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Conserved domains on  [gi|499641002|ref|WP_011321736|]
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type II glyceraldehyde-3-phosphate dehydrogenase [Natronomonas pharaonis]

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;
3-337 0e+00

type II glyceraldehyde-3-phosphate dehydrogenase;


:

Pssm-ID: 179786 [Multi-domain]  Cd Length: 341  Bit Score: 586.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002   3 IQVAVNGYGTIGKRVADAVTLQPDMELVGVAKTSPNHEAELAVENDYPLYAAIEDRIDDFEAAGIDLAGTVDELVEAADI 82
Cdd:PRK04207   2 IKVGVNGYGTIGKRVADAVAAQPDMELVGVAKTKPDYEARVAVEKGYPLYVADPEREKAFEEAGIPVAGTIEDLLEKADI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002  83 VVDACPSGIGADNKSLYEAHDTPALYQGGESADLVDVSFNARSNFEAAADADHVRVVSCNTTGLSRLLAPLQEEYGVEKA 162
Cdd:PRK04207  82 VVDATPGGVGAKNKELYEKAGVKAIFQGGEKAEVAGVSFNALANYEEALGKDYVRVVSCNTTGLCRTLCALDRAFGVKKV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002 163 RVTLVRRGGDPGQTGRGPINDILPNPVSLPSHHGPDVNTIFPDLDIDTLGLKVPATLMHTHSVNVTLESTPDAEAVADLL 242
Cdd:PRK04207 162 RATLVRRAADPKEVKRGPINAIVPDPVTVPSHHGPDVKTVLPDLDITTMAVKVPTTLMHMHSVNVELKKPVTKEEVLEAL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002 243 DEQDRTFLIPESYGIDGAGKLKEFAMDRGRPRADIWENCIWAESVSMEGSDLYLFQAIHQESDVVPENIDAIRAVLGTA- 321
Cdd:PRK04207 242 ENTPRILLVRASDGIDSTAELIEYARDLGRPRGDLYENAVWEDSITVDGNELYLMQAVHQESIVVPENIDAIRAMLGLEd 321

                        330
                 ....*....|....*.
gi 499641002 322 DADESRETTNETLGVG 337
Cdd:PRK04207 322 DEEKSIEKTNKALGIG 337
 
Name Accession Description Interval E-value
PRK04207 PRK04207
type II glyceraldehyde-3-phosphate dehydrogenase;
3-337 0e+00

type II glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 179786 [Multi-domain]  Cd Length: 341  Bit Score: 586.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002   3 IQVAVNGYGTIGKRVADAVTLQPDMELVGVAKTSPNHEAELAVENDYPLYAAIEDRIDDFEAAGIDLAGTVDELVEAADI 82
Cdd:PRK04207   2 IKVGVNGYGTIGKRVADAVAAQPDMELVGVAKTKPDYEARVAVEKGYPLYVADPEREKAFEEAGIPVAGTIEDLLEKADI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002  83 VVDACPSGIGADNKSLYEAHDTPALYQGGESADLVDVSFNARSNFEAAADADHVRVVSCNTTGLSRLLAPLQEEYGVEKA 162
Cdd:PRK04207  82 VVDATPGGVGAKNKELYEKAGVKAIFQGGEKAEVAGVSFNALANYEEALGKDYVRVVSCNTTGLCRTLCALDRAFGVKKV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002 163 RVTLVRRGGDPGQTGRGPINDILPNPVSLPSHHGPDVNTIFPDLDIDTLGLKVPATLMHTHSVNVTLESTPDAEAVADLL 242
Cdd:PRK04207 162 RATLVRRAADPKEVKRGPINAIVPDPVTVPSHHGPDVKTVLPDLDITTMAVKVPTTLMHMHSVNVELKKPVTKEEVLEAL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002 243 DEQDRTFLIPESYGIDGAGKLKEFAMDRGRPRADIWENCIWAESVSMEGSDLYLFQAIHQESDVVPENIDAIRAVLGTA- 321
Cdd:PRK04207 242 ENTPRILLVRASDGIDSTAELIEYARDLGRPRGDLYENAVWEDSITVDGNELYLMQAVHQESIVVPENIDAIRAMLGLEd 321

