ID   SDHD_CUPPJ              Reviewed;         443 AA.
AC   Q46X58;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 90.
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=Reut_A2915;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
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; CP000090; AAZ62275.1; -; Genomic_DNA.
DR   RefSeq; WP_011299060.1; NC_007347.1.
DR   AlphaFoldDB; Q46X58; -.
DR   SMR; Q46X58; -.
DR   STRING; 264198.Reut_A2915; -.
DR   EnsemblBacteria; AAZ62275; AAZ62275; Reut_A2915.
DR   KEGG; reu:Reut_A2915; -.
DR   eggNOG; COG3048; Bacteria.
DR   HOGENOM; CLU_035707_0_0_4; -.
DR   OMA; ESDPNCF; -.
DR   OrthoDB; 912282at2; -.
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..443
FT                   /note="Probable D-serine dehydratase"
FT                   /id="PRO_0000291738"
FT   MOD_RES         106
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ   SEQUENCE   443 AA;  46704 MW;  5168A7877E95A088 CRC64;
     MVTLSLTPEL LAKLQSRQPL LWVNPRLGQP LPASAPSLEL IAAAEARLAR CAPLMAALFP
     ELASSHGQVE SQLMPATGLQ YALGEGAEGA WFIKRDDQLP TAGSIKARGG FHEVLAIAES
     IAIEHGMLDP DGDRRVLATE AARKLFSQYS VTVGSTGNLG LSIGVMAAAL GFDAVVHMSA
     DAKAWKKDRL RKRGVRVVEH EGDYAQAVAA GREQALGATR CHFVDDERSA LLFFGYAAAA
     RHLARQLAEA GRVVDAAHPL FVYLPCGVGG APGGITYGLK ALLGDHVHCF FAEPVASPCV
     LVQLASGSDD PVSVYDIGLD NRTDADGLAV GQASHLVSPL MASQLAGVFT VPDDQLYVQL
     LALKTSMGVE VEPSAAAGIG GPGWLRDSPE GRAYVRDHGL DMRDATHVIW ATGGSLVPRE
     ELHRFQAYAT ALAHVPGAMH KAA