| Tag | Content |
|---|
| CPLM ID | CPLM-006020 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Bifunctional NAD(P)H-hydrate repair enzyme Nnr |
Protein Synonyms/Alias | Nicotinamide nucleotide repair protein; ADP-dependent (S)-NAD(P)H-hydrate dehydratase; ADP-dependent NAD(P)HX dehydratase; NAD(P)H-hydrate epimerase; NAD(P)HX epimerase |
Gene Name | nnr |
Gene Synonyms/Alias | yjeF; b4167; JW4125 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 243 | EQLSHWLKPRRPTSH | acetylation | [1] | | 342 | WGKKALQKVENFRKP | acetylation | [1] | | 366 | LLAINPDKRHNRVIT | acetylation | [1] |
|
Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. |
Sequence Annotation | DOMAIN 23 225 YjeF N-terminal.
DOMAIN 234 501 YjeF C-terminal.
NP_BIND 412 416 ADP (By similarity).
NP_BIND 432 441 ADP (By similarity).
REGION 1 227 NAD(P)H-hydrate epimerase (By
REGION 71 75 NAD(P)HX (for epimerase activity) (By
REGION 139 145 NAD(P)HX (for epimerase activity) (By
REGION 235 515 ADP-dependent (S)-NAD(P)H-hydrate
REGION 375 381 NAD(P)HX (for dehydratase activity) (By
METAL 72 72 Potassium (By similarity).
METAL 135 135 Potassium (By similarity).
METAL 171 171 Potassium (By similarity).
BINDING 168 168 NAD(P)HX (for epimerase activity) (By
BINDING 329 329 NAD(P)HX (for dehydratase activity); via
BINDING 442 442 NAD(P)HX (for dehydratase activity) (By |
Keyword | ATP-binding; Complete proteome; Isomerase; Lyase; Metal-binding; Multifunctional enzyme; NAD; NADP; Nucleotide-binding; Potassium; Reference proteome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 515 AA |
Protein Sequence | MTDHTMKKNP VSIPHTVWYA DDIRRGEREA ADVLGLTLYE LMLRAGEAAF QVCRSAYPDA 60
RHWLVLCGHG NNGGDGYVVA RLAKAVGIEV TLLAQESDKP LPEEAALARE AWLNAGGEIH 120
ASNIVWPESV DLIVDALLGT GLRQAPRESI SQLIDHANSH PAPIVAVDIP SGLLAETGAT 180
PGAVINADHT ITFIALKPGL LTGKARDVTG QLHFDSLGLD SWLAGQETKI QRFSAEQLSH 240
WLKPRRPTSH KGDHGRLVII GGDHGTAGAI RMTGEAALRA GAGLVRVLTR SENIAPLLTA 300
RPELMVHELT MDSLTESLEW ADVVVIGPGL GQQEWGKKAL QKVENFRKPM LWDADALNLL 360
AINPDKRHNR VITPHPGEAA RLLGCSVAEI ESDRLHCAKR LVQRYGGVAV LKGAGTVVAA 420
HPDALGIIDA GNAGMASGGM GDVLSGIIGA LLGQKLSPYD AACAGCVAHG AAADVLAARF 480
GTRGMLATDL FSTLQRIVNP EVTDKNHDES SNSAP 515 |
Gene Ontology | GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IDA:EcoCyc. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0052856; F:NADHX epimerase activity; IDA:EcoCyc. GO:0052857; F:NADPHX epimerase activity; IDA:EcoCyc. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |