DCYD_KLEP7
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 25-MAY-2022, entry version 70.
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; Proteobacteria; 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 EnsemblBacteria; ABR77840; ABR77840; KPN_02417.
DR KEGG; kpn:KPN_02417; -.
DR HOGENOM; CLU_048897_1_0_6; -.
DR OMA; LVQEKWV; -.
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 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 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