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Conserved domains on  [gi|499597459|ref|WP_011278193|]
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phosphorylating glyceraldehyde-3-phosphate dehydrogenase [Sulfolobus acidocaldarius]

Protein Classification

type II glyceraldehyde-3-phosphate dehydrogenase( domain architecture ID 11480225)

type II glyceraldehyde-3-phosphate dehydrogenase catalyses the oxidative phosphorylation of d-glyceraldehyde-3-phosphate to form 1,3 diphosphoglycerate; shows dual cofactor specificity and uses NADP+ in preference to NAD+

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK04207 PRK04207
type II glyceraldehyde-3-phosphate dehydrogenase;
3-342 0e+00

type II glyceraldehyde-3-phosphate dehydrogenase;


:

Pssm-ID: 179786 [Multi-domain]  Cd Length: 341  Bit Score: 579.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459   3 KVKVAINGYGTIGKRVADAIRLQPDMELIGVAKTSPNYEAFTAMRKGYKLYTTKENIQK-FQNSGINVAGSIEDMIKDSD 81
Cdd:PRK04207   1 MIKVGVNGYGTIGKRVADAVAAQPDMELVGVAKTKPDYEARVAVEKGYPLYVADPEREKaFEEAGIPVAGTIEDLLEKAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459  82 IIIDATPGGVGANYKKIYQEYGKKAIFQGGEKSDVADVSFSALCNYNDAINKNYIRVVSCNTTGILRVLCTINNFDKIEK 161
Cdd:PRK04207  81 IVVDATPGGVGAKNKELYEKAGVKAIFQGGEKAEVAGVSFNALANYEEALGKDYVRVVSCNTTGLCRTLCALDRAFGVKK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459 162 VRGTIVRRAADPKEVKKGPINSIVADPARIPSHHAKDVLTVLKGIDIITSALVAPTTLMHLHTLFITTRNKVSKEDLLNI 241
Cdd:PRK04207 161 VRATLVRRAADPKEVKRGPINAIVPDPVTVPSHHGPDVKTVLPDLDITTMAVKVPTTLMHMHSVNVELKKPVTKEEVLEA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459 242 LSNTPRILLLNTEkADAESTAEIMEIARDLGRYRNDVPETVIFEDSIYTNGNEIFLMYGVHQESIVVPENIDAIRASLNI 321
Cdd:PRK04207 241 LENTPRILLVRAS-DGIDSTAELIEYARDLGRPRGDLYENAVWEDSITVDGNELYLMQAVHQESIVVPENIDAIRAMLGL 319

                        330       340
                 ....*....|....*....|..
gi 499597459 322 MS-RDESIRLTNETLKIGKGYL 342
Cdd:PRK04207 320 EDdEEKSIEKTNKALGIGKGKL 341
 
Name Accession Description Interval E-value
PRK04207 PRK04207
type II glyceraldehyde-3-phosphate dehydrogenase;
3-342 0e+00

type II glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 179786 [Multi-domain]  Cd Length: 341  Bit Score: 579.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459   3 KVKVAINGYGTIGKRVADAIRLQPDMELIGVAKTSPNYEAFTAMRKGYKLYTTKENIQK-FQNSGINVAGSIEDMIKDSD 81
Cdd:PRK04207   1 MIKVGVNGYGTIGKRVADAVAAQPDMELVGVAKTKPDYEARVAVEKGYPLYVADPEREKaFEEAGIPVAGTIEDLLEKAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459  82 IIIDATPGGVGANYKKIYQEYGKKAIFQGGEKSDVADVSFSALCNYNDAINKNYIRVVSCNTTGILRVLCTINNFDKIEK 161
Cdd:PRK04207  81 IVVDATPGGVGAKNKELYEKAGVKAIFQGGEKAEVAGVSFNALANYEEALGKDYVRVVSCNTTGLCRTLCALDRAFGVKK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459 162 VRGTIVRRAADPKEVKKGPINSIVADPARIPSHHAKDVLTVLKGIDIITSALVAPTTLMHLHTLFITTRNKVSKEDLLNI 241
Cdd:PRK04207 161 VRATLVRRAADPKEVKRGPINAIVPDPVTVPSHHGPDVKTVLPDLDITTMAVKVPTTLMHMHSVNVELKKPVTKEEVLEA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459 242 LSNTPRILLLNTEkADAESTAEIMEIARDLGRYRNDVPETVIFEDSIYTNGNEIFLMYGVHQESIVVPENIDAIRASLNI 321
Cdd:PRK04207 241 LENTPRILLVRAS-DGIDSTAELIEYARDLGRPRGDLYENAVWEDSITVDGNELYLMQAVHQESIVVPENIDAIRAMLGL 319

