ID   NADD_THEMA              Reviewed;         205 AA.
AC   Q9WXV2;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 125.
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=TM_0097;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
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; AE000512; AAD35191.1; -; Genomic_DNA.
DR   PIR; A72418; A72418.
DR   RefSeq; NP_227913.1; NC_000853.1.
DR   RefSeq; WP_010865050.1; NZ_CP011107.1.
DR   AlphaFoldDB; Q9WXV2; -.
DR   SMR; Q9WXV2; -.
DR   STRING; 243274.THEMA_04320; -.
DR   EnsemblBacteria; AAD35191; AAD35191; TM_0097.
DR   KEGG; tma:TM0097; -.
DR   eggNOG; COG1057; Bacteria.
DR   InParanoid; Q9WXV2; -.
DR   OMA; IHIGHLI; -.
DR   OrthoDB; 1433958at2; -.
DR   UniPathway; UPA00253; UER00332.
DR   Proteomes; UP000008183; 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..205
FT                   /note="Probable nicotinate-nucleotide adenylyltransferase"
FT                   /id="PRO_0000181460"
SQ   SEQUENCE   205 AA;  23796 MW;  CBC6518FC579753B CRC64;
     MLSGSETSSL NTGNRIGIFG GSFDPVHTGH VLVSVYTLEI LDLDRLIVVP VFNPPHKKTV
     APFEKRFEWL KKVFEGMEKM EVSDYEKRRG GVSYSIFTIE YFSEIYKTKP FFIVGEDALS
     YFEKWYRYRD ILKKSTLVVY PRYCGKPYHE HARRVLGDLS EIVFLDMPIV QISSTEIRER
     ARLGKTLKGF VPEEIRKEVE VFYGG