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C8U8V8

- C8U8V8_ECO10

UniProt

C8U8V8 - C8U8V8_ECO10

Protein

3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component

Gene

hcaD

Organism
Escherichia coli O103:H2 (strain 12009 / EHEC)
Status
Unreviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 38 (01 Oct 2014)
      Sequence version 1 (03 Nov 2009)
      Previous versions | rss
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    Functioni

    Part of the multicomponent 3-phenylpropionate dioxygenase, that converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-dihydrodiol (CI-dihydrodiol), respectively.UniRule annotation

    Catalytic activityi

    Reduced ferredoxin + NAD+ = oxidized ferredoxin + NADH.UniRule annotation

    Cofactori

    FAD.UniRule annotation

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi5 – 3632FADUniRule annotationAdd
    BLAST
    Nucleotide bindingi146 – 17429NADUniRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. 3-phenylpropionate dioxygenase activity Source: UniProtKB-HAMAP
    2. ferredoxin-NAD+ reductase activity Source: UniProtKB-EC
    3. flavin adenine dinucleotide binding Source: InterPro

    GO - Biological processi

    1. 3-phenylpropionate catabolic process Source: UniProtKB-UniPathway
    2. cell redox homeostasis Source: InterPro

    Keywords - Molecular functioni

    DioxygenaseImported, Oxidoreductase

    Keywords - Biological processi

    Aromatic hydrocarbons catabolismUniRule annotation

    Keywords - Ligandi

    FADUniRule annotation, Flavoprotein, NADUniRule annotation

    Enzyme and pathway databases

    BioCyciECOL585395:GJA9-3161-MONOMER.
    UniPathwayiUPA00714.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase componentUniRule annotation (EC:1.18.1.3UniRule annotation)
    Alternative name(s):
    Digoxigenin system ferredoxin--NAD(+) reductase componentUniRule annotation
    Gene namesi
    Name:hcaDUniRule annotationImported
    Ordered Locus Names:ECO103_3062Imported
    OrganismiEscherichia coli O103:H2 (strain 12009 / EHEC)Imported
    Taxonomic identifieri585395 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000959: Chromosome

    Interactioni

    Subunit structurei

    This dioxygenase system consists of four proteins: the two subunits of the hydroxylase component (HcaE and HcaF), a ferredoxin (HcaC) and a ferredoxin reductase (HcaD).UniRule annotation

    Protein-protein interaction databases

    STRINGi585395.ECO103_3062.

    Structurei

    3D structure databases

    ProteinModelPortaliC8U8V8.
    SMRiC8U8V8. Positions 4-400.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the bacterial ring-hydroxylating dioxygenase ferredoxin reductase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0446.
    HOGENOMiHOG000276711.
    KOiK00529.
    OMAiRLPPPWF.
    OrthoDBiEOG6T4RXM.

    Family and domain databases

    Gene3Di3.30.390.30. 1 hit.
    HAMAPiMF_01651. HcaD.
    InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR023744. HcaD.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
    IPR001327. Pyr_OxRdtase_NAD-bd_dom.
    IPR028202. Reductase_C.
    [Graphical view]
    PfamiPF00070. Pyr_redox. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    PF14759. Reductase_C. 1 hit.
    [Graphical view]
    PRINTSiPR00368. FADPNR.
    SUPFAMiSSF55424. SSF55424. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    C8U8V8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKEKTIIIVG GGQAAAMAAA SLRQQGFTGE LHLFSDERHL PYERPPLSKS    50
    MLLEDSPQLQ QVLPANWWQE NNVHLHSGVT IKTLGRDTRE LVLTNGESWH 100
    WDQLFIATGA AARPLPLLDA LGERCFTLRH AGDAARLREV LQPERSVVIV 150
    GAGTIGLELA ASATQRRCKV TVIELAATVM GRNAPPPVQR YLLQRHQQAG 200
    VRILLNNAIE HVVDGEKVEL TLQSGETLQA DVVIYGIGIS ANEQLAREAN 250
    LDTANGIVID EACRTCDPAI FAGGDVAITR LDNGALHRCE SWENANNQAQ 300
    IAAAAMLGLP LPLLPPPWFW SDQYSDNLQF IGDMRGDDWL CRGNPETQKA 350
    IWFNLQNGVL IGAVTLNQGR EIRPIRKWIQ SGKTFDAKLL IDENIALKSL 400
    Length:400
    Mass (Da):43,964
    Last modified:November 3, 2009 - v1
    Checksum:iF5A1A7CF4F1DF2A6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP010958 Genomic DNA. Translation: BAI31817.1.
    RefSeqiYP_003222951.1. NC_013353.1.

    Genome annotation databases

    EnsemblBacteriaiBAI31817; BAI31817; ECO103_3062.
    GeneIDi8475575.
    KEGGieoh:ECO103_3062.
    PATRICi32098074. VBIEscCol146794_3208.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP010958 Genomic DNA. Translation: BAI31817.1 .
    RefSeqi YP_003222951.1. NC_013353.1.

    3D structure databases

    ProteinModelPortali C8U8V8.
    SMRi C8U8V8. Positions 4-400.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 585395.ECO103_3062.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAI31817 ; BAI31817 ; ECO103_3062 .
    GeneIDi 8475575.
    KEGGi eoh:ECO103_3062.
    PATRICi 32098074. VBIEscCol146794_3208.

    Phylogenomic databases

    eggNOGi COG0446.
    HOGENOMi HOG000276711.
    KOi K00529.
    OMAi RLPPPWF.
    OrthoDBi EOG6T4RXM.

    Enzyme and pathway databases

    UniPathwayi UPA00714 .
    BioCyci ECOL585395:GJA9-3161-MONOMER.

    Family and domain databases

    Gene3Di 3.30.390.30. 1 hit.
    HAMAPi MF_01651. HcaD.
    InterProi IPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR023744. HcaD.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
    IPR001327. Pyr_OxRdtase_NAD-bd_dom.
    IPR028202. Reductase_C.
    [Graphical view ]
    Pfami PF00070. Pyr_redox. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    PF14759. Reductase_C. 1 hit.
    [Graphical view ]
    PRINTSi PR00368. FADPNR.
    SUPFAMi SSF55424. SSF55424. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Comparative genomics reveal the mechanism of the parallel evolution of O157 and non-O157 enterohemorrhagic Escherichia coli."
      Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K., Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M., Hayashi T.
      Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 12009 / EHECImported.

    Entry informationi

    Entry nameiC8U8V8_ECO10
    AccessioniPrimary (citable) accession number: C8U8V8
    Entry historyi
    Integrated into UniProtKB/TrEMBL: November 3, 2009
    Last sequence update: November 3, 2009
    Last modified: October 1, 2014
    This is version 38 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteomeImported

    External Data

    Dasty 3