ID   NADD_BORAP              Reviewed;         193 AA.
AC   Q0SM71; G0IRW3;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 96.
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};
GN   OrderedLocusNames=BAPKO_0832, BafPKo_0808;
OS   Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J.,
RA   Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo;
RX   PubMed=22123755; DOI=10.1128/jb.05951-11;
RA   Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J.,
RA   Fraser-Liggett C.M., Schutzer S.E.;
RT   "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT   Lyme disease agent isolates.";
RL   J. Bacteriol. 193:6995-6996(2011).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000395; ABH02057.1; -; Genomic_DNA.
DR   EMBL; CP002933; AEL69998.1; -; Genomic_DNA.
DR   RefSeq; WP_004789866.1; NC_017238.1.
DR   AlphaFoldDB; Q0SM71; -.
DR   SMR; Q0SM71; -.
DR   STRING; 390236.BafPKo_0808; -.
DR   EnsemblBacteria; AEL69998; AEL69998; BafPKo_0808.
DR   KEGG; baf:BAPKO_0832; -.
DR   KEGG; bafz:BafPKo_0808; -.
DR   PATRIC; fig|390236.22.peg.771; -.
DR   eggNOG; COG1057; Bacteria.
DR   HOGENOM; CLU_069765_1_0_12; -.
DR   OMA; IHIGHLI; -.
DR   OrthoDB; 1433958at2; -.
DR   UniPathway; UPA00253; UER00332.
DR   Proteomes; UP000005216; 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..193
FT                   /note="Probable nicotinate-nucleotide adenylyltransferase"
FT                   /id="PRO_0000310100"
SQ   SEQUENCE   193 AA;  22078 MW;  DB0D9498A55BC151 CRC64;
     MRIAILGGTY NPVHIGHIFL AKEIEYLLNI DKIIFIPTCN PTHKLIGEGV SVKNRIDMLK
     LALKNENKMF IDDCDIINGG ITYTIDTISC VKKKYKNDKL FLVIGDDLFQ NFDSWKDPQS
     IASSVDLVVA HRIYKERLKS SFKHIYIDNK IIPISSSEIR NRIANGFPVS YLLPFGVLKY
     IKDNNLYVKK VNV