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Protein

4-hydroxyphenylacetate 3-monooxygenase, reductase component

Gene

TTHA0961

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the reduction of free flavins (FMN, FAD and riboflavin) by NADH. Subsequently, the reduced flavins diffuse to the large HpaB component. It utilizes NADH, but not NADPH as an electron donor, and both FAD and FMN as electron acceptors.1 Publication

Catalytic activityi

Reduced flavin + NAD+ = flavin + NADH.1 Publication

Kineticsi

  1. KM=8.9 µM for FAD (at 30 degrees Celsius and pH 7.0)1 Publication
  2. KM=36.8 µM for FMN (at 30 degrees Celsius and pH 7.0)1 Publication

    Pathwayi: 4-hydroxyphenylacetate degradation

    This protein is involved in step 1 of the subpathway that synthesizes pyruvate and succinate semialdehyde from 4-hydroxyphenylacetate.1 Publication
    Proteins known to be involved in the 7 steps of the subpathway in this organism are:
    1. 4-hydroxyphenylacetate 3-monooxygenase, reductase component (TTHA0961), 4-hydroxyphenylacetate 3-monooxygenase oxygenase component (TTHA0960)
    2. no protein annotated in this organism
    3. no protein annotated in this organism
    4. no protein annotated in this organism
    5. no protein annotated in this organism
    6. no protein annotated in this organism
    7. no protein annotated in this organism
    This subpathway is part of the pathway 4-hydroxyphenylacetate degradation, which is itself part of Aromatic compound metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate and succinate semialdehyde from 4-hydroxyphenylacetate, the pathway 4-hydroxyphenylacetate degradation and in Aromatic compound metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei37NADCombined sources1 Publication1
    Binding sitei80FADCombined sources1 Publication1
    Binding sitei116NADCombined sources1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi27 – 34FADCombined sources1 Publication8
    Nucleotide bindingi48 – 50FADCombined sources1 Publication3
    Nucleotide bindingi54 – 55FADCombined sources1 Publication2
    Nucleotide bindingi137 – 140NADCombined sources1 Publication4

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionOxidoreductase
    Biological processAromatic hydrocarbons catabolism
    LigandFAD, Flavoprotein, FMN, NAD

    Enzyme and pathway databases

    BioCyciTTHE300852:G1GKC-971-MONOMER
    SABIO-RKiQ5SJP7
    UniPathwayiUPA00208; UER00416

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    4-hydroxyphenylacetate 3-monooxygenase, reductase component1 Publication (EC:1.5.1.361 Publication)
    Alternative name(s):
    4-HPA 3-monooxygenase small component
    Flavin:NADH reductase
    Gene namesi
    Ordered Locus Names:TTHA0961
    OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
    Taxonomic identifieri300852 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
    Proteomesi
    • UP000000532 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00003879971 – 1494-hydroxyphenylacetate 3-monooxygenase, reductase componentAdd BLAST149

    Interactioni

    Subunit structurei

    Homodimer. 4-HPA 3-monooxygenase consists of a reductase component HpaC and an oxygenase component HpaB.1 Publication

    Protein-protein interaction databases

    STRINGi300852.TTHA0961

    Structurei

    Secondary structure

    1149
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi3 – 10Combined sources8
    Beta strandi17 – 23Combined sources7
    Beta strandi26 – 33Combined sources8
    Beta strandi35 – 39Combined sources5
    Turni40 – 43Combined sources4
    Beta strandi44 – 50Combined sources7
    Helixi55 – 62Combined sources8
    Beta strandi64 – 69Combined sources6
    Helixi75 – 80Combined sources6
    Turni81 – 83Combined sources3
    Beta strandi100 – 113Combined sources14
    Beta strandi116 – 128Combined sources13
    Beta strandi139 – 143Combined sources5

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2ECRX-ray1.60A/B1-149[»]
    2ECUX-ray1.30A/B1-149[»]
    2ED4X-ray1.85A/B1-149[»]
    ProteinModelPortaliQ5SJP7
    SMRiQ5SJP7
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5SJP7

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105MXW Bacteria
    COG1853 LUCA
    HOGENOMiHOG000115783
    KOiK00484
    OMAiWFDRGYH
    PhylomeDBiQ5SJP7

    Family and domain databases

    Gene3Di2.30.110.10, 1 hit
    InterProiView protein in InterPro
    IPR002563 Flavin_Rdtase-like_dom
    IPR012349 Split_barrel_FMN-bd
    PfamiView protein in Pfam
    PF01613 Flavin_Reduct, 1 hit
    SMARTiView protein in SMART
    SM00903 Flavin_Reduct, 1 hit

    Sequencei

    Sequence statusi: Complete.

    Q5SJP7-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKEAFKEALA RFASGVTVVA ARLGEEERGM TATAFMSLSL EPPLVALAVS
    60 70 80 90 100
    ERAKLLPVLE GAGAFTVSLL REGQEAVSEH FAGRPKEGIA LEEGRVKGAL
    110 120 130 140
    AVLRCRLHAL YPGGDHRIVV GLVEEVELGE EGPPLVYFQR GYRRLVWPS
    Length:149
    Mass (Da):16,111
    Last modified:December 21, 2004 - v1
    Checksum:iCD963ADB68B1D66A
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AP008226 Genomic DNA Translation: BAD70784.1
    RefSeqiWP_011228329.1, NC_006461.1
    YP_144227.1, NC_006461.1

    Genome annotation databases

    EnsemblBacteriaiBAD70784; BAD70784; BAD70784
    GeneIDi3170068
    KEGGittj:TTHA0961
    PATRICifig|300852.9.peg.943

    Similar proteinsi

    Entry informationi

    Entry nameiHPAC_THET8
    AccessioniPrimary (citable) accession number: Q5SJP7
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 3, 2009
    Last sequence update: December 21, 2004
    Last modified: April 25, 2018
    This is version 76 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome
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    Main funding by: National Institutes of Health