aminodeoxychorismate lyase [Escherichia coli].

LOCUS       WP_000478717             269 aa            linear   BCT 11-DEC-2019
ACCESSION   WP_000478717
VERSION     WP_000478717.1
KEYWORDS    RefSeq.
SOURCE      Escherichia coli
  ORGANISM  Escherichia coli
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Escherichia.
REFERENCE   1  (residues 1 to 269)
  AUTHORS   Hoang,T.T., Karkhoff-Schweizer,R.R., Kutchma,A.J. and
            Schweizer,H.P.
  TITLE     A broad-host-range Flp-FRT recombination system for site-specific
            excision of chromosomally-located DNA sequences: application for
            isolation of unmarked Pseudomonas aeruginosa mutants
  JOURNAL   Gene 212 (1), 77-86 (1998)
   PUBMED   9661666
REFERENCE   2  (residues 1 to 269)
  AUTHORS   Shen,Z. and Byers,D.M.
  TITLE     Isolation of Vibrio harveyi acyl carrier protein and the fabG,
            acpP, and fabF genes involved in fatty acid biosynthesis
  JOURNAL   J. Bacteriol. 178 (2), 571-573 (1996)
   PUBMED   8550484
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 :: NF004761.0
            Evidence Source    :: NCBI Protein Cluster (PRK)
            Source Identifier  :: PRK06092
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..269
                     /organism="Escherichia coli"
                     /db_xref="taxon:562"
     gene            1..269
                     /gene="pabC"
     Protein         1..269
                     /product="aminodeoxychorismate lyase"
                     /EC_number="4.1.3.38"
                     /GO_function="GO:0008696 - 4-amino-4-deoxychorismate lyase
                     activity [Evidence IEA]"
                     /GO_function="GO:0030170 - pyridoxal phosphate binding
                     [Evidence IEA]"
                     /GO_process="GO:0046656 - folic acid biosynthetic process
                     [Evidence IEA]"
                     /calculated_mol_wt=29534
     Region          1..268
                     /region_name="PRK06092"
                     /note="4-amino-4-deoxychorismate lyase; Reviewed"
                     /db_xref="CDD:235696"
     Site            order(45,140,173)
                     /site_type="other"
                     /note="pyridoxal 5'-phosphate binding site [chemical
                     binding]"
                     /db_xref="CDD:238800"
     Site            140
                     /site_type="active"
                     /note="catalytic residue [active]"
                     /db_xref="CDD:238800"
ORIGIN      
        1 mflingykqe slsvsdratq fgdgcfttar vidgkvslls ahiqrlqdac qrlmiscdfw
       61 pqleqemktl aaeqqngvlk vvisrgsggr gystlnsgpa trilsvtayp ahydrlrneg
      121 itlalspvrl grnphlagik hlnrleqvli rshleqtnad ealvldsegg vteccaanlf
      181 wrkgnvvytp rldqagvngi mrqfcirlla qssyqlvevq asleealqad emvicnalmp
      241 vmpvracgdv sfssatlyey laplcerpn