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Entry: DCYD_ECOLI
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Original site: 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   27-MAR-2024, entry version 161.
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; Pseudomonadota; 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; 511145-b1919; -.
DR   EnsemblBacteria; AAC74986; AAC74986; b1919.
DR   GeneID; 75205835; -.
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; GIQSNHA; -.
DR   OrthoDB; 9801249at2; -.
DR   PhylomeDB; P76316; -.
DR   BioCyc; EcoCyc:DCYSDESULF-MONOMER; -.
DR   BioCyc; MetaCyc:DCYSDESULF-MONOMER; -.
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:0042803; F:protein homodimerization activity; IDA:EcoCyc.
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   CDD; cd06449; ACCD; 1.
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; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR01275; ACC_deam_rel; 1.
DR   PANTHER; PTHR43780; 1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE-RELATED; 1.
DR   PANTHER; PTHR43780:SF2; 1-AMINOCYCLOPROPANE-1-CARBOXYLATE DEAMINASE-RELATED; 1.
DR   Pfam; PF00291; PALP; 1.
DR   PIRSF; PIRSF006278; ACCD_DCysDesulf; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 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
//
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