ID DCYD_SALNS Reviewed; 328 AA. AC B4SW60; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 1. DT 27-MAR-2024, entry version 72. 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=SNSL254_A2115; OS Salmonella newport (strain SL254). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=423368; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SL254; RX PubMed=21602358; DOI=10.1128/jb.00297-11; RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., RA Leclerc J.E., Ravel J., Cebula T.A.; RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for RT CRISPR-mediated adaptive sublineage evolution."; RL J. Bacteriol. 193:3556-3568(2011). 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; CP001113; ACF64770.1; -; Genomic_DNA. DR RefSeq; WP_001128188.1; NZ_CCMR01000003.1. DR AlphaFoldDB; B4SW60; -. DR SMR; B4SW60; -. DR KEGG; see:SNSL254_A2115; -. DR HOGENOM; CLU_048897_1_0_6; -. DR Proteomes; UP000008824; 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_1000136170" FT MOD_RES 51 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01045" SQ SEQUENCE 328 AA; 34877 MW; C37BFB7AE420ED2D CRC64; MPLHHLTRFP RLELIGAPTP LEYLPRLSDY LGREIYIKRD DVTPIAMGGN KLRKLEFLVA DALREGADTL ITAGAIQSNH VRQTAAVAAK LGLHCVALLE NPIGTTAENY LTNGNRLLLD LFNTQIEMCD ALTDPDAQLQ TLATRIEAQG FRPYVIPVGG SSALGAMGYV ESALEIAQQC EEVVGLSSVV VASGSAGTHA GLAVGLEHLM PDVELIGVTV SRSVAEQKPK VIALQQAIAG QLALTATADI HLWDDYFAPG YGVPNDAGME AVKLLASLEG VLLDPVYTGK AMAGLIDGIS QKRFNDDGPI LFIHTGGAPA LFAYHPHV //