ID   DCYD_YERE8              Reviewed;         330 AA.
AC   A1JSN4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
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}; OrderedLocusNames=YE2517;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
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; AM286415; CAL12560.1; -; Genomic_DNA.
DR   RefSeq; WP_011816587.1; NC_008800.1.
DR   RefSeq; YP_001006724.1; NC_008800.1.
DR   AlphaFoldDB; A1JSN4; -.
DR   SMR; A1JSN4; -.
DR   STRING; 393305.YE2517; -.
DR   EnsemblBacteria; CAL12560; CAL12560; YE2517.
DR   KEGG; yen:YE2517; -.
DR   PATRIC; fig|393305.7.peg.2671; -.
DR   eggNOG; COG2515; Bacteria.
DR   HOGENOM; CLU_048897_1_0_6; -.
DR   OMA; LVQEKWV; -.
DR   Proteomes; UP000000642; 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   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; PLP-dep.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   PANTHER; PTHR43780; PTHR43780; 1.
DR   Pfam; PF00291; PALP; 1.
DR   PIRSF; PIRSF006278; ACCD_DCysDesulf; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR01275; ACC_deam_rel; 1.
PE   3: Inferred from homology;
KW   Lyase; Pyridoxal phosphate.
FT   CHAIN           1..330
FT                   /note="D-cysteine desulfhydrase"
FT                   /id="PRO_1000064269"
FT   MOD_RES         52
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01045"
SQ   SEQUENCE   330 AA;  35196 MW;  6510478456C33701 CRC64;
     MTLQHKLAQF PRLDLVGNAT PLEKLSRLSD YLGREIYIKR DDVTPLALGG NKLRKLEFLA
     ADALRQGADT LVTAGAIQSN HVRQTAAVAA KLGLHCVALL ENPIGTSQEN YLTNGNRLLL
     DLFNVEVVMC DGLHDPNQQL AELATRIEAQ GFRPYVVPVG GSNAFGALGY VQCALEIAAQ
     SAGNVTFSSV VVASGSAGTH AGLAVGLQQL LPQTELIGVT VSRKAEEQRP KVIHIQQELA
     TSLGVTSGPA DITLWDDYFA PQYGMPNEEG LAAIGLLARL EGILLDPVYT GKAMAGLLDG
     LEQKKFRDDG PILFIHTGGA PALFAYHPQV