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Conserved domains on  [gi|21263613|sp|P58837|]
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RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 1; Short=GAPDH 1; AltName: Full=NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase 1

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;
3-335 0e+00

type II glyceraldehyde-3-phosphate dehydrogenase;


:

Pssm-ID: 179786 [Multi-domain]  Cd Length: 341  Bit Score: 620.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613    3 KAKIAVNGYGTIGKRVADAVKAQDDMEVVGISKRTPNYEAAVAHQLGYDIYAPAENVG-AFEKAGMPAAGSVEEMIEKAD 81
Cdd:PRK04207   1 MIKVGVNGYGTIGKRVADAVAAQPDMELVGVAKTKPDYEARVAVEKGYPLYVADPEREkAFEEAGIPVAGTIEDLLEKAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613   82 LVVDCTPGGVGEKNKPLYEKAGVKAIWQGGESHPIAGFSFNAVSNYEGALGRDLVRVVSCNTTGLCRTITPIDRELGVKK 161
Cdd:PRK04207  81 IVVDATPGGVGAKNKELYEKAGVKAIFQGGEKAEVAGVSFNALANYEEALGKDYVRVVSCNTTGLCRTLCALDRAFGVKK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613  162 VRAILARRATDPNDIKKGPINAIVLHPVKLPSHHGPDVRSVIPHINITSAALLVPTTLMHLHTVNMEVDTDCTAEDIKKI 241
Cdd:PRK04207 161 VRATLVRRAADPKEVKRGPINAIVPDPVTVPSHHGPDVKTVLPDLDITTMAVKVPTTLMHMHSVNVELKKPVTKEEVLEA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613  242 FSSQSRIRFI--GQGITSTAEIMEVARDIKRPRNDMWENCIWPESITVDEKEFYFFQAIHQESIVVPENVDAIRAMMELE 319
Cdd:PRK04207 241 LENTPRILLVraSDGIDSTAELIEYARDLGRPRGDLYENAVWEDSITVDGNELYLMQAVHQESIVVPENIDAIRAMLGLE 320

                        330
                 ....*....|....*.
gi 21263613  320 SDGAKSIEKTNKALGM 335
Cdd:PRK04207 321 DDEEKSIEKTNKALGI 336
 
Name Accession Description Interval E-value
PRK04207 PRK04207
type II glyceraldehyde-3-phosphate dehydrogenase;
3-335 0e+00

type II glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 179786 [Multi-domain]  Cd Length: 341  Bit Score: 620.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613    3 KAKIAVNGYGTIGKRVADAVKAQDDMEVVGISKRTPNYEAAVAHQLGYDIYAPAENVG-AFEKAGMPAAGSVEEMIEKAD 81
Cdd:PRK04207   1 MIKVGVNGYGTIGKRVADAVAAQPDMELVGVAKTKPDYEARVAVEKGYPLYVADPEREkAFEEAGIPVAGTIEDLLEKAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613   82 LVVDCTPGGVGEKNKPLYEKAGVKAIWQGGESHPIAGFSFNAVSNYEGALGRDLVRVVSCNTTGLCRTITPIDRELGVKK 161
Cdd:PRK04207  81 IVVDATPGGVGAKNKELYEKAGVKAIFQGGEKAEVAGVSFNALANYEEALGKDYVRVVSCNTTGLCRTLCALDRAFGVKK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613  162 VRAILARRATDPNDIKKGPINAIVLHPVKLPSHHGPDVRSVIPHINITSAALLVPTTLMHLHTVNMEVDTDCTAEDIKKI 241
Cdd:PRK04207 161 VRATLVRRAADPKEVKRGPINAIVPDPVTVPSHHGPDVKTVLPDLDITTMAVKVPTTLMHMHSVNVELKKPVTKEEVLEA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613  242 FSSQSRIRFI--GQGITSTAEIMEVARDIKRPRNDMWENCIWPESITVDEKEFYFFQAIHQESIVVPENVDAIRAMMELE 319
Cdd:PRK04207 241 LENTPRILLVraSDGIDSTAELIEYARDLGRPRGDLYENAVWEDSITVDGNELYLMQAVHQESIVVPENIDAIRAMLGLE 320

                        330
                 ....*....|....*.
gi 21263613  320 SDGAKSIEKTNKALGM 335
Cdd:PRK04207 321 DDEEKSIEKTNKALGI 336
GAPDH-II_archae TIGR01546
glyceraldehyde-3-phosphate dehydrogenase, type II; This model describes the type II ...
 6-335 1.27e-160

