Reviewed, UniProtKB/Swiss-Prot Q0VD50 (NMNA1_BOVIN)

Names and origin

Protein names

Recommended name:
    Nicotinamide mononucleotide adenylyltransferase 1
      Short name=NMN adenylyltransferase 1
    EC=2.7.7.1
Alternative name(s):
    Nicotinate-nucleotide adenylyltransferase 1
      Short name=NaMN adenylyltransferase 1
    EC=2.7.7.18

Gene names

Name:

NMNAT1

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	281 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

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. Fails to cleave phosphorylated dinucleotides NADP+, NADPH and NAADP+. Protects against axonal degeneration following mechanical or toxic insults By similarity.
Catalytic activity	ATP + nicotinamide ribonucleotide = diphosphate + NAD+. ATP + nicotinate ribonucleotide = diphosphate + deamido-NAD+.
Cofactor	Divalent metal cations. Zinc confers higher activity than magnesium By similarity.
Enzyme regulation	Activity is strongly inhibited by galotannin. Inhibited by P1-(adenosine-5')-P4-(nicotinic-acid-riboside-5')-tetraphosphate (Nap4AD) By similarity.
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide ribonucleotide: step 1/1.
Subunit structure	Homohexamer. Interacts with ADPRT/PARP1 By similarity.
Subcellular location	Nucleus By similarity.
Post-translational modification	Phosphorylated By similarity.
Sequence similarities	Belongs to the eukaryotic NMN adenylyltransferase family.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Cellular component	Nucleus
Ligand	ATP-binding Magnesium NAD Nucleotide-binding Zinc
Molecular function	Nucleotidyltransferase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	NAD biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW nicotinamide-nucleotide adenylyltransferase activity Inferred from electronic annotation. Source: EC nicotinate-nucleotide adenylyltransferase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 281	281	Nicotinamide mononucleotide adenylyltransferase 1		PRO_0000262882
Regions
	Nucleotide binding	15 – 24	10	ATP Potential
	Nucleotide binding	224 – 229	6	ATP Potential
	Motif	123 – 129	7	Nuclear localization signal Potential
Sites
	Binding site	16	1	Substrate By similarity
	Binding site	55	1	Substrate By similarity
	Binding site	160	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0VD50-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: ECAF9116729138FA	FASTA	281	32,200
	10 20 30 40 50 60 MENSEKTEVV LLACGSFNPI TNMHLRLFEL AKDYMNGTGK YKVIKGIISP VGDAYKKKGL 70 80 90 100 110 120 ISAYHRVIMA ELATKNSKWV EVDTWESLQK EWTETAKVLR HHQEKLEASI CDPQQNSPVL 130 140 150 160 170 180 EKPGRKRKWA EQKQDISEKK SLEQTKTKGV PKVKLLCGAD FLESFGVPNL WKSEDITKIL 190 200 210 220 230 240 GDYGLICITR AGNDAQKFIY ESDVLWKHQN NIHLVNEWIT NDISSTKIRR ALRRGQSIRY 250 260 270 280 LVPDLVEEYI EKHNLYSSES EERNVGVVLA PLQRNTTEVK A

References

[1]	NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Ascending colon.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BC119834 mRNA. Translation: AAI19835.1.
IPI	IPI00691671.
RefSeq	NP_001069302.1.
UniGene	Bt.59388
3D structure databases
SMR	Q0VD50. Positions 5-276.
ModBase	Search...
Genome annotation databases
Ensembl	ENSBTAG00000001361. Bos taurus. [Contig view]
GeneID	522863.
KEGG	bta:522863.
Phylogenomic databases
HOVERGEN	Q0VD50.
Enzyme and pathway databases
BRENDA	2.7.7.1. 251.
Family and domain databases
InterPro	IPR004820. Cytidylyltransf. IPR005248. NAMN_adtrnsfrase. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Gene3D	G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHER	PTHR12039. NAMN_adtrnsfrase. 1 hit.
Pfam	PF01467. CTP_transf_2. 1 hit. [Graphical view]
TIGRFAMs	TIGR00482. NAMN_adtrnsfrase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

NMNA1_BOVIN

Accession

Primary (citable) accession number: Q0VD50

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	September 5, 2006
Last modified:	June 16, 2009
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)