ID   NADM_METMA              Reviewed;         173 AA.
AC   Q8PZ68;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   25-MAY-2022, entry version 114.
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=MM_0626;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM30322.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; AE008384; AAM30322.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_015411232.1; NC_003901.1.
DR   AlphaFoldDB; Q8PZ68; -.
DR   SMR; Q8PZ68; -.
DR   STRING; 192952.MM_0626; -.
DR   EnsemblBacteria; AAM30322; AAM30322; MM_0626.
DR   GeneID; 44086161; -.
DR   GeneID; 66134210; -.
DR   KEGG; mma:MM_0626; -.
DR   PATRIC; fig|192952.21.peg.738; -.
DR   eggNOG; arCOG00972; Archaea.
DR   HOGENOM; CLU_108783_0_0_2; -.
DR   OMA; NSVWVSH; -.
DR   UniPathway; UPA00253; UER00600.
DR   Proteomes; UP000000595; 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..173
FT                   /note="Nicotinamide-nucleotide adenylyltransferase"
FT                   /id="PRO_0000134993"
SQ   SEQUENCE   173 AA;  19970 MW;  D8D7EE0C6640B3D8 CRC64;
     MTRAFYIGRF QPYHFGHHAV IARIAEEVDE LVIGIGSAQK SHEAIDPFTA GERVLMVYNA
     LEHLSIRHYV VPIEDVRYNS IWVHHVVSRT PRFDVVYSNN PLVIQLFREA GFCVKESPLY
     VRERYSGTEI RRRMIEGEKW EHLVPKPVAE VIKSFDGVSR LKNVSTSDSN FSL