ID   DCYD_ECO57              Reviewed;         328 AA.
AC   Q8XBC7; Q8X2H0; Q8X2H1;
DT   22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 104.
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=Z3008, ECs2657/ECs2658;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAG56934.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAB36080.1; Type=Frameshift; Note=Produces two separate ORFs.; Evidence={ECO:0000305};
CC       Sequence=BAB36081.1; Type=Frameshift; Note=Produces two separate ORFs.; Evidence={ECO:0000305};
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DR   EMBL; AE005174; AAG56934.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BA000007; BAB36080.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; BA000007; BAB36081.1; ALT_FRAME; Genomic_DNA.
DR   PIR; A90961; A90961.
DR   PIR; B85809; B85809.
DR   PIR; B90961; B90961.
DR   RefSeq; WP_001128225.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; Q8XBC7; -.
DR   SMR; Q8XBC7; -.
DR   STRING; 155864.EDL933_2926; -.
DR   EnsemblBacteria; AAG56934; AAG56934; Z3008.
DR   KEGG; ece:Z3008; -.
DR   PATRIC; fig|83334.175.peg.615; -.
DR   eggNOG; COG2515; Bacteria.
DR   HOGENOM; CLU_163716_0_0_6; -.
DR   OMA; LVQEKWV; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..328
FT                   /note="D-cysteine desulfhydrase"
FT                   /id="PRO_0000184515"
FT   MOD_RES         51
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01045"
SQ   SEQUENCE   328 AA;  35181 MW;  59D6392CF3EC62D8 CRC64;
     MPLHNLTRFP RLEFIGAPTP LEYLPRFSDY LGREIFIKRD DVTPMAMGGN KLRKLEFLAA
     DALREGADTL ITAGAIQSNH VRQTAAVAAK LGLHCVALLE NPIGTTAENY LTNGNRLLLD
     LFNTQIEMCD ALTDPNAQLE ELATRVEAQG FRPYVIPVGG SNALGALGYV ESALEIAQQC
     EGAVNISSVV VASGSAGTHA GLAVGLEHLM PESELIGVTV SRSVADQLPK VVNLQQAIAK
     ELELTASVEI LLWDDYFAPG YGVPNDEGME AVKLLARLEG ILLDPVYTGK AMAGLIDGIS
     QKRFKDEGPI LFIHTGGAPA LFAYHPHV