                        330       340
                 ....*....|....*....|..
gi 499597459 322 MS-RDESIRLTNETLKIGKGYL 342
Cdd:PRK04207 320 EDdEEKSIEKTNKALGIGKGKL 341
GAPDH-II_archae TIGR01546
glyceraldehyde-3-phosphate dehydrogenase, type II; This model describes the type II ...
 6-337 1.81e-166

glyceraldehyde-3-phosphate dehydrogenase, type II; This model describes the type II glyceraldehyde-3-phosphate dehydrogenases which are limited to archaea. These enzymes catalyze the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. In archaea, either NAD or NADP may be utilized as the cofactor. The class I GAPDH's from bacteria and eukaryotes are covered by TIGR01534. All of the members of the seed are characterized. See, for instance. This model is very solid, there are no species falling between trusted and noise at this time. The closest relatives scoring in the noise are the class I GAPDH's.


Pssm-ID: 130609  Cd Length: 333  Bit Score: 467.04  E-value: 1.81e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459    6 VAINGYGTIGKRVADAIRLQPDMELIGVAKTSPNYEAFTAMRKGYKLY-TTKENIQKFQNSGINVAGSIEDMIKDSDIII 84
Cdd:TIGR01546   1 VGVNGYGTIGKRVADAVTKQDDMKLVGVTKTSPDFEAYRAKELGIPVYaASEEFIPRFEEAGIEVAGTLEDLLEKVDIVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459   85 DATPGGVGANYKKIYQEYGKKAIFQGGEKSDVADVSFSALCNYNDAINKNYIRVVSCNTTGILRVLCTINNFDKIEKVRG 164
Cdd:TIGR01546  81 DATPGGIGAKNKPLYEKAGVKAIFQGGEKAEVADVSFVAQANYEAALGKDYVRVVSCNTTGLVRTLNAINDYSKVDKVRA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459  165 TIVRRAADPKEVKKGPINSIVADPARIPSHHAKDVLTVLKGIDIITSALVAPTTLMHLHTLFITTRNKVSKEDLLNILSN 244
Cdd:TIGR01546 161 VMVRRAADPNDVKKGPINAIVPDPVTVPSHHGPDVQTVIPNLNIETMAFVVPTTLMHVHSIMVELKKPVTKDDIIDILEN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459  245 TPRILLLNTEKaDAESTAEIMEIARDLGRYRNDVPETVIFEDSIYTNGNEIFLMYGVHQESIVVPENIDAIRASLNIMSR 324
Cdd:TIGR01546 241 TPRVLLFEKKK-GFESTAELIEFARDLHRERNDLYEIAVWKESINVKDNELFYMQAVHQESDVVPENIDAIRAMFELADK 319

                         330
                  ....*....|...
gi 499597459  325 DESIRLTNETLKI 337
Cdd:TIGR01546 320 WDSIKKTNKSLGI 332
GAPDH_II_C cd18127
C-terminal catalytic domain of type II glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 140-304 5.17e-77

C-terminal catalytic domain of type II 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 type II NADP+ utilizing GAPDHs, mainly from archaea.


