MULTISPECIES: serine hydroxymethyltransferase [Pseudomonas].

LOCUS       WP_003148380             417 aa            linear   BCT 31-DEC-2024
ACCESSION   WP_003148380
VERSION     WP_003148380.1
KEYWORDS    RefSeq.
SOURCE      Pseudomonas
  ORGANISM  Pseudomonas
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Pseudomonadales; Pseudomonadaceae.
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   Schneider,G., Kack,H. and Lindqvist,Y.
  TITLE     The manifold of vitamin B6 dependent enzymes
  JOURNAL   Structure 8 (1), R1-R6 (2000)
   PUBMED   10673430
REFERENCE   3  (residues 1 to 417)
  AUTHORS   Mehta,P.K. and Christen,P.
  TITLE     The molecular evolution of pyridoxal-5'-phosphate-dependent enzymes
  JOURNAL   Adv Enzymol Relat Areas Mol Biol 74, 129-184 (2000)
   PUBMED   10800595
REFERENCE   4  (residues 1 to 417)
  AUTHORS   Chan,V.L. and Bingham,H.L.
  TITLE     Complete sequence of the Campylobacter jejuni glyA gene encoding
            serine hydroxymethyltransferase
  JOURNAL   Gene 101 (1), 51-58 (1991)
   PUBMED   2060796
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 10793727
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..417
                     /organism="Pseudomonas"
                     /db_xref="taxon:286"
     Protein         1..417
                     /product="serine hydroxymethyltransferase"
                     /EC_number="2.1.2.1"
                     /GO_function="GO:0004372 - glycine
                     hydroxymethyltransferase activity [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0019264 - glycine biosynthetic process
                     from serine [Evidence IEA]"
                     /calculated_mol_wt=44569
     Region          1..416
                     /region_name="PRK13034"
                     /note="serine hydroxymethyltransferase; Reviewed"
                     /db_xref="CDD:237280"
     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 mfskhdqirg yddellaamd aeearqedhl eliasenyts krvmqaqgsg 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 islvrqgltg keadaalgrv gitvnknavp ndpqspfvts
      361 girigtpait trglqeaqsr elagwicdil dhlgdadvea kvatqvaglc adfpvyr