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   16-JUN-2009, entry version 26.
DE   RecName: Full=Nicotinamide-nucleotide adenylyltransferase 2;
DE            EC=2.7.7.1;
DE   AltName: Full=NAD(+) pyrophosphorylase 2;
DE   AltName: Full=NAD(+) diphosphorylase 2;
DE   AltName: Full=NMN adenylyltransferase 2;
GN   OrderedLocusNames=Saci_0720;
OS   Sulfolobus acidocaldarius.
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=2285;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / IFO 15157 / JCM 8929 / NCIB 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: ATP + nicotinamide ribonucleotide =
CC       diphosphate + NAD(+).
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC       nicotinamide ribonucleotide: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the archaeal NMN adenylyltransferase
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000077; AAY80099.1; -; Genomic_DNA.
DR   RefSeq; YP_255392.1; -.
DR   GeneID; 3472566; -.
DR   GenomeReviews; CP000077_GR; Saci_0720.
DR   KEGG; sai:Saci_0720; -.
DR   NMPDR; fig|330779.3.peg.70; -.
DR   HOGENOM; Q4JAT0; -.
DR   OMA; Q4JAT0; IGRFQPY.
DR   BioCyc; SACI330779:SACI_0720-MON; -.
DR   BRENDA; 2.7.7.1; 434.
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...; IEA:HAMAP.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00243; -; 1.
DR   InterPro; IPR004821; Cyt_trans_rel.
DR   InterPro; IPR004820; Cytidylyltransf.
DR   InterPro; IPR006418; NMN_Atrans_arc.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   Pfam; PF01467; CTP_transf_2; 1.
DR   TIGRFAMs; TIGR01527; arch_NMN_Atrans; 1.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; NAD; Nucleotide-binding;
KW   Nucleotidyltransferase; Pyridine nucleotide biosynthesis; Transferase.
FT   CHAIN         1    171       Nicotinamide-nucleotide
FT                                adenylyltransferase 2.
FT                                /FTId=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
//