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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_ECOLI              Reviewed;         410 AA.
P27278; P76819; Q2M5S7;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 2.
31-JAN-2018, entry version 143.
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; OrderedLocusNames=b4390, JW5800;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=7610040; DOI=10.1093/nar/23.12.2105;
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.,
Blattner F.R.;
"Analysis of the Escherichia coli genome VI: DNA sequence of the
region from 92.8 through 100 minutes.";
Nucleic Acids Res. 23:2105-2119(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-122.
STRAIN=K12;
PubMed=1327967; DOI=10.1016/0378-1119(92)90002-7;
Neuwald A.F., Berg D.E., Stauffer G.V.;
"Mutational analysis of the Escherichia coli serB promoter region
reveals transcriptional linkage to a downstream gene.";
Gene 120:1-9(1992).
[5]
IDENTIFICATION.
Rudd K.E.;
Unpublished observations (JUL-1992).
[6]
FUNCTION AS NMN ADENYLYLTRANSFERASE, AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=10464228;
Raffaelli N., Lorenzi T., Mariani P.L., Emanuelli M., Amici A.,
Ruggieri S., Magni G.;
"The Escherichia coli NadR regulator is endowed with nicotinamide
mononucleotide adenylyltransferase activity.";
J. Bacteriol. 181:5509-5511(1999).
-!- 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:10464228}.
-!- CATALYTIC ACTIVITY: ATP + nicotinamide ribonucleotide =
diphosphate + NAD(+).
-!- CATALYTIC ACTIVITY: ATP + 1-(beta-D-ribofuranosyl)-nicotinamide =
ADP + beta-nicotinamide D-ribonucleotide.
-!- 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 (By similarity). {ECO:0000250}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.7 mM for NMN {ECO:0000269|PubMed:10464228};
KM=1.7 uM for ATP {ECO:0000269|PubMed:10464228};
pH dependence:
Optimum pH is 8.6. {ECO:0000269|PubMed:10464228};
-!- 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}.
-!- SEQUENCE CAUTION:
Sequence=AAA97286.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; U14003; AAA97286.1; ALT_INIT; Genomic_DNA.
EMBL; U00096; AAC77343.2; -; Genomic_DNA.
EMBL; AP009048; BAE78379.1; -; Genomic_DNA.
EMBL; X63155; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; S56614; S56614.
RefSeq; NP_418807.4; NC_000913.3.
RefSeq; WP_000093814.1; NZ_LN832404.1.
ProteinModelPortal; P27278; -.
SMR; P27278; -.
BioGrid; 4260800; 3.
STRING; 316385.ECDH10B_4548; -.
PaxDb; P27278; -.
PRIDE; P27278; -.
EnsemblBacteria; AAC77343; AAC77343; b4390.
EnsemblBacteria; BAE78379; BAE78379; BAE78379.
GeneID; 948911; -.
KEGG; ecj:JW5800; -.
KEGG; eco:b4390; -.
PATRIC; fig|1411691.4.peg.2295; -.
EchoBASE; EB1311; -.
EcoGene; EG11335; nadR.
eggNOG; ENOG4107VZS; Bacteria.
eggNOG; COG1056; LUCA.
eggNOG; COG1396; LUCA.
eggNOG; COG3172; LUCA.
HOGENOM; HOG000127874; -.
InParanoid; P27278; -.
KO; K06211; -.
BioCyc; EcoCyc:PD04413; -.
BioCyc; MetaCyc:PD04413; -.
SABIO-RK; P27278; -.
UniPathway; UPA00253; -.
UniPathway; UPA00253; UER00600.
PRO; PR:P27278; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IDA:CAFA.
GO; GO:0000986; F:bacterial-type proximal promoter sequence-specific DNA binding; IDA:EcoCyc.
GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IDA:EcoCyc.
GO; GO:0050262; F:ribosylnicotinamide kinase activity; IEA:UniProtKB-EC.
GO; GO:0071248; P:cellular response to metal ion; IDA:CAFA.
GO; GO:0009435; P:NAD biosynthetic process; IDA:CAFA.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
GO; GO:0051289; P:protein homotetramerization; IDA:CAFA.
GO; GO:0010446; P:response to alkaline pH; IDA:CAFA.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006810; P:transport; IEA:InterPro.
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; IPR006417; NadR_NMN_Atrans.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR014729; Rossmann-like_a/b/a_fold.
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_0000149728.
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}.
SEQUENCE 410 AA; 47346 MW; BCBC26CD3ABA2F99 CRC64;
MSSFDYLKTA IKQQGCTLQQ VADASGMTKG YLSQLLNAKI KSPSAQKLEA LHRFLGLEFP
RQKKTIGVVF GKFYPLHTGH IYLIQRACSQ VDELHIIMGF DDTRDRALFE DSAMSQQPTV
PDRLRWLLQT FKYQKNIRIH AFNEEGMEPY PHGWDVWSNG IKKFMAEKGI QPDLIYTSEE
ADAPQYMEHL GIETVLVDPK RTFMSISGAQ IRENPFRYWE YIPTEVKPFF VRTVAILGGE
SSGKSTLVNK LANIFNTTSA WEYGRDYVFS HLGGDEIALQ YSDYDKIALG HAQYIDFAVK
YANKVAFIDT DFVTTQAFCK KYEGREHPFV QALIDEYRFD LVILLENNTP WVADGLRSLG
SSVDRKEFQN LLVEMLEENN IEFVRVEEED YDSRFLRCVE LVREMMGEQR


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