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Trifunctional NAD biosynthesis/regulator protein NadR [Includes: Transcriptional regulator NadR; Nicotinamide mononucleotide adenylyltransferase (NMN adenylyltransferase) (NMN-AT) (NMNAT) (EC 2.7.7.1) (Nicotinamide ribonucleotide adenylyltransferase) (Nicotinamide-nucleotide adenylyltransferase); Ribosylnicotinamide kinase (RNK) (EC 2.7.1.22) (Nicotinamide riboside kinase) (NRK) (NmR-K)]

 NADR_SALTY              Reviewed;         410 AA.
P24518;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
23-JAN-2002, sequence version 2.
25-APR-2018, entry version 131.
RecName: Full=Trifunctional NAD biosynthesis/regulator protein NadR;
Includes:
RecName: Full=Transcriptional regulator NadR;
Includes:
RecName: Full=Nicotinamide mononucleotide adenylyltransferase;
Short=NMN adenylyltransferase;
Short=NMN-AT;
Short=NMNAT;
EC=2.7.7.1;
AltName: Full=Nicotinamide ribonucleotide adenylyltransferase;
AltName: Full=Nicotinamide-nucleotide adenylyltransferase;
Includes:
RecName: Full=Ribosylnicotinamide kinase;
Short=RNK;
EC=2.7.1.22;
AltName: Full=Nicotinamide riboside kinase;
Short=NRK;
Short=NmR-K;
Name=nadR; Synonyms=nadI, pnuA; OrderedLocusNames=STM4580;
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Salmonella.
NCBI_TaxID=99287;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=LT2;
PubMed=2198247; DOI=10.1128/jb.172.8.4187-4196.1990;
Foster J.W., Park Y.K., Penfound T., Fenger T., Spector M.P.;
"Regulation of NAD metabolism in Salmonella typhimurium: molecular
sequence analysis of the bifunctional nadR regulator and the nadA-pnuC
operon.";
J. Bacteriol. 172:4187-4196(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=LT2 / SGSC1412 / ATCC 700720;
PubMed=11677609; DOI=10.1038/35101614;
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
Waterston R., Wilson R.K.;
"Complete genome sequence of Salmonella enterica serovar Typhimurium
LT2.";
Nature 413:852-856(2001).
[3]
CHARACTERIZATION, AND MUTAGENESIS.
PubMed=1991723; DOI=10.1128/jb.173.3.1302-1310.1991;
Zhu N., Roth J.R.;
"The nadI region of Salmonella typhimurium encodes a bifunctional
regulatory protein.";
J. Bacteriol. 173:1302-1310(1991).
[4]
MUTAGENESIS OF HIS-77 AND HIS-80.
PubMed=12446641; DOI=10.1128/JB.184.24.6906-6917.2002;
Kurnasov O.V., Polanuyer B.M., Ananta S., Sloutsky R., Tam A.,
Gerdes S.Y., Osterman A.L.;
"Ribosylnicotinamide kinase domain of NadR protein: identification and
implications in NAD biosynthesis.";
J. Bacteriol. 184:6906-6917(2002).
[5]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=15805524; DOI=10.1128/JB.187.8.2774-2782.2005;
Grose J.H., Bergthorsson U., Roth J.R.;
"Regulation of NAD synthesis by the trifunctional NadR protein of
Salmonella enterica.";
J. Bacteriol. 187:2774-2782(2005).
-!- FUNCTION: This enzyme has three activities: DNA binding,
nicotinamide mononucleotide (NMN) adenylyltransferase and
ribosylnicotinamide (RN) kinase. The DNA-binding domain binds to
the nadB operator sequence in an NAD- and ATP-dependent manner. As
NAD levels increase within the cell, the affinity of NadR for the
nadB operator regions of nadA, nadB, and pncB increases,
repressing the transcription of these genes. The RN kinase
activity catalyzes the phosphorylation of RN to form nicotinamide
ribonucleotide. The NMN adenylyltransferase activity catalyzes the
transfer of the AMP moiety of ATP to nicotinamide ribonucleotide
to form NAD(+). The NMN adenylyltransferase domain also functions
as the NAD and ATP sensor. {ECO:0000269|PubMed:15805524}.
