serine hydroxymethyltransferase [Pseudomonas aeruginosa].

LOCUS       WP_010895616             418 aa            linear   BCT 29-MAR-2023
ACCESSION   WP_010895616
VERSION     WP_010895616.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 418)
  AUTHORS   Appaji Rao,N., Ambili,M., Jala,V.R., Subramanya,H.S. and
            Savithri,H.S.
  TITLE     Structure-function relationship in serine hydroxymethyltransferase
  JOURNAL   Biochim Biophys Acta 1647 (1-2), 24-29 (2003)
   PUBMED   12686103
REFERENCE   2  (residues 1 to 418)
  AUTHORS   Stover,P. and Schirch,V.
  TITLE     Serine hydroxymethyltransferase catalyzes the hydrolysis of
            5,10-methenyltetrahydrofolate to 5-formyltetrahydrofolate
  JOURNAL   J Biol Chem 265 (24), 14227-14233 (1990)
   PUBMED   2201683
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 10011056
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..418
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..418
                     /gene="glyA"
     Protein         1..418
                     /product="serine hydroxymethyltransferase"
                     /EC_number="2.1.2.1"
                     /GO_function="GO:0004372 - glycine
                     hydroxymethyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0008270 - zinc ion binding [Evidence
                     IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_function="GO:0070905 - serine binding [Evidence IEA]"
                     /GO_process="GO:0019264 - glycine biosynthetic process
                     from serine [Evidence IEA]"
                     /calculated_mol_wt=44843
     Region          4..418
                     /region_name="glyA"
                     /note="serine hydroxymethyltransferase; Reviewed;
                     PRK00011"
                     /db_xref="CDD:234571"
     Site            order(12,14,21..22,31,36,54,72..73,81,96,103,138..139,265,
                     283)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:99733"
     Site            order(35,55,65,98..99,126,176,201,204,229..230,236,363)
                     /site_type="other"
                     /note="glycine-pyridoxal phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99733"
     Site            order(35,126,230,363)
                     /site_type="active"
                     /db_xref="CDD:99733"
     Site            order(57,64,121,125,127,257,347)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:99733"
ORIGIN      
        1 mfskhdqlqg yddellaamd aedrrqedhi eliasenyas krvmqaqggg ltnkyaegyp
       61 gkryyggceh vdkverlaid rarqlfgady anvqphsgss anaavylall nagdtilgms
      121 lahgghlthg akvsssgkly navqygldta tglidydeve rlavehkpkm ivagfsaysk
      181 tldfprfrai adkvgallfv dmahvaglva aglypnpipf advvtttthk tlrgprggli
      241 laraneeiek klnsavfpga qggplmhvia akavcfkeal epgfkdyqaq virnakamae
      301 vfigrgydvv sggtdnhlml islvkqgltg kaadaalgaa hitvnknavp ndpqspfvts
      361 girigtpavt trgfregecr elagwicdil ddidnpevge rvrgqvgefc rhfpvyad