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P59329 (DCYD_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:c2333
OrganismEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier199310 [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.

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_0000184514

Amino acid modifications

Modified residue511N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P59329 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: F7A9C7BE9F01FB02

FASTA32835,123
        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 VLATRVEAQG FRPYVIPVGG SNALGALGYV ESALEIAQQC 

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

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

       310        320 
QKRFKDEGPI LFIHTGGAPA LFAYHPHV 

« Hide

References

[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014075 Genomic DNA. Translation: AAN80792.1.
RefSeqNP_754225.1. NC_004431.1.

3D structure databases

ProteinModelPortalP59329.
SMRP59329. Positions 4-328.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING199310.c2333.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN80792; AAN80792; c2333.
GeneID1036963.
KEGGecc:c2333.
PATRIC18282553. VBIEscCol75197_2190.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000022459.
KOK05396.
OMATLWDDYF.
OrthoDBEOG6FBX0P.
ProtClustDBPRK03910.

Enzyme and pathway databases

BioCycECOL199310:C2333-MONOMER.

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_ECOL6
AccessionPrimary (citable) accession number: P59329
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2003
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 68 of the entry and version 2 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