ID   SDHD_BACC2              Reviewed;         443 AA.
AC   B7IR88;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 62.
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=BCG9842_B3545;
OS   Bacillus cereus (strain G9842).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405531;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G9842;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus G9842.";
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; CP001186; ACK93239.1; -; Genomic_DNA.
DR   RefSeq; WP_000658548.1; NC_011772.1.
DR   AlphaFoldDB; B7IR88; -.
DR   SMR; B7IR88; -.
DR   EnsemblBacteria; ACK93239; ACK93239; BCG9842_B3545.
DR   KEGG; bcg:BCG9842_B3545; -.
DR   HOGENOM; CLU_035707_0_0_9; -.
DR   OMA; ESDPNCF; -.
DR   Proteomes; UP000006744; 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_1000135755"
FT   MOD_RES         116
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ   SEQUENCE   443 AA;  49143 MW;  BD0A03ED67B0118C CRC64;
     MKEIGALQAE YPLVNKLIAT KEVFWINPHI EKYERAIKDS PLNEENVKDA EERLKRFAPY
     IAKVFPETKG TNGIIESPLV KIPSMKEALE TNYKQTILGE LLLKCDSHLP ISGSIKARGG
     IYEVLKHAEQ LALQHGMLTE EDDYSILDSD TCREFFSKYS IAVGSTGNLG LSIGIMSANL
     GFNVTVHMSA DAKEWKKSLL RSKGVNVIEY EDDYSKAVEE GRRQADADPS CYFVDDENSH
     DLFLGYSVAA SRLQKQLEEL EVVVDEDHPL FVYLPCGVGG GPGGVAFGLK LLYKDNVHCF
     FAEPTHSPCM LLGLMTGLHD KIAVQDIGID NVTDADGLAV GRPSGFVGKT MEPFLSGNYT
     VNDEELYRLL KELADTENIY LEPSALAGMI GPVKVCKEDE YLQKQQLTEK VKKGTHIVWG
     TGGSMVPKDV MNEYYRKGLE LTI