ID   SDHD_PSEAB              Reviewed;         448 AA.
AC   Q02QJ1;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-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=PA14_20650;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA   Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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; CP000438; ABJ12608.1; -; Genomic_DNA.
DR   RefSeq; WP_003138263.1; NZ_CP034244.1.
DR   AlphaFoldDB; Q02QJ1; -.
DR   SMR; Q02QJ1; -.
DR   PRIDE; Q02QJ1; -.
DR   EnsemblBacteria; ABJ12608; ABJ12608; PA14_20650.
DR   KEGG; pau:PA14_20650; -.
DR   HOGENOM; CLU_035707_0_0_6; -.
DR   OMA; ESDPNCF; -.
DR   BioCyc; PAER208963:G1G74-1704-MON; -.
DR   Proteomes; UP000000653; 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..448
FT                   /note="Probable D-serine dehydratase"
FT                   /id="PRO_0000291737"
FT   MOD_RES         119
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ   SEQUENCE   448 AA;  48198 MW;  2C0A876135BEE3A9 CRC64;
     MILGTPKADW LAEFPRLADL IALRPSEWFN PAIAPSAEAL ADVGLGAADV ADASARLQRF
     APLIARLFPE TAASGGIIES DLVEVAAFHD ALRQHYAAEL PGRLWLKRDS HLPISGSIKA
     RGGIYEVLAH AERLALEHGL IGLDDDYSRL AEADCRAFFA RHRIAVGSTG NLGLSIGIIG
     AALGFQASVH MSADARQWKK DKLRAHGVTV VEYASDYSVA VEQGRREAAG DPYTHFVDDE
     NSRDLFLGYA VAAERLRGQL DAAGIRVDSE HPLFVHLPCG VGGGPGGVAF GLKLAFGDAV
     HCLFAEPTHS PCMFLGVYTG RHEQVSVQDF GIDNRTAADG LAVGRPSGFV GRAMQRLLDG
     YYTVDDDELF RLLALLERSQ GIRLEPSALA GAPGIARVTR EPQGYRERMG LTSARLANAT
     HLVWATGGGM VPETEMRAYL KRGRSLLD