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Protein

1,3,6,8-tetrahydroxynaphthalene synthase

Gene

SCO1206

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of melanin but also various secondary metabolites containing a naphthoquinone ring. Catalyzes the iterative condensation of five CoA-linked malonyl units to form a pentaketide intermediate. THNS subsequently catalyzes the dual intramolecular Claisen and aldol condensations of this linear intermediate to produce the fused ring of 1,3,6,8-tetrahydroxynaphthalene (THN).2 Publications

Catalytic activityi

5 malonyl-CoA = 1,3,6,8-tetrahydroxynaphthalene + 5 CoA + 5 CO2 + H2O.2 Publications

Kineticsi

Kcat is 0.48 min(-1) for THN synthase activity with THN as substrate.1 Publication

  1. KM=3.58 µM for 5 malonyl-CoA1 Publication

    Pathwayi: melanin biosynthesis

    This protein is involved in the pathway melanin biosynthesis, which is part of Pigment biosynthesis.By similarity
    View all proteins of this organism that are known to be involved in the pathway melanin biosynthesis and in Pigment biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei138 – 1381By similarity

    GO - Molecular functioni

    GO - Biological processi

    • melanin biosynthetic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Melanin biosynthesis

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14457.
    UniPathwayiUPA00785.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    1,3,6,8-tetrahydroxynaphthalene synthase1 Publication (EC:2.3.1.2332 Publications)
    Short name:
    THNS1 Publication
    Alternative name(s):
    1,3,6,8-tetrahydroxynaphthalene synthesis polyketide synthase type IIICurated
    Gene namesi
    Ordered Locus Names:SCO1206
    OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
    Taxonomic identifieri100226 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
    Proteomesi
    • UP000001973 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi106 – 1061C → S: Still able to produce THN. 1 Publication
    Mutagenesisi168 – 1681C → S: Still able to produce THN. 1 Publication
    Mutagenesisi171 – 1711C → S: Still able to produce THN. 1 Publication
    Mutagenesisi184 – 1841C → S: Still able to produce THN. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3743741,3,6,8-tetrahydroxynaphthalene synthasePRO_0000430880Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi100226.SCO1206.

    Structurei

    Secondary structure

    1
    374
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 103Combined sources
    Beta strandi13 – 175Combined sources
    Helixi18 – 2912Combined sources
    Helixi35 – 4410Combined sources
    Beta strandi49 – 546Combined sources
    Helixi56 – 594Combined sources
    Helixi65 – 9127Combined sources
    Helixi95 – 973Combined sources
    Beta strandi99 – 1046Combined sources
    Beta strandi106 – 1083Combined sources
    Helixi114 – 1218Combined sources
    Beta strandi129 – 1335Combined sources
    Helixi137 – 1393Combined sources
    Helixi140 – 15415Combined sources
    Beta strandi159 – 1679Combined sources
    Helixi168 – 1714Combined sources
    Helixi179 – 1879Combined sources
    Beta strandi190 – 1989Combined sources
    Turni199 – 2013Combined sources
    Beta strandi203 – 21412Combined sources
    Turni219 – 2213Combined sources
    Beta strandi222 – 2276Combined sources
    Beta strandi230 – 2356Combined sources
    Turni237 – 2393Combined sources
    Helixi240 – 2423Combined sources
    Helixi243 – 25513Combined sources
    Beta strandi268 – 2703Combined sources
    Helixi273 – 28311Combined sources
    Helixi288 – 2914Combined sources
    Helixi292 – 3009Combined sources
    Helixi307 – 31812Combined sources
    Beta strandi329 – 3346Combined sources
    Turni335 – 3373Combined sources
    Beta strandi338 – 34710Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1U0MX-ray2.22A/B1-374[»]
    ProteinModelPortaliQ9FCA7.
    SMRiQ9FCA7. Positions 2-349.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9FCA7.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the chalcone/stilbene synthases family.Curated

    Phylogenomic databases

    eggNOGiENOG41065KQ. Bacteria.
    COG3424. LUCA.
    HOGENOMiHOG000245461.
    InParanoidiQ9FCA7.
    KOiK19580.
    OMAiDFFIFHT.
    OrthoDBiPOG091H0CJ8.
    PhylomeDBiQ9FCA7.

