Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

4-hydroxyphenylacetate 3-monooxygenase reductase component

Gene

TTHA0961

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-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.1 Publication

Catalytic activityi

Reduced flavin + NAD+ = flavin + NADH.

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.
    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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei37 – 371NAD1 Publication
    Binding sitei116 – 1161NAD1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi27 – 315FAD1 Publication
    Nucleotide bindingi33 – 342FAD1 Publication
    Nucleotide bindingi48 – 503FAD1 Publication
    Nucleotide bindingi54 – 552FAD1 Publication
    Nucleotide bindingi80 – 812FAD1 Publication
    Nucleotide bindingi137 – 1404NAD1 Publication

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Aromatic hydrocarbons catabolism

    Keywords - Ligandi

    FAD, Flavoprotein, FMN, NAD

    Enzyme and pathway databases

    BioCyciTTHE300852:GH8R-992-MONOMER.
    SABIO-RKQ5SJP7.
    UniPathwayiUPA00208; UER00416.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    4-hydroxyphenylacetate 3-monooxygenase reductase component (EC:1.5.1.36)
    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)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 1491494-hydroxyphenylacetate 3-monooxygenase reductase componentPRO_0000387997Add
    BLAST

    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

    1
    149
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 108Combined sources
    Beta strandi17 – 237Combined sources
    Beta strandi26 – 338Combined sources
    Beta strandi35 – 395Combined sources
    Turni40 – 434Combined sources
    Beta strandi44 – 507Combined sources
    Helixi55 – 628Combined sources
    Beta strandi64 – 696Combined sources
    Helixi75 – 806Combined sources
    Turni81 – 833Combined sources
    Beta strandi100 – 11314Combined sources
    Beta strandi116 – 12813Combined sources
    Beta strandi139 – 1435Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ECRX-ray1.60A/B1-149[»]
    2ECUX-ray1.30A/B1-149[»]
    2ED4X-ray1.85A/B1-149[»]
    ProteinModelPortaliQ5SJP7.
    SMRiQ5SJP7. Positions 1-149.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5SJP7.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105MXW. Bacteria.
    COG1853. LUCA.
    HOGENOMiHOG000115783.
    KOiK00484.
    OMAiHFCTGIA.
    PhylomeDBiQ5SJP7.

    Family and domain databases

    Gene3Di2.30.110.10. 1 hit.
    InterProiIPR002563. Flavin_Rdtase-like_dom.
    IPR012349. Split_barrel_FMN-bd.
    [Graphical view]
    PfamiPF01613. Flavin_Reduct. 1 hit.
    [Graphical view]
    SMARTiSM00903. Flavin_Reduct. 1 hit.
    [Graphical view]
    SUPFAMiSSF50475. SSF50475. 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.
    PATRICi23956884. VBITheThe93045_0943.

    Cross-referencesi

    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ECRX-ray1.60A/B1-149[»]
    2ECUX-ray1.30A/B1-149[»]
    2ED4X-ray1.85A/B1-149[»]
    ProteinModelPortaliQ5SJP7.
    SMRiQ5SJP7. Positions 1-149.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi300852.TTHA0961.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiBAD70784; BAD70784; BAD70784.
    GeneIDi3170068.
    KEGGittj:TTHA0961.
    PATRICi23956884. VBITheThe93045_0943.

    Phylogenomic databases

    eggNOGiENOG4105MXW. Bacteria.
    COG1853. LUCA.
    HOGENOMiHOG000115783.
    KOiK00484.
    OMAiHFCTGIA.
    PhylomeDBiQ5SJP7.

    Enzyme and pathway databases

    UniPathwayiUPA00208; UER00416.
    BioCyciTTHE300852:GH8R-992-MONOMER.
    SABIO-RKQ5SJP7.

    Miscellaneous databases

    EvolutionaryTraceiQ5SJP7.

    Family and domain databases

    Gene3Di2.30.110.10. 1 hit.
    InterProiIPR002563. Flavin_Rdtase-like_dom.
    IPR012349. Split_barrel_FMN-bd.
    [Graphical view]
    PfamiPF01613. Flavin_Reduct. 1 hit.
    [Graphical view]
    SMARTiSM00903. Flavin_Reduct. 1 hit.
    [Graphical view]
    SUPFAMiSSF50475. SSF50475. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiHPAC_THET8
    AccessioniPrimary (citable) accession number: Q5SJP7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 3, 2009
    Last sequence update: December 21, 2004
    Last modified: September 7, 2016
    This is version 71 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.