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: 452.02  E-value: 1.27e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613     6 IAVNGYGTIGKRVADAVKAQDDMEVVGISKRTPNYEAAVAHQLGYDIYAPA-ENVGAFEKAGMPAAGSVEEMIEKADLVV 84
Cdd:TIGR01546   1 VGVNGYGTIGKRVADAVTKQDDMKLVGVTKTSPDFEAYRAKELGIPVYAASeEFIPRFEEAGIEVAGTLEDLLEKVDIVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613    85 DCTPGGVGEKNKPLYEKAGVKAIWQGGESHPIAGFSFNAVSNYEGALGRDLVRVVSCNTTGLCRTITPIDRELGVKKVRA 164
Cdd:TIGR01546  81 DATPGGIGAKNKPLYEKAGVKAIFQGGEKAEVADVSFVAQANYEAALGKDYVRVVSCNTTGLVRTLNAINDYSKVDKVRA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613   165 ILARRATDPNDIKKGPINAIVLHPVKLPSHHGPDVRSVIPHINITSAALLVPTTLMHLHTVNMEVDTDCTAEDIKKIFSS 244
Cdd:TIGR01546 161 VMVRRAADPNDVKKGPINAIVPDPVTVPSHHGPDVQTVIPNLNIETMAFVVPTTLMHVHSIMVELKKPVTKDDIIDILEN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613   245 QSRIRFIG--QGITSTAEIMEVARDIKRPRNDMWENCIWPESITVDEKEFYFFQAIHQESIVVPENVDAIRAMMELEsDG 322
Cdd:TIGR01546 241 TPRVLLFEkkKGFESTAELIEFARDLHRERNDLYEIAVWKESINVKDNELFYMQAVHQESDVVPENIDAIRAMFELA-DK 319

                         330
                  ....*....|...
gi 21263613   323 AKSIEKTNKALGM 335
Cdd:TIGR01546 320 WDSIKKTNKSLGI 332
GAPDH_II_C cd18127
C-terminal catalytic domain of type II glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 140-301 2.55e-79

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: 239.03  E-value: 2.55e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613 140 SCNTTGLCRTITPIDRELGVKKVRAILARRATDPNDIKKGPINAIVLHPVKlPSHHGPDVRSVIPHINITSAALLVPTTL 219
Cdd:cd18127   1 SCNTTGLSRVLKALDRAFGLKRVRATIVRRAADPGKHKKGVINAIVPEPKD-PSHHAPDVKTVFPDLDITTSAVKVPTTL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613 220 MHLHTVNMEVDTDCTAEDIKKIFSSQSRIRFIGQGI-TSTAEIMEVARDIKRPRNDMWENCIWPESITVDEKEFYFFQAI 298
Cdd:cd18127  80 MHLHTINVELKRKVSREEVLEALASNPRIALVDKEDgTSTNQVFELARDLGRPRGDIYEVAVWEDSIVVDGNELYLFYAV 159


                ...
gi 21263613 299 HQE 301
Cdd:cd18127 160 PQE 162
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 5-141 1.01e-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: 110.72  E-value: 1.01e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613      5 KIAVNGYGTIGKRVADAVKAQDDMEVVGISKRT-PNYEaavAHQLGYD-IYAPAENVGAFEKAGMPAAGSVEEMIEK--- 79
Cdd:smart00846   2 KVGINGFGRIGRLVLRAALERPDVEVVAINDLTdPEYL---AYLLKYDsVHGRFPGTVEVEGDGLVVNGKAIKVFAErdp 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21263613     80 ---------ADLVVDCTPGGVGEKNKPLYEKAGVKAIWQGGESHPIAGfSFNAVSNYEGALGRD-LVRVVSC 141
Cdd:smart00846  79 anlpwgelgVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDADP-TFVYGVNHDEYDGEDhIISNASC 149
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 146-297 7.59e-29

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: 108.83  E-value: 7.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613   146 LCRTITPIDRELGVKKVRAILARRATDP---------NDIKKGPINAivLHPVKLPSHHGPDVRSVIPH--INITSAALL 214
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDqklldgphhKDLRRGRAAA--PNIIPTSTGAAKAVGLVLPElkGKLDGMAVR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613   215 VPTTLMHLHTVNMEVDTDCTAEDIKKIFSSQSRIRFigQGITSTAEIMEVARDIKRPRNDmwENCIWPESITVDEKEFYF 294
Cdd:pfam02800  79 VPTPNVSVVDLVVELEKPVTVEEVNAALKEAAEGAL--KGILSYTEDPLVSSDFIGDPHS--SIFDAKETIVVNGNFVKV 154


