MULTISPECIES: acid phosphatase [Klebsiella].

LOCUS       WP_002921266             423 aa            linear   BCT 24-DEC-2024
ACCESSION   WP_002921266
VERSION     WP_002921266.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
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="Klebsiella"
                     /db_xref="taxon:570"
     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=45977
     Region          76..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 mkrqlsllav alllaqpvla kdiplnraaa lansvtpaas sqayddleqq alaqlrhalq
       61 gdaatltrdr lahtkqnqtq adtawlkasg ydfqtranqq agiallsafs tlpetvvkqn
      121 latvtainrd avqttrrqal adaegisyly flsdalgprl gkafltaydq galgkaaali
      181 kasevstgea kkhfnnprpf lvqgntihlv pddvvvkdnq pytadggsfp sghtntgytd
      241 alllaamipe rydalvarga rygfsrivlg vhypldvigs rmvaernvah ylndphyrvl
      301 fneardqlra alakacgtsl aecakssvkd dpwrdpamrd fsrftmtydl pqqkgpqprl
      361 qvpegaevll edalphlsaa qrralmvnta lpagyplsga tpeqqfwqrl nlsaawemaq
      421 krh