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B1LQT7

- DCYD_ECOSM

UniProt

B1LQT7 - DCYD_ECOSM

Protein

D-cysteine desulfhydrase

Gene

dcyD

Organism
Escherichia coli (strain SMS-3-5 / SECEC)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 42 (01 Oct 2014)
      Sequence version 1 (29 Apr 2008)
      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

    Enzyme and pathway databases

    BioCyciECOL439855:GHHB-1261-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    D-cysteine desulfhydraseUniRule annotation (EC:4.4.1.15UniRule annotation)
    Gene namesi
    Name:dcyDUniRule annotation
    Ordered Locus Names:EcSMS35_1263
    OrganismiEscherichia coli (strain SMS-3-5 / SECEC)
    Taxonomic identifieri439855 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000007011: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 328328D-cysteine desulfhydrasePRO_1000136162Add
    BLAST

    Amino acid modifications

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

    Proteomic databases

    PRIDEiB1LQT7.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation

    Protein-protein interaction databases

    STRINGi439855.EcSMS35_1263.

    Structurei

    3D structure databases

    ProteinModelPortaliB1LQT7.
    SMRiB1LQT7. Positions 7-328.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG2515.
    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.

    B1LQT7-1 [UniParc]FASTAAdd to Basket

    « Hide

    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 ELELTASAEI 250
    LLWDDYFAPG YGVPNDEGME AVKLLARLEG ILLDPVYTGK AMAGLIDGIS 300
    QKRFKDEGPI LFIHTGGAPA LFAYHPHV 328
    Length:328
    Mass (Da):35,153
    Last modified:April 29, 2008 - v1
    Checksum:i4179DE645C0B32D8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000970 Genomic DNA. Translation: ACB19636.1.
    RefSeqiYP_001743324.1. NC_010498.1.

    Genome annotation databases

    EnsemblBacteriaiACB19636; ACB19636; EcSMS35_1263.
    GeneIDi6144001.
    KEGGiecm:EcSMS35_1263.
    PATRICi18431393. VBIEscCol6161_1424.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000970 Genomic DNA. Translation: ACB19636.1 .
    RefSeqi YP_001743324.1. NC_010498.1.

    3D structure databases

    ProteinModelPortali B1LQT7.
    SMRi B1LQT7. Positions 7-328.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 439855.EcSMS35_1263.

    Proteomic databases

    PRIDEi B1LQT7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACB19636 ; ACB19636 ; EcSMS35_1263 .
    GeneIDi 6144001.
    KEGGi ecm:EcSMS35_1263.
    PATRICi 18431393. VBIEscCol6161_1424.

    Phylogenomic databases

    eggNOGi COG2515.
    HOGENOMi HOG000022459.
    KOi K05396.
    OMAi PYLVPIG.
    OrthoDBi EOG6FBX0P.

    Enzyme and pathway databases

    BioCyci ECOL439855:GHHB-1261-MONOMER.

    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. "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.

    Entry informationi

    Entry nameiDCYD_ECOSM
    AccessioniPrimary (citable) accession number: B1LQT7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 14, 2009
    Last sequence update: April 29, 2008
    Last modified: October 1, 2014
    This is version 42 of the entry and version 1 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