ID   NADM2_SULAC             Reviewed;         171 AA.
AC   Q4JAT0;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Nicotinamide-nucleotide adenylyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00243};
DE            EC=2.7.7.1 {ECO:0000255|HAMAP-Rule:MF_00243};
DE   AltName: Full=NAD(+) diphosphorylase 2 {ECO:0000255|HAMAP-Rule:MF_00243};
DE   AltName: Full=NAD(+) pyrophosphorylase 2 {ECO:0000255|HAMAP-Rule:MF_00243};
DE   AltName: Full=NMN adenylyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00243};
GN   OrderedLocusNames=Saci_0720;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
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; CP000077; AAY80099.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4JAT0; -.
DR   SMR; Q4JAT0; -.
DR   STRING; 330779.Saci_0720; -.
DR   EnsemblBacteria; AAY80099; AAY80099; Saci_0720.
DR   KEGG; sai:Saci_0720; -.
DR   PATRIC; fig|330779.12.peg.687; -.
DR   eggNOG; arCOG00972; Archaea.
DR   HOGENOM; CLU_108783_0_0_2; -.
DR   OMA; NSVWVSH; -.
DR   UniPathway; UPA00253; UER00600.
DR   Proteomes; UP000001018; 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..171
FT                   /note="Nicotinamide-nucleotide adenylyltransferase 2"
FT                   /id="PRO_0000135004"
SQ   SEQUENCE   171 AA;  19935 MW;  399149E197E76C4E CRC64;
     MHRGLYPGRF QPFHIGHLEV VKWSMKHVDE LIIVIGSAQE SHTLSNPFTA GERIEMIRRT
     LDKENLDLSK VYIIPIPDIM MNSVWVSHIK TFAPNFDVII SRNPLVNRLF KEANVEVLQP
     PPFDRHKYNS TLIRRYIIEG NEEWKKLVPK SVLDYLLEIH GDERLRSIAG L