ID   NADD_STAAC              Reviewed;         189 AA.
AC   Q5HFG7;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 100.
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=SACOL1650;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA   Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA   Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA   Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA   Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA   Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete genome
RT   analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT   a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT   strain.";
RL   J. Bacteriol. 187:2426-2438(2005).
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; CP000046; AAW38266.1; -; Genomic_DNA.
DR   RefSeq; WP_000725162.1; NC_002951.2.
DR   PDB; 2H29; X-ray; 2.00 A; A/B=1-189.
DR   PDB; 2H2A; X-ray; 2.10 A; A/B=1-189.
DR   PDBsum; 2H29; -.
DR   PDBsum; 2H2A; -.
DR   AlphaFoldDB; Q5HFG7; -.
DR   SMR; Q5HFG7; -.
DR   EnsemblBacteria; AAW38266; AAW38266; SACOL1650.
DR   KEGG; sac:SACOL1650; -.
DR   HOGENOM; CLU_069765_3_1_9; -.
DR   OMA; IHIGHLI; -.
DR   BRENDA; 2.7.7.18; 3352.
DR   UniPathway; UPA00253; UER00332.
DR   EvolutionaryTrace; Q5HFG7; -.
DR   Proteomes; UP000000530; 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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; NAD; Nucleotide-binding; Nucleotidyltransferase;
KW   Pyridine nucleotide biosynthesis; Transferase.
FT   CHAIN           1..189
FT                   /note="Probable nicotinate-nucleotide adenylyltransferase"
FT                   /id="PRO_0000181443"
FT   STRAND          2..9
FT                   /evidence="ECO:0007829|PDB:2H29"
FT   HELIX           16..29
FT                   /evidence="ECO:0007829|PDB:2H29"
FT   STRAND          32..38
FT                   /evidence="ECO:0007829|PDB:2H29"
FT   HELIX           54..67
FT                   /evidence="ECO:0007829|PDB:2H29"
FT   HELIX           75..79
FT                   /evidence="ECO:0007829|PDB:2H29"
FT   HELIX           85..95
FT                   /evidence="ECO:0007829|PDB:2H29"
FT   STRAND          99..106
FT                   /evidence="ECO:0007829|PDB:2H29"
FT   HELIX           107..110
FT                   /evidence="ECO:0007829|PDB:2H29"
FT   HELIX           111..115
FT                   /evidence="ECO:0007829|PDB:2H29"
FT   HELIX           119..125
FT                   /evidence="ECO:0007829|PDB:2H29"
FT   STRAND          127..131
FT                   /evidence="ECO:0007829|PDB:2H29"
FT   STRAND          134..136
FT                   /evidence="ECO:0007829|PDB:2H29"
FT   STRAND          144..147
FT                   /evidence="ECO:0007829|PDB:2H29"
FT   HELIX           156..164
FT                   /evidence="ECO:0007829|PDB:2H29"
FT   HELIX           175..184
FT                   /evidence="ECO:0007829|PDB:2H29"
FT   TURN            185..187
FT                   /evidence="ECO:0007829|PDB:2H29"
SQ   SEQUENCE   189 AA;  22127 MW;  084E8721EB3EC11E CRC64;
     MKKIVLYGGQ FNPIHTAHMI VASEVFHELQ PDEFYFLPSF MSPLKKHHDF IDVQHRLTMI
     QMIIDELGFG DICDDEIKRG GQSYTYDTIK AFKEQHKDSE LYFVIGTDQY NQLEKWYQIE
     YLKEMVTFVV VNRDKNSQNV ENAMIAIQIP RVDISSTMIR QRVSEGKSIQ VLVPKSVENY
     IKGEGLYEH