ID   FSDH_RALPI              Reviewed;         326 AA.
AC   Q10725; Q8GI87;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Phenylserine dehydratase;
DE            EC=4.2.1.-;
GN   Name=psdht {ECO:0000312|EMBL:BAC53614.1};
OS   Ralstonia pickettii (Burkholderia pickettii).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=329;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAC53614.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=PS22 {ECO:0000312|EMBL:BAC53614.1};
RX   PubMed=12596884; DOI=10.1271/bbb.66.2755;
RA   Okuda H., Nagata S., Misono H.;
RT   "Cloning, sequencing, and overexpression in Escherichia coli of a
RT   phenylserine dehydratase gene from Ralstonia pickettii PS22.";
RL   Biosci. Biotechnol. Biochem. 66:2755-2758(2002).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-24 AND 28-61, CATALYTIC ACTIVITY, ACTIVITY
RP   REGULATION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP   INDUCTION.
RC   STRAIN=PS22 {ECO:0000269|PubMed:8743570};
RX   PubMed=8743570; DOI=10.1093/oxfordjournals.jbchem.a021297;
RA   Okuda H., Nagata S., Misono H.;
RT   "A novel phenylserine dehydratase from Pseudomonas pickettii PS22:
RT   purification, characterization, and sequence of its phosphopyridoxyl
RT   peptide.";
RL   J. Biochem. 119:690-696(1996).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threo-3-phenylserine = 3-phenylpyruvate + NH4(+);
CC         Xref=Rhea:RHEA:46328, ChEBI:CHEBI:18005, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57901; Evidence={ECO:0000269|PubMed:12596884,
CC         ECO:0000269|PubMed:8743570};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:8743570};
CC   -!- ACTIVITY REGULATION: Inhibited by phenylhydrazine, hydroxylamine, p-
CC       chloromercuribenzoate, and HgCl(2). {ECO:0000269|PubMed:8743570}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.20 mM for L-threo-3-phenylserine {ECO:0000269|PubMed:12596884,
CC         ECO:0000269|PubMed:8743570};
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:12596884,
CC         ECO:0000269|PubMed:8743570};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8743570}.
CC   -!- INDUCTION: By L-threo-3-phenylserine. {ECO:0000269|PubMed:8743570}.
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DR   EMBL; AB076802; BAC53614.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q10725; -.
DR   SMR; Q10725; -.
DR   GO; GO:0016829; F:lyase activity; IDA:UniProtKB.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Lyase; Pyridoxal phosphate.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8743570"
FT   CHAIN           2..326
FT                   /note="Phenylserine dehydratase"
FT                   /id="PRO_0000076220"
SQ   SEQUENCE   326 AA;  34482 MW;  B9C13A23844F52BA CRC64;
     MTQLDTTTLP DLSAIAGLRA RLKQWVRTTP VFDKTDFEPV PGTAVNFKLE LLQASGTFKA
     RGAFSNLLAL DDDQRAAGVT CVSAGNHAVG VAYAAMRLGI PAKVVMIKTA SPARVALCRQ
     YGAEVVLAEN GQTAFDTVHR IESEEGRFFV HPFNGYRTVL GTATLGHEWL EQAGALDAVI
     VPIGGGGLMA GVSTAVKLLA PQCQVIGVEP EGADAMHRSF ETGGPVKMGS MQSIADSLMA
     PHTEQYSYEL CRRNVDRLVK VSDDELRAAM RLLFDQLKLA TEPACATATA ALVGGLKAEL
     AGKRVGVLLC GTNTDAATFA RHLGLG