-GTVEVKDGHLVVNG-KTIRVTAERDPANLKWNEVNVDVVAE 77
Cdd:PLN02358   22 RVVLQRDDVELVAVNDpFITTEYMTYMFKYDSVHGQWKhHELKVKDDKTLLFGeKPVTVFGIRNPEDIPWGEAGADFVVE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143  78 ATGLFLTDETARKHIAAGAKKVVLTGPSKDdTPMFVMGVNHKTYAGQ-EIVSNASCTTNCLAPLAKVINDNFGIVEALMT 156
Cdd:PLN02358  102 STGVFTDKDKAAAHLKGGAKKVVISAPSKD-APMFVVGVNEHEYKSDlDIVSNASCTTNCLAPLAKVINDRFGIVEGLMT 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143 157 TVHATTATQKTVDGPSHKDWRGGRGAAQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTARLEKPASYK 236
Cdd:PLN02358  181 TVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPSLNGKLTGMSFRVPTVDVSVVDLTVRLEKAATYD 260

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2168678143 237 EICAAIKAASEGELKGVLGYTEDEVVSTDFNGEKLTSVFDAK 278
Cdd:PLN02358  261 EIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAK 302
PTZ00434 PTZ00434
cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional
 7-278 1.13e-111

cytosolic glyceraldehyde 3-phosphate dehydrogenase; Provisional


Pssm-ID: 185614 [Multi-domain]  Cd Length: 361  Bit Score: 326.63  E-value: 1.13e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143   7 SDIEIVAINDL-LDAEYMAYMLKYDSTHGRFDGTVEV--------KDGHLVVNGKTIR-VTAERDPANLKWNEVNVDVVA 76
Cdd:PTZ00434   30 TEIDVVAVVDMsTNAEYFAYQMKYDTVHGRPKYTVETtksspsvkTDDVLVVNGHRIKcVKAQRNPADLPWGKLGVDYVI 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143  77 EATGLFLTDETARKHIAAGAKKVVLTGPSKDDTPMFVMGVNHKTYAGQE--IVSNASCTTNCLAPLAKVI-NDNFGIVEA 153
Cdd:PTZ00434  110 ESTGLFTDKLAAEGHLKGGAKKVVISAPASGGAKTIVMGVNQHEYSPTEhhVVSNASCTTNCLAPIVHVLtKEGFGIETG 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143 154 LMTTVHATTATQKTVDGPSHKDWRGGRGAAQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTARLEKPA 233
Cdd:PTZ00434  190 LMTTIHSYTATQKTVDGVSVKDWRGGRAAAVNIIPSTTGAAKAVGMVIPSTKGKLTGMSFRVPTPDVSVVDLTFRATRDT 269

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2168678143 234 SYKEICAAIKAASEGELKGVLGYTEDEVVSTDFNGEKLTSVFDAK 278
Cdd:PTZ00434  270 SIQEIDAAIKRASQTYMKGILGFTDDELVSADFINDNRSSIYDSK 314
PRK07403 PRK07403
type I glyceraldehyde-3-phosphate dehydrogenase;
4-277 1.71e-107

type I glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 180962 [Multi-domain]  Cd Length: 337  Bit Score: 314.92  E-value: 1.71e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143   4 QERSDIEIVAINDLLDAEYMAYMLKYDSTHGRFDGTVEVKDGHLVVNGKTIRVTAERDPANLKWNEVNVDVVAEATGLFL 83
Cdd:PRK07403   23 RENSQLELVAINDTSDPRTNAHLLKYDSMLGKLNADISADENSITVNGKTIKCVSDRNPLNLPWKEWGIDLIIESTGVFV 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143  84 TDETARKHIAAGAKKVVLTGPSK-DDTPMFVMGVNHKTYAGQE--IVSNASCTTNCLAPLAKVINDNFGIVEALMTTVHA 160
Cdd:PRK07403  103 TKEGASKHIQAGAKKVLITAPGKgEDIGTYVVGVNHHEYDHEDhnIISNASCTTNCLAPIAKVLHDNFGIIKGTMTTTHS 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143 161 TTATQKTVDGpSHKDWRGGRGAAQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTARLEKPASYKEICA 240
Cdd:PRK07403  183 YTGDQRILDA-SHRDLRRARAAAVNIVPTSTGAAKAVALVIPELKGKLNGIALRVPTPNVSVVDLVVQVEKRTITEQVNE 261

