ID   SDHD_ACISJ              Reviewed;         451 AA.
AC   A1W838;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=Ajs_2250;
OS   Acidovorax sp. (strain JS42).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax; unclassified Acidovorax.
OX   NCBI_TaxID=232721;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS42;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of chromosome 1 of Acidovorax sp. JS42.";
RL   Submitted (DEC-2006) 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; CP000539; ABM42413.1; -; Genomic_DNA.
DR   RefSeq; WP_011805458.1; NC_008782.1.
DR   AlphaFoldDB; A1W838; -.
DR   SMR; A1W838; -.
DR   STRING; 232721.Ajs_2250; -.
DR   EnsemblBacteria; ABM42413; ABM42413; Ajs_2250.
DR   KEGG; ajs:Ajs_2250; -.
DR   eggNOG; COG3048; Bacteria.
DR   HOGENOM; CLU_035707_0_0_4; -.
DR   OMA; ESDPNCF; -.
DR   Proteomes; UP000000645; 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; Reference proteome.
FT   CHAIN           1..451
FT                   /note="Probable D-serine dehydratase"
FT                   /id="PRO_0000291717"
FT   MOD_RES         119
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ   SEQUENCE   451 AA;  47831 MW;  9045D39EB3F1718D CRC64;
     MPSVVSPQDH LQDDAPAAQL RRAEPCLWLN PHRQPIPAAR QAVAGDHISL DDTEKAAARF
     ARFAPLLEGV FPELQATGGV IESPLLPASS LHAAAGLVAG QGALWIKADH RLPVAGSIKA
     RGGIHEVLEL AERLALQHGL LTPQSDADDY RALANPAARA VFARYTVAVG STGNLGLSIG
     VAASALGFHA VVHMSADAKE WKKQRLRQRG VQVVEHAGDY EGAVAAGRAQ AAQDPFSHFV
     DDERSLSLLL GYSAAALHLR QQLRDAGIVV DAQHPLFVYL PCGVGGAPAG ITFGLRQVLG
     AHVHCFFAEP VQSPCFMVQM MAGQGAHPSV YDWGLTNRTE ADGLAVPRAS LPAAELMEPL
     LAGCFTVCDD TLFRQLVQVL DATGERIEPS AAAGLSGPGF LTGTETGRTW LHAQGLWPHL
     AQATHLVWTT GGLYVPPEAY ARFEERGRAL G