ID   SDHD_SINMW              Reviewed;         442 AA.
AC   A6UB95;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=Smed_2092;
OS   Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=366394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM419;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA   Richardson P.;
RT   "Complete sequence of Sinorhizobium medicae WSM419 chromosome.";
RL   Submitted (JUN-2007) 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; CP000738; ABR60925.1; -; Genomic_DNA.
DR   RefSeq; WP_011976222.1; NC_009636.1.
DR   RefSeq; YP_001327760.1; NC_009636.1.
DR   AlphaFoldDB; A6UB95; -.
DR   SMR; A6UB95; -.
DR   STRING; 366394.Smed_2092; -.
DR   EnsemblBacteria; ABR60925; ABR60925; Smed_2092.
DR   GeneID; 61613002; -.
DR   KEGG; smd:Smed_2092; -.
DR   PATRIC; fig|366394.8.peg.5250; -.
DR   eggNOG; COG3048; Bacteria.
DR   HOGENOM; CLU_035707_0_0_5; -.
DR   OMA; ESDPNCF; -.
DR   OrthoDB; 912282at2; -.
DR   Proteomes; UP000001108; 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; 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.
PE   3: Inferred from homology;
KW   Lyase; Pyridoxal phosphate.
FT   CHAIN           1..442
FT                   /note="Probable D-serine dehydratase"
FT                   /id="PRO_1000149392"
FT   MOD_RES         111
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ   SEQUENCE   442 AA;  47799 MW;  8BEDDDD4FDBCFDCF CRC64;
     MTLQLPNDPA RSDVLSARPT LWINSLYRDD AIGDTCLPLV PDQVDVAQSD WERLAPLLET
     CFPELKKTAG AIRSDLTELH ALREALGYGG GEFGRVFAKA DSALPVAGSI KARGGVYEVF
     VFAEELARRE GLIGDREDIR HLASAEARAF FSSYSIAVGS TGNLGLSVGV AARALGFEAT
     VHMSSDAKPW KVERLRKLGV KVVQHEADYT TAVENARSAA EDDPAVYFVD DEQSRRLFLG
     YSVAASELVD QLQTFGVAVD ADRPLFLYLP CGIGGAPGGV TYGAKKVFGD NAHCFFVEPV
     QSPCALVHMM SGSEELVSVY DVGLTNSTEA DGMAVARMSA FVATVMRNML AGVFTVDDAS
     LFRWLLLAHE VQGLRLEPSA AAGFAGPGFI VKHPQGRAFC ERLKLSDRLR QATHVVWTTG
     GSFVPQEQFD QFLEIAQASR SR