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2168678143 241 AIKAASEGELKGVLGYTEDEVVSTDFNGEKLTSVFDA 277
Cdd:PRK07403  262 VLKDASEGPLKGILEYSDLPLVSSDYRGTDASSIVDA 298
GAPDH_I_C cd18126
C-terminal catalytic domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 132-278 3.63e-106

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: 305.15  E-value: 3.63e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143 132 CTTNCLAPLAKVINDNFGIVEALMTTVHATTATQKTVDGPsHKDWRGGRGAAQNIIPSSTGAAKAVGKVIPELNGKLTGM 211
Cdd:cd18126     1 CTTNCLAPVAKVLNDNFGIEEGLMTTVHAYTNDQKLVDGP-HKDLRRARAAAQNIIPTSTGAAKAVGLVIPELKGKLTGM 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2168678143 212 AFRVPTPNVSVVDLTARLEKPASYKEICAAIKAASEGELKGVLGYTEDEVVSTDFNGEKLTSVFDAK 278
Cdd:cd18126    80 AFRVPTPNVSVVDLTVRLEKPVTVEEVNAALKKAAEGPLKGILGYTEDPLVSSDFVGDPHSSIFDAT 146
G3PDH_Arsen NF033735
ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;
1-277 1.83e-96

ArsJ-associated glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 468158 [Multi-domain]  Cd Length: 324  Bit Score: 286.44  E-value: 1.83e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143   1 RAAQERSDIEIVAINDLL-DAEYMAYMLKYDSTHGRFDGTVEVKDGHLVVNGKTIRVTAERDPANLKWNEvNVDVVAEAT 79
Cdd:NF033735   15 RALWGRPGLEIVHINDLAgDAATLAHLLEFDSVHGRWDAEVTAEEDSIVIDGKRISFSSNKDIEDTPWGD-GVDVVIECT 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143  80 GLFLTDETARKHIAAGAKKVVLTGPSKDDTPM-FVMGVNHKTYAGQE--IVSNASCTTNCLAPLAKVINDNFGIVEALMT 156
Cdd:NF033735   94 GKFKTPEKLQPYFDQGVKKVVVSAPVKEEGVLnIVYGVNDHLYDPARhrIVTAASCTTNCLAPVVKVIHEKIGIKHGSIT 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143 157 TVHATTATQKTVDGPsHKDWRGGRGAAQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTARLEKPASYK 236
Cdd:NF033735  174 TIHDITNTQTIVDAP-HKDLRRARSCGMSLIPTTTGSATAITLIFPELKGKLNGHAVRVPLLNASLTDCVFEVERPTTVE 252

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2168678143 237 EICAAIKAASEGELKGVLGYTEDEVVSTDFNGEKLTSVFDA 277
Cdd:NF033735  253 EVNALFKAAAEGPLKGILGYEERPLVSVDYVNDPRSSIIDA 293
PLN03096 PLN03096
glyceraldehyde-3-phosphate dehydrogenase A; Provisional
 7-277 3.47e-94

glyceraldehyde-3-phosphate dehydrogenase A; Provisional


Pssm-ID: 215572 [Multi-domain]  Cd Length: 395  Bit Score: 282.97  E-value: 3.47e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143   7 SDIEIVAINDLLDAEYMAYMLKYDSTHGRFDGTVE-VKDGHLVVNGKTIRVTAERDPANLKWNEVNVDVVAEATGLFLTD 85
Cdd:PLN03096   85 SPLDVVAINDTGGVKQASHLLKYDSTLGTFDADVKpVGDDAISVDGKVIKVVSDRNPLNLPWGELGIDLVIEGTGVFVDR 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143  86 ETARKHIAAGAKKVVLTGPSKDDTPMFVMGVNHKTYAGQE-IVSNASCTTNCLAPLAKVINDNFGIVEALMTTVHATTAT 164
Cdd:PLN03096  165 EGAGKHIQAGAKKVLITAPGKGDIPTYVVGVNADDYKHSDpIISNASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGD 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143 165 QKTVDGpSHKDWRGGRGAAQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTARLEKPASYKEICAAIKA 244
Cdd:PLN03096  245 QRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVALVLPNLKGKLNGIALRVPTPNVSVVDLVVQVEKKTFAEEVNAAFRD 323

