CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002924
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 N-acetylneuraminate lyase 
Protein Synonyms/Alias
 N-acetylneuraminate pyruvate-lyase; N-acetylneuraminic acid aldolase; NALase; Sialate lyase; Sialic acid aldolase; Sialic acid lyase 
Gene Name
 nanA 
Gene Synonyms/Alias
 npl; b3225; JW3194 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
24DQQQALDKASLRRLVacetylation[1]
165LPGVGALKQTSGDLYacetylation[2]
280PFGPVDEKYLPELKAacetylation[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]
 [2] The diversity of lysine-acetylated proteins in Escherichia coli.
 Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG.
 J Microbiol Biotechnol. 2008 Sep;18(9):1529-36. [PMID: 18852508
Functional Description
 Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate. 
Sequence Annotation
 REGION 47 48 Substrate binding.
 ACT_SITE 165 165 Schiff-base intermediate with substrate.  
Keyword
 3D-structure; Carbohydrate metabolism; Complete proteome; Cytoplasm; Direct protein sequencing; Lyase; Reference proteome; Schiff base. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 297 AA 
Protein Sequence
MATNLRGVMA ALLTPFDQQQ ALDKASLRRL VQFNIQQGID GLYVGGSTGE AFVQSLSERE 60
QVLEIVAEEA KGKIKLIAHV GCVSTAESQQ LAASAKRYGF DAVSAVTPFY YPFSFEEHCD 120
HYRAIIDSAD GLPMVVYNIP ALSGVKLTLD QINTLVTLPG VGALKQTSGD LYQMEQIRRE 180
HPDLVLYNGY DEIFASGLLA GADGGIGSTY NIMGWRYQGI VKALKEGDIQ TAQKLQTECN 240
KVIDLLIKTG VFRGLKTVLH YMDVVSVPLC RKPFGPVDEK YLPELKALAQ QLMQERG 297 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0008747; F:N-acetylneuraminate lyase activity; IDA:EcoCyc.
 GO:0005975; P:carbohydrate metabolic process; IEA:HAMAP.
 GO:0019262; P:N-acetylneuraminate catabolic process; IMP:EcoCyc. 
Interpro
 IPR013785; Aldolase_TIM.
 IPR002220; Dihydrodipicolinate_synth-like.
 IPR020625; Dihydrodipicolinate_synth_AS.
 IPR020624; Dihydrodipicolinate_synth_CS.
 IPR005264; NanA. 
Pfam
 PF00701; DHDPS 
SMART
  
PROSITE
 PS00665; DHDPS_1
 PS00666; DHDPS_2 
PRINTS
 PR00146; DHPICSNTHASE.