ID   SDHD_DESHY              Reviewed;         444 AA.
AC   Q24WR0;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=DSY1743;
OS   Desulfitobacterium hafniense (strain Y51).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=138119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y51;
RX   PubMed=16513756; DOI=10.1128/jb.188.6.2262-2274.2006;
RA   Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA   Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT   "Complete genome sequence of the dehalorespiring bacterium
RT   Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT   ethenogenes 195.";
RL   J. Bacteriol. 188:2262-2274(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; AP008230; BAE83532.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q24WR0; -.
DR   SMR; Q24WR0; -.
DR   STRING; 138119.DSY1743; -.
DR   EnsemblBacteria; BAE83532; BAE83532; DSY1743.
DR   KEGG; dsy:DSY1743; -.
DR   eggNOG; COG3048; Bacteria.
DR   HOGENOM; CLU_035707_0_0_9; -.
DR   OMA; ESDPNCF; -.
DR   Proteomes; UP000001946; 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..444
FT                   /note="Probable D-serine dehydratase"
FT                   /id="PRO_0000291725"
FT   MOD_RES         118
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ   SEQUENCE   444 AA;  48903 MW;  95D265ED968BFB97 CRC64;
     MTGKSPEVIP HTPVVQDLRA AREIFWINPH YRATKEFKEA QFGISLSDIH DAEERLRRFA
     PYLAKAFPET QPAQGLIESP IVPIKRMQSY LESRYGVQIP GDIWLKCDHQ LPISGSIKAR
     GGIYEVLKHA EETLIKQGLL TREDDYARLK DSSFRDVLSH YKIAVGSTGN LGLSIGVMGA
     ELGFKVTVHM SADAKGWKKA LLRSKGVEVI EYTSDYSKAV EEGRRQAEGD SRCHFIDDEN
     SRDLFLGYAV AGLRLKEQLE KLNRKVDADH PLFVYLPCGV GGGPGGVTFG LKQVFQEHVH
     CFFAEPTHSP CMVLGLATGL HDGIAVQDIG LDNKTEADGL AVGRASRFVG KIMAGLLSGA
     FTVEDAELFR LLQALDHAEG IQCEPSALAG MAGPARLLLC KEGLQYIREH RLEEGLKRGT
     HLIWATGGSL VPVEVMKDYL SRGK