ID   DCYD_KLEP7              Reviewed;         328 AA.
AC   A6TB69;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 76.
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=KPN78578_23790; ORFNames=KPN_02417;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000647; ABR77840.1; -; Genomic_DNA.
DR   RefSeq; WP_004180445.1; NC_009648.1.
DR   AlphaFoldDB; A6TB69; -.
DR   SMR; A6TB69; -.
DR   STRING; 272620.KPN_02417; -.
DR   PaxDb; 272620-KPN_02417; -.
DR   EnsemblBacteria; ABR77840; ABR77840; KPN_02417.
DR   KEGG; kpn:KPN_02417; -.
DR   HOGENOM; CLU_048897_1_0_6; -.
DR   Proteomes; UP000000265; 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_1000064263"
FT   MOD_RES         51
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01045"
SQ   SEQUENCE   328 AA;  34914 MW;  9FA7292775764144 CRC64;
     MSLQNLTRFP RLELIGAPTP LEYLPRLSDH LGREIFIKRD DTTPLAMGGN KLRKLEFLAA
     DALREGADTL ITAGAIQSNH VRQTAAVAAK LGLHCVALLE NPIGTRAENY LSNGNRLLLD
     LFNTQVEMCD ALTDPAAQLD ELATRIEAQG YRPYVIPVGG SNALGALGYV ESALEISQQC
     EDAVAISSVV VASGSAGTHA GLAVGLEQLM PQAELIGVTV SRSVADQLPK VVALQQAVAN
     SLELQAKAEI ILWDDYFAPG YGTPNEDGMA AVKLLAQLEG ILLDPVYTGK AMAGLIDGIT
     QKRFKDEGPI LFVHTGGAPA LFAYHPHL
//