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2168678143 245 ASEGELKGVLGYTEDEVVSTDFNGEKLTSVFDA 277
Cdd:PLN03096  324 AAEKELKGILAVCDEPLVSVDFRCSDVSSTIDS 356
PLN02237 PLN02237
glyceraldehyde-3-phosphate dehydrogenase B
 3-277 1.75e-88

glyceraldehyde-3-phosphate dehydrogenase B


Pssm-ID: 215131 [Multi-domain]  Cd Length: 442  Bit Score: 270.23  E-value: 1.75e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143   3 AQERSDIEIVAINDLLDAEYMAYMLKYDSTHGRFDGTVEVKDGHLV-VNGKTIRVTAERDPANLKWNEVNVDVVAEATGL 81
Cdd:PLN02237   96 GRKDSPLDVVVVNDSGGVKNASHLLKYDSMLGTFKADVKIVDDETIsVDGKPIKVVSNRDPLKLPWAELGIDIVIEGTGV 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143  82 FLTDETARKHIAAGAKKVVLTGPSK-DDTPMFVMGVNHKTYAGQ--EIVSNASCTTNCLAPLAKVINDNFGIVEALMTTV 158
Cdd:PLN02237  176 FVDGPGAGKHIQAGAKKVIITAPAKgADIPTYVVGVNEDDYDHEvaNIVSNASCTTNCLAPFVKVLDEEFGIVKGTMTTT 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143 159 HATTATQKTVDGpSHKDWRGGRGAAQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTARLEKPA-SYKE 237
Cdd:PLN02237  256 HSYTGDQRLLDA-SHRDLRRARAAALNIVPTSTGAAKAVSLVLPQLKGKLNGIALRVPTPNVSVVDLVVNVEKKGiTAED 334

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2168678143 238 ICAAIKAASEGELKGVLGYTEDEVVSTDFNGEKLTSVFDA 277
Cdd:PLN02237  335 VNAAFRKAADGPLKGILAVCDVPLVSVDFRCSDVSSTIDA 374
PRK13535 PRK13535
erythrose 4-phosphate dehydrogenase; Provisional
 1-276 5.26e-85

erythrose 4-phosphate dehydrogenase; Provisional


Pssm-ID: 184122 [Multi-domain]  Cd Length: 336  Bit Score: 257.68  E-value: 5.26e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143   1 RAAQE---RSDIEIVAINDLLDAEYMAYMLKYDSTHGRFDGTVEVKDGHLVVNGKTIRVTAERDPANLKWNEVNVDVVAE 77
Cdd:PRK13535   18 RALYEsgrRAEITVVAINELADAEGMAHLLKYDTSHGRFAWDVRQERDQLFVGDDAIRLLHERDIASLPWRELGVDVVLD 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143  78 ATGLFLTDETARKHIAAGAKKVVLTGPSKDDT-PMFVMGVNHKTY-AGQEIVSNASCTTNCLAPLAKVINDNFGIVEALM 155
Cdd:PRK13535   98 CTGVYGSREDGEAHIAAGAKKVLFSHPGSNDLdATVVYGVNHDQLrAEHRIVSNASCTTNCIIPVIKLLDDAFGIESGTV 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143 156 TTVHATTATQKTVDGpSHKDWRGGRGAAQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTARLEKPASY 235
Cdd:PRK13535  178 TTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLAAGITRIFPQFNDRFEAISVRVPTINVTAIDLSVTVKKPVKV 256

