Tag | Content |
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CPLM ID | CPLM-002968 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Nicotinate-nucleotide adenylyltransferase |
Protein Synonyms/Alias | Deamido-NAD(+) diphosphorylase; Deamido-NAD(+) pyrophosphorylase; Nicotinate mononucleotide adenylyltransferase; NaMN adenylyltransferase |
Gene Name | nadD |
Gene Synonyms/Alias | ybeN; b0639; JW0634 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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78 | TLDERELKRNAPSYT | acetylation | [1] | 90 | SYTAQTLKEWRQEQG | acetylation | [1] |
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Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] |
Functional Description | Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). |
Sequence Annotation | |
Keyword | 3D-structure; ATP-binding; Complete proteome; NAD; Nucleotide-binding; Nucleotidyltransferase; Pyridine nucleotide biosynthesis; Reference proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 213 AA |
Protein Sequence | MKSLQALFGG TFDPVHYGHL KPVETLANLI GLTRVTIIPN NVPPHRPQPE ANSVQRKHML 60 ELAIADKPLF TLDERELKRN APSYTAQTLK EWRQEQGPDV PLAFIIGQDS LLTFPTWYEY 120 ETILDNAHLI VCRRPGYPLE MAQPQYQQWL EDHLTHNPED LHLQPAGKIY LAETPWFNIS 180 ATIIRERLQN GESCEDLLPE PVLTYINQQG LYR 213 |
Gene Ontology | GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0004515; F:nicotinate-nucleotide adenylyltransferase activity; IDA:EcoCyc. GO:0034628; P:de novo NAD biosynthetic process from aspartate; IMP:EcoCyc. GO:0034355; P:NAD salvage; IMP:EcoCyc. |
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Pfam | |
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