                        330
                 ....*....|....*.
gi 499641002 322 DADESRETTNETLGVG 337
Cdd:PRK04207 322 DEEKSIEKTNKALGIG 337
GAPDH-II_archae TIGR01546
glyceraldehyde-3-phosphate dehydrogenase, type II; This model describes the type II ...
 5-336 5.84e-143

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: 407.33  E-value: 5.84e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002    5 VAVNGYGTIGKRVADAVTLQPDMELVGVAKTSPNHEAELAVENDYPLYAAIEDRIDDFEAAGIDLAGTVDELVEAADIVV 84
Cdd:TIGR01546   1 VGVNGYGTIGKRVADAVTKQDDMKLVGVTKTSPDFEAYRAKELGIPVYAASEEFIPRFEEAGIEVAGTLEDLLEKVDIVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002   85 DACPSGIGADNKSLYEAHDTPALYQGGESADLVDVSFNARSNFEAAADADHVRVVSCNTTGLSRLLAPLQEEYGVEKARV 164
Cdd:TIGR01546  81 DATPGGIGAKNKPLYEKAGVKAIFQGGEKAEVADVSFVAQANYEAALGKDYVRVVSCNTTGLVRTLNAINDYSKVDKVRA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002  165 TLVRRGGDPGQTGRGPINDILPNPVSLPSHHGPDVNTIFPDLDIDTLGLKVPATLMHTHSVNVTLESTPDAEAVADLLDE 244
Cdd:TIGR01546 161 VMVRRAADPNDVKKGPINAIVPDPVTVPSHHGPDVQTVIPNLNIETMAFVVPTTLMHVHSIMVELKKPVTKDDIIDILEN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002  245 QDRTFLIPESYGIDGAGKLKEFAMDRGRPRADIWENCIWAESVSMEGSDLYLFQAIHQESDVVPENIDAIRAVLGTADAD 324
Cdd:TIGR01546 241 TPRVLLFEKKKGFESTAELIEFARDLHRERNDLYEIAVWKESINVKDNELFYMQAVHQESDVVPENIDAIRAMFELADKW 320

                         330
                  ....*....|..
gi 499641002  325 ESRETTNETLGV 336
Cdd:TIGR01546 321 DSIKKTNKSLGI 332
GAPDH_II_C cd18127
C-terminal catalytic domain of type II glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 140-303 6.94e-72

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: 220.15  E-value: 6.94e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002 140 SCNTTGLSRLLAPLQEEYGVEKARVTLVRRGGDPGQTGRGPINDILPNPVSlPSHHGPDVNTIFPDLDIDTLGLKVPATL 219
Cdd:cd18127    1 SCNTTGLSRVLKALDRAFGLKRVRATIVRRAADPGKHKKGVINAIVPEPKD-PSHHAPDVKTVFPDLDITTSAVKVPTTL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002 220 MHTHSVNVTLESTPDAEAVADLLDEQDRTFLIPESYGiDGAGKLKEFAMDRGRPRADIWENCIWAESVSMEGSDLYLFQA 299
Cdd:cd18127   80 MHLHTINVELKRKVSREEVLEALASNPRIALVDKEDG-TSTNQVFELARDLGRPRGDIYEVAVWEDSIVVDGNELYLFYA 158


                 ....
gi 499641002 300 IHQE 303
Cdd:cd18127  159 VPQE 162
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 3-141 4.49e-25

