ID   SDHD_POLNA              Reviewed;         455 AA.
AC   A1VWK8;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-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=Pnap_4614;
OS   Polaromonas naphthalenivorans (strain CJ2).
OG   Plasmid pPNAP04.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=365044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ2;
RX   PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA   Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT   "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT   tar-contaminated sediment, reveals physiological and metabolic versatility
RT   and evolution through extensive horizontal gene transfer.";
RL   Environ. Microbiol. 11:2253-2270(2009).
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; CP000533; ABM40036.1; -; Genomic_DNA.
DR   RefSeq; WP_011798407.1; NC_008760.1.
DR   AlphaFoldDB; A1VWK8; -.
DR   SMR; A1VWK8; -.
DR   EnsemblBacteria; ABM40036; ABM40036; Pnap_4614.
DR   KEGG; pna:Pnap_4614; -.
DR   HOGENOM; CLU_035707_0_0_4; -.
DR   OMA; ESDPNCF; -.
DR   OrthoDB; 912282at2; -.
DR   Proteomes; UP000000644; Plasmid pPNAP04.
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; Plasmid; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..455
FT                   /note="Probable D-serine dehydratase"
FT                   /id="PRO_0000291736"
FT   MOD_RES         119
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ   SEQUENCE   455 AA;  48460 MW;  03FEB2327E7F6927 CRC64;
     MRSIQSPSSH AAEQESFFSL AALQVGLPLM WASPRPSPNL PDKEDSSIGS ADVVRTGERL
     ARFAPLLAQL FPELEAAGGI IESDLLAAPR LQEALNMPAD TGTLLVKADH ALPIAGSIKA
     RGGIHEVLEH AETLALQHGL LASHEADYRV LAEPTARALF SRHQIAVGST GNLGLAIGVM
     AAALGFQAVV HMSADAKEWK KERLRKRGVT VVEHAGDYAK AVAAGRAAAE ADPRCHFVDD
     ERSLSLLLGY AAAAPRLARQ LVAQGRRVDA EHPLFVYLPC GVGGAPGGIA LGLSQIYGEH
     VHCFFAEPTR SPCFLVQMLA GTPELAHLGA HPSVYDLGLD NRTEADGLAV PRASVLAAEV
     VRPFLAGVYT VNDEALFRHL HLAATTEGFR IEPSAAACLP GPAMLMGTAE GRAYLQREQL
     EHHMARSTHI AWTTGGLFVP DDEYARFRVR GALTS