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Bifunctional NAD biosynthesis protein NadR [Includes: 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_HAEIN              Reviewed;         421 AA.
P44308;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
25-APR-2018, entry version 123.
RecName: Full=Bifunctional NAD biosynthesis protein 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; OrderedLocusNames=HI_0763;
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
Pasteurellaceae; Haemophilus.
NCBI_TaxID=71421;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
PubMed=7542800; DOI=10.1126/science.7542800;
Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M.,
Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D.,
Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C.,
Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M.,
Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O.,
Venter J.C.;
"Whole-genome random sequencing and assembly of Haemophilus influenzae
Rd.";
Science 269:496-512(1995).
[2]
FUNCTION, CATALYTIC ACTIVITY, ALTERNATIVE INITIATION, AND
BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
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).
[3]
MUTAGENESIS OF LYS-126; GLY-238; TRP-256; TYR-292; ASP-304 AND
ARG-352, AND SUBCELLULAR LOCATION.
STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
PubMed=15968050; DOI=10.1128/JB.187.13.4410-4420.2005;
Merdanovic M., Sauer E., Reidl J.;
"Coupling of NAD+ biosynthesis and nicotinamide ribosyl transport:
characterization of NadR ribonucleotide kinase mutants of Haemophilus
influenzae.";
J. Bacteriol. 187:4410-4420(2005).
[4]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 57-421 IN COMPLEX WITH NAD,
AND SUBUNIT.
PubMed=12068016; DOI=10.1074/jbc.M204368200;
Singh S.K., Kurnasov O.V., Chen B., Robinson H., Grishin N.V.,
Osterman A.L., Zhang H.;
"Crystal structure of Haemophilus influenzae NadR protein. A
bifunctional enzyme endowed with NMN adenyltransferase and
ribosylnicotinimide kinase activities.";
J. Biol. Chem. 277:33291-33299(2002).
-!- FUNCTION: This enzyme has two activities: nicotinamide
mononucleotide (NMN) adenylyltransferase and ribosylnicotinamide
(RN) kinase. 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(+).
{ECO:0000269|PubMed:12446641}.
-!- CATALYTIC ACTIVITY: ATP + nicotinamide ribonucleotide =
diphosphate + NAD(+). {ECO:0000269|PubMed:12446641}.
-!- CATALYTIC ACTIVITY: ATP + 1-(beta-D-ribofuranosyl)-nicotinamide =
ADP + beta-nicotinamide D-ribonucleotide.
{ECO:0000269|PubMed:12446641}.
-!- ENZYME REGULATION: Feed-back regulated by NAD. At high levels of
NAD the RN kinase activity is inhibited.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.14 mM for NMN {ECO:0000269|PubMed:12446641};
-!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis [regulation].
-!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
nicotinamide D-ribonucleotide: step 1/1.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12068016}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15968050};
Peripheral membrane protein {ECO:0000269|PubMed:15968050}.
Cytoplasm {ECO:0000269|PubMed:15968050}. Note=Found as a soluble
cytoplasmic protein as well as a membrane-associated protein. In
combination with corepressor (NAD), the cytoplasmic form of NadR
would be capable of acting as a transcriptional repressor.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=Long;
IsoId=P44308-1; Sequence=Displayed;
Name=Short;
IsoId=P44308-2; Sequence=VSP_040071;
Note=Shows the same catalytic activity as isoform Long.;
-!- SIMILARITY: In the N-terminal 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; L42023; AAC22421.1; -; Genomic_DNA.
PIR; D64091; D64091.
RefSeq; NP_438922.1; NC_000907.1. [P44308-1]
RefSeq; WP_005690353.1; NC_000907.1.
PDB; 1LW7; X-ray; 2.90 A; A=57-421.
PDBsum; 1LW7; -.
ProteinModelPortal; P44308; -.
SMR; P44308; -.
STRING; 71421.HI0763; -.
TCDB; 4.B.1.1.2; the nicotinamide ribonucleoside (nr) uptake permease (pnuc) family.
EnsemblBacteria; AAC22421; AAC22421; HI_0763.
GeneID; 950800; -.
KEGG; hin:HI0763; -.
PATRIC; fig|71421.8.peg.802; -.
eggNOG; ENOG4107VZS; Bacteria.
eggNOG; COG1056; LUCA.
eggNOG; COG3172; LUCA.
KO; K06211; -.
OMA; KFYPPHA; -.
PhylomeDB; P44308; -.
BioCyc; HINF71421:G1GJ1-803-MONOMER; -.
BioCyc; MetaCyc:MONOMER-8322; -.
UniPathway; UPA00253; -.
UniPathway; UPA00253; UER00600.
EvolutionaryTrace; P44308; -.
Proteomes; UP000000579; 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:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
Gene3D; 3.40.50.620; -; 1.
InterPro; IPR016429; Bifunc_transcrip_reg_NadR.
InterPro; IPR004821; Cyt_trans-like.
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; PF01467; CTP_transf_like; 1.
PIRSF; PIRSF004776; NadR_NMNAT/RNK; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
TIGRFAMs; TIGR01526; nadR_NMN_Atrans; 1.
1: Evidence at protein level;
3D-structure; Alternative initiation; ATP-binding; Cell membrane;
Complete proteome; Cytoplasm; Kinase; Membrane;
Multifunctional enzyme; NAD; Nucleotide-binding;
Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
CHAIN 1 421 Bifunctional NAD biosynthesis protein
NadR.
/FTId=PRO_0000096689.
