ID   SDHD_SALCH              Reviewed;         440 AA.
AC   Q57I32;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=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=SCH_3724;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(2005).
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   -!- SUBUNIT: Monomer. {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; AE017220; AAX67630.1; -; Genomic_DNA.
DR   RefSeq; WP_000427990.1; NC_006905.1.
DR   AlphaFoldDB; Q57I32; -.
DR   SMR; Q57I32; -.
DR   EnsemblBacteria; AAX67630; AAX67630; SCH_3724.
DR   KEGG; sec:SCH_3724; -.
DR   HOGENOM; CLU_035707_0_0_6; -.
DR   OMA; ESDPNCF; -.
DR   Proteomes; UP000000538; 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..440
FT                   /note="D-serine dehydratase"
FT                   /id="PRO_0000291739"
FT   MOD_RES         116
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ   SEQUENCE   440 AA;  47354 MW;  2861A8CAAC3E9E41 CRC64;
     MENIQKLIAR YPLVEDLVAL KETTWFNPGA TSLAQGLPYV GLTEQDVNAA HDRLARFAPY
     LAKAFPQTAA AGGMIESDVV AIPAMQKRLE KEYGQTIDGE MLLKKDSHLA ISGSIKARGG
     IYEVLTHAEK LALEAGLLTT DDDYSVLLSP EFKQFFSQYS IAVGSTGNLG LSIGIMSACI
     GFKVTVHMSA DARAWKKAKL RSHGVTVVEY EDDYGVAVEQ GRKAAQSDPN CFFIDDENSR
     TLFLGYAVAG QRLKAQFAQQ GRVVDASHPL FVYLPCGVGG GPGGVAFGLK LAFGDNVHCF
     FAEPTHSPCM LLGVYTGLHD AISVQDIGID NLTAADGLAV GRASGFVGRA MERLLDGLYT
     LDDQTMYDML GWLAQEEGIR LEPSALAGMA GPQRICAAVA YQQRHGFSQT QLGNATHLVW
     ATGGGMVPED EMEQYLAKGR