NMNA1_BOVIN
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 03-AUG-2022, entry version 103.
DE RecName: Full=Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1 {ECO:0000305};
DE Short=NMN/NaMN adenylyltransferase 1;
DE EC=2.7.7.1 {ECO:0000250|UniProtKB:Q9HAN9};
DE EC=2.7.7.18 {ECO:0000250|UniProtKB:Q9HAN9};
DE AltName: Full=Nicotinamide mononucleotide adenylyltransferase 1;
DE Short=NMN adenylyltransferase 1;
DE AltName: Full=Nicotinate-nucleotide adenylyltransferase 1;
DE Short=NaMN adenylyltransferase 1;
GN Name=NMNAT1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC 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. Also
CC catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of
CC NAD(+). For the pyrophosphorolytic activity, prefers NAD(+) and NaAD as
CC substrates and degrades NADH, nicotinic acid adenine dinucleotide
CC phosphate (NHD) and nicotinamide guanine dinucleotide (NGD) less
CC effectively. Involved in the synthesis of ATP in the nucleus, together
CC with PARP1, PARG and NUDT5. Nuclear ATP generation is required for
CC extensive chromatin remodeling events that are energy-consuming. Fails
CC to cleave phosphorylated dinucleotides NADP(+), NADPH and NaADP(+) (By
CC similarity). Protects against axonal degeneration following mechanical
CC or toxic insults (By similarity). {ECO:0000250|UniProtKB:Q9EPA7,
CC ECO:0000250|UniProtKB:Q9HAN9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate
CC + NAD(+); Xref=Rhea:RHEA:21360, ChEBI:CHEBI:14649, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540; EC=2.7.7.1;
CC Evidence={ECO:0000250|UniProtKB:Q9HAN9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21361;
CC Evidence={ECO:0000250|UniProtKB:Q9HAN9};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21362;
CC Evidence={ECO:0000250|UniProtKB:Q9HAN9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+)
CC + diphosphate; Xref=Rhea:RHEA:22860, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57502,
CC ChEBI:CHEBI:58437; EC=2.7.7.18;
CC Evidence={ECO:0000250|UniProtKB:Q9HAN9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22861;
CC Evidence={ECO:0000250|UniProtKB:Q9HAN9};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22862;
CC Evidence={ECO:0000250|UniProtKB:Q9HAN9};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9HAN9};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9HAN9};
CC Note=Divalent metal cations. Zn(2+) confers higher activity as compared
CC to Mg(2+). {ECO:0000250|UniProtKB:Q9HAN9};
CC -!- ACTIVITY REGULATION: Activity is strongly inhibited by galotannin.
CC Inhibited by P1-(adenosine-5')-P4-(nicotinic-acid-riboside-5')-
CC tetraphosphate (Nap4AD). {ECO:0000250|UniProtKB:Q9HAN9}.
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC nicotinamide D-ribonucleotide: step 1/1.
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+)
CC from nicotinate D-ribonucleotide: step 1/1.
CC -!- SUBUNIT: Homohexamer. Interacts with ADPRT/PARP1.
CC {ECO:0000250|UniProtKB:Q9HAN9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9HAN9}.
CC -!- SIMILARITY: Belongs to the eukaryotic NMN adenylyltransferase family.
CC {ECO:0000305}.
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DR EMBL; BC119834; AAI19835.1; -; mRNA.
DR RefSeq; NP_001069302.1; NM_001075834.1.
DR AlphaFoldDB; Q0VD50; -.
DR SMR; Q0VD50; -.
DR STRING; 9913.ENSBTAP00000048652; -.
DR PaxDb; Q0VD50; -.
DR PRIDE; Q0VD50; -.
DR Ensembl; ENSBTAT00000082151; ENSBTAP00000059876; ENSBTAG00000051897.
DR GeneID; 522863; -.
DR KEGG; bta:522863; -.
DR CTD; 64802; -.
DR VEuPathDB; HostDB:ENSBTAG00000051897; -.
DR VGNC; VGNC:32132; NMNAT1.
DR eggNOG; KOG3199; Eukaryota.
DR GeneTree; ENSGT00950000183179; -.
DR HOGENOM; CLU_033366_3_0_1; -.
DR InParanoid; Q0VD50; -.
DR OMA; QPWKENI; -.
DR OrthoDB; 1308027at2759; -.
DR TreeFam; TF315035; -.
DR Reactome; R-BTA-196807; Nicotinate metabolism.
DR UniPathway; UPA00253; UER00332.
DR UniPathway; UPA00253; UER00600.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000051897; Expressed in longissimus thoracis muscle and 104 other tissues.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:1990966; P:ATP generation from poly-ADP-D-ribose; ISS:UniProtKB.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:1901215; P:negative regulation of neuron death; IEA:Ensembl.
DR GO; GO:0009611; P:response to wounding; IEA:Ensembl.
DR CDD; cd09286; NMNAT_Eukarya; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR005248; NadD/NMNAT.
DR InterPro; IPR045094; NMNAT_euk.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF01467; CTP_transf_like; 1.
DR TIGRFAMs; TIGR00482; TIGR00482; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Magnesium; NAD; Nucleotide-binding; Nucleotidyltransferase;
KW Nucleus; Phosphoprotein; Pyridine nucleotide biosynthesis;
KW Reference proteome; Transferase; Zinc.
FT CHAIN 1..281
FT /note="Nicotinamide/nicotinic acid mononucleotide
FT adenylyltransferase 1"
FT /id="PRO_0000262882"
FT REGION 113..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 123..129
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 121..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 15..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66,
FT ECO:0000250|UniProtKB:Q9HAN9"
FT BINDING 24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 55..57
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HAN9"
FT BINDING 58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 92..95
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HAN9"
FT BINDING 158..160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT BINDING 170..171
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HAN9"
FT BINDING 226..229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q96T66"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HAN9"
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