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2168678143 236 KEICAAIKAASEGELKGVLGYTEDEVVSTDFNGEKLTSVFD 276
Cdd:PRK13535  257 NEVNQLLQKAAQGAFHGIVDYTELPLVSIDFNHDPHSAIVD 297
PRK08955 PRK08955
glyceraldehyde-3-phosphate dehydrogenase; Validated
 1-277 1.19e-84

glyceraldehyde-3-phosphate dehydrogenase; Validated


Pssm-ID: 169599 [Multi-domain]  Cd Length: 334  Bit Score: 256.58  E-value: 1.19e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143   1 RAAQERSDIEIVAINDLL-DAEYMAYMLKYDSTHGRFDGTVEVKDGHLVVNGKTIRVTAERDPANLKWNevNVDVVAEAT 79
Cdd:PRK08955   19 RAAWDWPELEFVQINDPAgDAATLAHLLEFDSVHGRWHHEVTAEGDAIVINGKRIRTTQNKAIADTDWS--GCDVVIEAS 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143  80 GLFLTDETARKHIAAGAKKVVLTGPSKDDTPM-FVMGVNHKTY--AGQEIVSNASCTTNCLAPLAKVINDNFGIVEALMT 156
Cdd:PRK08955   97 GVMKTKALLQAYLDQGVKRVVVTAPVKEEGVLnIVMGVNDHLFdpAIHPIVTAASCTTNCLAPVVKVIHEKLGIKHGSMT 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143 157 TVHATTATQKTVDGPsHKDWRGGRGAAQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTARLEKPASYK 236
Cdd:PRK08955  177 TIHDLTNTQTILDAP-HKDLRRARACGMSLIPTTTGSATAITEIFPELKGKLNGHAVRVPLANASLTDCVFEVERDTTVE 255

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2168678143 237 EICAAIKAASEGELKGVLGYTEDEVVSTDFNGEKLTSVFDA 277
Cdd:PRK08955  256 EVNALLKEAAEGELKGILGYEERPLVSIDYKTDPRSSIVDA 296
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 137-278 2.29e-82

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: 244.42  E-value: 2.29e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143 137 LAPLAKVINDNFGIVEALMTTVHATTATQKTVDGPSHKDWRGGRGAAQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVP 216
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLDGPHHKDLRRGRAAAPNIIPTSTGAAKAVGLVLPELKGKLDGMAVRVP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2168678143 217 TPNVSVVDLTARLEKPASYKEICAAIKAASEGELKGVLGYTEDEVVSTDFNGEKLTSVFDAK 278
Cdd:pfam02800  81 TPNVSVVDLVVELEKPVTVEEVNAALKEAAEGALKGILSYTEDPLVSSDFIGDPHSSIFDAK 142
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 1-131 3.75e-80

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: 238.83  E-value: 3.75e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143   1 RAAQERSDIEIVAINDLLDAEYMAYMLKYDSTHGRFDGTVEVKDGHLVVNGKTIRVTAERDPANLKWNEVNVDVVAEATG 80
Cdd:cd05214    17 RAALERDDIEVVAINDLTDDETLAYLLKYDSVHGRFDGEVEVDDDALIVNGKKIKVFAERDPAELPWGELGVDIVIESTG 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2168678143  81 LFLTDETARKHIAAGAKKVVLTGPSKDDTPMFVMGVNHKTY-AGQEIVSNAS 131
Cdd:cd05214    97 VFTTKEKASAHLKAGAKKVIISAPAKDDDPTIVMGVNHDKYdADDKIISNAS 148
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 132-278 7.16e-75

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


Pssm-ID: 467673  Cd Length: 164  Bit Score: 225.57  E-value: 7.16e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143 132 CTTNCLAPLAKVINDNFGIVEALMTTVHATTATQKTVDGPSHKDWRGGRGAAQNIIPSSTGAAKAVGKVIPELNGKLTGM 211
Cdd:cd18123     1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTVDGPSGKDWRASRGAVNNIIPNPTGAAKAVGKVLPELNGKLTGM 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2168678143 212 AFRVPTPNVSVVDLTARLEKPASYKEICAAIKAASEGelKGVLGYTEDEVVSTDFNGEKLTSVFDAK 278
Cdd:cd18123    81 AVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPEG--KGRLGYTEAEDVSSDFRGDIFESVFDAE 145
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-132 8.14e-73

