MULTISPECIES: N-acetylneuraminate lyase [Salmonella].

LOCUS       WP_001029667             297 aa            linear   BCT 03-JUN-2024
ACCESSION   WP_001029667
VERSION     WP_001029667.1
KEYWORDS    RefSeq.
SOURCE      Salmonella
  ORGANISM  Salmonella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Grobe,K., Sartori,B., Traving,C., Schauer,R. and Roggentin,P.
  TITLE     Enzymatic and molecular properties of the Clostridium tertium
            sialidase
  JOURNAL   J Biochem 124 (6), 1101-1110 (1998)
   PUBMED   9832614
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Lilley,G.G., Barbosa,J.A. and Pearce,L.A.
  TITLE     Expression in Escherichia coli of the putative N-acetylneuraminate
            lyase gene (nanA) from Haemophilus influenzae: overproduction,
            purification, and crystallization
  JOURNAL   Protein Expr Purif 12 (3), 295-304 (1998)
   PUBMED   9535696
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: TIGR00683.1
            Evidence Source    :: JCVI
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Salmonella"
                     /db_xref="taxon:590"
     gene            1..297
                     /gene="nanA"
     Protein         1..297
                     /product="N-acetylneuraminate lyase"
                     /EC_number="4.1.3.3"
                     /GO_function="GO:0008747 - N-acetylneuraminate lyase
                     activity [Evidence IEA]"
                     /GO_process="GO:0005975 - carbohydrate metabolic process
                     [Evidence IEA]"
                     /calculated_mol_wt=32324
     Region          2..295
                     /region_name="PRK04147"
                     /note="N-acetylneuraminate lyase; Provisional"
                     /db_xref="CDD:179749"
     Site            order(11,43,46..48,137,165)
                     /site_type="inhibition"
                     /note="inhibitor site"
                     /db_xref="CDD:188641"
     Site            order(43,46..48,137,165,206)
                     /site_type="active"
                     /db_xref="CDD:188641"
     Site            order(47,52..53,84..85,109..110,117,121,272..273)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:188641"
     Site            165
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:188641"
ORIGIN      
        1 makalqgvma alltpfdhqq qldseslrrl vrfnigqgid glyvggstge afvqslaere
       61 qvleivaeea kgkitliahv gtvstaesqq lasaakrygf davsavtpfy ypfsfeehcd
      121 hyraiidsad glpmvvynip alsgvkltld qintlvtlpg vsalkqtsgd lfqmeqirra
      181 hpdlvlyngy deifasglla gadggigsty nimgwryqgi vqalregdva kaqrlqtecn
      241 kvidlliktg vfrglktvlh ymdvvsvplc rkpfapvdek ylpalkalaq qlmeeka