ID   SDHD_BACHK              Reviewed;         446 AA.
AC   Q6HKG3;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=BT9727_1631;
OS   Bacillus thuringiensis subsp. konkukian (strain 97-27).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=281309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=97-27;
RX   PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA   Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA   Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA   Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA   Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA   Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
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; AE017355; AAT63288.1; -; Genomic_DNA.
DR   RefSeq; WP_000658347.1; NC_005957.1.
DR   RefSeq; YP_035963.1; NC_005957.1.
DR   AlphaFoldDB; Q6HKG3; -.
DR   SMR; Q6HKG3; -.
DR   EnsemblBacteria; AAT63288; AAT63288; BT9727_1631.
DR   KEGG; btk:BT9727_1631; -.
DR   PATRIC; fig|281309.8.peg.1717; -.
DR   HOGENOM; CLU_035707_0_0_9; -.
DR   OMA; ESDPNCF; -.
DR   Proteomes; UP000001301; 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_0000185605"
FT   MOD_RES         116
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ   SEQUENCE   446 AA;  49453 MW;  29144A49497031AE CRC64;
     MKEIEKLKEE YPLLNKLIAT EEVFWVNPNM EKYETAIKDS PLSEENVKDA EERLKRFASY
     IAKVFPETKE TKGIIESPLL KIPSMKQALE KNYEQPILGE LLLKCDSHLP ISGSIKARGG
     IYEVLKHAEQ LALQHGMLTE EDNYAILDSD TCREFFATYS IAVGSTGNLG LSIGIMSAKL
     GFNVTVHMSA DAKQWKKDLL RSKGVNVIEY EADYSKAVEE GRRQADADPS CYFVDDENSH
     DLFLGYAVAA SRLQKQLEEL KIVVDEEHPL FVYLPCGVGG GPGGVAFGLK LLYKDNVHCF
     FAEPTHSPCM LIGLMTGLHD KIAVQDIGID NVTDADGLAV GRPSGFVGKT MEPFLSGNYT
     VSDEELYRLL KELADTENIY LEPSALAGMI GPVKVCKEDA YLQKQQLMEK VQKGTHIVWG
     TGGSMVPEDV MNGYYKTGEA LTILEK