NADD_BACFN
ID NADD_BACFN Reviewed; 201 AA.
AC Q5L9N8;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=BF3501;
OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS / NCTC 9343 / Onslow).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=272559;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow;
RX PubMed=15746427; DOI=10.1126/science.1107008;
RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA Barrell B.G., Parkhill J.;
RT "Extensive DNA inversions in the B. fragilis genome control variable gene
RT expression.";
RL Science 307:1463-1465(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; CR626927; CAH09189.1; -; Genomic_DNA.
DR RefSeq; WP_005797930.1; NC_003228.3.
DR AlphaFoldDB; Q5L9N8; -.
DR SMR; Q5L9N8; -.
DR STRING; 272559.BF9343_3408; -.
DR EnsemblBacteria; CAH09189; CAH09189; BF9343_3408.
DR GeneID; 66331657; -.
DR KEGG; bfs:BF9343_3408; -.
DR eggNOG; COG1057; Bacteria.
DR HOGENOM; CLU_069765_3_3_10; -.
DR OMA; IHIGHLI; -.
DR OrthoDB; 1433958at2; -.
DR UniPathway; UPA00253; UER00332.
DR Proteomes; UP000006731; 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; Reference proteome; Transferase.
FT CHAIN 1..201
FT /note="Probable nicotinate-nucleotide adenylyltransferase"
FT /id="PRO_0000181381"
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