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: 98.78  E-value: 4.49e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002     3 IQVAVNGYGTIGKRVADAVTLQPDMELVGVAK-TSPNHEAELAvEND--YPLYAAIEdridDFEAAGIDLAGTVDELVEA 79
Cdd:smart00846   1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDlTDPEYLAYLL-KYDsvHGRFPGTV----EVEGDGLVVNGKAIKVFAE 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499641002    80 ------------ADIVVDaCPSGIGADNK-SLYEAHDTPALYQGGESADlVDVSFNARSNFEAAADADH-VRVVSC 141
Cdd:smart00846  76 rdpanlpwgelgVDIVVE-CTGGFTTREKaSAHLKAGAKKVIISAPSKD-ADPTFVYGVNHDEYDGEDHiISNASC 149
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 146-299 1.28e-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: 78.79  E-value: 1.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002  146 LSRLLAPLQEEYGVEKARVTLVRRGGDPGQTG---------RGPINdiLPNPVSLPSHHGPDVNTIFPDLD--IDTLGLK 214
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLdgphhkdlrRGRAA--APNIIPTSTGAAKAVGLVLPELKgkLDGMAVR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002  215 VPATLMHTHSVNVTLESTPDAEAVADLLDEQDRTflipESYGIDGAGKLKEFAMD-RGRPRAdiwENCIWAESVSMEGSD 293
Cdd:pfam02800  79 VPTPNVSVVDLVVELEKPVTVEEVNAALKEAAEG----ALKGILSYTEDPLVSSDfIGDPHS---SIFDAKETIVVNGNF 151


                  ....*.
gi 499641002  294 LYLFQA 299
Cdd:pfam02800 152 VKVVAW 157
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-88 2.68e-04

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 42.22  E-value: 2.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002   1 MSIQVAVNGYGTIGKRVADAVTLQPDMELVGVAKTSPNHEAELAvendyplyaaiedriddfEAAGIDLAGTVDELVEAA 80
Cdd:COG0673    2 DKLRVGIIGAGGIGRAHAPALAALPGVELVAVADRDPERAEAFA------------------EEYGVRVYTDYEELLADP 63

                         90
                 ....*....|
gi 499641002  81 DI--VVDACP 88
Cdd:COG0673   64 DIdaVVIATP 73
 
Name Accession Description Interval E-value
PRK04207 PRK04207
type II glyceraldehyde-3-phosphate dehydrogenase;
3-337 0e+00

type II glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 179786 [Multi-domain]  Cd Length: 341  Bit Score: 586.41  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002   3 IQVAVNGYGTIGKRVADAVTLQPDMELVGVAKTSPNHEAELAVENDYPLYAAIEDRIDDFEAAGIDLAGTVDELVEAADI 82
Cdd:PRK04207   2 IKVGVNGYGTIGKRVADAVAAQPDMELVGVAKTKPDYEARVAVEKGYPLYVADPEREKAFEEAGIPVAGTIEDLLEKADI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002  83 VVDACPSGIGADNKSLYEAHDTPALYQGGESADLVDVSFNARSNFEAAADADHVRVVSCNTTGLSRLLAPLQEEYGVEKA 162
Cdd:PRK04207  82 VVDATPGGVGAKNKELYEKAGVKAIFQGGEKAEVAGVSFNALANYEEALGKDYVRVVSCNTTGLCRTLCALDRAFGVKKV 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002 163 RVTLVRRGGDPGQTGRGPINDILPNPVSLPSHHGPDVNTIFPDLDIDTLGLKVPATLMHTHSVNVTLESTPDAEAVADLL 242
Cdd:PRK04207 162 RATLVRRAADPKEVKRGPINAIVPDPVTVPSHHGPDVKTVLPDLDITTMAVKVPTTLMHMHSVNVELKKPVTKEEVLEAL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002 243 DEQDRTFLIPESYGIDGAGKLKEFAMDRGRPRADIWENCIWAESVSMEGSDLYLFQAIHQESDVVPENIDAIRAVLGTA- 321
Cdd:PRK04207 242 ENTPRILLVRASDGIDSTAELIEYARDLGRPRGDLYENAVWEDSITVDGNELYLMQAVHQESIVVPENIDAIRAMLGLEd 321

