NADD_HELPY
ID NADD_HELPY Reviewed; 174 AA.
AC O25895;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=HP_1337;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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; AE000511; AAD08379.1; -; Genomic_DNA.
DR PIR; A64687; A64687.
DR RefSeq; NP_208129.1; NC_000915.1.
DR RefSeq; WP_001095125.1; NC_018939.1.
DR AlphaFoldDB; O25895; -.
DR SMR; O25895; -.
DR IntAct; O25895; 7.
DR STRING; 85962.C694_06900; -.
DR PaxDb; O25895; -.
DR EnsemblBacteria; AAD08379; AAD08379; HP_1337.
DR KEGG; hpy:HP_1337; -.
DR PATRIC; fig|85962.8.peg.1399; -.
DR eggNOG; COG1057; Bacteria.
DR OMA; AYQNPFK; -.
DR PhylomeDB; O25895; -.
DR UniPathway; UPA00253; UER00332.
DR Proteomes; UP000000429; 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..174
FT /note="Probable nicotinate-nucleotide adenylyltransferase"
FT /id="PRO_0000181415"
SQ SEQUENCE 174 AA; 19829 MW; 8D6DA444AF155B38 CRC64;
MNTMNSVLKY KELALYGGSF DPLHKAHLAI IEQTLELLPS AKLIVLPAYQ NPFKKPCFLD
AQTRFKELER ALKGIDRVLL SDFEIKQERA VPTIESVLHF QKLYHPQTLY LVIGADCLRH
LSSWTNAKEL LKRVELVVFE RIGYEEIQFK GHYHPLKGID APISSSAIRA SLGV
