ID   SDHD_ACIAC              Reviewed;         451 AA.
AC   A1TPW5;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   25-MAY-2022, entry version 74.
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=Aave_2428;
OS   Acidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=397945;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAC00-1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
RL   Submitted (DEC-2006) 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABM33003.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000512; ABM33003.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A1TPW5; -.
DR   SMR; A1TPW5; -.
DR   STRING; 397945.Aave_2428; -.
DR   EnsemblBacteria; ABM33003; ABM33003; Aave_2428.
DR   KEGG; aav:Aave_2428; -.
DR   eggNOG; COG3048; Bacteria.
DR   HOGENOM; CLU_035707_0_0_4; -.
DR   Proteomes; UP000002596; 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; 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.
PE   3: Inferred from homology;
KW   Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..451
FT                   /note="Probable D-serine dehydratase"
FT                   /id="PRO_0000291716"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         118
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01030"
SQ   SEQUENCE   451 AA;  47903 MW;  36C0959FABC45AAD CRC64;
     MPGRTRPSCR LAITFTPRPD SATPRAGRAA PATGRRSNRS RSTLSATASP MPRRPHRIRS
     LGLLDRRDNY LDMLRTGGGI ESPLIEAGAL SDAMGLEPGC GRLWIKADHG LPVAGSIKAR
     GGIHEVLEFA ETLAVREGLL SPGQDCRVLA EPAAREVFGR HQVAVGSTGN LGLSIGVAAS
     ALGFRAAVHM SADAKEWKKE RLRRRGVEVV EHAGDYERAV AAGRSQAQAD PFSHFVDDER
     SLSLLLGYSA AALHLRGQLA EQGIVVDAKH PLFVYLPCGV GGAPAGITFG LRQLLGPHVH
     CFFAEPVQSP CFLVQMAAPA GTHPSVYDLG LTNRTEADGL AVPRASLLAA GLMQPLLSGI
     FTVRDDTLFE HLVRVLDATG ERIEPSAAAG FSGPALLTGS DGGRLWLRAQ GLDVQLPQAT
     HLVWTTGGLF VPEAEHQRFE ARGRSLLEAA A