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MULTISPECIES: aminodeoxychorismate lyase [Klebsiella].


LOCUS       WP_002900669             269 aa            linear   BCT 29-JUN-2020
ACCESSION   WP_002900669
VERSION     WP_002900669.1
KEYWORDS    RefSeq.
SOURCE      Klebsiella
  ORGANISM  Klebsiella
            Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
            Enterobacterales; Enterobacteriaceae; Klebsiella/Raoultella group.
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="Klebsiella"
                     /db_xref="taxon:570"
     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=30112
     Region          1..266
                     /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 mflingvvqd tlaandratq fgdgcfttar iqqgqvalld ahlqrlqttc eklhipfndw
       61 ltlseemqrl arphaqgvlk vtltrgvggr gystagcvsp trilsfspfp ahyarwreeg
      121 itltqspvpl grnswlaglk hlnrleqvli rshleqtdad ealvldsdgw lteccaanlf
      181 wrqgrdvftp rldyagvngi mrqrciaqla pstfrvvevt arpetlread evlicnalmp
      241 lvpvrrweet twssrelyhf laplcelsg