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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

Manual assertion based on experiment ini

  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)DescriptionActionsGraphical viewLength
    Active sitei138By similarity1

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi106C → S: Still able to produce THN. 1 Publication1
    Mutagenesisi168C → S: Still able to produce THN. 1 Publication1
    Mutagenesisi171C → S: Still able to produce THN. 1 Publication1
    Mutagenesisi184C → S: Still able to produce THN. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004308801 – 3741,3,6,8-tetrahydroxynaphthalene synthaseAdd BLAST374

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi100226.SCO1206.

    Structurei

    Secondary structure

    1374
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi8 – 10Combined sources3
    Beta strandi13 – 17Combined sources5
    Helixi18 – 29Combined sources12
    Helixi35 – 44Combined sources10
    Beta strandi49 – 54Combined sources6
    Helixi56 – 59Combined sources4
    Helixi65 – 91Combined sources27
    Helixi95 – 97Combined sources3
    Beta strandi99 – 104Combined sources6
    Beta strandi106 – 108Combined sources3
    Helixi114 – 121Combined sources8
    Beta strandi129 – 133Combined sources5
    Helixi137 – 139Combined sources3
    Helixi140 – 154Combined sources15
    Beta strandi159 – 167Combined sources9
    Helixi168 – 171Combined sources4
    Helixi179 – 187Combined sources9
    Beta strandi190 – 198Combined sources9
    Turni199 – 201Combined sources3
    Beta strandi203 – 214Combined sources12
    Turni219 – 221Combined sources3
    Beta strandi222 – 227Combined sources6
    Beta strandi230 – 235Combined sources6
    Turni237 – 239Combined sources3
    Helixi240 – 242Combined sources3
    Helixi243 – 255Combined sources13
    Beta strandi268 – 270Combined sources3
    Helixi273 – 283Combined sources11
    Helixi288 – 291Combined sources4
    Helixi292 – 300Combined sources9
    Helixi307 – 318Combined sources12
    Beta strandi329 – 334Combined sources6
    Turni335 – 337Combined sources3
    Beta strandi338 – 347Combined sources10

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1U0MX-ray2.22A/B1-374[»]
    ProteinModelPortaliQ9FCA7.
    SMRiQ9FCA7.
    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1U0MX-ray2.22A/B1-374[»]
    ProteinModelPortaliQ9FCA7.
    SMRiQ9FCA7.
    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: November 2, 2016
    This is version 94 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.