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Q8XBC7 (DCYD_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
D-cysteine desulfhydrase

EC=4.4.1.15
Gene names
Name:dcyD
Ordered Locus Names:Z3008, ECs2657/ECs2658
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length328 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. It could be a defense mechanism against D-cysteine By similarity. HAMAP-Rule MF_01045

Catalytic activity

D-cysteine + H2O = H2S + NH3 + pyruvate. HAMAP-Rule MF_01045

Cofactor

Pyridoxal phosphate By similarity. HAMAP-Rule MF_01045

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01045

Sequence similarities

Belongs to the ACC deaminase/D-cysteine desulfhydrase family.

Sequence caution

The sequence AAG56934.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB36080.1 differs from that shown. Reason: Frameshift at position 139. Produces two separate ORFs.

The sequence BAB36081.1 differs from that shown. Reason: Frameshift at position 139. Produces two separate ORFs.

Ontologies

Keywords
   LigandPyridoxal phosphate
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processD-amino acid metabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionD-cysteine desulfhydrase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 328327D-cysteine desulfhydrase HAMAP-Rule MF_01045
PRO_0000184515

Amino acid modifications

Modified residue511N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8XBC7 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 59D6392CF3EC62D8

FASTA32835,181
        10         20         30         40         50         60 
MPLHNLTRFP RLEFIGAPTP LEYLPRFSDY LGREIFIKRD DVTPMAMGGN KLRKLEFLAA 

        70         80         90        100        110        120 
DALREGADTL ITAGAIQSNH VRQTAAVAAK LGLHCVALLE NPIGTTAENY LTNGNRLLLD 

       130        140        150        160        170        180 
LFNTQIEMCD ALTDPNAQLE ELATRVEAQG FRPYVIPVGG SNALGALGYV ESALEIAQQC 

       190        200        210        220        230        240 
EGAVNISSVV VASGSAGTHA GLAVGLEHLM PESELIGVTV SRSVADQLPK VVNLQQAIAK 

       250        260        270        280        290        300 
ELELTASVEI LLWDDYFAPG YGVPNDEGME AVKLLARLEG ILLDPVYTGK AMAGLIDGIS 

       310        320 
QKRFKDEGPI LFIHTGGAPA LFAYHPHV 

« Hide

References

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG56934.1. Different initiation.
BA000007 Genomic DNA. Translation: BAB36080.1. Frameshift.
BA000007 Genomic DNA. Translation: BAB36081.1. Frameshift.
PIRA90961.
B85809.
B90961.
RefSeqNP_288380.2. NC_002655.2.

3D structure databases

ProteinModelPortalQ8XBC7.
SMRQ8XBC7. Positions 4-327.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z3008.

Proteomic databases

PRIDEQ8XBC7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG56934; AAG56934; Z3008.
BAB36080; BAB36080; BAB36080.
BAB36081; BAB36081; BAB36081.
GeneID961917.
KEGGece:Z3008.
PATRIC18354700. VBIEscCol44059_2558.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000022459.
KOK05396.
OMAPYLVPIG.
OrthoDBEOG6FBX0P.

Family and domain databases

HAMAPMF_01045. D_Cys_desulfhydr.
InterProIPR027278. ACCD_DCysDesulf.
IPR005966. D-Cys_desShydrase.
IPR023702. D_Cys_desulphydr_bac.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]
PfamPF00291. PALP. 1 hit.
[Graphical view]
PIRSFPIRSF006278. ACCD_DCysDesulf. 1 hit.
SUPFAMSSF53686. SSF53686. 1 hit.
TIGRFAMsTIGR01275. ACC_deam_rel. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDCYD_ECO57
AccessionPrimary (citable) accession number: Q8XBC7
Secondary accession number(s): Q8X2H0, Q8X2H1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2003
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 68 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families