ID   SDHD_STAS1              Reviewed;         433 AA.
AC   Q4A041;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 95.
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=SSP0432;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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   -!- SIMILARITY: Belongs to the serine/threonine dehydratase family. DsdA
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01030}.
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DR   EMBL; AP008934; BAE17577.1; -; Genomic_DNA.
DR   RefSeq; WP_011302399.1; NZ_MTGA01000036.1.
DR   AlphaFoldDB; Q4A041; -.
DR   SMR; Q4A041; -.
DR   STRING; 342451.SSP0432; -.
DR   EnsemblBacteria; BAE17577; BAE17577; SSP0432.
DR   KEGG; ssp:SSP0432; -.
DR   PATRIC; fig|342451.11.peg.437; -.
DR   eggNOG; COG3048; Bacteria.
DR   HOGENOM; CLU_035707_0_0_9; -.
DR   OMA; ESDPNCF; -.
DR   OrthoDB; 912282at2; -.
DR   BRENDA; 4.3.1.18; 5880.
DR   Proteomes; UP000006371; 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..433
FT                   /note="Probable D-serine dehydratase"
FT                   /id="PRO_0000291745"
FT   MOD_RES         112
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ   SEQUENCE   433 AA;  48000 MW;  FFE3D605DD45A407 CRC64;
     MNDLATLKQD FPLIDSMQNY KPIFWENPNF RKPASLTFTL KDMEDAAQRL ERFSSYISTV
     FPETENNHGL IESPLKHIPF MQNTLTNIES LPIEGKLWLK CDSHLAISGS IKARGGIYEV
     LKLAETIAMQ DGDLKETADY RVLAEQKYQD LFSKYNVAVG STGNLGLSIG IMSAKLGFKV
     TVHMSTDARQ WKKDLLRSRG VEVIEHQSDY QYAVAEGRKH AENDPTCHFV DDEGSSDLFL
     GYTVAALRLK AQLAAENIQI DAEHPLFVYI PCGVGGGPGG VTFGLKQVFG EHVYCIFTEP
     THAPCMLLGM MTQLHDKISV KDIGIDGNTD ADGLAVARPS RLVGQIMNTL LYGIQTVSDS
     EMYRYLYLLS EKEDIFIEPS AASGFAGIKS AITLAKQQGI QMNQANHIVW ATGGNMVPKE
     EMLKYVNHGK SCL