DCYD_SHIFL
ID DCYD_SHIFL Reviewed; 328 AA.
AC P59330;
DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 111.
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=SF1962, S2058;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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=AAN43513.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAP17343.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005674; AAN43513.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE014073; AAP17343.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_707806.3; NC_004337.2.
DR RefSeq; WP_001128248.1; NZ_WPGW01000033.1.
DR AlphaFoldDB; P59330; -.
DR SMR; P59330; -.
DR STRING; 198214.SF1962; -.
DR EnsemblBacteria; AAN43513; AAN43513; SF1962.
DR EnsemblBacteria; AAP17343; AAP17343; S2058.
DR GeneID; 1025173; -.
DR GeneID; 58389819; -.
DR KEGG; sfl:SF1962; -.
DR KEGG; sfx:S2058; -.
DR PATRIC; fig|198214.7.peg.2342; -.
DR HOGENOM; CLU_048897_1_0_6; -.
DR OMA; LVQEKWV; -.
DR OrthoDB; 1714795at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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_0000184518"
FT MOD_RES 51
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01045"
SQ SEQUENCE 328 AA; 35167 MW; 2CB80214A65497D8 CRC64;
MPLHNLTRFP RLEFIGAPTP LEYLPRFSDY LGREIFIKRD EVTPMAMGGN KLRKLEFLAA
DALREGADTL ITAGAIQSNH VRQTAAVAAK LGLHCVALLE NPIGTTAENY LTNGNRLLLD
LFNTQIEMCD ALTDPNAQLE ELATRVEAQG FRPYVIPVGG SNALGALGYV ESALEIAQQC
EGAVNISSVV VASGSAGTHA GLAVGLEHLM PESELIGVTV SRSVADQLPK VVNLQQAIAK
ELELTASAEI LLWDDYFAPG YGVPNDEGME AVKLLARLEG ILLDPVYTGK AMAGLIDGIS
QKRFKDEGPI LFIHTGGAPA LFAYHPHV
