ID DCYD_SALCH Reviewed; 328 AA. AC Q57N48; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2005, sequence version 1. DT 27-MAR-2024, entry version 91. 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=SCH_1957; OS Salmonella choleraesuis (strain SC-B67). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=321314; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SC-B67; RX PubMed=15781495; DOI=10.1093/nar/gki297; RA Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S., RA Lee Y.-S.; RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly RT invasive and resistant zoonotic pathogen."; RL Nucleic Acids Res. 33:1690-1698(2005). 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}. 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; AE017220; AAX65863.1; -; Genomic_DNA. DR RefSeq; WP_001540272.1; NC_006905.1. DR AlphaFoldDB; Q57N48; -. DR SMR; Q57N48; -. DR KEGG; sec:SCH_1957; -. DR HOGENOM; CLU_048897_1_0_6; -. DR Proteomes; UP000000538; 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_1000064264" FT MOD_RES 51 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01045" SQ SEQUENCE 328 AA; 34863 MW; 9CEB4AF7961F84D8 CRC64; MPLHHLTRFP RLELIGAPTP LEYLPRLSDY LGREIYIKRD DVTPIAMGGN KLRKLEFLVA DALREGADTL ITAGAIQSNH VRQTAAVAAK LGLHCVALLE NPIGTTAENY LTNGNRLLLD LFNTQIEMCD ALTDPDAQLQ TLATRIEAQG FRPYVIPVGG SSALGAMGYV ESALEIAQQC AEVVGLSSVV VASGSAGTHA GLAVGLEHLM PDVELIGVTV SRSVAEQKPR VISLQQAIAG QLALTATADI HLWDDYFAPG YGVPNDAGME AVKLLASLEG VLLDPVYTGK AMAGLIDGIS QKRFNDDGPI LFIHTGGAPA LFAYHPHV //