                        330
                 ....*....|....*.
gi 499641002 322 DADESRETTNETLGVG 337
Cdd:PRK04207 322 DEEKSIEKTNKALGIG 337
GAPDH-II_archae TIGR01546
glyceraldehyde-3-phosphate dehydrogenase, type II; This model describes the type II ...
 5-336 5.84e-143

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: 407.33  E-value: 5.84e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002    5 VAVNGYGTIGKRVADAVTLQPDMELVGVAKTSPNHEAELAVENDYPLYAAIEDRIDDFEAAGIDLAGTVDELVEAADIVV 84
Cdd:TIGR01546   1 VGVNGYGTIGKRVADAVTKQDDMKLVGVTKTSPDFEAYRAKELGIPVYAASEEFIPRFEEAGIEVAGTLEDLLEKVDIVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002   85 DACPSGIGADNKSLYEAHDTPALYQGGESADLVDVSFNARSNFEAAADADHVRVVSCNTTGLSRLLAPLQEEYGVEKARV 164
Cdd:TIGR01546  81 DATPGGIGAKNKPLYEKAGVKAIFQGGEKAEVADVSFVAQANYEAALGKDYVRVVSCNTTGLVRTLNAINDYSKVDKVRA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002  165 TLVRRGGDPGQTGRGPINDILPNPVSLPSHHGPDVNTIFPDLDIDTLGLKVPATLMHTHSVNVTLESTPDAEAVADLLDE 244
Cdd:TIGR01546 161 VMVRRAADPNDVKKGPINAIVPDPVTVPSHHGPDVQTVIPNLNIETMAFVVPTTLMHVHSIMVELKKPVTKDDIIDILEN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002  245 QDRTFLIPESYGIDGAGKLKEFAMDRGRPRADIWENCIWAESVSMEGSDLYLFQAIHQESDVVPENIDAIRAVLGTADAD 324
Cdd:TIGR01546 241 TPRVLLFEKKKGFESTAELIEFARDLHRERNDLYEIAVWKESINVKDNELFYMQAVHQESDVVPENIDAIRAMFELADKW 320

                         330
                  ....*....|..
gi 499641002  325 ESRETTNETLGV 336
Cdd:TIGR01546 321 DSIKKTNKSLGI 332
GAPDH_II_C cd18127
C-terminal catalytic domain of type II glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 140-303 6.94e-72

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: 220.15  E-value: 6.94e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002 140 SCNTTGLSRLLAPLQEEYGVEKARVTLVRRGGDPGQTGRGPINDILPNPVSlPSHHGPDVNTIFPDLDIDTLGLKVPATL 219
Cdd:cd18127    1 SCNTTGLSRVLKALDRAFGLKRVRATIVRRAADPGKHKKGVINAIVPEPKD-PSHHAPDVKTVFPDLDITTSAVKVPTTL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002 220 MHTHSVNVTLESTPDAEAVADLLDEQDRTFLIPESYGiDGAGKLKEFAMDRGRPRADIWENCIWAESVSMEGSDLYLFQA 299
Cdd:cd18127   80 MHLHTINVELKRKVSREEVLEALASNPRIALVDKEDG-TSTNQVFELARDLGRPRGDIYEVAVWEDSIVVDGNELYLFYA 158


                 ....
gi 499641002 300 IHQE 303
Cdd:cd18127  159 VPQE 162
GAPDH_II_N cd02278
N-terminal NAD(P)-binding domain of type II glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 3-140 7.57e-66

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: 205.10  E-value: 7.57e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002   3 IQVAVNGYGTIGKRVADAVTLQPDMELVGVAKTSPNHEAELAVENDYPLYAAIEDRIDDFEAAGIDLAGTVDELVEAADI 82
Cdd:cd02278    1 IKVGVNGYGTIGKRVADAVLLQDDMELVGVAKRSPDYEAKPAVERGIPLYVPDESRAEKFEEAGIPVAGTLEDLLEKADV 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499641002  83 VVDACPSGIGADNKSLYEAHDTPALYQGGESADLVDVSFNARSNFEAAADADHVRVVS 140
Cdd:cd02278   81 VVDCTPKGIGAKNKELYYKAGVKAIFQGGEKHFVAGVSFNAGANYEEALGKQFVRVVS 138
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 141-303 6.28e-26

