DCYD_ECOLI
ID DCYD_ECOLI Reviewed; 328 AA.
AC P76316; O08478; O08479;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 153.
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}; Synonyms=yedO;
GN OrderedLocusNames=b1919, JW5313;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP PROTEIN SEQUENCE OF 2-9, CHARACTERIZATION, AND INDUCTION.
RC STRAIN=K37;
RX PubMed=11527960; DOI=10.1074/jbc.m102375200;
RA Soutourina J., Blanquet S., Plateau P.;
RT "Role of D-cysteine desulfhydrase in the adaptation of Escherichia coli to
RT D-cysteine.";
RL J. Biol. Chem. 276:40864-40872(2001).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=3908101; DOI=10.1111/j.1432-1033.1985.tb09335.x;
RA Nagasawa T., Ishii T., Kumagai H., Yamada H.;
RT "D-cysteine desulfhydrase of Escherichia coli. Purification and
RT characterization.";
RL Eur. J. Biochem. 153:541-551(1985).
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. Can also catalyze the degradation of 3-chloro-D-
CC alanine. {ECO:0000255|HAMAP-Rule:MF_01045, ECO:0000269|PubMed:3908101}.
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, ECO:0000269|PubMed:3908101};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01045,
CC ECO:0000269|PubMed:3908101};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:3908101};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius.
CC {ECO:0000269|PubMed:3908101};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:3908101}.
CC -!- INTERACTION:
CC P76316; P0A761: nanE; NbExp=2; IntAct=EBI-562060, EBI-561432;
CC -!- INDUCTION: By sulfate starvation. {ECO:0000269|PubMed:11527960}.
CC -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase
CC family. {ECO:0000255|HAMAP-Rule:MF_01045}.
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DR EMBL; U00096; AAC74986.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15739.2; -; Genomic_DNA.
DR PIR; D64955; D64955.
DR RefSeq; NP_416429.4; NC_000913.3.
DR RefSeq; WP_001128215.1; NZ_SSZK01000069.1.
DR AlphaFoldDB; P76316; -.
DR SMR; P76316; -.
DR BioGRID; 4260752; 9.
DR DIP; DIP-11847N; -.
DR IntAct; P76316; 24.
DR STRING; 511145.b1919; -.
DR jPOST; P76316; -.
DR PaxDb; P76316; -.
DR PRIDE; P76316; -.
DR EnsemblBacteria; AAC74986; AAC74986; b1919.
DR EnsemblBacteria; BAA15739; BAA15739; BAA15739.
DR GeneID; 946831; -.
DR KEGG; ecj:JW5313; -.
DR KEGG; eco:b1919; -.
DR PATRIC; fig|1411691.4.peg.330; -.
DR EchoBASE; EB3792; -.
DR eggNOG; COG2515; Bacteria.
DR HOGENOM; CLU_048897_1_0_6; -.
DR InParanoid; P76316; -.
DR OMA; LVQEKWV; -.
DR PhylomeDB; P76316; -.
DR BioCyc; EcoCyc:DCYSDESULF-MON; -.
DR BioCyc; MetaCyc:DCYSDESULF-MON; -.
DR PRO; PR:P76316; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0019149; F:3-chloro-D-alanine dehydrochlorinase activity; IDA:EcoCyc.
DR GO; GO:0019148; F:D-cysteine desulfhydrase activity; IDA:EcoliWiki.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoCyc.
DR GO; GO:0010438; P:cellular response to sulfur starvation; IEP:EcoCyc.
DR GO; GO:0046416; P:D-amino acid metabolic process; IDA:EcoliWiki.
DR GO; GO:0019447; P:D-cysteine catabolic process; IMP:EcoCyc.
DR GO; GO:0006790; P:sulfur compound metabolic process; IDA:EcoliWiki.
DR GO; GO:0006791; P:sulfur utilization; IMP:EcoCyc.
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 Direct protein sequencing; Lyase; Pyridoxal phosphate; Reference proteome;
KW Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11527960"
FT CHAIN 2..328
FT /note="D-cysteine desulfhydrase"
FT /id="PRO_0000184513"
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