Pssm-ID: 467677  Cd Length: 162  Bit Score: 233.25  E-value: 5.17e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459 140 SCNTTGILRVLCTINNFDKIEKVRGTIVRRAADPKEVKKGPINSIVADPArIPSHHAKDVLTVLKGIDIITSALVAPTTL 219
Cdd:cd18127    1 SCNTTGLSRVLKALDRAFGLKRVRATIVRRAADPGKHKKGVINAIVPEPK-DPSHHAPDVKTVFPDLDITTSAVKVPTTL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459 220 MHLHTLFITTRNKVSKEDLLNILSNTPRILLlnTEKADAESTAEIMEIARDLGRYRNDVPETVIFEDSIYTNGNEIFLMY 299
Cdd:cd18127   80 MHLHTINVELKRKVSREEVLEALASNPRIAL--VDKEDGTSTNQVFELARDLGRPRGDIYEVAVWEDSIVVDGNELYLFY 157


                 ....*
gi 499597459 300 GVHQE 304
Cdd:cd18127  158 AVPQE 162
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 4-141 3.32e-29

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: 109.56  E-value: 3.32e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459     4 VKVAINGYGTIGKRVADAIRLQPDMELIGVAK-TSPNYEAFTAMR-KGYKLYTTKEniqKFQNSGINVAGSIEDMIKDS- 80
Cdd:smart00846   1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDlTDPEYLAYLLKYdSVHGRFPGTV---EVEGDGLVVNGKAIKVFAERd 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499597459    81 -----------DIIIDATPGGVGANYKKIYQEYGKKAIFQGGEKSDvADVSFSALCNYNDAINK-NYIRVVSC 141
Cdd:smart00846  78 panlpwgelgvDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKD-ADPTFVYGVNHDEYDGEdHIISNASC 149
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 155-298 6.88e-17

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: 76.86  E-value: 6.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459  155 NFDkIEKVRGTIVRRAADP---------KEVKKGPINSivADPARIPSHHAKDVLTVLK--GIDIITSALVAPTTLMHLH 223
Cdd:pfam02800  11 NFG-IKKGLMTTVHAYTNDqklldgphhKDLRRGRAAA--PNIIPTSTGAAKAVGLVLPelKGKLDGMAVRVPTPNVSVV 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499597459  224 TLFITTRNKVSKEDLLNILSNTPRilllnTEKADAESTAEIMEIARDLGRYRNDvpETVIFEDSIYTNGNEIFLM 298
Cdd:pfam02800  88 DLVVELEKPVTVEEVNAALKEAAE-----GALKGILSYTEDPLVSSDFIGDPHS--SIFDAKETIVVNGNFVKVV 155
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-88 2.07e-07

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 51.85  E-value: 2.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459   1 MVKVKVAINGYGTIGKRVADAIRLQPDMELIGVAktSPNYEAFTAMRKGYklyttkeniqkfqnsGINVAGSIEDMIKDS 80
Cdd:COG0673    1 MDKLRVGIIGAGGIGRAHAPALAALPGVELVAVA--DRDPERAEAFAEEY---------------GVRVYTDYEELLADP 63

                         90
                 ....*....|
gi 499597459  81 DI--IIDATP 88
Cdd:COG0673   64 DIdaVVIATP 73
 
Name Accession Description Interval E-value
PRK04207 PRK04207
type II glyceraldehyde-3-phosphate dehydrogenase;
3-342 0e+00

