ID   NADM_PICTO              Reviewed;         169 AA.
AC   Q6L2T8;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Nicotinamide-nucleotide adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00243};
DE            EC=2.7.7.1 {ECO:0000255|HAMAP-Rule:MF_00243};
DE   AltName: Full=NAD(+) diphosphorylase {ECO:0000255|HAMAP-Rule:MF_00243};
DE   AltName: Full=NAD(+) pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00243};
DE   AltName: Full=NMN adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00243};
GN   OrderedLocusNames=PTO0129;
OS   Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS   100828).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Picrophilaceae; Picrophilus.
OX   NCBI_TaxID=263820;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX   PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA   Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RT   "Genome sequence of Picrophilus torridus and its implications for life
RT   around pH 0.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate
CC         + NAD(+); Xref=Rhea:RHEA:21360, ChEBI:CHEBI:14649, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540; EC=2.7.7.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00243};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC       nicotinamide D-ribonucleotide: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_00243}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00243}.
CC   -!- SIMILARITY: Belongs to the archaeal NMN adenylyltransferase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00243}.
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DR   EMBL; AE017261; AAT42714.1; -; Genomic_DNA.
DR   RefSeq; WP_011176930.1; NC_005877.1.
DR   AlphaFoldDB; Q6L2T8; -.
DR   SMR; Q6L2T8; -.
DR   STRING; 263820.PTO0129; -.
DR   EnsemblBacteria; AAT42714; AAT42714; PTO0129.
DR   GeneID; 2845340; -.
DR   KEGG; pto:PTO0129; -.
DR   PATRIC; fig|263820.9.peg.142; -.
DR   eggNOG; arCOG00972; Archaea.
DR   HOGENOM; CLU_108783_0_0_2; -.
DR   OMA; NSVWVSH; -.
DR   OrthoDB; 90722at2157; -.
DR   UniPathway; UPA00253; UER00600.
DR   Proteomes; UP000000438; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02166; NMNAT_Archaea; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00243; NMN_adenylyltr; 1.
DR   InterPro; IPR004821; Cyt_trans-like.
DR   InterPro; IPR006418; NMN_Atrans_arc.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF01467; CTP_transf_like; 1.
DR   TIGRFAMs; TIGR01527; arch_NMN_Atrans; 1.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; NAD; Nucleotide-binding; Nucleotidyltransferase;
KW   Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..169
FT                   /note="Nicotinamide-nucleotide adenylyltransferase"
FT                   /id="PRO_0000134997"
SQ   SEQUENCE   169 AA;  19459 MW;  8232A539D5690055 CRC64;
     MRAFIVGRFQ PFHNGHMEIL KRILHENDSV IIGIGSAQFS HTLKDPFTAG ERHLMISSAL
     EESGVYNYYL VPIEDVNSNP LWVSHVESLT PPFQRVYTNN PLVKRLFYEK GYEVLSMDLL
     NRKEWSGTSI RNKMIRGENW KKDVPPAVAR VIDEIDGVSR IRDLSESDE