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: 101.54  E-value: 6.28e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002 141 CNTTGLSRLLAPLQEEYGVEKARVTLVRRGGDPGQT-----------GRGPINDILPNPVslpsHHGPDVNTIFPDLD-- 207
Cdd:cd18123    1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTvdgpsgkdwraSRGAVNNIIPNPT----GAAKAVGKVLPELNgk 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002 208 IDTLGLKVPATLMHTHSVNVTLESTPDAEAVADLLDEQdrtfliPESYGIDGAGKLKEFAMDRgrpRADIWENCIWAES- 286
Cdd:cd18123   77 LTGMAVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQA------PEGKGRLGYTEAEDVSSDF---RGDIFESVFDAESi 147

                        170
                 ....*....|....*..
gi 499641002 287 VSMEGSDLYLFQAIHQE 303
Cdd:cd18123  148 IAVNDNEVKLMQWYDNE 164
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 3-141 4.49e-25

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: 98.78  E-value: 4.49e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002     3 IQVAVNGYGTIGKRVADAVTLQPDMELVGVAK-TSPNHEAELAvEND--YPLYAAIEdridDFEAAGIDLAGTVDELVEA 79
Cdd:smart00846   1 IKVGINGFGRIGRLVLRAALERPDVEVVAINDlTDPEYLAYLL-KYDsvHGRFPGTV----EVEGDGLVVNGKAIKVFAE 75

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499641002    80 ------------ADIVVDaCPSGIGADNK-SLYEAHDTPALYQGGESADlVDVSFNARSNFEAAADADH-VRVVSC 141
Cdd:smart00846  76 rdpanlpwgelgVDIVVE-CTGGFTTREKaSAHLKAGAKKVIISAPSKD-ADPTFVYGVNHDEYDGEDHiISNASC 149
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 141-303 8.52e-23

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: 92.97  E-value: 8.52e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002 141 CNTTGLSRLLAPLQEEYGVEKARVTLVRRGGDPGQTGRGPI-----NDILPNPVSLPSHHGPDVNTIFPDLD----IDTL 211
Cdd:cd18122    1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPIlksevRAIIPNIPKNETKHAPETGKVLGEIGkpikVDGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002 212 GLKVPATLMHTHSVNVTLESTPDAEAVADLLDEQDRTFLIpesYGIDGAGKLKEFamdrGRPRADIWENCIWAES-VSME 290
Cdd:cd18122   81 AVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEEVQI---SAEDGLTYAKVS----TRSVGGVYGVPVGRQReFAFD 153

                        170
                 ....*....|...
gi 499641002 291 GSDLYLFQAIHQE 303
Cdd:cd18122  154 DNKLKVFSAVDNE 166
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 146-299 1.28e-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: 78.79  E-value: 1.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002  146 LSRLLAPLQEEYGVEKARVTLVRRGGDPGQTG---------RGPINdiLPNPVSLPSHHGPDVNTIFPDLD--IDTLGLK 214
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDQKLLdgphhkdlrRGRAA--APNIIPTSTGAAKAVGLVLPELKgkLDGMAVR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002  215 VPATLMHTHSVNVTLESTPDAEAVADLLDEQDRTflipESYGIDGAGKLKEFAMD-RGRPRAdiwENCIWAESVSMEGSD 293
Cdd:pfam02800  79 VPTPNVSVVDLVVELEKPVTVEEVNAALKEAAEG----ALKGILSYTEDPLVSSDfIGDPHS---SIFDAKETIVVNGNF 151


                  ....*.
gi 499641002  294 LYLFQA 299
Cdd:pfam02800 152 VKVVAW 157
meso-DAPDH_N cd02270
N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and ...
 3-32 1.03e-06

