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Protein

Atromentin synthetase

Gene

atrA

Organism
Tapinella panuoides (Oyster rollrim mushroom) (Paxillus panuoides)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

The L-tyrosine:2-oxoglutarate aminotransferase atrD and the atromentin synthetase atrA catalyze consecutive steps to turn over L-tyrosine into atromentin, which represents the generic precursor molecule for the entire terphenylquinone and pulvinic acid family of pigments, which are widely distributed secondary metabolites in homobasidiomycetes (PubMed:18805498). The first step is catalyzed by atrD which converts L-tyrosine in to 4-hydroxyphenylpyruvate (4-HPP) (PubMed:18805498). Adenylation of two 4-HPP monomers by the atrA adenylation (A) domain, ester bond formation between monomers and atrA, and symmetric C-C-bond formation between two monomers by atrA leads to atromentin (PubMed:18805498).1 Publication

Kineticsi

  1. KM=1.37 µM for 4-hydroxyphenylpyruvic acid1 Publication
  2. KM=590 µM for 2-oxoglutarate1 Publication

    pH dependencei

    Optimum pH is 6.5.1 Publication

    Temperature dependencei

    Optimum temperature is 25 degrees Celsius.1 Publication

    Pathwayi: Secondary metabolite biosynthesis

    This protein is involved in Secondary metabolite biosynthesis.1 Publication
    View all proteins of this organism that are known to be involved in Secondary metabolite biosynthesis.

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionTransferase

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-18722

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Atromentin synthetase1 Publication (EC:2.3.1.-1 Publication)
    Alternative name(s):
    Atromentin biosynthesis protein ACurated
    Nonribosomal peptide synthase atrACurated
    Gene namesi
    Name:atrA1 Publication
    OrganismiTapinella panuoides (Oyster rollrim mushroom) (Paxillus panuoides)
    Taxonomic identifieri80604 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeBoletalesTapinellineaeTapinellaceaeTapinella

    Pathology & Biotechi

    Biotechnological usei

    Atromentin has been shown to induce caspase-3 and poly (ADP-ribose) polymerase (PARP) in human leukemia U937 cells (PubMed:19809251). It has also anticoagulant activity (PubMed:5862512). Moreover, atromentin has antimicrobial activity (PubMed:6541963). It acts especially as an inhibitor of FabK, the enoyl-acyl carrier protein (ACP) reductase of S.pneumoniae (PubMed:17323650).4 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004376781 – 957Atromentin synthetaseAdd BLAST957

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei633O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

    Keywords - PTMi

    Phosphopantetheine, Phosphoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliB7STY1
    SMRiB7STY1
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini596 – 674CarrierPROSITE-ProRule annotationAdd BLAST79

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni59 – 464Adenylation (A) domainSequence analysisAdd BLAST406
    Regioni601 – 671Thiolation and peptide carrier (T) domainSequence analysisAdd BLAST71
    Regioni697 – 947Thioesterase (TE) domainSequence analysisAdd BLAST251

    Sequence similaritiesi

    Family and domain databases

    Gene3Di1.10.1200.10, 1 hit
    3.40.50.1820, 1 hit
    InterProiView protein in InterPro
    IPR029058 AB_hydrolase
    IPR036736 ACP-like_sf
    IPR020845 AMP-binding_CS
    IPR000873 AMP-dep_Synth/Lig
    IPR020802 PKS_thioesterase
    IPR009081 PP-bd_ACP
    IPR001031 Thioesterase
    PfamiView protein in Pfam
    PF00501 AMP-binding, 1 hit
    PF00550 PP-binding, 1 hit
    PF00975 Thioesterase, 1 hit
    SMARTiView protein in SMART
    SM00824 PKS_TE, 1 hit
    SUPFAMiSSF47336 SSF47336, 1 hit
    SSF53474 SSF53474, 1 hit
    PROSITEiView protein in PROSITE
    PS00455 AMP_BINDING, 1 hit
    PS50075 CARRIER, 1 hit

    Sequencei

    Sequence statusi: Complete.

