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C4ZQJ7 (DCYD_ECOBW) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 32. 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:BWG_1728
OrganismEscherichia coli (strain K12 / MC4100 / BW2952) [Complete proteome] [HAMAP]
Taxonomic identifier595496 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length328 AA.
Sequence statusComplete.
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

Chain1 – 328328D-cysteine desulfhydrase HAMAP-Rule MF_01045
PRO_1000213420

Amino acid modifications

Modified residue511N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
C4ZQJ7 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: 4179DE645C0B32D8

FASTA32835,153
        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 
ELELTASAEI LLWDDYFAPG YGVPNDEGME AVKLLARLEG ILLDPVYTGK AMAGLIDGIS 

       310        320 
QKRFKDEGPI LFIHTGGAPA LFAYHPHV 

« Hide

References

[1]"Genomic sequencing reveals regulatory mutations and recombinational events in the widely used MC4100 lineage of Escherichia coli K-12."
Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R., Wang L.
J. Bacteriol. 191:4025-4029(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MC4100 / BW2952.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001396 Genomic DNA. Translation: ACR62738.1.
RefSeqYP_002926924.1. NC_012759.1.

3D structure databases

ProteinModelPortalC4ZQJ7.
SMRC4ZQJ7. Positions 7-328.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING595496.BWG_1728.

Proteomic databases

PRIDEC4ZQJ7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACR62738; ACR62738; BWG_1728.
GeneID7955728.
KEGGebw:BWG_1728.
PATRIC18272723. VBIEscCol60876_1891.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2515.
HOGENOMHOG000022459.
KOK05396.
OMATLWDDYF.
OrthoDBEOG6FBX0P.
ProtClustDBPRK03910.

Enzyme and pathway databases

BioCycECOL595496:GI18-1784-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_ECOBW
AccessionPrimary (citable) accession number: C4ZQJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: February 19, 2014
This is version 32 of the entry and version 1 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