Q0HA29 (NMNA2_RAT) Reviewed, UniProtKB/Swiss-Prot

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

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	307 AA.
Sequence status	Complete.
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 D-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
Technical term	Complete proteome Reference proteome
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_0000328662
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)
	Q0HA29 [UniParc]. Last modified October 3, 2006. Version 1. Checksum: EDE5DAB7B03AE1AA	FASTA	307	34,445
	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 SMTPVIGQPQ HENTQPIYQN SNVPTKPTAA KILGKVGESL GRICCVRPPV ERFTFVDENA 190 200 210 220 230 240 NLGTVMRYEE IELRILLLCG SDLLESFCIP GLWNEADMEV IVGDFGIVVV PRDAADADRI 250 260 270 280 290 300 MNHSSILRKY KNNIMVVKDD INHPMSVVSS TKSRLALQHG DGHVVDYLSQ PVIDYILKSQ LYINASG

References

[1]	"Nicotinamide nucleotide adenylyltransferase is neuroprotective against ischemic injury." Xing J., Cao G., Zhang L., Chen J. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Brain.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DQ022370 mRNA. Translation: AAY87457.1.
IPI	IPI00371496.
RefSeq	NP_001041507.1. NM_001048042.1.
UniGene	Rn.145458.
3D structure databases
ProteinModelPortal	Q0HA29.
SMR	Q0HA29. Positions 9-109.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0HA29.
Proteomic databases
PRIDE	Q0HA29.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	289095.
KEGG	rno:289095.
Organism-specific databases
CTD	23057.
RGD	1307331. Nmnat2.
Phylogenomic databases
eggNOG	roNOG07648.
GeneTree	ENSGT00530000063189.
HOVERGEN	HBG052640.
InParanoid	Q0HA29.
OrthoDB	EOG4N30PB.
PhylomeDB	Q0HA29.
Gene expression databases
ArrayExpress	Q0HA29.
Genevestigator	Q0HA29.
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. 2 hits.
KO	K06210.
PANTHER	PTHR12039. NAMN_adtrnsfrase. 1 hit.
Pfam	PF01467. CTP_transf_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	629238.

Entry information

Entry name

NMNA2_RAT

Accession

Primary (citable) accession number: Q0HA29

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	October 3, 2006
Last modified:	November 16, 2011
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program