ID   NADD_MYCLE              Reviewed;         214 AA.
AC   Q9CBZ8;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 107.
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=ML1454;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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; AL583922; CAC30404.1; -; Genomic_DNA.
DR   PIR; G87090; G87090.
DR   RefSeq; NP_302026.1; NC_002677.1.
DR   RefSeq; WP_010908347.1; NC_002677.1.
DR   AlphaFoldDB; Q9CBZ8; -.
DR   SMR; Q9CBZ8; -.
DR   STRING; 272631.ML1454; -.
DR   EnsemblBacteria; CAC30404; CAC30404; CAC30404.
DR   KEGG; mle:ML1454; -.
DR   PATRIC; fig|272631.5.peg.2717; -.
DR   Leproma; ML1454; -.
DR   eggNOG; COG1057; Bacteria.
DR   HOGENOM; CLU_069765_1_1_11; -.
DR   OMA; IHIGHLI; -.
DR   UniPathway; UPA00253; UER00332.
DR   Proteomes; UP000000806; 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..214
FT                   /note="Probable nicotinate-nucleotide adenylyltransferase"
FT                   /id="PRO_0000181426"
SQ   SEQUENCE   214 AA;  23700 MW;  4CF67AE8E2A902F7 CRC64;
     MGGTFDPIHY GHLVAASEVA HMFELDEVMF VPSGQPWQKG RHVSAAEDRY LMTVIATASN
     PRFSVSRVDI DRTGPTYTRD TVHDLHALNP DSELYFITGA DALASILSWQ GWDELFDLAR
     FVGVSRPGYE LGQEHITGVM GELPADALTL VEIPALAISS TDCRQRVEQR QPLWYLMPDG
     VVQYVFKRRL YRGPHGVAGT GRLTTPSLVV GNNT