Q0VD50 (NMNA1_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 42.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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 |
| ||
| 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. |
| 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 D-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 |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Cellular component | nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW nicotinamide-nucleotide adenylyltransferase activityInferred from electronic annotation. Source: EC nicotinate-nucleotide adenylyltransferase activityInferred 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 – 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 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 117 | 1 | Phosphoserine By similarity | ||||||
Sequences
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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 | |
|---|---|
| EMBL GenBank DDBJ | BC119834 mRNA. Translation: AAI19835.1. |
| IPI | IPI00906676. |
| RefSeq | NP_001069302.1. NM_001075834.1. |
| UniGene | Bt.59388. |
3D structure databases | |
| ProteinModelPortal | Q0VD50. |
| SMR | Q0VD50. Positions 5-276. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q0VD50. |
Proteomic databases | |
| PRIDE | Q0VD50. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSBTAT00000056287; ENSBTAP00000048652; ENSBTAG00000001361. |
| GeneID | 522863. |
| KEGG | bta:522863. |
Organism-specific databases | |
| CTD | 64802. |
Phylogenomic databases | |
| eggNOG | maNOG14935. |
| GeneTree | ENSGT00530000063189. |
| HOVERGEN | HBG052640. |
| OrthoDB | EOG48SGV2. |
| PhylomeDB | Q0VD50. |
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. |
| KO | K06210. |
| PANTHER | PTHR12039. NAMN_adtrnsfrase. 1 hit. |
| Pfam | PF01467. CTP_transf_2. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00482. TIGR00482. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | NMNA1_BOVIN | ||||||||
| Accession | Primary (citable) accession number: Q0VD50 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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