                  ...
gi 21263613   295 FQA 297
Cdd:pfam02800 155 VAW 157
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-88 2.26e-07

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 51.46  E-value: 2.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613   1 MAKAKIAVNGYGTIGKRVADAVKAQDDMEVVGISKRTPNYEAAVAHQLGYDIYApaenvgafekagmpaagSVEEMIE-- 78
Cdd:COG0673   1 MDKLRVGIIGAGGIGRAHAPALAALPGVELVAVADRDPERAEAFAEEYGVRVYT-----------------DYEELLAdp 63

                        90
                ....*....|
gi 21263613  79 KADLVVDCTP 88
Cdd:COG0673  64 DIDAVVIATP 73
 
Name Accession Description Interval E-value
PRK04207 PRK04207
type II glyceraldehyde-3-phosphate dehydrogenase;
3-335 0e+00

type II glyceraldehyde-3-phosphate dehydrogenase;


Pssm-ID: 179786 [Multi-domain]  Cd Length: 341  Bit Score: 620.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613    3 KAKIAVNGYGTIGKRVADAVKAQDDMEVVGISKRTPNYEAAVAHQLGYDIYAPAENVG-AFEKAGMPAAGSVEEMIEKAD 81
Cdd:PRK04207   1 MIKVGVNGYGTIGKRVADAVAAQPDMELVGVAKTKPDYEARVAVEKGYPLYVADPEREkAFEEAGIPVAGTIEDLLEKAD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613   82 LVVDCTPGGVGEKNKPLYEKAGVKAIWQGGESHPIAGFSFNAVSNYEGALGRDLVRVVSCNTTGLCRTITPIDRELGVKK 161
Cdd:PRK04207  81 IVVDATPGGVGAKNKELYEKAGVKAIFQGGEKAEVAGVSFNALANYEEALGKDYVRVVSCNTTGLCRTLCALDRAFGVKK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613  162 VRAILARRATDPNDIKKGPINAIVLHPVKLPSHHGPDVRSVIPHINITSAALLVPTTLMHLHTVNMEVDTDCTAEDIKKI 241
Cdd:PRK04207 161 VRATLVRRAADPKEVKRGPINAIVPDPVTVPSHHGPDVKTVLPDLDITTMAVKVPTTLMHMHSVNVELKKPVTKEEVLEA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613  242 FSSQSRIRFI--GQGITSTAEIMEVARDIKRPRNDMWENCIWPESITVDEKEFYFFQAIHQESIVVPENVDAIRAMMELE 319
Cdd:PRK04207 241 LENTPRILLVraSDGIDSTAELIEYARDLGRPRGDLYENAVWEDSITVDGNELYLMQAVHQESIVVPENIDAIRAMLGLE 320

                        330
                 ....*....|....*.
gi 21263613  320 SDGAKSIEKTNKALGM 335
Cdd:PRK04207 321 DDEEKSIEKTNKALGI 336
GAPDH-II_archae TIGR01546
glyceraldehyde-3-phosphate dehydrogenase, type II; This model describes the type II ...
 6-335 1.27e-160

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: 452.02  E-value: 1.27e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613     6 IAVNGYGTIGKRVADAVKAQDDMEVVGISKRTPNYEAAVAHQLGYDIYAPA-ENVGAFEKAGMPAAGSVEEMIEKADLVV 84
Cdd:TIGR01546   1 VGVNGYGTIGKRVADAVTKQDDMKLVGVTKTSPDFEAYRAKELGIPVYAASeEFIPRFEEAGIEVAGTLEDLLEKVDIVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613    85 DCTPGGVGEKNKPLYEKAGVKAIWQGGESHPIAGFSFNAVSNYEGALGRDLVRVVSCNTTGLCRTITPIDRELGVKKVRA 164
Cdd:TIGR01546  81 DATPGGIGAKNKPLYEKAGVKAIFQGGEKAEVADVSFVAQANYEAALGKDYVRVVSCNTTGLVRTLNAINDYSKVDKVRA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613   165 ILARRATDPNDIKKGPINAIVLHPVKLPSHHGPDVRSVIPHINITSAALLVPTTLMHLHTVNMEVDTDCTAEDIKKIFSS 244
Cdd:TIGR01546 161 VMVRRAADPNDVKKGPINAIVPDPVTVPSHHGPDVQTVIPNLNIETMAFVVPTTLMHVHSIMVELKKPVTKDDIIDILEN 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613   245 QSRIRFIG--QGITSTAEIMEVARDIKRPRNDMWENCIWPESITVDEKEFYFFQAIHQESIVVPENVDAIRAMMELEsDG 322
Cdd:TIGR01546 241 TPRVLLFEkkKGFESTAELIEFARDLHRERNDLYEIAVWKESINVKDNELFYMQAVHQESDVVPENIDAIRAMFELA-DK 319

