ID   NADM_METB6              Reviewed;         168 AA.
AC   A7I937;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=Mboo_1731;
OS   Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX   NCBI_TaxID=456442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21154 / JCM 14090 / 6A8;
RX   PubMed=25998264; DOI=10.1099/mic.0.000117;
RA   Braeuer S., Cadillo-Quiroz H., Kyrpides N., Woyke T., Goodwin L.,
RA   Detter C., Podell S., Yavitt J.B., Zinder S.H.;
RT   "Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic
RT   peatland environments.";
RL   Microbiology 161:1572-1581(2015).
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; CP000780; ABS56248.1; -; Genomic_DNA.
DR   RefSeq; WP_012107296.1; NC_009712.1.
DR   AlphaFoldDB; A7I937; -.
DR   SMR; A7I937; -.
DR   STRING; 456442.Mboo_1731; -.
DR   EnsemblBacteria; ABS56248; ABS56248; Mboo_1731.
DR   GeneID; 5411963; -.
DR   KEGG; mbn:Mboo_1731; -.
DR   eggNOG; arCOG00972; Archaea.
DR   HOGENOM; CLU_108783_0_0_2; -.
DR   OMA; NSVWVSH; -.
DR   OrthoDB; 90722at2157; -.
DR   UniPathway; UPA00253; UER00600.
DR   Proteomes; UP000002408; 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..168
FT                   /note="Nicotinamide-nucleotide adenylyltransferase"
FT                   /id="PRO_1000005734"
SQ   SEQUENCE   168 AA;  19069 MW;  2863B39988AD3B34 CRC64;
     MKRGFYVGRF QPYHNGHQAV LSELARTCDE IILGVGSAQL SHTLENPFTA GERVLMITRA
     LTDLRCPYYV IPIEDVQRNA LWAAHVRSMT PPFDTCYSSN PLVVRLFFEA GVDVQSPAMY
     ERDRHSGTEI RRRMLAGEPW ENLVPPAVVT VVREIDGVER LREIARAD