3-phosphoserine/phosphohydroxythreonine transaminase [Escherichia

LOCUS       WP_000057165             362 aa            linear   BCT 01-JUN-2019
            coli].
ACCESSION   WP_000057165
VERSION     WP_000057165.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
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  :: HMM
            Evidence Accession :: NF003764.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK05355
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..362
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..362
                     /gene="serC"
     Protein         1..362
                     /product="3-phosphoserine/phosphohydroxythreonine
                     transaminase"
                     /EC_number="2.6.1.52"
                     /GO_function="GO:0003824 - catalytic activity [Evidence
                     IEA]"
                     /GO_function="GO:0004648 -
                     O-phospho-L-serine:2-oxoglutarate aminotransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006564 - L-serine biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=39723
     Region          1..362
                     /region_name="PRK05355"
                     /note="3-phosphoserine/phosphohydroxythreonine
                     transaminase"
                     /db_xref="CDD:235428"
     Site            order(6,11..12,14,73..74,77,109,112..113,203,239..241)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:99736"
     Site            order(9,76..77,102,153,174,197..198,328)
                     /site_type="active"
                     /note="substrate-cofactor binding pocket [active]"
                     /db_xref="CDD:99736"
     Site            order(75..77,102,153,174,176,197..198)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:99736"
     Site            198
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:99736"
ORIGIN      
        1 maqifnfssg pamlpvevlk qaqqelrdwn glgtsvmevs hrgkefiqva eeaekdfrdl
       61 lnvpsnykvl fchgggrgqf aavplnilgd kttadyvdag ywaasaikea kkyctpnvfd
      121 akvtvdglra vkpmrewqls dnaaymhycp netidgiaid etpdfgkdvv vaadfsstil
      181 srpidvsryg viyagaqkni gpagltiviv redllgkanv acpsildysi lndngsmfnt
      241 pptfawylsg lvfkwlkang gvaemdkinq qkaellygvi dnsdfyrndv akanrsrmnv
      301 pfqladsald klfleesfaa glhalkghrv vggmrasiyn amplegvkal tdfmveferr
      361 hg