                         330
                  ....*....|...
gi 21263613   323 AKSIEKTNKALGM 335
Cdd:TIGR01546 320 WDSIKKTNKSLGI 332
GAPDH_II_C cd18127
C-terminal catalytic domain of type II glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and ...
 140-301 2.55e-79

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: 239.03  E-value: 2.55e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613 140 SCNTTGLCRTITPIDRELGVKKVRAILARRATDPNDIKKGPINAIVLHPVKlPSHHGPDVRSVIPHINITSAALLVPTTL 219
Cdd:cd18127   1 SCNTTGLSRVLKALDRAFGLKRVRATIVRRAADPGKHKKGVINAIVPEPKD-PSHHAPDVKTVFPDLDITTSAVKVPTTL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613 220 MHLHTVNMEVDTDCTAEDIKKIFSSQSRIRFIGQGI-TSTAEIMEVARDIKRPRNDMWENCIWPESITVDEKEFYFFQAI 298
Cdd:cd18127  80 MHLHTINVELKRKVSREEVLEALASNPRIALVDKEDgTSTNQVFELARDLGRPRGDIYEVAVWEDSIVVDGNELYLFYAV 159


                ...
gi 21263613 299 HQE 301
Cdd:cd18127 160 PQE 162
GAPDH_II_N cd02278
N-terminal NAD(P)-binding domain of type II glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 5-140 2.18e-70

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: 216.66  E-value: 2.18e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613   5 KIAVNGYGTIGKRVADAVKAQDDMEVVGISKRTPNYEAAVAHQLGYDIYAPAE-NVGAFEKAGMPAAGSVEEMIEKADLV 83
Cdd:cd02278   2 KVGVNGYGTIGKRVADAVLLQDDMELVGVAKRSPDYEAKPAVERGIPLYVPDEsRAEKFEEAGIPVAGTLEDLLEKADVV 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21263613  84 VDCTPGGVGEKNKPLYEKAGVKAIWQGGESHPIAGFSFNAVSNYEGALGRDLVRVVS 140
Cdd:cd02278  82 VDCTPKGIGAKNKELYYKAGVKAIFQGGEKHFVAGVSFNAGANYEEALGKQFVRVVS 138
GAPDH_C cd18123
C-terminal catalytic domain of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and similar ...
 141-301 6.41e-34

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: 122.34  E-value: 6.41e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613 141 CNTTGLCRTITPIDRELGVKKVRAILARRATDPNDI-----------KKGPINAIVLHPVklpsHHGPDVRSVIP--HIN 207
Cdd:cd18123   1 CTTNCLAPLAKAIHDSFGIKKGRMTTVHAATDTQKTvdgpsgkdwraSRGAVNNIIPNPT----GAAKAVGKVLPelNGK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613 208 ITSAALLVPTTLMHLHTVNMEVDTDCTAEDIKKIFSSQSRirfiGQGITSTAEIMEVARDIkrpRNDMWENCIWPESI-T 286
Cdd:cd18123  77 LTGMAVRVPTTLMSVHDLMVELEKDVTYDDIKEAVKQAPE----GKGRLGYTEAEDVSSDF---RGDIFESVFDAESIiA 149

                       170
                ....*....|....*
gi 21263613 287 VDEKEFYFFQAIHQE 301
Cdd:cd18123 150 VNDNEVKLMQWYDNE 164
Gp_dh_N smart00846
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 5-141 1.01e-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: 110.72  E-value: 1.01e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613      5 KIAVNGYGTIGKRVADAVKAQDDMEVVGISKRT-PNYEaavAHQLGYD-IYAPAENVGAFEKAGMPAAGSVEEMIEK--- 79
Cdd:smart00846   2 KVGINGFGRIGRLVLRAALERPDVEVVAINDLTdPEYL---AYLLKYDsVHGRFPGTVEVEGDGLVVNGKAIKVFAErdp 78

