ID   NADM_METTI              Reviewed;         173 AA.
AC   Q9UXN8;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Nicotinamide-nucleotide adenylyltransferase;
DE            EC=2.7.7.1;
DE   AltName: Full=NAD(+) diphosphorylase;
DE   AltName: Full=NAD(+) pyrophosphorylase;
DE   AltName: Full=NMN adenylyltransferase;
GN   Name=ffdC;
OS   Methanolobus tindarius.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanolobus.
OX   NCBI_TaxID=2221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35996 / DSM 2278 / OCM 150 / Tindari 3;
RX   PubMed=9933933; DOI=10.1111/j.1574-6968.1999.tb13399.x;
RA   Westenberg D.J., Braune A., Ruppert C., Mueller V., Herzberg C.,
RA   Gottschalk G., Blaut M.;
RT   "The F420H2-dehydrogenase from Methanolobus tindarius: cloning of the ffd
RT   operon and expression of the genes in Escherichia coli.";
RL   FEMS Microbiol. Lett. 170:389-398(1999).
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   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC       nicotinamide D-ribonucleotide: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the archaeal NMN adenylyltransferase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB56641.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ011519; CAB56641.1; ALT_INIT; Genomic_DNA.
DR   PIR; T45228; T45228.
DR   AlphaFoldDB; Q9UXN8; -.
DR   SMR; Q9UXN8; -.
DR   UniPathway; UPA00253; UER00600.
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; Transferase.
FT   CHAIN           1..173
FT                   /note="Nicotinamide-nucleotide adenylyltransferase"
FT                   /id="PRO_0000134996"
SQ   SEQUENCE   173 AA;  19738 MW;  C9471E6B3A432A5F CRC64;
     MRRAFYIGRF QPFHLGHYSL IKDIARDADE VVIGIGSAQK SHEPKNPFTA GERVMMIKHA
     LEDAGIKHYA IPLEDLQRNA VWVSHIISMT PPFDVVYSNN PLVVRLFQES GILVEQPPMY
     QREGYSGSEI RKRMLRGEDW KSLVPAAVID VIDEIDGVNR LKSVSKSDKD YRD