ID   NADD_ECOL6              Reviewed;         213 AA.
AC   Q8FJZ1;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-AUG-2003, sequence version 2.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=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=c0730;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN79203.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN79203.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000838881.1; NC_004431.1.
DR   AlphaFoldDB; Q8FJZ1; -.
DR   SMR; Q8FJZ1; -.
DR   STRING; 199310.c0730; -.
DR   EnsemblBacteria; AAN79203; AAN79203; c0730.
DR   KEGG; ecc:c0730; -.
DR   eggNOG; COG1057; Bacteria.
DR   HOGENOM; CLU_069765_0_0_6; -.
DR   OMA; IHIGHLI; -.
DR   UniPathway; UPA00253; UER00332.
DR   Proteomes; UP000001410; 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; Transferase.
FT   CHAIN           1..213
FT                   /note="Nicotinate-nucleotide adenylyltransferase"
FT                   /id="PRO_0000181409"
SQ   SEQUENCE   213 AA;  24560 MW;  74DEE403D25518AB CRC64;
     MKSLQALFGG TFDPVHYGHL KPVETLANLI GLTRVTIIPN NVPPHRPQPE ANSMQRKHML
     ELAIADKPLF TLDERELKRN APSYTAQTLK EWRQEQGPDV PLAFIIGQDS LLTFPTWYEY
     ETILDNAHLI VCRRPGYPLE MAQPQYQQWL EDHLTHNPED LHLQPAGKIY LAETPWFNIS
     ATIIRERLQN GESCEDLLPE PVLTYINQQG LYR