CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
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
186LSDAFLIKENHIIASacetylation[1]
265VSGNVTDKTLREFAEacetylation[1]
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. 
Interpro
 IPR013785; Aldolase_TIM.
 IPR004393; NadC.
 IPR027277; NadC/ModD.
 IPR002638; Quinolinate_PRibosylTrfase_C.
 IPR022412; Quinolinate_PRibosylTrfase_N. 
Pfam
 PF01729; QRPTase_C
 PF02749; QRPTase_N 
SMART
  
PROSITE
  
PRINTS