Reviewed, UniProtKB/Swiss-Prot Q0VC59 (NMNA2_BOVIN)

Names and origin

Protein names

Recommended name:
    Nicotinamide mononucleotide adenylyltransferase 2
      Short name=NMN adenylyltransferase 2
    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:

NMNAT2

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	307 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 but with a lower efficiency. Cannnot use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD+. For the pyrophosphorolytic activity prefers NAD+, NADH and NAAD as substrates and degrades nicotinic acid adenine dinucleotide phosphate (NHD) less effectively. Fails to cleave phosphorylated dinucleotides NADP+, NADPH and NAADP+ By similarity.
Catalytic activity	ATP + nicotinamide ribonucleotide = diphosphate + NAD+. ATP + nicotinate ribonucleotide = diphosphate + deamido-NAD+.
Cofactor	Divalent metal cations. Magnesium confers the highest activity By similarity.
Enzyme regulation	Inhibited by P1-(adenosine-5')-P3-(nicotinamide-riboside-5')-triphosphate (Np3AD) and P1-(adenosine-5')-P4-(nicotinamide-riboside-5')-tetraphosphate (Np4AD) By similarity.
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide ribonucleotide: step 1/1.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity. Golgi apparatus By similarity.
Sequence similarities	Belongs to the eukaryotic NMN adenylyltransferase family.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Cellular component	Cytoplasm Golgi apparatus
Ligand	ATP-binding NAD Nucleotide-binding
Molecular function	Nucleotidyltransferase Transferase
Gene Ontology (GO)
Biological process	NAD biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP 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
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 307	307	Nicotinamide mononucleotide adenylyltransferase 2		PRO_0000328660
Regions
	Nucleotide binding	15 – 24	10	ATP Potential
	Nucleotide binding	269 – 274	6	ATP Potential
Sites
	Binding site	16	1	Substrate By similarity
	Binding site	55	1	Substrate By similarity
	Binding site	202	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0VC59-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 0E037406187B85DF	FASTA	307	34,468
	10 20 30 40 50 60 MTETTKTHVI LLACGSFNPI TKGHIQMFER ARDYLHKTGR FIVIGGIVSP VHDSYGKQGL 70 80 90 100 110 120 VSSRHRLIMC QLAVQNSDWI RVDPWECYQD TWQTTCSVLE HHRDLMKRVT GCILSNVNTP 130 140 150 160 170 180 SMTPVIGQPR NETSQPIYQN NNAPSKPTAA KILGKVGESL SRICCVRPPV ERFTFVDENA 190 200 210 220 230 240 NLGTVMRYEE IELRILLLCG SDLLESFCIP GLWNEADMEV IVGDFGIVVV PRDAADTDRI 250 260 270 280 290 300 MNHSSILRKY KNNIMVVKDD INHPMSVVSS TKSRLALQHG DGHVVDYLSQ PVIDYILKSQ LYINASG

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: Brain cortex.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BC120344 mRNA. Translation: AAI20345.1.
IPI	IPI00690702.
RefSeq	NP_001068954.1.
UniGene	Bt.32896
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	ENSBTAG00000000795. Bos taurus. [Contig view]
GeneID	511042.
KEGG	bta:511042.
Phylogenomic databases
HOVERGEN	Q0VC59.
OMA	Q0VC59. IGQPQHE.
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

NMNA2_BOVIN

Accession

Primary (citable) accession number: Q0VC59

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	September 5, 2006
Last modified:	June 16, 2009
This is version 28 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)