ID   SDHD_BACC3              Reviewed;         446 AA.
AC   C1EPF1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 60.
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=BCA_1793;
OS   Bacillus cereus (strain 03BB102).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=572264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=03BB102;
RA   Dodson R.J., Jackson P., Munk A.C., Brettin T., Bruce D., Detter C.,
RA   Tapia R., Han C., Sutton G., Sims D.;
RT   "Genome sequence of Bacillus cereus 03BB102.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001407; ACO29992.1; -; Genomic_DNA.
DR   RefSeq; WP_000658357.1; NZ_CP009318.1.
DR   AlphaFoldDB; C1EPF1; -.
DR   SMR; C1EPF1; -.
DR   EnsemblBacteria; ACO29992; ACO29992; BCA_1793.
DR   KEGG; bcx:BCA_1793; -.
DR   PATRIC; fig|572264.18.peg.1735; -.
DR   OMA; ESDPNCF; -.
DR   Proteomes; UP000002210; Chromosome.
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..446
FT                   /note="Probable D-serine dehydratase"
FT                   /id="PRO_1000149385"
FT   MOD_RES         116
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ   SEQUENCE   446 AA;  49596 MW;  9B37C3878A194921 CRC64;
     MKEIEKLKEE YPLLNKLIET EEVLWVNPNM EKYETAIKDS PLSEENVKDA KERLKRFASY
     IAKVFPETKE TKGIIESPLL KIPSMKQALE KNYEQPILGE LLLKCDSHLP ISGSIKARGG
     IYEVLKHAEQ LALQHGMLTE EDDYSILDSD TCREFFAKYS IAVGSTGNLG LSIGIMSAKL
     GFNVTVHMSA DAKQWKKDLL RSKGVNVIEY EADYSKAVEE GRRQADADPS CYFVDDENSH
     DLFLGYAVAA SRLQKQLEEL EIIVDEEHPL FVYLPCGVGG GPGGVAFGLK LLYKDNVHCF
     FAEPTHSPCM LIGLMTGLHD KIAVQDIGID NVTDADGLAV GRPSGFVGKT MEPFLSGDYT
     VSDEELYRLL KELADTENIY LEPSALAGMI GPVRVCKEDA YLQKQQLMEK MQKGTHIVWG
     TGGSMVPEDV MNGYYKTGEA LTILEK