ID   SDHD_ACIAD              Reviewed;         441 AA.
AC   Q6FDC1;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=ACIAD1048;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR543861; CAG67937.1; -; Genomic_DNA.
DR   RefSeq; WP_004921695.1; NC_005966.1.
DR   AlphaFoldDB; Q6FDC1; -.
DR   SMR; Q6FDC1; -.
DR   STRING; 62977.ACIAD1048; -.
DR   EnsemblBacteria; CAG67937; CAG67937; ACIAD1048.
DR   GeneID; 45233491; -.
DR   KEGG; aci:ACIAD1048; -.
DR   eggNOG; COG3048; Bacteria.
DR   HOGENOM; CLU_035707_0_0_6; -.
DR   OMA; ESDPNCF; -.
DR   OrthoDB; 912282at2; -.
DR   BioCyc; ASP62977:ACIAD_RS04830-MON; -.
DR   Proteomes; UP000000430; 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; Reference proteome.
FT   CHAIN           1..441
FT                   /note="Probable D-serine dehydratase"
FT                   /id="PRO_0000185599"
FT   MOD_RES         117
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ   SEQUENCE   441 AA;  48568 MW;  F5D21C383C1FD3DC CRC64;
     MTTLNIQAIQ QDSLIKSLKN YEEIFWFQPE PTPIEQGLKR TSLTLADIQD AEARLTRFAP
     YLEKVFPELR STQGKIESEI VSIPTMQHDC SKRFAIEPNG TWWLKKDSHL PISGSIKARG
     GIYEVLAHAE KLALKAGLVT LQDNYSQLDS DQARQFFSNY QIAVGSTGNL GLSIGIMSAK
     LGFRVSVHMS ADARQWKKDK LRSLGVNVVE YASDYGVAVE QGRKAAESDP NCFFIDDENS
     TTLFLGYAVA GLRLKQQLID QNIQVDAEHP LFVYLPCGVG GGPGGVSFGL KHALGEHVHC
     IFAEPTHSPC MLLGVYTGLH DQICVADIGL DNATAADGLA VGRASGFVGR AMQDLIDGYY
     TISDQHLFEF IRLMDQTQSI QLEPSAVAGV LGIYHVNTNK SYQQAYHLNA IQLKNATHLI
     WATGGGMVPP NEMQKYLKQC E