type II glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 179786 [Multi-domain]  Cd Length: 341  Bit Score: 579.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459   3 KVKVAINGYGTIGKRVADAIRLQPDMELIGVAKTSPNYEAFTAMRKGYKLYTTKENIQK-FQNSGINVAGSIEDMIKDSD 81
Cdd:PRK04207   1 MIKVGVNGYGTIGKRVADAVAAQPDMELVGVAKTKPDYEARVAVEKGYPLYVADPEREKaFEEAGIPVAGTIEDLLEKAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459  82 IIIDATPGGVGANYKKIYQEYGKKAIFQGGEKSDVADVSFSALCNYNDAINKNYIRVVSCNTTGILRVLCTINNFDKIEK 161
Cdd:PRK04207  81 IVVDATPGGVGAKNKELYEKAGVKAIFQGGEKAEVAGVSFNALANYEEALGKDYVRVVSCNTTGLCRTLCALDRAFGVKK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459 162 VRGTIVRRAADPKEVKKGPINSIVADPARIPSHHAKDVLTVLKGIDIITSALVAPTTLMHLHTLFITTRNKVSKEDLLNI 241
Cdd:PRK04207 161 VRATLVRRAADPKEVKRGPINAIVPDPVTVPSHHGPDVKTVLPDLDITTMAVKVPTTLMHMHSVNVELKKPVTKEEVLEA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459 242 LSNTPRILLLNTEkADAESTAEIMEIARDLGRYRNDVPETVIFEDSIYTNGNEIFLMYGVHQESIVVPENIDAIRASLNI 321
Cdd:PRK04207 241 LENTPRILLVRAS-DGIDSTAELIEYARDLGRPRGDLYENAVWEDSITVDGNELYLMQAVHQESIVVPENIDAIRAMLGL 319

                        330       340
                 ....*....|....*....|..
gi 499597459 322 MS-RDESIRLTNETLKIGKGYL 342
Cdd:PRK04207 320 EDdEEKSIEKTNKALGIGKGKL 341
GAPDH-II_archae TIGR01546
glyceraldehyde-3-phosphate dehydrogenase, type II; This model describes the type II ...
 6-337 1.81e-166

glyceraldehyde-3-phosphate dehydrogenase, type II; This model describes the type II glyceraldehyde-3-phosphate dehydrogenases which are limited to archaea. These enzymes catalyze the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. In archaea, either NAD or NADP may be utilized as the cofactor. The class I GAPDH's from bacteria and eukaryotes are covered by TIGR01534. All of the members of the seed are characterized. See, for instance. This model is very solid, there are no species falling between trusted and noise at this time. The closest relatives scoring in the noise are the class I GAPDH's.


Pssm-ID: 130609  Cd Length: 333  Bit Score: 467.04  E-value: 1.81e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459    6 VAINGYGTIGKRVADAIRLQPDMELIGVAKTSPNYEAFTAMRKGYKLY-TTKENIQKFQNSGINVAGSIEDMIKDSDIII 84
Cdd:TIGR01546   1 VGVNGYGTIGKRVADAVTKQDDMKLVGVTKTSPDFEAYRAKELGIPVYaASEEFIPRFEEAGIEVAGTLEDLLEKVDIVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459   85 DATPGGVGANYKKIYQEYGKKAIFQGGEKSDVADVSFSALCNYNDAINKNYIRVVSCNTTGILRVLCTINNFDKIEKVRG 164
Cdd:TIGR01546  81 DATPGGIGAKNKPLYEKAGVKAIFQGGEKAEVADVSFVAQANYEAALGKDYVRVVSCNTTGLVRTLNAINDYSKVDKVRA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459  165 TIVRRAADPKEVKKGPINSIVADPARIPSHHAKDVLTVLKGIDIITSALVAPTTLMHLHTLFITTRNKVSKEDLLNILSN 244
Cdd:TIGR01546 161 VMVRRAADPNDVKKGPINAIVPDPVTVPSHHGPDVQTVIPNLNIETMAFVVPTTLMHVHSIMVELKKPVTKDDIIDILEN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459  245 TPRILLLNTEKaDAESTAEIMEIARDLGRYRNDVPETVIFEDSIYTNGNEIFLMYGVHQESIVVPENIDAIRASLNIMSR 324
Cdd:TIGR01546 241 TPRVLLFEKKK-GFESTAELIEFARDLHRERNDLYEIAVWKESINVKDNELFYMQAVHQESDVVPENIDAIRAMFELADK 319

                         330
                  ....*....|...
gi 499597459  325 DESIRLTNETLKI 337
Cdd:TIGR01546 320 WDSIKKTNKSLGI 332
GAPDH_II_C cd18127
C-terminal catalytic domain of type II glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 140-304 5.17e-77

C-terminal catalytic domain of type II 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 type II NADP+ utilizing GAPDHs, mainly from archaea.


