ID   NMNA1_BOVIN             Reviewed;         281 AA.
AC   Q0VD50;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
DE   RecName: Full=Nicotinamide mononucleotide adenylyltransferase 1;
DE            Short=NMN adenylyltransferase 1;
DE            EC=2.7.7.1;
DE   AltName: Full=Nicotinate-nucleotide adenylyltransferase 1;
DE            Short=NaMN adenylyltransferase 1;
DE            EC=2.7.7.18;
GN   Name=NMNAT1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of NAD(+) from nicotinamide
CC       mononucleotide (NMN) and ATP. Can also use the deamidated form;
CC       nicotinic acid mononucleotide (NaMN) as substrate with the same
CC       efficiency. Can use triazofurin monophosphate (TrMP) as substrate.
CC       Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic
CC       cleavage of NAD(+). For the pyrophosphorolytic activity, prefers
CC       NAD(+) and NAAD as substrates and degrades NADH, nicotinic acid
CC       adenine dinucleotide phosphate (NHD) and nicotinamide guanine
CC       dinucleotide (NGD) less effectively. Fails to cleave
CC       phosphorylated dinucleotides NADP(+), NADPH and NAADP(+). Protects
CC       against axonal degeneration following mechanical or toxic insults
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + nicotinamide ribonucleotide =
CC       diphosphate + NAD(+).
CC   -!- CATALYTIC ACTIVITY: ATP + nicotinate ribonucleotide = diphosphate
CC       + deamido-NAD(+).
CC   -!- COFACTOR: Divalent metal cations. Zinc confers higher activity
CC       than magnesium (By similarity).
CC   -!- ENZYME REGULATION: Activity is strongly inhibited by galotannin.
CC       Inhibited by P1-(adenosine-5')-P4-(nicotinic-acid-riboside-5')-
CC       tetraphosphate (Nap4AD) (By similarity).
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC       nicotinamide ribonucleotide: step 1/1.
CC   -!- SUBUNIT: Homohexamer. Interacts with ADPRT/PARP1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- PTM: Phosphorylated (By similarity).
CC   -!- SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase
CC       family.
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DR   EMBL; BC119834; AAI19835.1; -; mRNA.
DR   IPI; IPI00691671; -.
DR   RefSeq; NP_001069302.1; -.
DR   UniGene; Bt.59388; -.
DR   SMR; Q0VD50; 5-276.
DR   Ensembl; ENSBTAG00000001361; Bos taurus.
DR   GeneID; 522863; -.
DR   KEGG; bta:522863; -.
DR   HOVERGEN; Q0VD50; -.
DR   BRENDA; 2.7.7.1; 251.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase...; IEA:EC.
DR   GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase a...; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009435; P:NAD biosynthetic process; IEA:InterPro.
DR   InterPro; IPR004820; Cytidylyltransf.
DR   InterPro; IPR005248; NAMN_adtrnsfrase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   PANTHER; PTHR12039; NAMN_adtrnsfrase; 1.
DR   Pfam; PF01467; CTP_transf_2; 1.
DR   TIGRFAMs; TIGR00482; NAMN_adtrnsfrase; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Magnesium; NAD; Nucleotide-binding;
KW   Nucleotidyltransferase; Nucleus; Phosphoprotein;
KW   Pyridine nucleotide biosynthesis; Transferase; Zinc.
FT   CHAIN         1    281       Nicotinamide mononucleotide
FT                                adenylyltransferase 1.
FT                                /FTId=PRO_0000262882.
FT   NP_BIND      15     24       ATP (Potential).
FT   NP_BIND     224    229       ATP (Potential).
FT   MOTIF       123    129       Nuclear localization signal (Potential).
FT   BINDING      16     16       Substrate (By similarity).
FT   BINDING      55     55       Substrate (By similarity).
FT   BINDING     160    160       Substrate (By similarity).
SQ   SEQUENCE   281 AA;  32200 MW;  ECAF9116729138FA CRC64;
     MENSEKTEVV LLACGSFNPI TNMHLRLFEL AKDYMNGTGK YKVIKGIISP VGDAYKKKGL
     ISAYHRVIMA ELATKNSKWV EVDTWESLQK EWTETAKVLR HHQEKLEASI CDPQQNSPVL
     EKPGRKRKWA EQKQDISEKK SLEQTKTKGV PKVKLLCGAD FLESFGVPNL WKSEDITKIL
     GDYGLICITR AGNDAQKFIY ESDVLWKHQN NIHLVNEWIT NDISSTKIRR ALRRGQSIRY
     LVPDLVEEYI EKHNLYSSES EERNVGVVLA PLQRNTTEVK A
//