ID   SDHD_BURPS              Reviewed;         445 AA.
AC   Q63IF8;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=BPSS2116;
OS   Burkholderia pseudomallei (strain K96243).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=272560;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243;
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA   Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA   Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA   Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA   Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA   Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA   Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA   Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA   Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT   pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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; BX571966; CAH39596.1; -; Genomic_DNA.
DR   RefSeq; WP_004524797.1; NZ_CP009537.1.
DR   RefSeq; YP_112114.1; NC_006351.1.
DR   AlphaFoldDB; Q63IF8; -.
DR   SMR; Q63IF8; -.
DR   STRING; 272560.BPSS2116; -.
DR   EnsemblBacteria; CAH39596; CAH39596; BPSS2116.
DR   KEGG; bps:BPSS2116; -.
DR   PATRIC; fig|272560.51.peg.5662; -.
DR   eggNOG; COG3048; Bacteria.
DR   OMA; ESDPNCF; -.
DR   Proteomes; UP000000605; Chromosome 2.
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; Reference proteome.
FT   CHAIN           1..445
FT                   /note="Probable D-serine dehydratase"
FT                   /id="PRO_0000185609"
FT   MOD_RES         111
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ   SEQUENCE   445 AA;  46320 MW;  F0184C08A28ABAD6 CRC64;
     MPVGRSLSLD PNLLAQLQSH SPTLWLNPHQ GMPLPDFAPT AADLADADAR LRRCAGLLAE
     LFAELRPSGG LIASPLQPAE PLKRAARAGH AQAGAWYVKR DDALPVAGSI 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