| General Information |
| MoonProt ID | 486 |
| First appeared in release | 3.0 |
| Name(s) | Bifunctional NAD(P)H-hydrate repair enzyme; nnrD |
| UniProt ID | H2C3I7 (H2C3I7_9CREN) |
| GO terms | GO:0052855 ADP-dependent NAD(P)H-hydrate dehydratase activity
GO:0046872 metal ion binding
GO:0016829 lyase activity
GO:0000166 nucleotide binding
GO:0016853 isomerase activity
GO:0005524 ATP binding
GO:0052857 NADPHX epimerase activity
GO:0046496 nicotinamide nucleotide metabolic process
GO:0052856 NADHX epimerase activity |
| Organisms for which functions have been demonstrated | Metallosphaera yellowstonensis MK1 |
| Sequence length | 501 amino acids |
| FASTA sequence | >tr|H2C3I7|H2C3I7_9CREN Bifunctional NAD(P)H-hydrate repair enzyme OS=Metallosphaera yellowstonensis MK1 OX=671065 GN=nnrD PE=3 SV=1
MITSKRMRALEINSDSLGVSTLQLMENAGRAVVEEIEKEVSLDNVSATVFVGHGGKGGDGLVVARQLAGRGAKVRVILLGEIKHKDALVNLNAVMEMDYSVELKEVYDLSELTSTKSDVLIDAMLGTGVKGKIREPFVTAIEVFNKSQGFKVSIDVPSGLDPDTGESLGAHVTPDLVVTFHDMKVGLLKVGFRTVVKKIGIPPEAELYVGPGDLMVNLKPRDMKSRKGVGGRVLVVGGSKTFSGAPALAGMAALRTGADLVYIASPEETAKTIASYSPDLIVVKLRGENFNQRNLEELKPWAEKANAVIFGPGLGLDPETIEAALPFLEMLMSLGKPVVLDADGLKAAKGHRLNKNVVITPHPGEFKIFFGEDQELNERKRIQQVMRKAEECNCVILLKGYLDIISDGREFRLNKTGNPGMTTGGTGDTLTGIIGTLLAQGLTTFDAASIGALINSLAGTVAFSNYGAHITATDVIANIPYVMNDPVGAFKKKVYKRVISW |
| Structure Information |
| PDB ID | NA |
| Quaternary structure | NA |
| SCOP | |
| CATH | |
| TM Helix Prediction | no TM helices |
| DisProt Annotation | |
| Predicted Disorder Regions | Use FASTA sequence on the MFDp2 webserver.
tr_H2C3I7_H2C3I7_9CREN_B is 501 residues long, with 0 residues (0.00 %) predicted as disordered. The protein has 0 short (< 30 residues) disorder segments and 0 long (>= 30 residues) disorder segments. |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | catalyzes the epimerization of the S- and R-forms of NAD(P)HX |
| References for function | Marbaix AY, Noël G, Detroux AM, Vertommen D, Van Schaftingen E, Linster CL. Extremely conserved ATP-or ADP-dependent enzymatic system for nicotinamide nucleotide repair. Journal of Biological Chemistry. 2011 Dec 2;286(48):41246-52. |
| E.C. number | 5.1.99.6 |
| Location of functional site(s) | |
| Cellular location of function | cytoplasm |
| Comments | |
| Function 2 |
| Function description | catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP |
| References for function | Marbaix AY, Noël G, Detroux AM, Vertommen D, Van Schaftingen E, Linster CL. Extremely conserved ATP-or ADP-dependent enzymatic system for nicotinamide nucleotide repair. Journal of Biological Chemistry. 2011 Dec 2;286(48):41246-52. |
| E.C. number | 4.2.1.136 |
| Location of functional site(s) | |
| Cellular location of function | cytoplasm |
| Comments | |