DCYD_SALTY
ID DCYD_SALTY Reviewed; 328 AA.
AC Q8ZNT7;
DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 102.
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=STM1953;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; AE006468; AAL20865.1; -; Genomic_DNA.
DR RefSeq; NP_460906.1; NC_003197.2.
DR RefSeq; WP_001128180.1; NC_003197.2.
DR PDB; 4D8T; X-ray; 2.28 A; A/B/C/D=1-328.
DR PDB; 4D8U; X-ray; 3.30 A; A/B/C/D/E/F/G/H=1-328.
DR PDB; 4D8W; X-ray; 2.01 A; A/B/C/D=1-328.
DR PDB; 4D92; X-ray; 2.22 A; A/B/C/D=1-328.
DR PDB; 4D96; X-ray; 2.09 A; A/B/C/D=1-328.
DR PDB; 4D97; X-ray; 1.77 A; A/B/C/D=1-328.
DR PDB; 4D99; X-ray; 2.01 A; A/B/C/D=1-328.
DR PDB; 4D9B; X-ray; 1.67 A; A/B/C/D=1-328.
DR PDB; 4D9C; X-ray; 1.97 A; A/B/C/D=1-328.
DR PDB; 4D9E; X-ray; 2.47 A; A/B/C/D=1-328.
DR PDB; 4D9F; X-ray; 2.61 A; A/B/C/D=1-328.
DR PDBsum; 4D8T; -.
DR PDBsum; 4D8U; -.
DR PDBsum; 4D8W; -.
DR PDBsum; 4D92; -.
DR PDBsum; 4D96; -.
DR PDBsum; 4D97; -.
DR PDBsum; 4D99; -.
DR PDBsum; 4D9B; -.
DR PDBsum; 4D9C; -.
DR PDBsum; 4D9E; -.
DR PDBsum; 4D9F; -.
DR AlphaFoldDB; Q8ZNT7; -.
DR SMR; Q8ZNT7; -.
DR STRING; 99287.STM1953; -.
DR PaxDb; Q8ZNT7; -.
DR EnsemblBacteria; AAL20865; AAL20865; STM1953.
DR GeneID; 1253474; -.
DR KEGG; stm:STM1953; -.
DR PATRIC; fig|99287.12.peg.2068; -.
DR HOGENOM; CLU_048897_1_0_6; -.
DR OMA; LVQEKWV; -.
DR PhylomeDB; Q8ZNT7; -.
DR BioCyc; SENT99287:STM1953-MON; -.
DR BRENDA; 4.4.1.15; 5542.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0019148; F:D-cysteine desulfhydrase activity; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; 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_0000184517"
FT MOD_RES 51
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01045"
FT HELIX 4..8
FT /evidence="ECO:0007829|PDB:4D9B"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:4D9B"
FT HELIX 25..31
FT /evidence="ECO:0007829|PDB:4D9B"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:4D9B"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:4D9B"
FT HELIX 51..64
FT /evidence="ECO:0007829|PDB:4D9B"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:4D9B"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:4D9B"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:4D9B"
FT HELIX 108..112
FT /evidence="ECO:0007829|PDB:4D9B"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:4D9B"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:4D9B"
FT HELIX 135..148
FT /evidence="ECO:0007829|PDB:4D9B"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:4D9B"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:4D9B"
FT HELIX 163..180
FT /evidence="ECO:0007829|PDB:4D9B"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:4D9B"
FT STRAND 188..196
FT /evidence="ECO:0007829|PDB:4D9B"
FT HELIX 197..209
FT /evidence="ECO:0007829|PDB:4D9B"
FT STRAND 213..222
FT /evidence="ECO:0007829|PDB:4D9B"
FT HELIX 224..241
FT /evidence="ECO:0007829|PDB:4D9B"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:4D9B"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:4D92"
FT HELIX 266..279
FT /evidence="ECO:0007829|PDB:4D9B"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:4D9B"
FT HELIX 288..301
FT /evidence="ECO:0007829|PDB:4D9B"
FT STRAND 304..308
FT /evidence="ECO:0007829|PDB:4D9B"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:4D9B"
FT HELIX 320..324
FT /evidence="ECO:0007829|PDB:4D9B"
SQ SEQUENCE 328 AA; 34911 MW; 417DBD984622496B CRC64;
MPLHHLTRFP RLEFIGAPTP LEYLPRLSDY LGREIYIKRD DVTPIAMGGN KLRKLEFLVA
DALREGADTL ITAGAIQSNH VRQTAAVAAK LGLHCVALLE NPIGTTAENY LTNGNRLLLD
LFNTQIEMCD ALTDPDAQLQ TLATRIEAQG FRPYVIPVGG SSALGAMGYV ESALEIAQQC
EEVVGLSSVV VASGSAGTHA GLAVGLEHLM PDVELIGVTV SRSVAEQKPK VIALQQAIAG
QLALTATADI HLWDDYFAPG YGVPNDAGME AVKLLASLEG VLLDPVYTGK AMAGLIDGIS
QKRFNDDGPI LFIHTGGAPA LFAYHPHV
