ID   NADD_BACFR              Reviewed;         201 AA.
AC   Q64PY0;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Probable nicotinate-nucleotide adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00244};
DE            EC=2.7.7.18 {ECO:0000255|HAMAP-Rule:MF_00244};
DE   AltName: Full=Deamido-NAD(+) diphosphorylase {ECO:0000255|HAMAP-Rule:MF_00244};
DE   AltName: Full=Deamido-NAD(+) pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00244};
DE   AltName: Full=Nicotinate mononucleotide adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00244};
DE            Short=NaMN adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00244};
GN   Name=nadD {ECO:0000255|HAMAP-Rule:MF_00244}; OrderedLocusNames=BF3708;
OS   Bacteroides fragilis (strain YCH46).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=295405;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCH46;
RX   PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA   Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA   Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT   "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT   regulating cell surface adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
CC   -!- FUNCTION: Catalyzes the reversible adenylation of nicotinate
CC       mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
CC       {ECO:0000255|HAMAP-Rule:MF_00244}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00244};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+)
CC       from nicotinate D-ribonucleotide: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_00244}.
CC   -!- SIMILARITY: Belongs to the NadD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00244}.
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DR   EMBL; AP006841; BAD50451.1; -; Genomic_DNA.
DR   RefSeq; WP_005797930.1; NC_006347.1.
DR   RefSeq; YP_100985.1; NC_006347.1.
DR   AlphaFoldDB; Q64PY0; -.
DR   SMR; Q64PY0; -.
DR   STRING; 295405.BF3708; -.
DR   EnsemblBacteria; BAD50451; BAD50451; BF3708.
DR   GeneID; 66331657; -.
DR   KEGG; bfr:BF3708; -.
DR   PATRIC; fig|295405.11.peg.3559; -.
DR   HOGENOM; CLU_069765_3_3_10; -.
DR   OMA; IHIGHLI; -.
DR   UniPathway; UPA00253; UER00332.
DR   Proteomes; UP000002197; 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; TIGR00482; TIGR00482; 1.
PE   3: Inferred from homology;
KW   ATP-binding; NAD; Nucleotide-binding; Nucleotidyltransferase;
KW   Pyridine nucleotide biosynthesis; Transferase.
FT   CHAIN           1..201
FT                   /note="Probable nicotinate-nucleotide adenylyltransferase"
FT                   /id="PRO_0000181382"
SQ   SEQUENCE   201 AA;  23442 MW;  EF0F3331BB65739D CRC64;
     MAKTKTGIFS GSFNPIHIGH LALANYLCEF EGLDEVWFMV TPHNPFKNQA DLWPDELRLQ
     LVQLAIEGYP RFRVSDFEFH LPRPSYTIHT LNRLKQEYPE REFQLIIGSD NWMVFDRWFE
     SERIVSENKI LVYPRPGFSV DKSQLPPNVH VADSPIFEIS STFIREALAT GKDIRYFLHP
     AVYKRIIQQT DSIDSSHSCH T