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A9MU62 (DCYD_SALPB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 40. 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:SPAB_01203
OrganismSalmonella paratyphi B (strain ATCC BAA-1250 / SPB7) [Complete proteome] [HAMAP]
Taxonomic identifier1016998 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

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_1000084408

Amino acid modifications

Modified residue511N6-(pyridoxal phosphate)lysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A9MU62 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: C37BEBA08420ED2D

FASTA32834,851
        10         20         30         40         50         60 
MPLHHLTRFP RLELIGAPTP LEYLPRLSDY LGREIYIKRD DVTPIAMGGN KLRKLEFLVA 

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

       130        140        150        160        170        180 
LFNTQIEMCD ALTDPDAQLQ TLATRIEAQG FRPYVIPVGG SSALGAMGYV ESALEIAQQC 

       190        200        210        220        230        240 
EEVVGLSSVV VASGSAGTHA GLAVGLEHLM PDVELIGVTV SRSVAEQKPK VIALQQAIAG 

       250        260        270        280        290        300 
QLALTATADI HLWDDYFAPG YGVPNDAGME AVKLLASLEG VLLDPVYTGK AMAGLIDGIS 

       310        320 
QKRFNDDGPS LFIHTGGAPA LFAYHPHV 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000886 Genomic DNA. Translation: ABX66618.1.
RefSeqYP_001587451.1. NC_010102.1.

3D structure databases

ProteinModelPortalA9MU62.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272994.SPAB_01203.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX66618; ABX66618; SPAB_01203.
PATRIC18530242. VBISalEnt120821_1000.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2515.
HOGENOMHOG000022459.
OMAPYLVPIG.
OrthoDBEOG6FBX0P.

Enzyme and pathway databases

BioCycSENT28901:GH9O-1201-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_SALPB
AccessionPrimary (citable) accession number: A9MU62
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: May 14, 2014
This is version 40 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