ID   NADR_KLEPN              Reviewed;          47 AA.
AC   P47981;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Trifunctional NAD biosynthesis/regulator protein NadR;
DE   Includes:
DE     RecName: Full=Transcriptional regulator NadR;
DE   Includes:
DE     RecName: Full=Nicotinamide mononucleotide adenylyltransferase;
DE              Short=NMN adenylyltransferase;
DE              Short=NMN-AT;
DE              Short=NMNAT;
DE              EC=2.7.7.1;
DE     AltName: Full=Nicotinamide ribonucleotide adenylyltransferase;
DE     AltName: Full=Nicotinamide-nucleotide adenylyltransferase;
DE   Includes:
DE     RecName: Full=Ribosylnicotinamide kinase;
DE              Short=RNK;
DE              EC=2.7.1.22;
DE     AltName: Full=Nicotinamide riboside kinase;
DE              Short=NRK;
DE              Short=NmR-K;
DE   Flags: Fragment;
GN   Name=nadR;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3149945; DOI=10.1016/0378-1119(88)90171-0;
RA   Konyecsni W.M., Deretic V.;
RT   "Broad-host-range plasmid and M13 bacteriophage-derived vectors for
RT   promoter analysis in Escherichia coli and Pseudomonas aeruginosa.";
RL   Gene 74:375-386(1988).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=7920643; DOI=10.1038/ng0694-205;
RA   Robison K., Gilbert W., Church G.M.;
RT   "Large scale bacterial gene discovery by similarity search.";
RL   Nat. Genet. 7:205-214(1994).
CC   -!- FUNCTION: This enzyme has three activities: DNA binding, nicotinamide
CC       mononucleotide (NMN) adenylyltransferase and ribosylnicotinamide (RN)
CC       kinase. The DNA-binding domain binds to the nadB operator sequence in
CC       an NAD- and ATP-dependent manner. As NAD levels increase within the
CC       cell, the affinity of NadR for the nadB operator regions of nadA, nadB,
CC       and pncB increases, repressing the transcription of these genes. The RN
CC       kinase activity catalyzes the phosphorylation of RN to form
CC       nicotinamide ribonucleotide. The NMN adenylyltransferase activity
CC       catalyzes the transfer of the AMP moiety of ATP to nicotinamide
CC       ribonucleotide to form NAD(+). The NMN adenylyltransferase domain also
CC       functions as the NAD and ATP sensor (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate
CC         + NAD(+); Xref=Rhea:RHEA:21360, ChEBI:CHEBI:14649, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540; EC=2.7.7.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-nicotinamide D-riboside = ADP + beta-nicotinamide
CC         D-ribonucleotide + H(+); Xref=Rhea:RHEA:14017, ChEBI:CHEBI:14649,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15927, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:456216; EC=2.7.1.22;
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis [regulation].
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC       nicotinamide D-ribonucleotide: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC       Cytoplasm {ECO:0000250}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M28676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P47981; -.
DR   SMR; P47981; -.
DR   PRIDE; P47981; -.
DR   UniPathway; UPA00253; -.
DR   UniPathway; UPA00253; UER00600.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050262; F:ribosylnicotinamide kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   InterPro; IPR001387; Cro/C1-type_HTH.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR   SUPFAM; SSF47413; SSF47413; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Cytoplasm; DNA-binding; Kinase; Membrane;
KW   Multifunctional enzyme; NAD; Nucleotide-binding;
KW   Pyridine nucleotide biosynthesis; Repressor; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN           1..>47
FT                   /note="Trifunctional NAD biosynthesis/regulator protein
FT                   NadR"
FT                   /id="PRO_0000096690"
FT   DOMAIN          7..>47
FT                   /note="HTH cro/C1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT   DNA_BIND        18..37
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT   NON_TER         47
SQ   SEQUENCE   47 AA;  5278 MW;  7587ACFBECADF150 CRC64;
     MSSFDYLKSA IKQKGCTLDE VAEPSGMTKG YLSQLLNRKI KARARRS