carbonic anhydrase [Pseudomonas aeruginosa].

LOCUS       WP_003115027             242 aa            linear   BCT 21-MAR-2023
ACCESSION   WP_003115027
VERSION     WP_003115027.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 242)
  AUTHORS   Tripp,B.C., Smith,K. and Ferry,J.G.
  TITLE     Carbonic anhydrase: new insights for an ancient enzyme
  JOURNAL   J Biol Chem 276 (52), 48615-48618 (2001)
   PUBMED   11696553
REFERENCE   2  (residues 1 to 242)
  AUTHORS   Lindskog,S.
  TITLE     Structure and mechanism of carbonic anhydrase
  JOURNAL   Pharmacol Ther 74 (1), 1-20 (1997)
   PUBMED   9336012
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 10096759
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..242
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     Protein         1..242
                     /product="carbonic anhydrase"
                     /EC_number="4.2.1.1"
                     /GO_function="GO:0004089 - carbonate dehydratase activity
                     [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /calculated_mol_wt=26491
     Region          28..214
                     /region_name="beta_CA_cladeB"
                     /note="Carbonic anhydrases (CA) are zinc-containing
                     enzymes that catalyze the reversible hydration of carbon
                     dioxide in a two-step mechanism in which the nucleophilic
                     attack of a zinc-bound hydroxide ion on carbon dioxide is
                     followed by the regeneration of an...; cd00884"
                     /db_xref="CDD:238449"
     Site            order(51,53,60,62..64,76,79,104,109,119,122,204)
                     /site_type="active"
                     /note="active site clefts [active]"
                     /db_xref="CDD:238449"
     Site            order(60,62,119,122)
                     /site_type="other"
                     /note="zinc binding site [ion binding]"
                     /db_xref="CDD:238449"
     Site            order(61..64,66,68..71,76..78,80,82,99..100,103..104,143,
                     204,206..207,209,211)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:238449"
ORIGIN      
        1 mpdrmrgvks dspeqesadd alkrivdgfq hfrrevfpeq qalfkklans qrpramfitc
       61 adsrivpeli tqsspgdlfv trnvgnvvpp ygqmnggvst aieyavlalg vhhiivcghs
      121 dcgamravld pqtlermptv kawlrhaeva rtvvadncdc gashdtlgvl teenvvaqld
      181 hlrthpsvas rlasgqlfih gwvydiesaq iraydakqgr flpldgehpv pmatpapryl
      241 ss