ID   DCYD_SALPK              Reviewed;         328 AA.
AC   B5BGB4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   RecName: Full=D-cysteine desulfhydrase {ECO:0000255|HAMAP-Rule:MF_01045};
DE            EC=4.4.1.15 {ECO:0000255|HAMAP-Rule:MF_01045};
GN   Name=dcyD {ECO:0000255|HAMAP-Rule:MF_01045};
GN   OrderedLocusNames=SSPA0854;
OS   Salmonella paratyphi A (strain AKU_12601).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=554290;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AKU_12601;
RX   PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA   Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA   Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA   Mungall K., Dougan G., Parkhill J.;
RT   "Pseudogene accumulation in the evolutionary histories of Salmonella
RT   enterica serovars Paratyphi A and Typhi.";
RL   BMC Genomics 10:36-36(2009).
CC   -!- FUNCTION: Catalyzes the alpha,beta-elimination reaction of D-cysteine
CC       and of several D-cysteine derivatives. It could be a defense mechanism
CC       against D-cysteine. {ECO:0000255|HAMAP-Rule:MF_01045}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-cysteine + H2O = H(+) + hydrogen sulfide + NH4(+) +
CC         pyruvate; Xref=Rhea:RHEA:11268, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29919,
CC         ChEBI:CHEBI:35236; EC=4.4.1.15; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01045};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01045};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01045}.
CC   -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase
CC       family. {ECO:0000255|HAMAP-Rule:MF_01045}.
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DR   EMBL; FM200053; CAR58997.1; -; Genomic_DNA.
DR   RefSeq; WP_001128194.1; NC_011147.1.
DR   AlphaFoldDB; B5BGB4; -.
DR   SMR; B5BGB4; -.
DR   KEGG; sek:SSPA0854; -.
DR   HOGENOM; CLU_048897_1_0_6; -.
DR   Proteomes; UP000001869; Chromosome.
DR   GO; GO:0019148; F:D-cysteine desulfhydrase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046416; P:D-amino acid metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd06449; ACCD; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   HAMAP; MF_01045; D_Cys_desulfhydr; 1.
DR   InterPro; IPR027278; ACCD_DCysDesulf.
DR   InterPro; IPR005966; D-Cys_desShydrase.
DR   InterPro; IPR023702; D_Cys_desulphydr_bac.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR01275; ACC_deam_rel; 1.
DR   PANTHER; PTHR43780; 1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE-RELATED; 1.
DR   PANTHER; PTHR43780:SF2; 1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE-RELATED; 1.
DR   Pfam; PF00291; PALP; 1.
DR   PIRSF; PIRSF006278; ACCD_DCysDesulf; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE   3: Inferred from homology;
KW   Lyase; Pyridoxal phosphate.
FT   CHAIN           1..328
FT                   /note="D-cysteine desulfhydrase"
FT                   /id="PRO_1000136171"
FT   MOD_RES         51
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01045"
SQ   SEQUENCE   328 AA;  34889 MW;  EECC42CC46B5F25D CRC64;
     MPLHHLTRFP RLELIGAPTP LEYLPRLSDY PGREIYIKRD DVTPIAMGGN KLRKLEFLVA
     DALREGADTL ITAGAIQSNH VRQTAAVAAK LGLHCVALLE NPIGTTAENY LTNGNRLLLD
     LFNTQIEMCD VLTDPDAQLQ TLATRIEAQG FRPYVIPVGG SSALGAMGYV ESALEIAQQC
     EEVVGLSSVV VASGSAGTHA GLAVGLEHLM PDVELIGVTV SRSVAEQKPK VIALQQAIAG
     QLALTATADI HLWDDYFAPG YGVPNDAGME AVKLLASLEG VLLDPVYTGK AMAGLIDGIS
     QKRFNDDGPI LFIHTGGAPA LFAYHPHV
//