    Family and domain databases

    Gene3Di3.40.47.10. 2 hits.
    InterProiIPR012328. Chalcone/stilbene_synth_C.
    IPR001099. Chalcone/stilbene_synthase_N.
    IPR011141. Polyketide_synthase_type-III.
    IPR016039. Thiolase-like.
    [Graphical view]
    PfamiPF02797. Chal_sti_synt_C. 1 hit.
    PF00195. Chal_sti_synt_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000451. PKS_III. 1 hit.
    SUPFAMiSSF53901. SSF53901. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Q9FCA7-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MATLCRPSVS VPEHVITMEE TLELARRRHT DHPQLPLALR LIENTGVRTR
    60 70 80 90 100
    HIVQPIEDTL EHPGFEDRNK VYEREAKSRV PAVIQRALDD AELLATDIDV
    110 120 130 140 150
    IIYVSCTGFM MPSLTAWLIN EMGFDSTTRQ IPIAQLGCAA GGAAINRAHD
    160 170 180 190 200
    FCTAYPEANA LIVACEFCSL CYQPTDLGVG SLLCNGLFGD GIAAAVVRGR
    210 220 230 240 250
    GGTGVRLERN GSYLIPKTED WIMYDVKATG FHFLLDKRVP ATMEPLAPAL
    260 270 280 290 300
    KELAGEHGWD ASDLDFYIVH AGGPRILDDL STFLEVDPHA FRFSRATLTE
    310 320 330 340 350
    YGNIASAVVL DALRRLFDEG GVEEGARGLL AGFGPGITAE MSLGCWQTAD
    360 370
    VRRGIRQDVT RTAARGVSRR VRQA
    Length:374
    Mass (Da):40,934
    Last modified:March 1, 2001 - v1
    Checksum:i8907CCDC30B1AFC9
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL939108 Genomic DNA. Translation: CAC01488.1.
    RefSeqiNP_625495.1. NC_003888.3.
    WP_011027653.1. NC_003888.3.

    Genome annotation databases

    EnsemblBacteriaiCAC01488; CAC01488; CAC01488.
    GeneIDi1096629.
    KEGGisco:SCO1206.
    PATRICi23731964. VBIStrCoe124346_1205.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL939108 Genomic DNA. Translation: CAC01488.1.
    RefSeqiNP_625495.1. NC_003888.3.
    WP_011027653.1. NC_003888.3.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1U0MX-ray2.22A/B1-374[»]
    ProteinModelPortaliQ9FCA7.
    SMRiQ9FCA7. Positions 2-349.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi100226.SCO1206.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAC01488; CAC01488; CAC01488.
    GeneIDi1096629.
    KEGGisco:SCO1206.
    PATRICi23731964. VBIStrCoe124346_1205.

    Phylogenomic databases

    eggNOGiENOG41065KQ. Bacteria.
    COG3424. LUCA.
    HOGENOMiHOG000245461.
    InParanoidiQ9FCA7.
    KOiK19580.
    OMAiDFFIFHT.
    OrthoDBiPOG091H0CJ8.
    PhylomeDBiQ9FCA7.

    Enzyme and pathway databases

    UniPathwayiUPA00785.
    BioCyciMetaCyc:MONOMER-14457.

    Miscellaneous databases

    EvolutionaryTraceiQ9FCA7.

    Family and domain databases

    Gene3Di3.40.47.10. 2 hits.
    InterProiIPR012328. Chalcone/stilbene_synth_C.
    IPR001099. Chalcone/stilbene_synthase_N.
    IPR011141. Polyketide_synthase_type-III.
    IPR016039. Thiolase-like.
    [Graphical view]
    PfamiPF02797. Chal_sti_synt_C. 1 hit.
    PF00195. Chal_sti_synt_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000451. PKS_III. 1 hit.
    SUPFAMiSSF53901. SSF53901. 2 hits.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiRPPA_STRCO
    AccessioniPrimary (citable) accession number: Q9FCA7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 29, 2014
    Last sequence update: March 1, 2001
    Last modified: September 7, 2016
    This is version 92 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.