DCYD_ECODH
ID DCYD_ECODH Reviewed; 328 AA.
AC B1X677;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=ECDH10B_2060;
OS Escherichia coli (strain K12 / DH10B).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=316385;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / DH10B;
RX PubMed=18245285; DOI=10.1128/jb.01695-07;
RA Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA Posfai G., Weinstock G.M., Blattner F.R.;
RT "The complete genome sequence of Escherichia coli DH10B: insights into the
RT biology of a laboratory workhorse.";
RL J. Bacteriol. 190:2597-2606(2008).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000948; ACB03109.1; -; Genomic_DNA.
DR RefSeq; WP_001128215.1; NC_010473.1.
DR AlphaFoldDB; B1X677; -.
DR SMR; B1X677; -.
DR KEGG; ecd:ECDH10B_2060; -.
DR HOGENOM; CLU_048897_1_0_6; -.
DR OMA; LVQEKWV; -.
DR BioCyc; ECOL316385:ECDH10B_RS10550-MON; -.
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_1000136160"
FT MOD_RES 51
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01045"
SQ SEQUENCE 328 AA; 35153 MW; 4179DE645C0B32D8 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
ELELTASAEI LLWDDYFAPG YGVPNDEGME AVKLLARLEG ILLDPVYTGK AMAGLIDGIS
QKRFKDEGPI LFIHTGGAPA LFAYHPHV