    B7STY1-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MAPTAVFSNP ATNPVANLKA SVKTAEGVPA TLNDLLLQAT EMYPSHELSF
    60 70 80 90 100
    ITSSAHDSSV QARTFQDFNQ RVRNLASALA AWKKPAGEVV VVYLTEHEDN
    110 120 130 140 150
    MSAVWACLLA GLVPCLQPAL SAQQEHKEGH IAHIRKLFGS ATWLTNDAGA
    160 170 180 190 200
    MQLDTIKGLD VHLFSDLLAS AEKSSVAANY VARQSQPDDE AILFLTSGST
    210 220 230 240 250
    GFSKAVVHTH RTIINACIAK GANYRLTPQT NILNWVGFDH VAGSLEMHIA
    260 270 280 290 300
    PLLYGCSQLH VHASAILSDP LLLLRLIDER SIDIAFAPNF LLAKMVRDLE
    310 320 330 340 350
    KRTDLHGKFD LSSLRRMNSG GEAVVSKTAV AFVQLLKKLG RNPSKVSFKV
    360 370 380 390 400
    AAGFGMTETC AGCIYDVVDL AENSPKHEFL ALGAPVHGCE MRIVDPEDGA
    410 420 430 440 450
    TPRSDGQPGE LQVRGPMIFV RYYNNPEATK SSFVEGGWYR TGDIGIIENG
    460 470 480 490 500
    NMRLSGRIKD TVIVHGVSYG IPELETYLQT VQGVTHSFLA AAPYRAPGQE
    510 520 530 540 550
    TEGFVVFYAP TFDLQGDDAS KKLSETHRAI KDVSVKMMTL PPQHIVPIPM
    560 570 580 590 600
    DQMEKTTLGK LSRARLLSQF VQGALAKHVA RAEELISMAR GASFVTPSTD
    610 620 630 640 650
    DEKALAAIYA GIFNLQSNEV SARDNFFELG GTSIDVIRLK REGEAHFGLS
    660 670 680 690 700
    EIPIIQILKN PIVSDLAKYV NGLVNNDASA NEYDPIVPLQ LSGDKTPIFF
    710 720 730 740 750
    VHPGVGEVLI FVNLAKYFQN ERPFYAFRAR GFEPGHPFFG SMDEMVTSYA
    760 770 780 790 800
    NAMKKTQPKG PYAIAGYSYG GVVAFEVAKR LESMGEEVKF VGLINIPPHI
    810 820 830 840 850
    ADRMHEIDWT GGMLNLAYFL SLVTKQDATD LHPKLKTMTK EEQLEVVWKL
    860 870 880 890 900
    APPERVTELQ LTPGKLDHWV SIAGSLIECG KSYNPGGNVS AVDVFYAIPL
    910 920 930 940 950
    KGSKEDWLNK QLKPWSQFSR GEPQFIDVPG QHYTLMDFDH VPQFQKIFRG

    RLEARGL
    Length:957
    Mass (Da):105,038
    Last modified:February 10, 2009 - v1
    Checksum:i473D0BBFF8F3B527
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    EU711405 Genomic DNA Translation: ACH90386.1

    Similar proteinsi

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    EU711405 Genomic DNA Translation: ACH90386.1

    3D structure databases

    ProteinModelPortaliB7STY1
    SMRiB7STY1
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-18722

    Family and domain databases

    Gene3Di1.10.1200.10, 1 hit
    3.40.50.1820, 1 hit
    InterProiView protein in InterPro
    IPR029058 AB_hydrolase
    IPR036736 ACP-like_sf
    IPR020845 AMP-binding_CS
    IPR000873 AMP-dep_Synth/Lig
    IPR020802 PKS_thioesterase
    IPR009081 PP-bd_ACP
    IPR001031 Thioesterase
    PfamiView protein in Pfam
    PF00501 AMP-binding, 1 hit
    PF00550 PP-binding, 1 hit
    PF00975 Thioesterase, 1 hit
    SMARTiView protein in SMART
    SM00824 PKS_TE, 1 hit
    SUPFAMiSSF47336 SSF47336, 1 hit
    SSF53474 SSF53474, 1 hit
    PROSITEiView protein in PROSITE
    PS00455 AMP_BINDING, 1 hit
    PS50075 CARRIER, 1 hit
    ProtoNetiSearch...

    Entry informationi

    Entry nameiATRA_TAPPA
    AccessioniPrimary (citable) accession number: B7STY1
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 2, 2016
    Last sequence update: February 10, 2009
    Last modified: October 25, 2017
    This is version 25 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
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