ID   SDHD_BACC7              Reviewed;         443 AA.
AC   B7HMG6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 59.
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=BCAH187_A1907;
OS   Bacillus cereus (strain AH187).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405534;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AH187;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B.,
RA   Okstad O.A., Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus AH187.";
RL   Submitted (OCT-2008) 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; CP001177; ACJ80043.1; -; Genomic_DNA.
DR   RefSeq; WP_000675897.1; NC_011658.1.
DR   AlphaFoldDB; B7HMG6; -.
DR   SMR; B7HMG6; -.
DR   PRIDE; B7HMG6; -.
DR   EnsemblBacteria; ACJ80043; ACJ80043; BCAH187_A1907.
DR   KEGG; bcr:BCAH187_A1907; -.
DR   HOGENOM; CLU_035707_0_0_9; -.
DR   OMA; ESDPNCF; -.
DR   OrthoDB; 912282at2; -.
DR   Proteomes; UP000002214; 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..443
FT                   /note="Probable D-serine dehydratase"
FT                   /id="PRO_1000135757"
FT   MOD_RES         116
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ   SEQUENCE   443 AA;  49106 MW;  85090F5CC9B40034 CRC64;
     MKGIEKLKEG YPLLNKLIAT EEVFWVNPNM EKYETAIKDS PLSEENVKDA EERLKRFASY
     IAKVFPETKE TKGIIESPLL KIPSMKQALE KHYKQPILGE LLLKCDSHLP ISGSIKARGG
     IYEVLKHAEQ LALQHGMLTE EDDYSILDSD TCREFFAKYS IAVGSTGNLG LSIGIMSAKL
     GFNVTVHMSA DAKQWKKDLL RSKGVNVIEY EADYSKAVKE GRQQADTDPS CYFVDDENSH
     DLFLGYAVAA SRLQKQLEEL EIVVDEEHPL FVYLPCGVGG GPGGVAFGLK LLYKDNVHCF
     FAEPTHSPCM LLGLMTGLHD KIAVQDIGID NVTDADGLAV GRPSGFVGKT MEPFLSGNYT
     VSDEELYRLL KELADTENIY LEPSALAGMI GPVKVCKEDA YLQEQQLMKE MKKGTHIVWG
     TGGSMVPEDV INGYYKTGER LTI