MULTISPECIES: acid phosphatase [Salmonella].

LOCUS       WP_000766151             423 aa            linear   BCT 24-DEC-2024
ACCESSION   WP_000766151
VERSION     WP_000766151.1
KEYWORDS    RefSeq.
SOURCE      Salmonella
  ORGANISM  Salmonella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae.
REFERENCE   1  (residues 1 to 423)
  AUTHORS   Littlechild,J., Garcia-Rodriguez,E., Dalby,A. and Isupov,M.
  TITLE     Structural and functional comparisons between vanadium
            haloperoxidase and acid phosphatase enzymes
  JOURNAL   J Mol Recognit 15 (5), 291-296 (2002)
   PUBMED   12447906
REFERENCE   2  (residues 1 to 423)
  AUTHORS   Neuwald,A.F.
  TITLE     An unexpected structural relationship between integral membrane
            phosphatases and soluble haloperoxidases
  JOURNAL   Protein Sci 6 (8), 1764-1767 (1997)
   PUBMED   9260289
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  :: Conserved Domain (CDD)
            Evidence Accession :: Domain architecture ID 10130290
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..423
                     /organism="Salmonella"
                     /db_xref="taxon:590"
     Protein         1..423
                     /product="acid phosphatase"
                     /EC_number="3.1.3.2"
                     /GO_function="GO:0003993 - acid phosphatase activity
                     [Evidence IEA]"
                     /GO_process="GO:0016311 - dephosphorylation [Evidence
                     IEA]"
                     /calculated_mol_wt=46339
     Region          63..309
                     /region_name="PAP2_acid_phosphatase"
                     /note="PAP2, bacterial acid phosphatase or class A
                     non-specific acid phosphatases. These enzymes catalyze
                     phosphomonoester hydrolysis, with optimal activity in low
                     pH conditions. They are secreted into the periplasmic
                     space, and their physiological role remains...; cd03397"
                     /db_xref="CDD:239491"
     Site            order(191,198,231..233,266,272,276)
                     /site_type="active"
                     /db_xref="CDD:239491"
ORIGIN      
        1 mklhitvlas slalampala kdiplsqaes iaksvtpdsa svafndleaq wltqlrkalq
       61 gdtaaltrda laqmrqnsiq adnawlqasg ydfhttenqq mgitllsafn tlpeavlkdn
      121 latvtainhd advntrhqal adaesveyly flsdamgprl graflaaydk gelgkaaali
      181 kasevstgaa kkyfhyprpy qvpgntihlt pddvvvkdgh pytagggafp sghtntgytd
      241 allmaemipe rfdalvirga rygysrlvlg vhypldvmga rmvaqrnvah ylndpyyrtl
      301 fnearaqlre alvkecgtti vecaastgkd dpyrdpamht fyrftmtynl pqqkgehqpl
      361 kipkgadvll qtalpnlspa qrqalmeeta lpagyplsge tedqqfwqrl dlsaayemar
      421 ktr