ID   SDHD_BURTA              Reviewed;         444 AA.
AC   Q2T8Q2;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Probable D-serine dehydratase {ECO:0000255|HAMAP-Rule:MF_01030};
DE            EC=4.3.1.18 {ECO:0000255|HAMAP-Rule:MF_01030};
DE   AltName: Full=D-serine deaminase {ECO:0000255|HAMAP-Rule:MF_01030};
DE            Short=DSD {ECO:0000255|HAMAP-Rule:MF_01030};
GN   Name=dsdA {ECO:0000255|HAMAP-Rule:MF_01030}; OrderedLocusNames=BTH_II0245;
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS   E264).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:13977,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:35247; EC=4.3.1.18;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01030};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01030};
CC   -!- SIMILARITY: Belongs to the serine/threonine dehydratase family. DsdA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01030}.
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DR   EMBL; CP000085; ABC35346.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2T8Q2; -.
DR   SMR; Q2T8Q2; -.
DR   EnsemblBacteria; ABC35346; ABC35346; BTH_II0245.
DR   KEGG; bte:BTH_II0245; -.
DR   HOGENOM; CLU_035707_0_0_4; -.
DR   OMA; ESDPNCF; -.
DR   Proteomes; UP000001930; Chromosome II.
DR   GO; GO:0008721; F:D-serine ammonia-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016836; F:hydro-lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0046416; P:D-amino acid metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   HAMAP; MF_01030; D_Ser_dehydrat; 1.
DR   InterPro; IPR011780; D_Ser_am_lyase.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   PANTHER; PTHR48078:SF9; PTHR48078:SF9; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR02035; D_Ser_am_lyase; 1.
PE   3: Inferred from homology;
KW   Lyase; Pyridoxal phosphate.
FT   CHAIN           1..444
FT                   /note="Probable D-serine dehydratase"
FT                   /id="PRO_0000291722"
FT   MOD_RES         110
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ   SEQUENCE   444 AA;  46455 MW;  C32C1650AF6CB377 CRC64;
     MLMHDVRPLP LDPNLLAILQ AGSPTLWLNP HQGEPLPDFA PTAADLAEAG ARLHRCAGLL
     AELFPELRPL GGRIASPLQP AEPLKRADHA QAGAWFVKRD DALPVAGSIK ARGGFHEVLA
     LAESIAERHG LVSAGADRRA LASGEAHALF ARHTVMVGST GNLGLSIGML ASALGFRTVV
     HMSADAKAWK RARLRTRGVD VVEHAGDYAK AVDAGRRQAA GMPRCHFVDD EGSRMLFLGY
     ATAAAELAAQ LAQAGRPVDA RHPLFVHLPC GVGGAPGGIA YGLKARYGEH VHVFVAEPTA
     SPCVLVQLAS GGAHPVSVYD VGLDNRTEAD GLAVAQASHL AGPLLRAQAA GVFTVDDRQL
     FAHLLDARER LGIDLEPSAA AAFGGPAWLA GSEAGRAYLR GRGIVPEAAT HVIWATGGSL
     VPAEEHRRFQ ARACAQRRES GAGA