ID   SDHD_ACIET              Reviewed;         451 AA.
AC   B9MIR7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 61.
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=Dtpsy_1624;
OS   Acidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Diaphorobacter.
OX   NCBI_TaxID=535289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TPSY;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Coates J.D.;
RT   "Complete sequence of Diaphorobacter sp. TPSY.";
RL   Submitted (JAN-2009) 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; CP001392; ACM33083.1; -; Genomic_DNA.
DR   RefSeq; WP_015913178.1; NC_011992.1.
DR   AlphaFoldDB; B9MIR7; -.
DR   SMR; B9MIR7; -.
DR   STRING; 535289.Dtpsy_1624; -.
DR   EnsemblBacteria; ACM33083; ACM33083; Dtpsy_1624.
DR   KEGG; dia:Dtpsy_1624; -.
DR   eggNOG; COG3048; Bacteria.
DR   HOGENOM; CLU_035707_0_0_4; -.
DR   OMA; ESDPNCF; -.
DR   OrthoDB; 912282at2; -.
DR   Proteomes; UP000000450; 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..451
FT                   /note="Probable D-serine dehydratase"
FT                   /id="PRO_1000149386"
FT   MOD_RES         119
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ   SEQUENCE   451 AA;  47810 MW;  7C1388F68229FA72 CRC64;
     MPSVVSPQDR LQDDAPAAQL RRAEPCLWLN PHRQPIPAAR QAVAGDHISL DDTKEAAARF
     ARFAPLLEGV FPELQATGGV IESPLLPASS LHAAAGLVAG QGALWIKADH RLPVAGSIKA
     RGGIHEVLEL AERLALQHGL LTPQSDADDY RALANPAARA VFARYTVAVG STGNLGLSIG
     VAASALGFHA VVHMSADAKE WKKQRLRQRG VQVVEHAGDY EGAVAAGRAQ AAQDPFSHFV
     DDERSLSLLL GYSAAALHLR QQLQDAGIAV DAQHPLFVYL PCGVGGAPAG ITFGLRQVLG
     AHVHCFFAEP VQSPCFMVQM MAGQGAHPSV YDWGLTNRTE ADGLAVPRAS LPAAELMEPL
     LSGCFTVCDD TLFRQLVQVL DATGERIEPS AAAGLSGPGF LTGTETGRTW LHAQGLWPHL
     AQATHLVWTT GGLYVPPEAY ARFEERGRAL G