ID   SDHD_ALKCK              Reviewed;         440 AA.
AC   Q5WGL6;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=ABC1954;
OS   Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16;
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT   K16.";
RL   Submitted (OCT-2003) 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; AP006627; BAD64489.1; -; Genomic_DNA.
DR   RefSeq; WP_011246797.1; NC_006582.1.
DR   AlphaFoldDB; Q5WGL6; -.
DR   SMR; Q5WGL6; -.
DR   STRING; 66692.ABC1954; -.
DR   EnsemblBacteria; BAD64489; BAD64489; ABC1954.
DR   KEGG; bcl:ABC1954; -.
DR   eggNOG; COG3048; Bacteria.
DR   HOGENOM; CLU_035707_0_0_9; -.
DR   OMA; ESDPNCF; -.
DR   OrthoDB; 912282at2; -.
DR   Proteomes; UP000001168; 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; Reference proteome.
FT   CHAIN           1..440
FT                   /note="Probable D-serine dehydratase"
FT                   /id="PRO_0000185606"
FT   MOD_RES         120
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ   SEQUENCE   440 AA;  48073 MW;  A1B080C37A644C6F CRC64;
     MDIAGKNREQ WLAAYPLLQQ IVLTKEVWWA NPNRQPASEG LARLSLKEED VKEAEQRLRR
     FAPYIASVFP ETKGAGGLIE SPLIDIPTMK HKLDQRFGQN VPGRLLLKGD HALPISGSIK
     ARGGIYEVLK HAESLLVDQQ ILTKQDDYSL IATDAVQSFF SSYAIVVGST GNLGLSIGII
     SAKLGFRVTV HMSDDAKQWK KDMLREKGVR VVEHSADYSK AVEEGRKESD ADPNSYFIDD
     EHSIDLFVGY AVAAFRLKEQ LQEKGIAVTK DQPLHVYLPC GVGGGPGGVA FGLKLVFGDA
     VRCFFAEPTH SPCMLIGMLT GKHQHISVQD FGIDNQTAAD GLAVGRPSGF VGRMMAPLLE
     GIYTIADPML YTLLADLADA EGLYLEPSAV AGLYGPVQLE KRGLYTDAAT HLVWATGGSM
     VPKEIMETDY QLGVNLRTEQ