NADD_ECO57
ID NADD_ECO57 Reviewed; 213 AA.
AC Q8XBP0;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=Z0786, ECs0677;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG54973.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34100.1; -; Genomic_DNA.
DR PIR; A85564; A85564.
DR PIR; E90713; E90713.
DR RefSeq; NP_308704.1; NC_002695.1.
DR RefSeq; WP_000838887.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8XBP0; -.
DR SMR; Q8XBP0; -.
DR STRING; 155864.EDL933_0713; -.
DR EnsemblBacteria; AAG54973; AAG54973; Z0786.
DR EnsemblBacteria; BAB34100; BAB34100; ECs_0677.
DR GeneID; 917038; -.
DR KEGG; ece:Z0786; -.
DR KEGG; ecs:ECs_0677; -.
DR PATRIC; fig|386585.9.peg.789; -.
DR eggNOG; COG1057; Bacteria.
DR HOGENOM; CLU_069765_0_0_6; -.
DR OMA; IHIGHLI; -.
DR UniPathway; UPA00253; UER00332.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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..213
FT /note="Nicotinate-nucleotide adenylyltransferase"
FT /id="PRO_0000181408"
SQ SEQUENCE 213 AA; 24514 MW; EA2C6689F2400CF5 CRC64;
MKSLQALFGG TFDPVHYGHL KPVETLANLI GLTRVTIIPN NVPPHRPQPE ANSVQRKHML
ELAIADKPLF TLDERELKRN APSYTAQTLK EWRQEQGPDV PLAFIIGQDS LLTFPTWYEY
ETILDNAHLI VCRRPGYPLE MAQPQYQQWL EDHLTHNPED LHLQPAGKIY LAETPWFNIS
ATIIRERLQN GESCDDLLPE PVLTYINQQG LYR