ID   SDHD_BURP0              Reviewed;         445 AA.
AC   A3P975;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
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};
GN   OrderedLocusNames=BURPS1106A_A2856;
OS   Burkholderia pseudomallei (strain 1106a).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=357348;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1106a;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
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; CP000573; ABN93427.1; -; Genomic_DNA.
DR   RefSeq; WP_004537039.1; NC_009078.1.
DR   AlphaFoldDB; A3P975; -.
DR   SMR; A3P975; -.
DR   EnsemblBacteria; ABN93427; ABN93427; BURPS1106A_A2856.
DR   GeneID; 56531789; -.
DR   KEGG; bpl:BURPS1106A_A2856; -.
DR   HOGENOM; CLU_035707_0_0_4; -.
DR   OMA; ESDPNCF; -.
DR   Proteomes; UP000006738; 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..445
FT                   /note="Probable D-serine dehydratase"
FT                   /id="PRO_1000063708"
FT   MOD_RES         111
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ   SEQUENCE   445 AA;  46348 MW;  B1E0A9AF6C20359F CRC64;
     MPVGRSLSLD PNLLAQLQSH SPTLWLNPHQ GMPLPDFAPT AADLADADAR LRRCAGLLAE
     LFAELRPSGG LIASPLQPAE PLKRAARAGH AQAGAWYVKR DDVLPVAGSI KARGGFHEVL
     ALAESIAERH GLAGADTDRR ALASGAARAR FARHTVMVGS TGNLGLSIGM LASALGFRTV
     VHMSADAKAW KKARLRTRGV EVVEHAGDYA KAVDAGRRQA AGMPCCHFVD DEGSRMLFLG
     YATAAAELAA QLAQAGRPVD ARHPLFVHLP CGVGGAPGGI VYGLKALYGE HVHAFVAEPT
     ASPCVLVQLA GDAAHPRSVY DIGLDNRTEA DGLAVAQASP LAAALLRAQA AGAFTVDDRQ
     LFAHLLDARE RLGIDLEPSA AAAFGGPAWI AGSDAGRAYL RGRGIDPDAA THVIWATGGS
     LVPAQEHRRF QAHARAQRQV GGAGA