serine hydroxymethyltransferase [Pseudomonas aeruginosa].

LOCUS       WP_003112798             417 aa            linear   BCT 29-MAR-2023
ACCESSION   WP_003112798
VERSION     WP_003112798.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas aeruginosa
  ORGANISM  Pseudomonas aeruginosa
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae; Pseudomonas.
REFERENCE   1  (residues 1 to 417)
  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 417)
  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..417
                     /organism="Pseudomonas aeruginosa"
                     /db_xref="taxon:287"
     gene            1..417
                     /gene="glyA"
     Protein         1..417
                     /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=45026
     Region          7..417
                     /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..139,264,
                     282)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:99733"
     Site            order(35,55,65,98..99,126,175,200,203,228..229,235,362)
                     /site_type="other"
                     /note="glycine-pyridoxal phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99733"
     Site            order(35,126,229,362)
                     /site_type="active"
                     /db_xref="CDD:99733"
     Site            order(57,64,121,125,127,256,346)
                     /site_type="other"
                     /note="folate binding site [chemical binding]"
                     /db_xref="CDD:99733"
ORIGIN      
        1 mfsrdltlar ydaelfaame qeaqrqeehi eliasenyts pavmeaqgsv ltnkyaegyp
       61 hkryyggcey vdiveqlaid rakqlfgady anvqphagsq anaavylall sagdtilgms
      121 lahgghlthg asvsssgkly navqygidan glidydever lavehkpkmi vagfsaysqv
      181 ldfarfraia dkvgaylfvd mahvaglvaa gvypnpvpfa dvvtttthkt lrgprgglil
      241 araneeiekk lnsavfpsaq ggplehviaa kavcfkealq pefktyqqqv lknaqsmaqv
      301 fldrgfdvvs ggtqnhlfll slikqditgk dadaalgraf itvnknsvpn dprspfvtsg
      361 lrigtpavtt rgfkeaecre lagwicdile nmgdesvvdg vrekvkaica kfpvygn