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21263613     80 ---------ADLVVDCTPGGVGEKNKPLYEKAGVKAIWQGGESHPIAGfSFNAVSNYEGALGRD-LVRVVSC 141
Cdd:smart00846  79 anlpwgelgVDIVVECTGGFTTREKASAHLKAGAKKVIISAPSKDADP-TFVYGVNHDEYDGEDhIISNASC 149
Gp_dh_C pfam02800
Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain; GAPDH is a tetrameric NAD-binding ...
 146-297 7.59e-29

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: 108.83  E-value: 7.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613   146 LCRTITPIDRELGVKKVRAILARRATDP---------NDIKKGPINAivLHPVKLPSHHGPDVRSVIPH--INITSAALL 214
Cdd:pfam02800   1 LAPLAKVLNDNFGIKKGLMTTVHAYTNDqklldgphhKDLRRGRAAA--PNIIPTSTGAAKAVGLVLPElkGKLDGMAVR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613   215 VPTTLMHLHTVNMEVDTDCTAEDIKKIFSSQSRIRFigQGITSTAEIMEVARDIKRPRNDmwENCIWPESITVDEKEFYF 294
Cdd:pfam02800  79 VPTPNVSVVDLVVELEKPVTVEEVNAALKEAAEGAL--KGILSYTEDPLVSSDFIGDPHS--SIFDAKETIVVNGNFVKV 154


                  ...
gi 21263613   295 FQA 297
Cdd:pfam02800 155 VAW 157
GAPDH_like_C cd18122
C-terminal catalytic domain found in glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 141-301 6.32e-18

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: 79.87  E-value: 6.32e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613 141 CNTTGLCRTITPIDRELGVKKVRAILARRATDPNDIKKGPI-----NAIVLHPVKLPSHHGPDVRSVIPHI----NITSA 211
Cdd:cd18122   1 CTTTGLIPAAKALNDKFGIEEILVVTVQAVSGAGPKTKGPIlksevRAIIPNIPKNETKHAPETGKVLGEIgkpiKVDGI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613 212 ALLVPTTLMHLHTVNMEVDTDCTAEDIKKIFSSQSR-IRFIGQGITSTAEIMEvardikRPRNDMWENCIWPESIT-VDE 289
Cdd:cd18122  81 AVRVPATLGHLVTVTVKLEKTATLEQIAEAVAEAVEeVQISAEDGLTYAKVST------RSVGGVYGVPVGRQREFaFDD 154

                       170
                ....*....|..
gi 21263613 290 KEFYFFQAIHQE 301
Cdd:cd18122 155 NKLKVFSAVDNE 166
GAPDH-like_N cd05192
N-terminal NAD(P)-binding domain of the glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-like ...
 5-147 5.82e-10

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: 55.82  E-value: 5.82e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613   5 KIAVNGYGTIGKRVADAVKAQDDMEVVGISKRTpnyeaavahqlgydiyapaenvgafekagmpaagsveemiekaDLVV 84
Cdd:cd05192   2 RVAINGFGRIGRIVFRAIADQDDLDVVAINDRR-------------------------------------------DVVI 38

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21263613  85 DCTPGGVGEKN-KPLYEKAGVKAIWQGGESHPIAGFSFNaVSNYEGALGRDLVRVVscNTTGLC 147
Cdd:cd05192  39 ECTGSFTDDDNaEKHIKAGGKKAVITAPEKGDIPTIVVV-LNELAKSAGATVVSNA--NETSYS 99
DapB_N pfam01113
Dihydrodipicolinate reductase, N-terminus; Dihydrodipicolinate reductase (DapB) reduces the ...
 5-107 1.21e-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: 55.32  E-value: 1.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613     5 KIAVNGY-GTIGKRVADAVKAQDDMEVVGISKRTPNyeaavaHQLGYDIyapaenvGAFEKAGMPAAGSVEEMIEKADLV 83
Cdd:pfam01113   2 KIAVAGAsGRMGRELIKAVLEAPDLELVAAVDRPGS------SLLGSDA-------GELAPLGVPVTDDLEEVLADADVL 68

