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Q8XBC7

- DCYD_ECO57

UniProt

Q8XBC7 - DCYD_ECO57

Protein

D-cysteine desulfhydrase

Gene

dcyD

Organism
Escherichia coli O157:H7
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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 phosphate.UniRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

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

    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:Z3008, ECs2657/ECs2658
    OrganismiEscherichia coli O157:H7
    Taxonomic identifieri83334 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 328327D-cysteine desulfhydrasePRO_0000184515Add
    BLAST

    Amino acid modifications

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

    Proteomic databases

    PRIDEiQ8XBC7.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi155864.Z3008.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8XBC7.
    SMRiQ8XBC7. Positions 4-327.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    HOGENOMiHOG000022459.
    KOiK05396.
    OMAiPYLVPIG.
    OrthoDBiEOG6FBX0P.

    Family and domain databases

    HAMAPiMF_01045. D_Cys_desulfhydr.
    InterProiIPR027278. ACCD_DCysDesulf.
    IPR005966. D-Cys_desShydrase.
    IPR023702. D_Cys_desulphydr_bac.
    IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
    [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.

    Q8XBC7-1 [UniParc]FASTAAdd to Basket

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    MPLHNLTRFP RLEFIGAPTP LEYLPRFSDY LGREIFIKRD DVTPMAMGGN    50
    KLRKLEFLAA DALREGADTL ITAGAIQSNH VRQTAAVAAK LGLHCVALLE 100
    NPIGTTAENY LTNGNRLLLD LFNTQIEMCD ALTDPNAQLE ELATRVEAQG 150
    FRPYVIPVGG SNALGALGYV ESALEIAQQC EGAVNISSVV VASGSAGTHA 200
    GLAVGLEHLM PESELIGVTV SRSVADQLPK VVNLQQAIAK ELELTASVEI 250
    LLWDDYFAPG YGVPNDEGME AVKLLARLEG ILLDPVYTGK AMAGLIDGIS 300
    QKRFKDEGPI LFIHTGGAPA LFAYHPHV 328
    Length:328
    Mass (Da):35,181
    Last modified:January 23, 2007 - v3
    Checksum:i59D6392CF3EC62D8
    GO

    Sequence cautioni

    The sequence BAB36080.1 differs from that shown. Reason: Frameshift at position 139. Produces two separate ORFs.
    The sequence BAB36081.1 differs from that shown. Reason: Frameshift at position 139. Produces two separate ORFs.
    The sequence AAG56934.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG56934.1. Different initiation.
    BA000007 Genomic DNA. Translation: BAB36080.1. Frameshift.
    BA000007 Genomic DNA. Translation: BAB36081.1. Frameshift.
    PIRiA90961.
    B85809.
    B90961.
    RefSeqiNP_288380.2. NC_002655.2.

    Genome annotation databases

    EnsemblBacteriaiAAG56934; AAG56934; Z3008.
    BAB36080; BAB36080; BAB36080.
    BAB36081; BAB36081; BAB36081.
    GeneIDi961917.
    KEGGiece:Z3008.
    PATRICi18354700. VBIEscCol44059_2558.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE005174 Genomic DNA. Translation: AAG56934.1 . Different initiation.
    BA000007 Genomic DNA. Translation: BAB36080.1 . Frameshift.
    BA000007 Genomic DNA. Translation: BAB36081.1 . Frameshift.
    PIRi A90961.
    B85809.
    B90961.
    RefSeqi NP_288380.2. NC_002655.2.

    3D structure databases

    ProteinModelPortali Q8XBC7.
    SMRi Q8XBC7. Positions 4-327.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 155864.Z3008.

    Proteomic databases

    PRIDEi Q8XBC7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG56934 ; AAG56934 ; Z3008 .
    BAB36080 ; BAB36080 ; BAB36080 .
    BAB36081 ; BAB36081 ; BAB36081 .
    GeneIDi 961917.
    KEGGi ece:Z3008.
    PATRICi 18354700. VBIEscCol44059_2558.

    Phylogenomic databases

    HOGENOMi HOG000022459.
    KOi K05396.
    OMAi PYLVPIG.
    OrthoDBi EOG6FBX0P.

    Family and domain databases

    HAMAPi MF_01045. D_Cys_desulfhydr.
    InterProi IPR027278. ACCD_DCysDesulf.
    IPR005966. D-Cys_desShydrase.
    IPR023702. D_Cys_desulphydr_bac.
    IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
    [Graphical view ]
    Pfami PF00291. PALP. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006278. ACCD_DCysDesulf. 1 hit.
    SUPFAMi SSF53686. SSF53686. 1 hit.
    TIGRFAMsi TIGR01275. ACC_deam_rel. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
    2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
      Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
      , Kuhara S., Shiba T., Hattori M., Shinagawa H.
      DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

    Entry informationi

    Entry nameiDCYD_ECO57
    AccessioniPrimary (citable) accession number: Q8XBC7
    Secondary accession number(s): Q8X2H0, Q8X2H1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 22, 2003
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 69 of the entry and version 3 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