ID   SDHD_VIBC1              Reviewed;         443 AA.
AC   A7MYG2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
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=VIBHAR_02609;
OS   Vibrio campbellii (strain ATCC BAA-1116).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=2902295;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1116 / BB120;
RG   The Vibrio harveyi Genome Sequencing Project;
RA   Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA   Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA   Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA   Wilson R.K.;
RL   Submitted (AUG-2007) 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; CP000789; ABU71570.1; -; Genomic_DNA.
DR   RefSeq; WP_012128225.1; NC_022269.1.
DR   AlphaFoldDB; A7MYG2; -.
DR   SMR; A7MYG2; -.
DR   EnsemblBacteria; ABU71570; ABU71570; VIBHAR_02609.
DR   KEGG; vha:VIBHAR_02609; -.
DR   PATRIC; fig|338187.25.peg.98; -.
DR   OMA; ESDPNCF; -.
DR   OrthoDB; 912282at2; -.
DR   Proteomes; UP000008152; Chromosome I.
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..443
FT                   /note="Probable D-serine dehydratase"
FT                   /id="PRO_1000063717"
FT   MOD_RES         118
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ   SEQUENCE   443 AA;  48649 MW;  DCDAB26E7620CA52 CRC64;
     MTTHNICALI TEFPLVKRLI DLEEVVWFNP NITTLEEGLP YVGLGAANIK DASERLKRFA
     PYLMKAFPET AASNGIIESN VVEIDKMKSC LEAQYGTQIL GRLMLKKDSH LPISGSIKAR
     GGIYEVLTHA ERLAIEAGLL NESDDYSKLF SEEFRQFFQQ YSIAVSSTGN LGMSIGIMSA
     KLGFSVSVHM SSDAREWKKN KLRSHGVNVV EYEQDYGVAV EQGRKEAEKD PTCFFIDDEN
     SQTLFLGYSV AGERLKQQFD DMGIIVDAEH PLFVYLPCGV GGGPGGVAFG LKMAFGDHVH
     CIFAEPTHSP CMLLGVHTGL HDDIAVQDLG IDNITAADGL AVGRASGFVG RAMERLLDGY
     YTITDERMYH HLGELSEQED IRLEPSALAG MMGAVHVSQD QAYQARMQFS EDKMNNAIHL
     VWATGGGMVP EAEMSAYLAK SGR