                          90       100
                  ....*....|....*....|....*
gi 21263613    84 VDCT-PGGVGEKNKPLYEKaGVKAI 107
Cdd:pfam01113  69 IDFTtPEATLENLEFALKH-GVPLV 92
Gp_dh_N pfam00044
Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain; GAPDH is a tetrameric ...
 5-51 2.52e-08

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: 50.95  E-value: 2.52e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 21263613     5 KIAVNGYGTIGKRVADAVKAQDDMEVVGISKRTPNyeAAVAHQLGYD 51
Cdd:pfam00044   2 KVGINGFGRIGRLVLRAALERPDIEVVAINDLTDP--ETLAYLLKYD 46
MviM COG0673
Predicted dehydrogenase [General function prediction only];
1-88 2.26e-07

Predicted dehydrogenase [General function prediction only];


Pssm-ID: 440437 [Multi-domain]  Cd Length: 295  Bit Score: 51.46  E-value: 2.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613   1 MAKAKIAVNGYGTIGKRVADAVKAQDDMEVVGISKRTPNYEAAVAHQLGYDIYApaenvgafekagmpaagSVEEMIE-- 78
Cdd:COG0673   1 MDKLRVGIIGAGGIGRAHAPALAALPGVELVAVADRDPERAEAFAEEYGVRVYT-----------------DYEELLAdp 63

                        90
                ....*....|
gi 21263613  79 KADLVVDCTP 88
Cdd:COG0673  64 DIDAVVIATP 73
meso-DAPDH_N cd02270
N-terminal NAD(P)-binding domain of meso-diaminopimelate D-dehydrogenase (meso-DAPDH) and ...
 5-36 1.96e-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: 46.80  E-value: 1.96e-06
                        10        20        30
                ....*....|....*....|....*....|..
gi 21263613   5 KIAVNGYGTIGKRVADAVKAQDDMEVVGISKR 36
Cdd:cd02270   2 RVAIVGYGNLGRGVEEAIQANPDMELVGVFRR 33
DHDPR_N cd02274
N-terminal NAD(P)-binding domain of dihydrodipicolinate reductase (DHDPR) and similar proteins; ...
 5-107 9.11e-05

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: 41.78  E-value: 9.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613   5 KIAVNGY-GTIGKRVADAVKAQDDMEVVGISKRTPnyeaavAHQLGYDIYapaenVGAFEKAGMPAAGSVEEMIEKADLV 83
Cdd:cd02274   2 KVAVAGAtGRMGRELVKAILEAPDLELVGAVDRPG------SGLLGGDAG-----GLAGIGTGVIVSLDLELAAADADVV 70

                        90       100
                ....*....|....*....|....
gi 21263613  84 VDCTPGGVGEKNKPLYEKAGVKAI 107
Cdd:cd02274  71 IDFTTPEATLENLEAAAKAGVPLV 94
DAP-DH TIGR01921
diaminopimelate dehydrogenase; This model represents the diaminopimelate dehydrogenase enzyme ...
 1-52 1.42e-04

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: 43.01  E-value: 1.42e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21263613     1 MAKAKIAVNGYGTIGKRVADAVKAQDDMEVVGISKR---------TPNYEAAVA--HQLGYDI 52
Cdd:TIGR01921   1 MSKIRAAIVGYGNLGRSVEKAIQQQPDMELVGVFSRrgaetldteTPVYAVADDekHLDDVDV 63
DapB COG0289
4-hydroxy-tetrahydrodipicolinate reductase [Amino acid transport and metabolism]; ...
 5-107 2.19e-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: 42.03  E-value: 2.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613   5 KIAVNG-YGTIGKRVADAVKAQDDMEVVGISKRTPNYeaavahqlGYDIYAPAENVgafekagmPAAGSVEEMIEKADLV 83
Cdd:COG0289   2 KIAVAGaSGRMGRELIRAVLEAPDLELVAAIDRPGSP--------GQDAGELALGV--------PVTDDLEEALAKADVV 65

                        90       100
                ....*....|....*....|....
gi 21263613  84 VDCTPGGVGEKNKPLYEKAGVKAI 107
Cdd:COG0289  66 IDFTHPEATLENLEAALEAGVPVV 89
2-Hacid_dh_6 cd12165
Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze ...
 4-88 2.69e-04

Putative D-isomer specific 2-hydroxyacid dehydrogenases; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.


