MULTISPECIES: acid phosphatase [Pseudomonas].

LOCUS       WP_003083962             241 aa            linear   BCT 24-DEC-2024
ACCESSION   WP_003083962
VERSION     WP_003083962.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
REFERENCE   1  (residues 1 to 241)
  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 241)
  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..241
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..241
                     /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=25936
     Region          26..232
                     /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(125,132,154..156,189,195,199)
                     /site_type="active"
                     /db_xref="CDD:239491"
ORIGIN      
        1 mnnktlcpsl llclsllapl sclgetaaap yplahpprla dylppppaad saaavadlga
       61 vleaqrlrtp eqvrrvrahd qwednvfpfa gdllgasfdk erlpltrsff nraqenlvev
      121 lmpakkhfar prpyevtpkv kpvlpppege sypsghtmds yfkasllsml vpehhdaffa
      181 raeehaqsrv lagvhfpsdl eggqtaaaal vaslladpav aadfaavree lrgalglpkl
      241 q