ID   SDHD_RHIE6              Reviewed;         448 AA.
AC   B3PYT5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 69.
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};
GN   OrderedLocusNames=RHECIAT_CH0002054;
OS   Rhizobium etli (strain CIAT 652).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=491916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIAT 652;
RA   Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P.,
RA   Hernandez-Gonzalez I.L., Fernandez J.L., Diaz R., Flores M., Mora J.,
RA   Palacios R., Davila G.;
RT   "Genome diversity and DNA divergence of Rhizobium etli.";
RL   Submitted (APR-2008) 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; CP001074; ACE91014.1; -; Genomic_DNA.
DR   RefSeq; WP_012483704.1; NC_010994.1.
DR   AlphaFoldDB; B3PYT5; -.
DR   SMR; B3PYT5; -.
DR   EnsemblBacteria; ACE91014; ACE91014; RHECIAT_CH0002054.
DR   KEGG; rec:RHECIAT_CH0002054; -.
DR   eggNOG; COG3048; Bacteria.
DR   HOGENOM; CLU_035707_0_0_5; -.
DR   OMA; ESDPNCF; -.
DR   Proteomes; UP000008817; 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..448
FT                   /note="Probable D-serine dehydratase"
FT                   /id="PRO_1000149389"
FT   MOD_RES         111
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ   SEQUENCE   448 AA;  48925 MW;  C774874FFA2A7688 CRC64;
     MNTILPSDPA RDDVLAGRPT LWLNPSYRKQ AIDTSDLPVS PADVASARQN WQRLAPLLAE
     CFPELKDTGG DIRSELVELK ELREALGYRT REFGNVFIKA DSHLPVAGSI KARGGVYEVF
     LFADSLARQK GVLVDGEDIR KLATEEARSL FSGYTVAVGS TGNLGLSVGI AARALGFKAT
     VHMSSDAKAW KVERLRKLGV DVIQHEADYT TAVENARDIA DADPTIYFVD DEQSRHLFLG
     YSAAASELAS QLDERGITID EENPLFLYLP CGIGGAPGGV AFGAKAIFGD NVHAFFVEPV
     QSPCALVHMM SGKQELVSVY DVGLTNKTEA DGMAVARMSA FVAKVMREML AGVYTAADDD
     LFKLLRMAWI TQRQKLEPSA AAALLGPDFL LRHKEGRRFQ TLNVIEEKMS QATHVLWTTG
     GSFVPEEQFQ HFLDQAESIA APSDRNDE