ID   SDHD_GEOSE              Reviewed;         459 AA.
AC   Q75TH5;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 52.
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}; Synonyms=GSB10;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=HTA462;
RX   PubMed=15168170; DOI=10.1007/s00792-004-0394-3;
RA   Takami H., Nishi S., Lu J., Shimamura S., Takaki Y.;
RT   "Genomic characterization of thermophilic Geobacillus species isolated from
RT   the deepest sea mud of the Mariana Trench.";
RL   Extremophiles 8:351-356(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; AB126616; BAD18303.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q75TH5; -.
DR   SMR; Q75TH5; -.
DR   PRIDE; Q75TH5; -.
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; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
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.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   3: Inferred from homology;
KW   Lyase; Pyridoxal phosphate.
FT   CHAIN           1..459
FT                   /note="Probable D-serine dehydratase"
FT                   /id="PRO_0000185607"
FT   MOD_RES         119
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ   SEQUENCE   459 AA;  51196 MW;  0A71BB1D9CA429D8 CRC64;
     MMTKNEIQKW VKEFPLLKTI MAAEEVFWRN PKYHAFAQAI RTIPLRERDV KEAEERLRRF
     APYIAKAFPE TRTAHGIIES PLVRISNMKQ RLEKMFQTNI EGELLLKCDS HLPISGSIKA
     RGGIYEVLKH AEDLALANGM ITIGDDYAVM DSEKFRQFFS RYSLVVGSTG NLGLSIGIIG
     AKLGFRVTVH MSADAKQWKK DLLRSKGVTV IEHLTDYNKV VEEARRQSAE DPTSYFIDDE
     NSIHLFLGYA VAAFRLKKQL EDMNITVDEN HPLFVYLPCG VGGGPGGVTF GLKLVYGDHV
     HCFFAEPTHS PCMLLGLMTG EHDRVSVQDF GLDNKTEADG LAVGRPSRLV GNMLENVISG
     VYTVDDSTLY RLLAAMVETE EIYLEPSALA GVAGPVRLFR DLAGQTYVEA NGLKEKMKNA
     THIGWATGGS MVPKDVMEAY YREGVRIETM TGNGFSEGR