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B1LQT7 (DCYD_ECOSM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
D-cysteine desulfhydrase
EC=4.4.1.15
Gene names
Name:dcyD
Ordered Locus Names:EcSMS35_1263
OrganismEscherichia coli (strain SMS-3-5 / SECEC) [Complete proteome] [HAMAP]
Taxonomic identifier439855 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

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.

Subunit structure

Homodimer By similarity.

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: HAMAP

   Molecular_functionD-cysteine desulfhydrase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 328328D-cysteine desulfhydrase HAMAP-Rule MF_01045
PRO_1000136162

Amino acid modifications

Modified residue511N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B1LQT7 [UniParc].

Last modified April 29, 2008. 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]"Insights into the environmental resistance gene pool from the genome sequence of the multidrug-resistant environmental isolate Escherichia coli SMS-3-5."
Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C., Ravel J., Stepanauskas R.
J. Bacteriol. 190:6779-6794(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SMS-3-5 / SECEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000970 Genomic DNA. Translation: ACB19636.1.
RefSeqYP_001743324.1. NC_010498.1.

3D structure databases

ProteinModelPortalB1LQT7.
SMRB1LQT7. Positions 7-328.
ModBaseSearch...

Protein-protein interaction databases

STRING439855.EcSMS35_1263.

Proteomic databases

PRIDEB1LQT7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB19636; ACB19636; EcSMS35_1263.
GeneID6144001.
KEGGecm:EcSMS35_1263.
PATRIC18431393. VBIEscCol6161_1424.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2515.
HOGENOMHOG000022459.
KOK05396.
OMAPYLVPIG.
ProtClustDBPRK03910.

Enzyme and pathway databases

BioCycECOL439855:GHHB-4243-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. PyrdxlP-dep_enz_bsu. 1 hit.
TIGRFAMsTIGR01275. ACC_deam_rel. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDCYD_ECOSM
AccessionPrimary (citable) accession number: B1LQT7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: May 1, 2013
This is version 35 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

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