ID   SDHD_ECO81              Reviewed;         442 AA.
AC   B7MY25;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=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=ECED1_2813;
OS   Escherichia coli O81 (strain ED1a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ED1a;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(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   -!- SUBUNIT: Monomer. {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; CU928162; CAR08991.2; -; Genomic_DNA.
DR   RefSeq; WP_000426394.1; NC_011745.1.
DR   AlphaFoldDB; B7MY25; -.
DR   SMR; B7MY25; -.
DR   EnsemblBacteria; CAR08991; CAR08991; ECED1_2813.
DR   KEGG; ecq:ECED1_2813; -.
DR   HOGENOM; CLU_035707_0_0_6; -.
DR   OMA; ESDPNCF; -.
DR   Proteomes; UP000000748; 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; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
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.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   3: Inferred from homology;
KW   Lyase; Pyridoxal phosphate.
FT   CHAIN           1..442
FT                   /note="D-serine dehydratase"
FT                   /id="PRO_1000149388"
FT   MOD_RES         118
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ   SEQUENCE   442 AA;  47837 MW;  19AEB9B1CA573271 CRC64;
     MENAKMNSLI AQYPLVEDLV ALKETTWFNP GTTSLAEGLP YVGLTEQDVQ DAHARLSRFA
     PYLAKAFPET AAAGGIIESE LVAIPAMQKR LEKEYQQPIS GQLLLKKDSH LPISGSIKAR
     GGIYEVLAHA EKLALEAGLL TLEDDYSKLL SPEFKQFFSQ YSIAVGSTGN LGLSIGIMSA
     RIGFKVTVHM SADARAWKKA KLRSHGVTVV EYEQDYGVAV EEGRKAAQSD PNCFFIDDEN
     SRTLFLGYSV AGQRLKAQFA QQGRIVDADN PLFVYLPCGV GGGPGGVAFG LKLAFGDHVH
     CFFAEPTHSP CMLLGVHTGL HDQISVQDIG IDNLTAADGL AVGRASGFVG RAMERLLDGF
     YTLSDQTMYD MLGWLAQEEG IRLEPSALAG MAGPQRVCAS VSYQQLHGFS AEQLRNATHL
     VWATGGGMVP EEEMNQYLAK GR