Pssm-ID: 467677  Cd Length: 162  Bit Score: 233.25  E-value: 5.17e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459 140 SCNTTGILRVLCTINNFDKIEKVRGTIVRRAADPKEVKKGPINSIVADPArIPSHHAKDVLTVLKGIDIITSALVAPTTL 219
Cdd:cd18127    1 SCNTTGLSRVLKALDRAFGLKRVRATIVRRAADPGKHKKGVINAIVPEPK-DPSHHAPDVKTVFPDLDITTSAVKVPTTL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459 220 MHLHTLFITTRNKVSKEDLLNILSNTPRILLlnTEKADAESTAEIMEIARDLGRYRNDVPETVIFEDSIYTNGNEIFLMY 299
Cdd:cd18127   80 MHLHTINVELKRKVSREEVLEALASNPRIAL--VDKEDGTSTNQVFELARDLGRPRGDIYEVAVWEDSIVVDGNELYLFY 157


                 ....*
gi 499597459 300 GVHQE 304
Cdd:cd18127  158 AVPQE 162
GAPDH_II_N cd02278
N-terminal NAD(P)-binding domain of type II glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 4-140 2.20e-69

N-terminal NAD(P)-binding domain of type II 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 type II NADP+ utilizing GAPDHs mainly from archaea.


Pssm-ID: 467612  Cd Length: 171  Bit Score: 214.35  E-value: 2.20e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459   4 VKVAINGYGTIGKRVADAIRLQPDMELIGVAKTSPNYEAFTAMRKGYKLYTTKE-NIQKFQNSGINVAGSIEDMIKDSDI 82
Cdd:cd02278    1 IKVGVNGYGTIGKRVADAVLLQDDMELVGVAKRSPDYEAKPAVERGIPLYVPDEsRAEKFEEAGIPVAGTLEDLLEKADV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499597459  83 IIDATPGGVGANYKKIYQEYGKKAIFQGGEKSDVADVSFSALCNYNDAINKNYIRVVS 140
Cdd:cd02278   81 VVDCTPKGIGAKNKELYYKAGVKAIFQGGEKHFVAGVSFNAGANYEEALGKQFVRVVS 138
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 4-141 3.32e-29

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: 109.56  E-value: 3.32e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459     4 VKVAINGYGTIGKRVADAIRLQPDMELIGVAK-TSPNYEAFTAMR-KGYKLYTTKEniqKFQNSGINVAGSIEDMIKDS- 80
Cdd:smart00846   1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDlTDPEYLAYLLKYdSVHGRFPGTV---EVEGDGLVVNGKAIKVFAERd 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499597459    81 -----------DIIIDATPGGVGANYKKIYQEYGKKAIFQGGEKSDvADVSFSALCNYNDAINK-NYIRVVSC 141
Cdd:smart00846  78 panlpwgelgvDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKD-ADPTFVYGVNHDEYDGEdHIISNASC 149
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 141-304 8.83e-24

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: 95.76  E-value: 8.83e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459 141 CNTTGILRVLCTINNFDKIEKVRGTIVRRAADPKEV-----------KKGPINSIVadPAriPSHHAKDVLTVLK--GID 207
Cdd:cd18123    1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTvdgpsgkdwraSRGAVNNII--PN--PTGAAKAVGKVLPelNGK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459 208 IITSALVAPTTLMHLHTLFITTRNKVSKEDLLNILSNTP--RILLLNTEKADAESTaeimeiardlgrYRNDVPETVIFE 285
Cdd:cd18123   77 LTGMAVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPegKGRLGYTEAEDVSSD------------FRGDIFESVFDA 144

                        170       180
                 ....*....|....*....|
gi 499597459 286 DSIYT-NGNEIFLMYGVHQE 304
Cdd:cd18123  145 ESIIAvNDNEVKLMQWYDNE 164
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 155-298 6.88e-17

