ID   DCYD_ECOUT              Reviewed;         328 AA.
AC   Q1RAM1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=UTI89_C2120;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(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; CP000243; ABE07593.1; -; Genomic_DNA.
DR   RefSeq; WP_001128237.1; NC_007946.1.
DR   AlphaFoldDB; Q1RAM1; -.
DR   SMR; Q1RAM1; -.
DR   EnsemblBacteria; ABE07593; ABE07593; UTI89_C2120.
DR   KEGG; eci:UTI89_C2120; -.
DR   HOGENOM; CLU_048897_1_0_6; -.
DR   OMA; LVQEKWV; -.
DR   Proteomes; UP000001952; 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..328
FT                   /note="D-cysteine desulfhydrase"
FT                   /id="PRO_1000064262"
FT   MOD_RES         51
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01045"
SQ   SEQUENCE   328 AA;  35183 MW;  1C05BF69317B2EA1 CRC64;
     MPLHNLTRFP RLEFIGAPTP LEYLPRFSDY LGREIFIKRD DVTPMAMGGN KLRKLEFLAA
     DALREGADTL ITAGAIQSNH VRQTAAVAAK LGLHCVALLE NPIGTTAENY LTNGNRLLLD
     LFNTQIEMCD ALTDPNTQLE ELATRVEAQG FRPYVIPVGG SNALGALGYV ESALEIAQQC
     EGAVNISSVV VASGSAGTHA GLAVGLEHLM PESELIGVTV SRSVADQLPK VVNLQQAIAK
     ELELTASAEI LLWDDYFAPG YGVPNDEGME AVKLLARLEG ILLDPVYTGK AMAGLIDGIS
     QKRFKDEGPI LFIHTGGAPA LFAYHPHV