ID   SDHD_VIBCM              Reviewed;         441 AA.
AC   C3LWD9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 57.
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=VCM66_A0834;
OS   Vibrio cholerae serotype O1 (strain M66-2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=579112;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M66-2;
RX   PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA   Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA   Wang W., Wang J., Qian W., Li D., Wang L.;
RT   "A recalibrated molecular clock and independent origins for the cholera
RT   pandemic clones.";
RL   PLoS ONE 3:E4053-E4053(2008).
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; CP001234; ACP07794.1; -; Genomic_DNA.
DR   RefSeq; WP_001885353.1; NC_012580.1.
DR   AlphaFoldDB; C3LWD9; -.
DR   SMR; C3LWD9; -.
DR   EnsemblBacteria; ACP07794; ACP07794; VCM66_A0834.
DR   GeneID; 57742247; -.
DR   KEGG; vcm:VCM66_A0834; -.
DR   HOGENOM; CLU_035707_0_0_6; -.
DR   OMA; ESDPNCF; -.
DR   Proteomes; UP000001217; Chromosome II.
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..441
FT                   /note="Probable D-serine dehydratase"
FT                   /id="PRO_1000149393"
FT   MOD_RES         118
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ   SEQUENCE   441 AA;  48333 MW;  73AC3ED27F7348AB CRC64;
     MMTINIEQLT EQYPLVKELI ELKEVSWFNP SITRLEEGLS YVGLGSEDIQ DASQRLKRFA
     PYLAKAFPET AKTNGIIESE VVPISEMQSV LEREYDTPIQ GRLLLKKDSH LPISGSIKAR
     GGIYEVLTHA EKLAIEAGLL TESDDYSKLL NEEFRDFFKR FSIAVGSTGN LGMSIGIMSA
     KLGFSVSVHM SADARAWKKN RLRALGVNVI EYAQDYGVAV AQGRKEAEND PTCFFIDDEN
     SQTLFLGYSV AGERLKKQFD EKGIVVDAQH PLFVYLPCGV GGGPGGVAFG LKMAFGDNVH
     CIFAEPTHSP CMMLGVHTGL HDAISVQDIG IDNITAADGL AVGRASGFVG RAMERLLDGY
     LTISDERMYR LLGQLNEAEN IQLEPSALAG MIGPIVVTKS VEYRARMQFD DTVMGNATHL
     VWATGGGMVP AEEMDSYLKN R