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: 76.86  E-value: 6.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459  155 NFDkIEKVRGTIVRRAADP---------KEVKKGPINSivADPARIPSHHAKDVLTVLK--GIDIITSALVAPTTLMHLH 223
Cdd:pfam02800  11 NFG-IKKGLMTTVHAYTNDqklldgphhKDLRRGRAAA--PNIIPTSTGAAKAVGLVLPelKGKLDGMAVRVPTPNVSVV 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499597459  224 TLFITTRNKVSKEDLLNILSNTPRilllnTEKADAESTAEIMEIARDLGRYRNDvpETVIFEDSIYTNGNEIFLM 298
Cdd:pfam02800  88 DLVVELEKPVTVEEVNAALKEAAE-----GALKGILSYTEDPLVSSDFIGDPHS--SIFDAKETIVVNGNFVKVV 155
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 141-304 7.81e-12

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: 62.92  E-value: 7.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459 141 CNTTGILRVLCTINNFDKIEKVRGTIVRRAADPKEVKKGPINS-----IVADPARIPSHHAKDVLTVL----KGIDIITS 211
Cdd:cd18122    1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPILKsevraIIPNIPKNETKHAPETGKVLgeigKPIKVDGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459 212 ALVAPTTLMHLHTLFITTRNKVSKEDLLNILSNTPRILLLNTEkaDAESTAEImeiardLGRYRNDVPETVIFEDSIYT- 290
Cdd:cd18122   81 AVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQISAE--DGLTYAKV------STRSVGGVYGVPVGRQREFAf 152

                        170
                 ....*....|....
gi 499597459 291 NGNEIFLMYGVHQE 304
Cdd:cd18122  153 DDNKLKVFSAVDNE 166
DapB_N pfam01113
Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the ...
 4-120 2.12e-09

Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the alpha,beta-unsaturated cyclic imine, dihydro-dipicolinate. This reaction is the second committed step in the biosynthesis of L-lysine and its precursor meso-diaminopimelate, which are critical for both protein and cell wall biosynthesis. The N-terminal domain of DapB binds the dinucleotide NADPH.


Pssm-ID: 460069 [Multi-domain]  Cd Length: 121  Bit Score: 54.55  E-value: 2.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459    4 VKVAINGY-GTIGKRVADAIRLQPDMELIGVaktspnYEAFTAMRKGYklyttkeNIQKFQNSGINVAGSIEDMIKDSDI 82
Cdd:pfam01113   1 IKIAVAGAsGRMGRELIKAVLEAPDLELVAA------VDRPGSSLLGS-------DAGELAPLGVPVTDDLEEVLADADV 67

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 499597459   83 IIDAT-PGGVGANYKKIYQeYGKKAI-----FQGGEKSDVADVS 120
Cdd:pfam01113  68 LIDFTtPEATLENLEFALK-HGVPLVigttgFTEEQLAELKEAA 110
GAPDH-like_N cd05192
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ...
 4-122 4.94e-09

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: 53.51  E-value: 4.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459   4 VKVAINGYGTIGKRVADAIRLQPDMELIGVAKTspnyeaftamrkgyklyttkeniqkfqnsginvagsiedmikdSDII 83
Cdd:cd05192    1 IRVAINGFGRIGRIVFRAIADQDDLDVVAINDR-------------------------------------------RDVV 37

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 499597459  84 IDATPGGVG-ANYKKIYQEYGKKAIFQGGEKSDVADVSFS 122
Cdd:cd05192   38 IECTGSFTDdDNAEKHIKAGGKKAVITAPEKGDIPTIVVV 77
meso-DAPDH_N cd02270
N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and ...
 5-33 1.69e-07

N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and similar proteins; Meso-DAPDH (EC 1.4.1.16), also called diaminopimelate dehydrogenase, or meso-DAP dehydrogenase, probably plays a role in lysine biosynthesis. It catalyzes the reversible NADP(H)-dependent reductive amination of L-2-amino-6-oxopimelate, the acyclic form of L-tetrahydrodipicolinate, to generate the meso compound, D,L-2,6-diaminopimelate. DAPDH is a homodimer which is highly specific for meso-DAP and NADP(+) as substrates. Members of this family contain an N-terminal Rossmann fold NAD(P)-binding domain and a C-terminal dimerization domain.


