ID   NMNA2_RAT               Reviewed;         307 AA.
AC   Q0HA29;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Nicotinamide mononucleotide adenylyltransferase 2;
DE            Short=NMN adenylyltransferase 2;
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=Nmnat2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Xing J., Cao G., Zhang L., Chen J.;
RT   "Nicotinamide nucleotide adenylyltransferase is neuroprotective
RT   against ischemic injury.";
RL   Submitted (APR-2005) 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 but with a lower
CC       efficiency. Cannnot use triazofurin monophosphate (TrMP) as
CC       substrate. Also catalyzes the reverse reaction, i.e. the
CC       pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic
CC       activity prefers NAD(+), NADH and NAAD as substrates and degrades
CC       nicotinic acid adenine dinucleotide phosphate (NHD) less
CC       effectively. Fails to cleave phosphorylated dinucleotides NADP(+),
CC       NADPH and NAADP(+) (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. Magnesium confers the highest
CC       activity (By similarity).
CC   -!- ENZYME REGULATION: Inhibited by P1-(adenosine-5')-P3-
CC       (nicotinamide-riboside-5')-triphosphate (Np3AD) and P1-(adenosine-
CC       5')-P4-(nicotinamide-riboside-5')-tetraphosphate (Np4AD) (By
CC       similarity).
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC       nicotinamide ribonucleotide: step 1/1.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Golgi apparatus
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase
CC       family.
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DR   EMBL; DQ022370; AAY87457.1; -; mRNA.
DR   IPI; IPI00371496; -.
DR   RefSeq; NP_001041507.1; -.
DR   UniGene; Rn.145458; -.
DR   Ensembl; ENSRNOG00000027697; Rattus norvegicus.
DR   GeneID; 289095; -.
DR   KEGG; rno:289095; -.
DR   RGD; 1307331; Nmnat2.
DR   HOVERGEN; Q0HA29; -.
DR   BRENDA; 2.7.7.1; 248.
DR   NextBio; 629238; -.
DR   ArrayExpress; Q0HA29; -.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP 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: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; Cytoplasm; Golgi apparatus; NAD; Nucleotide-binding;
KW   Nucleotidyltransferase; Pyridine nucleotide biosynthesis; Transferase.
FT   CHAIN         1    307       Nicotinamide mononucleotide
FT                                adenylyltransferase 2.
FT                                /FTId=PRO_0000328662.
FT   NP_BIND      15     24       ATP (Potential).
FT   NP_BIND     269    274       ATP (Potential).
FT   BINDING      16     16       Substrate (By similarity).
FT   BINDING      55     55       Substrate (By similarity).
FT   BINDING     202    202       Substrate (By similarity).
SQ   SEQUENCE   307 AA;  34445 MW;  EDE5DAB7B03AE1AA CRC64;
     MTETTKTHVI LLACGSFNPI TKGHIQMFER ARDYLHKTGR FIVIGGIVSP VHDSYGKQGL
     VSSRHRLIMC QLAVQNSDWI RVDPWECYQD TWQTTCSVLE HHRDLMKRVT GCILSNVNTP
     SMTPVIGQPQ HENTQPIYQN SNVPTKPTAA KILGKVGESL GRICCVRPPV ERFTFVDENA
     NLGTVMRYEE IELRILLLCG SDLLESFCIP GLWNEADMEV IVGDFGIVVV PRDAADADRI
     MNHSSILRKY KNNIMVVKDD INHPMSVVSS TKSRLALQHG DGHVVDYLSQ PVIDYILKSQ
     LYINASG
//