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Protein

D-cysteine desulfhydrase

Gene

dcyD

Organism
Shigella flexneri
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. It could be a defense mechanism against D-cysteine.UniRule annotation

Catalytic activityi

D-cysteine + H2O = H2S + NH3 + pyruvate.UniRule annotation

Cofactori

pyridoxal 5'-phosphateUniRule annotation

GO - Molecular functioni

  1. D-cysteine desulfhydrase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. D-amino acid metabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Pyridoxal phosphate

Names & Taxonomyi

Protein namesi
Recommended name:
D-cysteine desulfhydraseUniRule annotation (EC:4.4.1.15UniRule annotation)
Gene namesi
Name:dcyDUniRule annotation
Ordered Locus Names:SF1962, S2058
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
ProteomesiUP000002673 Componenti: Chromosome UP000001006 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 328327D-cysteine desulfhydrasePRO_0000184518Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511N6-(pyridoxal phosphate)lysineUniRule annotation

Proteomic databases

PaxDbiP59330.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi198214.SF1962.

Structurei

3D structure databases

ProteinModelPortaliP59330.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG2515.
HOGENOMiHOG000022459.
KOiK05396.
OrthoDBiEOG6FBX0P.

Family and domain databases

HAMAPiMF_01045. D_Cys_desulfhydr.
InterProiIPR027278. ACCD_DCysDesulf.
IPR005966. D-Cys_desShydrase.
IPR023702. D_Cys_desulphydr_bac.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
PIRSFiPIRSF006278. ACCD_DCysDesulf. 1 hit.
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR01275. ACC_deam_rel. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P59330-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLHNLTRFP RLEFIGAPTP LEYLPRFSDY LGREIFIKRD EVTPMAMGGN
60 70 80 90 100
KLRKLEFLAA DALREGADTL ITAGAIQSNH VRQTAAVAAK LGLHCVALLE
110 120 130 140 150
NPIGTTAENY LTNGNRLLLD LFNTQIEMCD ALTDPNAQLE ELATRVEAQG
160 170 180 190 200
FRPYVIPVGG SNALGALGYV ESALEIAQQC EGAVNISSVV VASGSAGTHA
210 220 230 240 250
GLAVGLEHLM PESELIGVTV SRSVADQLPK VVNLQQAIAK ELELTASAEI
260 270 280 290 300
LLWDDYFAPG YGVPNDEGME AVKLLARLEG ILLDPVYTGK AMAGLIDGIS
310 320
QKRFKDEGPI LFIHTGGAPA LFAYHPHV
Length:328
Mass (Da):35,167
Last modified:January 23, 2007 - v2
Checksum:i2CB80214A65497D8
GO

Sequence cautioni

The sequence AAN43513.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAP17343.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN43513.1. Different initiation.
AE014073 Genomic DNA. Translation: AAP17343.1. Different initiation.
RefSeqiNP_707806.3. NC_004337.2.
NP_837534.2. NC_004741.1.
WP_001128248.1. NZ_KL503837.1.

Genome annotation databases

EnsemblBacteriaiAAN43513; AAN43513; SF1962.
AAP17343; AAP17343; S2058.
GeneIDi1025173.
1078375.
KEGGisfl:SF1962.
sfx:S2058.
PATRICi18705590. VBIShiFle31049_2283.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN43513.1. Different initiation.
AE014073 Genomic DNA. Translation: AAP17343.1. Different initiation.
RefSeqiNP_707806.3. NC_004337.2.
NP_837534.2. NC_004741.1.
WP_001128248.1. NZ_KL503837.1.

3D structure databases

ProteinModelPortaliP59330.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198214.SF1962.

Proteomic databases

PaxDbiP59330.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN43513; AAN43513; SF1962.
AAP17343; AAP17343; S2058.
GeneIDi1025173.
1078375.
KEGGisfl:SF1962.
sfx:S2058.
PATRICi18705590. VBIShiFle31049_2283.

Phylogenomic databases

eggNOGiCOG2515.
HOGENOMiHOG000022459.
KOiK05396.
OrthoDBiEOG6FBX0P.

Family and domain databases

HAMAPiMF_01045. D_Cys_desulfhydr.
InterProiIPR027278. ACCD_DCysDesulf.
IPR005966. D-Cys_desShydrase.
IPR023702. D_Cys_desulphydr_bac.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
PIRSFiPIRSF006278. ACCD_DCysDesulf. 1 hit.
SUPFAMiSSF53686. SSF53686. 1 hit.
TIGRFAMsiTIGR01275. ACC_deam_rel. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
    Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y.
    , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
    Nucleic Acids Res. 30:4432-4441(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 301 / Serotype 2a.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700930 / 2457T / Serotype 2a.

Entry informationi

Entry nameiDCYD_SHIFL
AccessioniPrimary (citable) accession number: P59330
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2003
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.