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: 219.73  E-value: 8.14e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143    1 RAAQERSDIEIVAINDLLDAEYMAYMLKYDSTHGRFDGTVEVKDGHLVVNGKTIRVTAERDPANLKWNEVNVDVVAEATG 80
Cdd:smart00846  17 RAALERPDVEVVAINDLTDPEYLAYLLKYDSVHGRFPGTVEVEGDGLVVNGKAIKVFAERDPANLPWGELGVDIVVECTG 96

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2168678143   81 LFLTDETARKHIAAGAKKVVLTGPSKDDTPMFVMGVNHKTYAGQE-IVSNASC 132
Cdd:smart00846  97 GFTTREKASAHLKAGAKKVIISAPSKDADPTFVYGVNHDEYDGEDhIISNASC 149
PRK08289 PRK08289
glyceraldehyde-3-phosphate dehydrogenase; Reviewed
 19-278 1.76e-70

glyceraldehyde-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 236219 [Multi-domain]  Cd Length: 477  Bit Score: 224.80  E-value: 1.76e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143  19 DAEYMAYMLKYDSTHGRFDGTVEVKDGH--LVVNGKTIRVTAERDPANLKWNEVNVD--VVAEATGLFLTDETARKHIAA 94
Cdd:PRK08289  170 DLEKRASLLRRDSVHGPFNGTITVDEENnaIIANGNYIQVIYANSPEEVDYTAYGINnaLVVDNTGKWRDEEGLSQHLKS 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143  95 -GAKKVVLTGPSKDDTPMFVMGVNHKTYAGQE-IVSNASCTTNCLAPLAKVINDNFGIVEALMTTVHATTATQKTVDGpS 172
Cdd:PRK08289  250 kGVAKVLLTAPGKGDIKNIVHGVNHSDITDEDkIVSAASCTTNAITPVLKAVNDKYGIVNGHVETVHSYTNDQNLIDN-Y 328

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143 173 HKDWRGGRGAAQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTARLEKPASYKEICAAIKAAS-EGELK 251
Cdd:PRK08289  329 HKGDRRGRSAPLNMVITETGAAKAVAKALPELAGKLTGNAIRVPTPNVSMAILNLNLEKETSREELNEYLRQMSlHSPLQ 408

                         250       260
                  ....*....|....*....|....*...
gi 2168678143 252 GVLGYTED-EVVSTDFNGEKLTSVFDAK 278
Cdd:PRK08289  409 NQIDYTDStEVVSSDFVGSRHAGVVDSQ 436
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 1-84 2.10e-46

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: 150.72  E-value: 2.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143   1 RAAQERSDIEIVAINDLLDAEYMAYMLKYDSTHGRFDGTVEVKDGHLVVNGKTIRVTAERDPANLKWNEVNVDVVAEATG 80
Cdd:pfam00044  17 RAALERPDIEVVAINDLTDPETLAYLLKYDSVHGRFPGEVEAEEDGLVVNGKKIKVFAERDPAELPWGDLGVDVVIESTG 96


                  ....
gi 2168678143  81 LFLT 84
Cdd:pfam00044  97 VFTT 100
GAPDH_N_E4PDH cd17892
N-terminal NAD(P)-binding domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 1-131 1.65e-45

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: 150.88  E-value: 1.65e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143   1 RAAQE---RSDIEIVAINDLLDAEYMAYMLKYDSTHGRFDGTVEVKDGHLVVNGKTIRVTAERDPANLKWNEVNVDVVAE 77
Cdd:cd17892    17 RALYEsgrRAEFQVVAINELADAETIAHLTKYDTTHGRFPGEVRVENDQLFVNGDKIRVLHEPDPENLPWRELGIDLVLE 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2168678143  78 ATGLFLTDETARKHIAAGAKKVVLTGPSKDDT-PMFVMGVNHKTYAGQE-IVSNAS 131
Cdd:cd17892    97 CTGVFGSREDAERHLAAGAKKVLFSHPASNDVdATIVYGINQDLLRAEHrIVSNAS 152
GAPDH_C_E4PDH cd23937
C-terminal catalytic domain of D-erythrose-4-phosphate dehydrogenase (E4PDH) and similar ...
 132-277 1.38e-42