Pssm-ID: 467610 [Multi-domain]  Cd Length: 151  Bit Score: 49.88  E-value: 1.69e-07
                         10        20
                 ....*....|....*....|....*....
gi 499597459   5 KVAINGYGTIGKRVADAIRLQPDMELIGV 33
Cdd:cd02270    2 RVAIVGYGNLGRGVEEAIQANPDMELVGV 30
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-88 2.07e-07

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 51.85  E-value: 2.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459   1 MVKVKVAINGYGTIGKRVADAIRLQPDMELIGVAktSPNYEAFTAMRKGYklyttkeniqkfqnsGINVAGSIEDMIKDS 80
Cdd:COG0673    1 MDKLRVGIIGAGGIGRAHAPALAALPGVELVAVA--DRDPERAEAFAEEY---------------GVRVYTDYEELLADP 63

                         90
                 ....*....|
gi 499597459  81 DI--IIDATP 88
Cdd:COG0673   64 DIdaVVIATP 73
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 4-42 7.37e-07

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: 47.10  E-value: 7.37e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 499597459    4 VKVAINGYGTIGKRVADAIRLQPDMELIGV-AKTSPNYEA 42
Cdd:pfam00044   1 VKVGINGFGRIGRLVLRAALERPDIEVVAInDLTDPETLA 40
DAP-DH TIGR01921
diaminopimelate dehydrogenase; This model represents the diaminopimelate dehydrogenase enzyme ...
 1-33 2.33e-06

diaminopimelate dehydrogenase; This model represents the diaminopimelate dehydrogenase enzyme which provides an alternate (shortcut) route of lysine buiosynthesis in Corynebacterium, Bacterioides, Porphyromonas and scattered other species. The enzyme from Corynebacterium glutamicum has been crystallized and characterized.


Pssm-ID: 273877 [Multi-domain]  Cd Length: 324  Bit Score: 48.78  E-value: 2.33e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 499597459    1 MVKVKVAINGYGTIGKRVADAIRLQPDMELIGV 33
Cdd:TIGR01921   1 MSKIRAAIVGYGNLGRSVEKAIQQQPDMELVGV 33
DHDPR_N cd02274
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; ...
 4-107 8.08e-03

N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; DHDPR (EC 1.17.1.8), also called 4-hydroxy-tetrahydrodipicolinate reductase, or HTPA reductase, is a product of an essential gene referred to as dapB. It catalyzes the NAD(P)H-dependent reduction of 2,3-dihydrodipicolinate (DHDP) to 2,3,4,5-tetrahydrodipicolinate (THDP). DHDPR could also function as a dehydratase in addition to the role of a nucleotide dependent reductase. DHDPR is a component of the biosynthetic pathway that generates meso-diaminopimelate, a component of bacterial cell walls, and the amino acid L-lysine in various bacteria, archaea, cyanobacteria and higher plants. The enzyme is a homotetramer where each monomer is composed of two domains, an N-terminal NAD(P)-binding domain which forms a Rossmann fold, and a C-terminal substrate-binding domain that forms an open, mixed alpha-beta sandwich.


Pssm-ID: 467611 [Multi-domain]  Cd Length: 139  Bit Score: 36.38  E-value: 8.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499597459   4 VKVAINGY-GTIGKRVADAIRLQPDMELIGVaktspnYEAFTAMRKGYKLYTTKENiqkfqNSGINVAGSIEDMIKDSDI 82
Cdd:cd02274    1 IKVAVAGAtGRMGRELVKAILEAPDLELVGA------VDRPGSGLLGGDAGGLAGI-----GTGVIVSLDLELAAADADV 69

                         90       100
                 ....*....|....*....|....*
gi 499597459  83 IIDATPGGVGANYKKIYQEYGKKAI 107
Cdd:cd02274   70 VIDFTTPEATLENLEAAAKAGVPLV 94
 
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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