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: 47.57  E-value: 1.03e-06
                         10        20        30
                 ....*....|....*....|....*....|
gi 499641002   3 IQVAVNGYGTIGKRVADAVTLQPDMELVGV 32
Cdd:cd02270    1 IRVAIVGYGNLGRGVEEAIQANPDMELVGV 30
GAPDH-like_N cd05192
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ...
 3-139 1.55e-06

N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like family; The GAPDH-like family includes glyceraldehyde-3-phosphate dehydrogenase (GAPDH), native NAD(P)H-dependent amine dehydrogenases (nat-AmDHs), 2,4-diaminopentanoate dehydrogenase (DAPDH), meso-diaminopimelate D-dehydrogenase (meso-DAPDH), and dihydrodipicolinate reductase (DHDPR). GAPDH plays an important role in glycolysis and gluconeogenesis by reversibly catalyzing the oxidation and phosphorylation of D-glyceraldehyde-3-phosphate to 1,3-diphospho-glycerate. nat-AmDHs catalyze the reductive amination of ketone and aldehyde substrates using NAD(P)H as the hydride source. They play important roles in the efficient asymmetric synthesis of alpha-chiral amines. DAPDH is involved in the ornithine fermentation pathway. It catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate ((2R,4S)-DAP) to yield 2-amino-4-ketopentanoate (AKP). DHDPR catalyzes the NAD(P)H-dependent reduction of 2,3-dihydrodipicolinate (DHDP) to 2,3,4,5-tetrahydrodipicolinate (THDP). It could also function as a dehydratase in addition to the role of a nucleotide dependent reductase. The model corresponds to the N-terminal NAD(P)-binding domain of GAPDH-like family proteins. It contains a Rossmann fold which combines with the catalytic cysteine-containing C-terminus to form a catalytic cleft.


Pssm-ID: 467613 [Multi-domain]  Cd Length: 109  Bit Score: 46.19  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002   3 IQVAVNGYGTIGKRVADAVTLQPDMELVGVAKTSpnheaelavendyplyaaiedriddfeaagidlagtvdelveaaDI 82
Cdd:cd05192    1 IRVAINGFGRIGRIVFRAIADQDDLDVVAINDRR--------------------------------------------DV 36

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 499641002  83 VVDACPSGIGADN-KSLYEAHDTPALYQGGESADLVDVSFNArSNFEAAADADHVRVV 139
Cdd:cd05192   37 VIECTGSFTDDDNaEKHIKAGGKKAVITAPEKGDIPTIVVVL-NELAKSAGATVVSNA 93
DapB_N pfam01113
Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the ...
 3-80 8.56e-06

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: 44.53  E-value: 8.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002    3 IQVAVNGY-GTIGKRVADAVTLQPDMELVGVAKTSPNHE----AELAVENDYPLYAAIEDRIDDFEAAgID--LAGTVDE 75
Cdd:pfam01113   1 IKIAVAGAsGRMGRELIKAVLEAPDLELVAAVDRPGSSLlgsdAGELAPLGVPVTDDLEEVLADADVL-IDftTPEATLE 79


                  ....*
gi 499641002   76 LVEAA 80
Cdd:pfam01113  80 NLEFA 84
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 3-43 8.18e-05

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: 40.93  E-value: 8.18e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 499641002    3 IQVAVNGYGTIGKRVADAVTLQPDMELVGV-AKTSPNHEAEL 43
Cdd:pfam00044   1 VKVGINGFGRIGRLVLRAALERPDIEVVAInDLTDPETLAYL 42
DAP-DH TIGR01921
diaminopimelate dehydrogenase; This model represents the diaminopimelate dehydrogenase enzyme ...
 3-80 9.22e-05

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: 43.78  E-value: 9.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002    3 IQVAVNGYGTIGKRVADAVTLQPDMELVGVAKTSPNHeaelAVENDYPLYAAIEdriDDFEAAGIDLA----GTVDELVE 78
Cdd:TIGR01921   4 IRAAIVGYGNLGRSVEKAIQQQPDMELVGVFSRRGAE----TLDTETPVYAVAD---DEKHLDDVDVLilcmGSATDIPE 76


