ID NADM_METBF Reviewed; 173 AA. AC Q46FV2; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 16-JUN-2009, entry version 22. DE RecName: Full=Nicotinamide-nucleotide adenylyltransferase; DE EC=2.7.7.1; DE AltName: Full=NAD(+) pyrophosphorylase; DE AltName: Full=NAD(+) diphosphorylase; DE AltName: Full=NMN adenylyltransferase; GN OrderedLocusNames=Mbar_A0256; OS Methanosarcina barkeri (strain Fusaro / DSM 804). OC Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales; OC Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=269797; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16980466; DOI=10.1128/JB.00810-06; RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., RA Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R., RA Sowers K.R.; RT "The Methanosarcina barkeri genome: comparative analysis with RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive RT rearrangement within methanosarcinal genomes."; RL J. Bacteriol. 188:7922-7931(2006). 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; CP000099; AAZ69240.1; -; Genomic_DNA. DR RefSeq; YP_303820.1; -. DR GeneID; 3624869; -. DR GenomeReviews; CP000099_GR; Mbar_A0256. DR KEGG; mba:Mbar_A0256; -. DR NMPDR; fig|269797.3.peg.372; -. DR HOGENOM; Q46FV2; -. DR OMA; Q46FV2; IGRFQPY. DR BioCyc; MBAR269797:MBAR_A0256-MON; -. 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 1 173 Nicotinamide-nucleotide FT adenylyltransferase. FT /FTId=PRO_1000005735. SQ SEQUENCE 173 AA; 19899 MW; 5CEFECD3F06E109C CRC64; MTRAFYIGRF QPYHFGHHTI IKQIAEEVDE LVVGIGSAQK SHESTDPFTA GERVLMVYNA LENLPIRHYV LPIEDIKYNS IWVHHVASRT PHFEVVYSNN PLVIQLFREA GVCVKQSPLY IRERYSGTEI RRRMIAGEKW EHLVPKSVVE VIKEIDGVTR LRNVSASDNN SSL //