Tag | Content |
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CPLM ID | CPLM-005820 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Nicotinate-nucleotide pyrophosphorylase [carboxylating] |
Protein Synonyms/Alias | Quinolinate phosphoribosyltransferase [decarboxylating]; QAPRTase |
Gene Name | nadC |
Gene Synonyms/Alias | b0109; JW0105 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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186 | LSDAFLIKENHIIAS | acetylation | [1] | 265 | VSGNVTDKTLREFAE | 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 | Involved in the catabolism of quinolinic acid (QA) (By similarity). |
Sequence Annotation | REGION 152 154 Substrate binding (By similarity). REGION 259 261 Substrate binding (By similarity). REGION 280 282 Substrate binding (By similarity). BINDING 119 119 Substrate (By similarity). BINDING 176 176 Substrate (By similarity). BINDING 186 186 Substrate (By similarity). BINDING 215 215 Substrate (By similarity). BINDING 236 236 Substrate (By similarity). |
Keyword | Complete proteome; Glycosyltransferase; Pyridine nucleotide biosynthesis; Reference proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 297 AA |
Protein Sequence | MPPRRYNPDT RRDELLERIN LDIPGAVAQA LREDLGGTVD ANNDITAKLL PENSRSHATV 60 ITRENGVFCG KRWVEEVFIQ LAGDDVTIIW HVDDGDVINA NQSLFELEGP SRVLLTGERT 120 ALNFVQTLSG VASKVRHYVE LLEGTNTQLL DTRKTLPGLR SALKYAVLCG GGANHRLGLS 180 DAFLIKENHI IASGSVRQAV EKASWLHPDA PVEVEVENLE ELDEALKAGA DIIMLDNFET 240 EQMREAVKRT NGKALLEVSG NVTDKTLREF AETGVDFISV GALTKHVQAL DLSMRFR 297 |
Gene Ontology | GO:0005737; C:cytoplasm; IDA:EcoliWiki. GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IDA:EcoCyc. GO:0034628; P:de novo NAD biosynthetic process from aspartate; IMP:EcoCyc. |
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Pfam | |
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