-!- CATALYTIC ACTIVITY: ATP + nicotinamide ribonucleotide =
diphosphate + NAD(+). {ECO:0000269|PubMed:15805524}.
-!- CATALYTIC ACTIVITY: ATP + 1-(beta-D-ribofuranosyl)-nicotinamide =
ADP + beta-nicotinamide D-ribonucleotide.
{ECO:0000269|PubMed:15805524}.
-!- ENZYME REGULATION: Feed-back regulated by NAD. A high level of NAD
causes NadR to lose enzymatic activity and repress several NAD
synthetic genes; conversely, a low NAD level activates the
assimilatory enzymatic activities and leads to derepression of
biosynthetic genes.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.08 mM for ribosylnicotinamide
{ECO:0000269|PubMed:15805524};
KM=1.2 mM for ATP (with ribosylnicotinamide as cosubstrate)
{ECO:0000269|PubMed:15805524};
KM=12.8 mM for NMN {ECO:0000269|PubMed:15805524};
KM=1.2 uM for ATP (with NMN as cosubstrate)
{ECO:0000269|PubMed:15805524};
-!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis [regulation].
-!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
nicotinamide D-ribonucleotide: step 1/1.
-!- SUBUNIT: Homotetramer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
Cytoplasm {ECO:0000250}.
-!- SIMILARITY: In the central section; belongs to the bacterial NMN
adenylyltransferase family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the bacterial
RNK family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M85181; AAA61953.1; -; Genomic_DNA.
EMBL; AE006468; AAL23395.1; -; Genomic_DNA.
PIR; B37753; B37753.
RefSeq; NP_463436.5; NC_003197.2.
RefSeq; WP_000093829.1; NC_003197.2.
ProteinModelPortal; P24518; -.
SMR; P24518; -.
STRING; 99287.STM4580.S; -.
TCDB; 4.B.1.1.1; the nicotinamide ribonucleoside (nr) uptake permease (pnuc) family.
PaxDb; P24518; -.
PRIDE; P24518; -.
EnsemblBacteria; AAL23395; AAL23395; STM4580.
GeneID; 1256106; -.
KEGG; stm:STM4580; -.
eggNOG; ENOG4107VZS; Bacteria.
eggNOG; COG1056; LUCA.
eggNOG; COG3172; LUCA.
KO; K06211; -.
OMA; KFYPPHA; -.
PhylomeDB; P24518; -.
UniPathway; UPA00253; -.
UniPathway; UPA00253; UER00600.
Proteomes; UP000001014; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0050262; F:ribosylnicotinamide kinase activity; IEA:UniProtKB-EC.
GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00093; HTH_XRE; 1.
Gene3D; 3.40.50.620; -; 1.
InterPro; IPR016429; Bifunc_transcrip_reg_NadR.
InterPro; IPR001387; Cro/C1-type_HTH.
InterPro; IPR004821; Cyt_trans-like.
InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
InterPro; IPR038727; NadR/Ttd14_AAA_dom.
InterPro; IPR006417; NadR_NMN_Atrans.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR014729; Rossmann-like_a/b/a_fold.
Pfam; PF13521; AAA_28; 1.
Pfam; PF01381; HTH_3; 1.
PIRSF; PIRSF004776; NadR_NMNAT/RNK; 1.
SMART; SM00530; HTH_XRE; 1.
SUPFAM; SSF47413; SSF47413; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
TIGRFAMs; TIGR01526; nadR_NMN_Atrans; 1.
