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Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 (NMN/NaMN adenylyltransferase 1) (EC 2.7.7.1) (EC 2.7.7.18) (Nicotinamide mononucleotide adenylyltransferase 1) (NMN adenylyltransferase 1) (Nicotinate-nucleotide adenylyltransferase 1) (NaMN adenylyltransferase 1)

 NMNA1_BOVIN             Reviewed;         281 AA.
Q0VD50;
28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
05-SEP-2006, sequence version 1.
07-JUN-2017, entry version 82.
RecName: Full=Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 {ECO:0000305};
Short=NMN/NaMN adenylyltransferase 1;
EC=2.7.7.1;
EC=2.7.7.18;
AltName: Full=Nicotinamide mononucleotide adenylyltransferase 1;
Short=NMN adenylyltransferase 1;
AltName: Full=Nicotinate-nucleotide adenylyltransferase 1;
Short=NaMN adenylyltransferase 1;
Name=NMNAT1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Ascending colon;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the formation of NAD(+) from nicotinamide
mononucleotide (NMN) and ATP. Can also use the deamidated form;
nicotinic acid mononucleotide (NaMN) as substrate with the same
efficiency. Can use triazofurin monophosphate (TrMP) as substrate.
Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic
cleavage of NAD(+). For the pyrophosphorolytic activity, prefers
NAD(+) and NaAD as substrates and degrades NADH, nicotinic acid
adenine dinucleotide phosphate (NHD) and nicotinamide guanine
dinucleotide (NGD) less effectively. Involved in the synthesis of
ATP in the nucleus, together with PARP1, PARG and NUDT5. Nuclear
ATP generation is required for extensive chromatin remodeling
events that are energy-consuming. Fails to cleave phosphorylated
dinucleotides NADP(+), NADPH and NaADP(+) (By similarity).
Protects against axonal degeneration following mechanical or toxic
insults (By similarity). {ECO:0000250|UniProtKB:Q9EPA7,
ECO:0000250|UniProtKB:Q9HAN9}.
-!- CATALYTIC ACTIVITY: ATP + nicotinamide ribonucleotide =
diphosphate + NAD(+).
-!- CATALYTIC ACTIVITY: ATP + beta-nicotinate-D-ribonucleotide =
diphosphate + deamido-NAD(+).
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:Q9HAN9};
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q9HAN9};
Note=Divalent metal cations. Zn(2+) confers higher activity as
compared to Mg(2+). {ECO:0000250|UniProtKB:Q9HAN9};
-!- ENZYME REGULATION: Activity is strongly inhibited by galotannin.
Inhibited by P1-(adenosine-5')-P4-(nicotinic-acid-riboside-5')-
tetraphosphate (Nap4AD). {ECO:0000250|UniProtKB:Q9HAN9}.
-!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
nicotinamide D-ribonucleotide: step 1/1.
-!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-
NAD(+) from nicotinate D-ribonucleotide: step 1/1.
-!- SUBUNIT: Homohexamer. Interacts with ADPRT/PARP1.
{ECO:0000250|UniProtKB:Q9HAN9}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9HAN9}.
-!- SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase
family. {ECO:0000305}.
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EMBL; BC119834; AAI19835.1; -; mRNA.
RefSeq; NP_001069302.1; NM_001075834.1.
UniGene; Bt.59388; -.
ProteinModelPortal; Q0VD50; -.
SMR; Q0VD50; -.
STRING; 9913.ENSBTAP00000048652; -.
PaxDb; Q0VD50; -.
PRIDE; Q0VD50; -.
Ensembl; ENSBTAT00000056287; ENSBTAP00000048652; ENSBTAG00000001361.
GeneID; 522863; -.
KEGG; bta:522863; -.
CTD; 64802; -.
eggNOG; KOG3199; Eukaryota.
eggNOG; COG1057; LUCA.
GeneTree; ENSGT00530000063189; -.
HOGENOM; HOG000216047; -.
HOVERGEN; HBG052640; -.
InParanoid; Q0VD50; -.
KO; K06210; -.
OMA; DHFDHEI; -.
OrthoDB; EOG091G0JTI; -.
TreeFam; TF315035; -.
Reactome; R-BTA-196807; Nicotinate metabolism.
UniPathway; UPA00253; UER00332.
UniPathway; UPA00253; UER00600.
Proteomes; UP000009136; Chromosome 16.
Bgee; ENSBTAG00000001361; -.
GO; GO:0016604; C:nuclear body; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IBA:GO_Central.
GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IBA:GO_Central.
GO; GO:0034628; P:'de novo' NAD biosynthetic process from aspartate; IBA:GO_Central.
GO; GO:1990966; P:ATP generation from poly-ADP-D-ribose; ISS:UniProtKB.
GO; GO:0009611; P:response to wounding; IEA:Ensembl.
Gene3D; 3.40.50.620; -; 1.
InterPro; IPR004821; Cyt_trans-like.
InterPro; IPR005248; NadD/NMNAT.
InterPro; IPR014729; Rossmann-like_a/b/a_fold.
Pfam; PF01467; CTP_transf_like; 1.
TIGRFAMs; TIGR00482; TIGR00482; 1.
2: Evidence at transcript level;
ATP-binding; Complete proteome; Magnesium; NAD; Nucleotide-binding;
Nucleotidyltransferase; Nucleus; Phosphoprotein;
Pyridine nucleotide biosynthesis; Reference proteome; Transferase;
Zinc.
CHAIN 1 281 Nicotinamide/nicotinic acid
mononucleotide adenylyltransferase 1.
/FTId=PRO_0000262882.
NP_BIND 15 17 ATP. {ECO:0000250|UniProtKB:Q96T66,
ECO:0000250|UniProtKB:Q9HAN9}.
NP_BIND 158 160 ATP. {ECO:0000250|UniProtKB:Q96T66}.
NP_BIND 226 229 ATP. {ECO:0000250|UniProtKB:Q96T66}.
REGION 55 57 Substrate binding.
{ECO:0000250|UniProtKB:Q9HAN9}.
REGION 92 95 Substrate binding.
{ECO:0000250|UniProtKB:Q9HAN9}.
REGION 170 171 Substrate binding.
{ECO:0000250|UniProtKB:Q9HAN9}.
MOTIF 123 129 Nuclear localization signal.
{ECO:0000255}.
BINDING 24 24 ATP. {ECO:0000250|UniProtKB:Q96T66}.
BINDING 58 58 ATP. {ECO:0000250|UniProtKB:Q96T66}.
MOD_RES 117 117 Phosphoserine.
{ECO:0000250|UniProtKB:Q9HAN9}.
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


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