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


Pssm-ID: 467686  Cd Length: 165  Bit Score: 143.32  E-value: 1.38e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143 132 CTTNCLAPLAKVINDNFGIVEALMTTVHATTATQKTVDGpSHKDWRGGRGAAQNIIPSSTGAAKAVGKVIPELNGKLTGM 211
Cdd:cd23937     1 CTTNCIVPVIKVLDEAFGIESGTITTIHSAMNDQQVIDA-YHPDLRRTRAASQSIIPVDTKLARGIERILPHLAGRFEAI 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2168678143 212 AFRVPTPNVSVVDLTARLEKPASYKEICAAIKAASEGELKGVLGYTEDEVVSTDFNGEKLTSVFDA 277
Cdd:cd23937    80 AVRVPTINVTAMDLSVTLKKDVTAEEVNRVLRQASQGRLKGILGYTEEPLVSVDFNHDPHSCIVDG 145
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 132-278 6.89e-42

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: 141.50  E-value: 6.89e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143 132 CTTNCLAPLAKVINDNFGIVEALMTTVHATTATQKTVDGPSHKDWrgGRGAAQNIIPSSTGAAKAVGKVIPELN--GKLT 209
Cdd:cd18122     1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKSE--VRAIIPNIPKNETKHAPETGKVLGEIGkpIKVD 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2168678143 210 GMAFRVPTPNVSVVDLTARLEKPASYKEICAAIKAASEGELKGVLGYTEDEVVSTDFNGEKLTSVFDAK 278
Cdd:cd18122    79 GIAVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAEDGLTYAKVSTRSVGGVYGVPVGRQ 147
PTZ00353 PTZ00353
glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional
 11-265 9.58e-39

glycosomal glyceraldehyde-3-phosphate dehydrogenase; Provisional


Pssm-ID: 173546 [Multi-domain]  Cd Length: 342  Bit Score: 138.47  E-value: 9.58e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143  11 IVAINDL-LDAEYMAYMLKYDSTHGRFDGT-VEVKDGHLVVNG-KTIRVTAERDPANLKWNEVNVDVVAEATGLFLTDET 87
Cdd:PTZ00353   29 VVAVNDAsVSIAYIAYVLEQESPLSAPDGAsIRVVGEQIVLNGtQKIRVSAKHDLVEIAWRDYGVQYVVECTGLYSTRSR 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143  88 ARKHIAAGAKKVVLTGPSKDdTPMFVMGVN-HKTYAGQEIVSNASCTTNCLAPLAKVINDNFGIVEALMTTVHATTAtQK 166
Cdd:PTZ00353  109 CWGHVTGGAKGVFVAGQSAD-APTVMAGSNdERLSASLPVCCAGAPIAVALAPVIRALHEVYGVEECSYTAIHGMQP-QE 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2168678143 167 TVDGPSH--KDWRGGRGAAQNIIPSSTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTARLEKPASYKEICAAIKA 244
Cdd:PTZ00353  187 PIAARSKnsQDWRQTRVAIDAIAPYRDNGAETVCKLLPHLVGRISGSAFQVPVKKGCAIDMLVRTKQPVSKEVVDSALAE 266

                         250       260
                  ....*....|....*....|.
gi 2168678143 245 ASEGELKGVLGYTEDEVVSTD 265
Cdd:PTZ00353  267 AASDRLNGVLCISKRDMISVD 287
GAPDH-like_N cd05192
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ...
 73-136 2.38e-12

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: 61.99  E-value: 2.38e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2168678143  73 DVVAEATGLFLTDETARKHIAAGAKKVVLTGPSKDDTPMFVMGVNH-KTYAGQEIVSNASCTTNC 136
Cdd:cd05192    35 DVVIECTGSFTDDDNAEKHIKAGGKKAVITAPEKGDIPTIVVVLNElAKSAGATVVSNANETSYS 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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