DCYD_ECO8A
ID DCYD_ECO8A Reviewed; 328 AA.
AC B7M363;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-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}; OrderedLocusNames=ECIAI1_2004;
OS Escherichia coli O8 (strain IAI1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585034;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAI1;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928160; CAQ98855.1; -; Genomic_DNA.
DR RefSeq; WP_001128219.1; NC_011741.1.
DR AlphaFoldDB; B7M363; -.
DR SMR; B7M363; -.
DR GeneID; 66674191; -.
DR KEGG; ecr:ECIAI1_2004; -.
DR HOGENOM; CLU_048897_1_0_6; -.
DR OMA; LVQEKWV; -.
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_1000136159"
FT MOD_RES 51
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01045"
SQ SEQUENCE 328 AA; 35095 MW; 6C560E645C0B32DB 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 AMAGLIGGIS
QKRFKDEGPI LFIHTGGAPA LFAYHPHV