ID   NADD_CAMJE              Reviewed;         181 AA.
AC   Q9PMQ3; Q0P8L0;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Probable nicotinate-nucleotide adenylyltransferase;
DE            EC=2.7.7.18;
DE   AltName: Full=Deamido-NAD(+) diphosphorylase;
DE   AltName: Full=Deamido-NAD(+) pyrophosphorylase;
DE   AltName: Full=Nicotinate mononucleotide adenylyltransferase;
DE            Short=NaMN adenylyltransferase;
GN   Name=nadD; OrderedLocusNames=Cj1404;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
CC   -!- FUNCTION: Catalyzes the reversible adenylation of nicotinate
CC       mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+)
CC         + diphosphate; Xref=Rhea:RHEA:22860, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502,
CC         ChEBI:CHEBI:58437; EC=2.7.7.18;
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+)
CC       from nicotinate D-ribonucleotide: step 1/1.
CC   -!- SIMILARITY: Belongs to the NadD family. {ECO:0000305}.
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DR   EMBL; AL111168; CAL35513.1; -; Genomic_DNA.
DR   PIR; D81285; D81285.
DR   RefSeq; WP_002780449.1; NC_002163.1.
DR   RefSeq; YP_002344787.1; NC_002163.1.
DR   AlphaFoldDB; Q9PMQ3; -.
DR   SMR; Q9PMQ3; -.
DR   IntAct; Q9PMQ3; 4.
DR   STRING; 192222.Cj1404; -.
DR   PaxDb; Q9PMQ3; -.
DR   PRIDE; Q9PMQ3; -.
DR   EnsemblBacteria; CAL35513; CAL35513; Cj1404.
DR   GeneID; 905693; -.
DR   KEGG; cje:Cj1404; -.
DR   PATRIC; fig|192222.6.peg.1385; -.
DR   eggNOG; COG1057; Bacteria.
DR   HOGENOM; CLU_069765_3_2_7; -.
DR   OMA; AYQNPFK; -.
DR   UniPathway; UPA00253; UER00332.
DR   Proteomes; UP000000799; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02165; NMNAT; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00244; NaMN_adenylyltr; 1.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR005248; NadD/NMNAT.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
DR   TIGRFAMs; TIGR00482; TIGR00482; 1.
PE   3: Inferred from homology;
KW   ATP-binding; NAD; Nucleotide-binding; Nucleotidyltransferase;
KW   Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..181
FT                   /note="Probable nicotinate-nucleotide adenylyltransferase"
FT                   /id="PRO_0000181400"
SQ   SEQUENCE   181 AA;  21312 MW;  7B9B437536992BCF CRC64;
     MKIALFGGSF DPPHNGHNSV VLEALEKLDI DKLIIMPTYI NPFKQSFSAD EKQRFLWVKK
     LWGHLPKVEI CDFEIRQKRP VPSIESVKYL YKLYNPSKFY LLIGADHLEK LHLWHDFEKL
     NSLVEFVIAN RNDIGIPKNF KDLKTNKKIA SSFIRDTLNT NEVCEEIKDE VKKYYEKLQK
     N