Pssm-ID: 240642 [Multi-domain]  Cd Length: 314  Bit Score: 42.23  E-value: 2.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613   4 AKIAVNGYGTIGKRVADAVKAQdDMEVVGISkRTPNYEAAVAHQLGYDiyapaenvgafekagmpaagSVEEMIEKADLV 83
Cdd:cd12165 138 KTVGILGYGHIGREIARLLKAF-GMRVIGVS-RSPKEDEGADFVGTLS--------------------DLDEALEQADVV 195


                ....*
gi 21263613  84 VDCTP 88
Cdd:cd12165 196 VVALP 200
2-Hacid_dh_1 cd05300
Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze ...
 10-89 1.96e-03

Putative D-isomer specific 2-hydroxyacid dehydrogenase; 2-Hydroxyacid dehydrogenases catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate/glycerate and related dehydrogenases of the D-specific 2-hydroxyacid dehydrogenase superfamily include groups such as formate dehydrogenase, glycerate dehydrogenase, L-alanine dehydrogenase, and S-adenosylhomocysteine hydrolase. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann fold NAD+ binding form. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomains but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of the hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases. FDHs are found in all methylotrophic microorganisms in energy production and in the stress responses of plants.


Pssm-ID: 240625 [Multi-domain]  Cd Length: 313  Bit Score: 39.43  E-value: 1.96e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613  10 GYGTIGKRVADAVKAQdDMEVVGIsKRTPNYEAAVAHQlgydIYAPAEnvgafekagmpaagsVEEMIEKADLVVDCTPG 89
Cdd:cd05300 141 GLGDIGREIARRAKAF-GMRVIGV-RRSGRPAPPVVDE----VYTPDE---------------LDELLPEADYVVNALPL 199
GAPDH_I_N cd05214
N-terminal NAD(P)-binding domain of type I glyceraldehyde-3-phosphate dehydrogenase (GAPDH) ...
 5-51 4.19e-03

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: 37.37  E-value: 4.19e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 21263613   5 KIAVNGYGTIGKRVADAVKAQDDMEVVGISKRTPNyeAAVAHQLGYD 51
Cdd:cd05214   2 KVGINGFGRIGRLVFRAALERDDIEVVAINDLTDD--ETLAYLLKYD 46
GapA COG0057
Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate ...
 1-51 5.07e-03

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: 38.07  E-value: 5.07e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 21263613   1 MAKaKIAVNGYGTIGKRVADA-VKAQDDMEVVGISKRTPNyeAAVAHQLGYD 51
Cdd:COG0057   1 MTI-RVAINGFGRIGRLVLRAlLERGPDIEVVAINDLGDA--ETLAHLLKYD 49
SerA COG0111
Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; ...
 10-88 6.99e-03

Phosphoglycerate dehydrogenase or related dehydrogenase [Coenzyme transport and metabolism]; Phosphoglycerate dehydrogenase or related dehydrogenase is part of the Pathway/BioSystem: Serine biosynthesis


Pssm-ID: 439881 [Multi-domain]  Cd Length: 314  Bit Score: 37.87  E-value: 6.99e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21263613  10 GYGTIGKRVADAVKAQdDMEVvgiskrtpnyeaavahqLGYDIYAPAEnvgAFEKAGMPAAGSVEEMIEKADLVVDCTP 88
Cdd:COG0111 147 GLGRIGRAVARRLRAF-GMRV-----------------LAYDPSPKPE---EAADLGVGLVDSLDELLAEADVVSLHLP 204
PRK13302 PRK13302
aspartate dehydrogenase;
1-107 7.93e-03

aspartate dehydrogenase;


Pssm-ID: 237341 [Multi-domain]  Cd Length: 271  Bit Score: 37.53  E-value: 7.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21263613    1 MAKAKIAVNGYGTIGKRVADAV-KAQDDMEVVGISKRTPNYEAAVAHQLGYDiyapaenvgafekagmPAAGSVEEMIEK 79
Cdd:PRK13302   4 RPELRVAIAGLGAIGKAIAQALdRGLPGLTLSAVAVRDPQRHADFIWGLRRP----------------PPVVPLDQLATH 67

                         90       100
                 ....*....|....*....|....*...
gi 21263613   80 ADLVVDCTPGGVGEKNKPLYEKAGVKAI 107
Cdd:PRK13302  68 ADIVVEAAPASVLRAIVEPVLAAGKKAI 95
 
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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