CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003931
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Quinolinate synthase A 
Protein Synonyms/Alias
  
Gene Name
 nadA 
Gene Synonyms/Alias
 nicA; b0750; JW0733 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
179KIIWAPDKHLGRYVQacetylation[1]
269TDRGIFYKMQQAVPDacetylation[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
 Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. 
Sequence Annotation
 BINDING 47 47 Iminoaspartate (By similarity).
 BINDING 68 68 Iminoaspartate; via amide nitrogen (By
 BINDING 139 139 Iminoaspartate (By similarity).
 BINDING 156 156 Iminoaspartate (By similarity).
 BINDING 226 226 Iminoaspartate (By similarity).
 BINDING 243 243 Iminoaspartate (By similarity).
 DISULFID 291 294 Redox-active.  
Keyword
 4Fe-4S; Complete proteome; Cytoplasm; Direct protein sequencing; Disulfide bond; Iron; Iron-sulfur; Metal-binding; Pyridine nucleotide biosynthesis; Redox-active center; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 347 AA 
Protein Sequence
MSVMFDPDTA IYPFPPKPTP LSIDEKAYYR EKIKRLLKER NAVMVAHYYT DPEIQQLAEE 60
TGGCISDSLE MARFGAKHPA STLLVAGVRF MGETAKILSP EKTILMPTLQ AECSLDLGCP 120
VEEFNAFCDA HPDRTVVVYA NTSAAVKARA DWVVTSSIAV ELIDHLDSLG EKIIWAPDKH 180
LGRYVQKQTG GDILCWQGAC IVHDEFKTQA LTRLQEEYPD AAILVHPESP QAIVDMADAV 240
GSTSQLIAAA KTLPHQRLIV ATDRGIFYKM QQAVPDKELL EAPTAGEGAT CRSCAHCPWM 300
AMNGLQAIAE ALEQEGSNHE VHVDERLRER ALVPLNRMLD FAATLRG 347 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0008987; F:quinolinate synthetase A activity; IDA:EcoCyc.
 GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
 GO:0034628; P:de novo NAD biosynthetic process from aspartate; IMP:EcoCyc. 
Interpro
 IPR003473; NadA.
 IPR023513; Quinolinate_synth_A_type1. 
Pfam
 PF02445; NadA 
SMART
  
PROSITE
  
PRINTS