serine O-acetyltransferase [Escherichia coli].

LOCUS       WP_000954203             190 aa            linear   BCT 21-MAR-2023
ACCESSION   WP_000954203
VERSION     WP_000954203.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 190)
  AUTHORS   Johnson,C.M., Roderick,S.L. and Cook,P.F.
  TITLE     The serine acetyltransferase reaction: acetyl transfer from an
            acylpantothenyl donor to an alcohol
  JOURNAL   Arch Biochem Biophys 433 (1), 85-95 (2005)
   PUBMED   15581568
REFERENCE   2  (residues 1 to 190)
  AUTHORS   Parisi,G. and Echave,J.
  TITLE     The structurally constrained protein evolution model accounts for
            sequence patterns of the LbetaH superfamily
  JOURNAL   BMC Evol Biol 4, 41 (2004)
   PUBMED   15500694
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 190)
  AUTHORS   Jenkins,J. and Pickersgill,R.
  TITLE     The architecture of parallel beta-helices and related folds
  JOURNAL   Prog Biophys Mol Biol 77 (2), 111-175 (2001)
   PUBMED   11747907
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 11437200
            Evidence Source    :: NCBI SPARCLE
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..190
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     Protein         1..190
                     /product="serine O-acetyltransferase"
                     /EC_number="2.3.1.30"
                     /GO_function="GO:0009001 - serine O-acetyltransferase
                     activity [Evidence IEA]"
                     /GO_process="GO:0006535 - cysteine biosynthetic process
                     from serine [Evidence IEA]"
                     /calculated_mol_wt=21382
     Region          82..178
                     /region_name="LbetaH"
                     /note="Left-handed parallel beta-Helix (LbetaH or LbH)
                     domain: The alignment contains 5 turns, each containing
                     three imperfect tandem repeats of a hexapeptide repeat
                     motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing
                     hexapeptide repeats are often enzymes...; cl00160"
                     /db_xref="CDD:469633"
     Site            order(97,99,105,107,117,123,125,143,148..149,151,162,166,
                     168,170)
                     /site_type="other"
                     /note="putative trimer interface [polypeptide binding]"
                     /db_xref="CDD:100038"
     Site            order(143,145..146,151,164,170)
                     /site_type="other"
                     /note="putative CoA binding site [chemical binding]"
                     /db_xref="CDD:100038"
ORIGIN      
        1 mlsylmaihf vlfgnstnlk nfwkhevirr krmdiwrllr ekkqrnrnfl fwwrlanemy
       61 ingnklhkka akklnskiin kfgceiglga nigkgltiph hagivvhfav dagenlvlrq
      121 nttigqidgd mpssrvkigs nvdigancci iglsrkigdn vkigamsfin kdipsnctyi
      181 tkksgvvlyk