                  ..
gi 499641002   79 AA 80
Cdd:TIGR01921  77 QA 78
ASADH_C_arch_fung_like cd18130
C-terminal catalytic domain of fungal/archaeal aspartate beta-semialdehyde dehydrogenase ...
 141-244 1.16e-04

C-terminal catalytic domain of fungal/archaeal aspartate beta-semialdehyde dehydrogenase (ASADH) and similar proteins; The family corresponds to a new branch of aspartate beta-semialdehyde dehydrogenase (ASADH) enzymes that has a similar overall fold and domain organization but share very little sequence homology with the typical bacterial ASADHs. They are mainly from archaea and fungi. ASADH (EC 1.2.1.11), also called ASA dehydrogenase (ASD), or aspartate-beta-semialdehyde dehydrogenase, catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate, which is the second step of the aspartate biosynthetic pathway. ASA can either be further reduced to homoserine, which leads to methionine, threonine, or isoleucine, or it can be condensed with pyruvate and cyclized into dihydrodipicolinate, and then converted into diaminopimelate, a component of bacterial cell walls, and finally decarboxylated to produce lysine. ASADH contains an N-terminal Rossmann fold NAD(P) binding domain and a C-terminal glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like catalytic domain and are members of the GAPDH superfamily of proteins. This family also includes NADP-dependent malonyl-CoA reductase (MCR, EC 1.2.1.75), which catalyzes the reduction of malonyl-CoA to malonate semialdehyde, a key step in the 3-hydroxypropanoate and the 3-hydroxypropanoate/4-hydroxybutyrate cycles. It can also use succinyl-CoA and succinate semialdehyde as substrates but at a lower rate than malonyl-CoA.


Pssm-ID: 467680 [Multi-domain]  Cd Length: 180  Bit Score: 42.22  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002 141 CNTTGLSRLLAPLQEEYGVEKARVTL---VRRGGDPGqtgrGPINDILPNPVSLPSHHGP----DVNTIFPDLD---IDT 210
Cdd:cd18130    1 CSTAGLALPLKPLHDFFGIEAVIVTTmqaISGAGYPG----VPSLDILDNVIPYIGGEEEkiesETKKILGTLNedkIEP 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 499641002 211 LGLKVPATLM-------HTHSVNVTLESTPDAEAVADLLDE 244
Cdd:cd18130   77 ADFKVSATCNrvpvidgHTESVSVKFKERPDPEEVKEALEN 117
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-88 2.68e-04

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 42.22  E-value: 2.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002   1 MSIQVAVNGYGTIGKRVADAVTLQPDMELVGVAKTSPNHEAELAvendyplyaaiedriddfEAAGIDLAGTVDELVEAA 80
Cdd:COG0673    2 DKLRVGIIGAGGIGRAHAPALAALPGVELVAVADRDPERAEAFA------------------EEYGVRVYTDYEELLADP 63

                         90
                 ....*....|
gi 499641002  81 DI--VVDACP 88
Cdd:COG0673   64 DIdaVVIATP 73
DapB COG0289
4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]; ...
 3-80 4.54e-04

4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]; 4-hydroxy-tetrahydrodipicolinate reductase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440058 [Multi-domain]  Cd Length: 257  Bit Score: 41.26  E-value: 4.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499641002   3 IQVAVNG-YGTIGKRVADAVTLQPDMELVG-VAKTSPNHEAELAVENDYPLYAAIEDRIDDFEAAgID--LAGTVDELVE 78
Cdd:COG0289    1 IKIAVAGaSGRMGRELIRAVLEAPDLELVAaIDRPGSPGQDAGELALGVPVTDDLEEALAKADVV-IDftHPEATLENLE 79


                 ..
gi 499641002  79 AA 80
Cdd:COG0289   80 AA 81
 
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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