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P77650

- HCAD_ECOLI

UniProt

P77650 - HCAD_ECOLI

Protein

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

Gene

hcaD

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      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.

    Catalytic activityi

    Reduced ferredoxin + NAD+ = oxidized ferredoxin + NADH.

    Cofactori

    FAD.

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi5 – 3632FADSequence AnalysisAdd
    BLAST
    Nucleotide bindingi146 – 17429NADSequence AnalysisAdd
    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
    4. protein binding Source: IntAct

    GO - Biological processi

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

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Aromatic hydrocarbons catabolism

    Keywords - Ligandi

    FAD, Flavoprotein, NAD

    Enzyme and pathway databases

    BioCyciEcoCyc:HCAD-MONOMER.
    ECOL316407:JW2526-MONOMER.
    MetaCyc:HCAD-MONOMER.
    UniPathwayiUPA00714.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component (EC:1.18.1.3)
    Alternative name(s):
    Digoxigenin system ferredoxin--NAD(+) reductase component
    Gene namesi
    Name:hcaD
    Synonyms:hcaA4, phdA, yfhY
    Ordered Locus Names:b2542, JW2526
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG13460. hcaD.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 4004003-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase componentPRO_0000167661Add
    BLAST

    Proteomic databases

    PaxDbiP77650.
    PRIDEiP77650.

    PTM databases

    PhosSiteiP0809399.

    Expressioni

    Gene expression databases

    GenevestigatoriP77650.

    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).

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    nikRP0A6Z62EBI-1129389,EBI-562488

    Protein-protein interaction databases

    IntActiP77650. 7 interactions.
    STRINGi511145.b2542.

    Structurei

    3D structure databases

    ProteinModelPortaliP77650.
    SMRiP77650. Positions 5-386.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0446.
    HOGENOMiHOG000276711.
    KOiK00529.
    OMAiRLPPPWF.
    OrthoDBiEOG6T4RXM.
    PhylomeDBiP77650.

    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.

    P77650-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKEKTIIIVG GGQAAAMAAA SLRQQGFTGE LHLFSDERHL PYERPPLSKS    50
    MLLEDSPQLQ QVLPANWWQE NNVHLHSGVT IKTLGRDTRE LVLTNGESWH 100
    WDQLFIATGA AARPLPLLDA LGERCFTLRH AGDAARLREV LQPERSVVII 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):43,978
    Last modified:February 1, 1997 - v1
    Checksum:iF5A1A06C4F1DFF36
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y11070 Genomic DNA. Translation: CAA71952.1.
    U00096 Genomic DNA. Translation: AAC75595.1.
    AP009048 Genomic DNA. Translation: BAA16445.1.
    PIRiE65031.
    RefSeqiNP_417037.1. NC_000913.3.
    YP_490770.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75595; AAC75595; b2542.
    BAA16445; BAA16445; BAA16445.
    GeneIDi12930468.
    945427.
    KEGGiecj:Y75_p2495.
    eco:b2542.
    PATRICi32120481. VBIEscCol129921_2643.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y11070 Genomic DNA. Translation: CAA71952.1 .
    U00096 Genomic DNA. Translation: AAC75595.1 .
    AP009048 Genomic DNA. Translation: BAA16445.1 .
    PIRi E65031.
    RefSeqi NP_417037.1. NC_000913.3.
    YP_490770.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P77650.
    SMRi P77650. Positions 5-386.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P77650. 7 interactions.
    STRINGi 511145.b2542.

    PTM databases

    PhosSitei P0809399.

    Proteomic databases

    PaxDbi P77650.
    PRIDEi P77650.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75595 ; AAC75595 ; b2542 .
    BAA16445 ; BAA16445 ; BAA16445 .
    GeneIDi 12930468.
    945427.
    KEGGi ecj:Y75_p2495.
    eco:b2542.
    PATRICi 32120481. VBIEscCol129921_2643.

    Organism-specific databases

    EchoBASEi EB3233.
    EcoGenei EG13460. hcaD.

    Phylogenomic databases

    eggNOGi COG0446.
    HOGENOMi HOG000276711.
    KOi K00529.
    OMAi RLPPPWF.
    OrthoDBi EOG6T4RXM.
    PhylomeDBi P77650.

    Enzyme and pathway databases

    UniPathwayi UPA00714 .
    BioCyci EcoCyc:HCAD-MONOMER.
    ECOL316407:JW2526-MONOMER.
    MetaCyc:HCAD-MONOMER.

    Miscellaneous databases

    PROi P77650.

    Gene expression databases

    Genevestigatori P77650.

    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. "Characterization of the hca cluster encoding the dioxygenolytic pathway for initial catabolism of 3-phenylpropionic acid in Escherichia coli K-12."
      Diaz E., Ferrandez A., Garcia J.L.
      J. Bacteriol. 180:2915-2923(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
      Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.
    2. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
      Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
      , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
      DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

    Entry informationi

    Entry nameiHCAD_ECOLI
    AccessioniPrimary (citable) accession number: P77650
    Secondary accession number(s): O08100
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 118 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, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3