NP_BIND 64 67 NAD 1. {ECO:0000269|PubMed:12068016}.
NP_BIND 139 152 NAD 1. {ECO:0000269|PubMed:12068016}.
NP_BIND 172 174 NAD 1. {ECO:0000269|PubMed:12068016}.
NP_BIND 199 201 NAD 1. {ECO:0000269|PubMed:12068016}.
NP_BIND 254 256 NAD 2. {ECO:0000269|PubMed:12068016}.
NP_BIND 289 292 NAD 2. {ECO:0000269|PubMed:12068016}.
REGION 57 224 Nicotinamide mononucleotide
adenylyltransferase.
REGION 225 421 Ribosylnicotinamide kinase.
BINDING 71 71 NAD 1. {ECO:0000269|PubMed:12068016}.
BINDING 98 98 NAD 1. {ECO:0000269|PubMed:12068016}.
VAR_SEQ 1 51 Missing (in isoform Short).
{ECO:0000305}.
/FTId=VSP_040071.
MUTAGEN 126 126 K->A,T: Significant reduction of RNK
activity, also NMN adenylyltransferase
activity is impaired.
{ECO:0000269|PubMed:15968050}.
MUTAGEN 238 238 G->N,S: Complete loss of RNK activity, no
effect on NMN adenylyltransferase
activity. {ECO:0000269|PubMed:15968050}.
MUTAGEN 256 256 W->F: No effect on enzyme activities, but
NAD feedback inhibition is almost lost.
{ECO:0000269|PubMed:15968050}.
MUTAGEN 292 292 Y->I: Almost no effect.
{ECO:0000269|PubMed:15968050}.
MUTAGEN 304 304 D->C,N,S: Complete loss of RNK activity,
no effect on NMN adenylyltransferase
activity. {ECO:0000269|PubMed:15968050}.
MUTAGEN 352 352 R->A,C,M,N: Complete loss of RNK
activity, no effect on NMN
adenylyltransferase activity.
{ECO:0000269|PubMed:15968050}.
STRAND 60 65 {ECO:0000244|PDB:1LW7}.
HELIX 72 82 {ECO:0000244|PDB:1LW7}.
STRAND 86 94 {ECO:0000244|PDB:1LW7}.
HELIX 96 105 {ECO:0000244|PDB:1LW7}.
HELIX 114 124 {ECO:0000244|PDB:1LW7}.
TURN 127 131 {ECO:0000244|PDB:1LW7}.
STRAND 132 138 {ECO:0000244|PDB:1LW7}.
STRAND 140 142 {ECO:0000244|PDB:1LW7}.
HELIX 149 162 {ECO:0000244|PDB:1LW7}.
STRAND 168 171 {ECO:0000244|PDB:1LW7}.
HELIX 175 177 {ECO:0000244|PDB:1LW7}.
HELIX 178 184 {ECO:0000244|PDB:1LW7}.
STRAND 188 190 {ECO:0000244|PDB:1LW7}.
HELIX 203 208 {ECO:0000244|PDB:1LW7}.
HELIX 210 216 {ECO:0000244|PDB:1LW7}.
TURN 219 221 {ECO:0000244|PDB:1LW7}.
HELIX 222 224 {ECO:0000244|PDB:1LW7}.
STRAND 227 232 {ECO:0000244|PDB:1LW7}.
HELIX 238 249 {ECO:0000244|PDB:1LW7}.
STRAND 253 255 {ECO:0000244|PDB:1LW7}.
HELIX 260 265 {ECO:0000244|PDB:1LW7}.
STRAND 266 269 {ECO:0000244|PDB:1LW7}.
TURN 276 278 {ECO:0000244|PDB:1LW7}.
HELIX 279 296 {ECO:0000244|PDB:1LW7}.
STRAND 298 305 {ECO:0000244|PDB:1LW7}.
HELIX 307 318 {ECO:0000244|PDB:1LW7}.
HELIX 323 331 {ECO:0000244|PDB:1LW7}.
STRAND 335 341 {ECO:0000244|PDB:1LW7}.
HELIX 360 372 {ECO:0000244|PDB:1LW7}.
HELIX 373 375 {ECO:0000244|PDB:1LW7}.
STRAND 379 382 {ECO:0000244|PDB:1LW7}.
HELIX 386 400 {ECO:0000244|PDB:1LW7}.
SEQUENCE 421 AA; 49432 MW; D9A4FD4970A6E7E8 CRC64;
MGFTTGREFH PALRMRAKYN AKYLGTKSER EKYFHLAYNK HTQFLRYQEQ IMSKTKEKKV
GVIFGKFYPV HTGHINMIYE AFSKVDELHV IVCSDTVRDL KLFYDSKMKR MPTVQDRLRW
MQQIFKYQKN QIFIHHLVED GIPSYPNGWQ SWSEAVKTLF HEKHFEPSIV FSSEPQDKAP
YEKYLGLEVS LVDPDRTFFN VSATKIRTTP FQYWKFIPKE ARPFFAKTVA ILGGESSGKS
VLVNKLAAVF NTTSAWEYGR EFVFEKLGGD EQAMQYSDYP QMALGHQRYI DYAVRHSHKI
AFIDTDFITT QAFCIQYEGK AHPFLDSMIK EYPFDVTILL KNNTEWVDDG LRSLGSQKQR
QQFQQLLKKL LDKYKVPYIE IESPSYLDRY NQVKAVIEKV LNEEEISELQ NTTFPIKGTS
Q


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