PROSITE; PS50943; HTH_CROC1; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Complete proteome; Cytoplasm; DNA-binding;
Kinase; Membrane; Multifunctional enzyme; NAD; Nucleotide-binding;
Pyridine nucleotide biosynthesis; Reference proteome; Repressor;
Transcription; Transcription regulation; Transferase.
CHAIN 1 410 Trifunctional NAD biosynthesis/regulator
protein NadR.
/FTId=PRO_0000149729.
DOMAIN 7 62 HTH cro/C1-type. {ECO:0000255|PROSITE-
ProRule:PRU00257}.
DNA_BIND 18 37 H-T-H motif. {ECO:0000305}.
NP_BIND 70 73 NAD 1. {ECO:0000250}.
NP_BIND 144 157 NAD 1. {ECO:0000250}.
NP_BIND 177 179 NAD 1. {ECO:0000250}.
NP_BIND 204 206 NAD 1. {ECO:0000250}.
NP_BIND 259 261 NAD 2. {ECO:0000250}.
NP_BIND 294 297 NAD 2. {ECO:0000250}.
REGION 63 229 Nicotinamide mononucleotide
adenylyltransferase.
REGION 230 410 Ribosylnicotinamide kinase.
BINDING 77 77 NAD 1. {ECO:0000250}.
BINDING 104 104 NAD 1. {ECO:0000250}.
MUTAGEN 21 21 V->M: Loss of DNA binding activity.
{ECO:0000269|PubMed:1991723}.
MUTAGEN 22 22 A->T: Loss of DNA binding activity.
{ECO:0000269|PubMed:1991723}.
MUTAGEN 43 43 P->L: Loss of DNA binding activity.
{ECO:0000269|PubMed:1991723}.
MUTAGEN 77 77 H->A: Complete loss of NMN
adenylyltransferase activity.
{ECO:0000269|PubMed:12446641}.
MUTAGEN 80 80 H->A: Complete loss of NMN
adenylyltransferase activity.
{ECO:0000269|PubMed:12446641}.
MUTAGEN 123 123 R->H: No NMN adenylyltransferase
activity. Binds DNA independently of NAD;
when associated with N-173.
{ECO:0000269|PubMed:1991723}.
MUTAGEN 173 173 S->N: No NMN adenylyltransferase
activity. Binds DNA independently of NAD;
when associated with H-123.
{ECO:0000269|PubMed:1991723}.
MUTAGEN 212 212 R->C: No NMN adenylyltransferase
activity. Binds DNA independently of NAD.
{ECO:0000269|PubMed:1991723}.
MUTAGEN 264 264 G->D: No RN kinase activity.
{ECO:0000269|PubMed:1991723}.
MUTAGEN 354 354 D->N: Affects RN kinase activity.
{ECO:0000269|PubMed:1991723}.
CONFLICT 22 24 ADA -> LT (in Ref. 1; AAA61953).
{ECO:0000305}.
SEQUENCE 410 AA; 47101 MW; E06B5EFE0E6101C2 CRC64;
MSSFDYLKTA IKQQGCTLQQ VADASGMTKG YLSQLLNAKI KSPSAQKLEA LHRFLGLEFP
RRQKNIGVVF GKFYPLHTGH IYLIQRACSQ VDELHIIMGY DDTRDRGLFE DSAMSQQPTV
SDRLRWLLQT FKYQKNIRIH AFNEEGMEPY PHGWDVWSNG IKAFMAEKGI QPSWIYTSEE
ADAPQYLEHL GIETVLVDPE RTFMNISGAQ IRENPFRYWE YIPTEVKPFF VRTVAILGGE
SSGKSTLVNK LANIFNTTSA WEYGRDYVFS HLGGDEMALQ YSDYDKIALG HAQYIDFAVK
YANKVAFIDT DFVTTQAFCK KYEGREHPFV QALIDEYRFD LVILLENNTP WVADGLRSLG
SSVDRKAFQN LLVEMLKENN IEFVHVKEAD YDGRFLRCVE LVKEMMGEQG


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