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Protein

Protostadienol synthase A

Gene

pdsA

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Protostadienol synthase; part of the gene cluster that mediates the biosynthesis of helvolic acid, an antibacterial nortriterpenoid (PubMed:19415934, PubMed:19216560, PubMed:19951700). Protostadienol synthase cyclizes (3S)-oxidosqualene to (17Z)-protosta-17(20),24-dien-3-beta-ol (protostadienol)(PubMed:19415934, PubMed:19216560, PubMed:19951700). The synthesis of protostadienol is followed by several steps of monooxygenation, dehydrogenation, and acyl transfer to yield the final helvolic acid (PubMed:19216560). After the formation of the basic carbon skeleton protostadienol, both sdr1 and cyp5081A1 presumably function together to catalyze the demethylation of C-29 (PubMed:19415934). Because both enzymes apparently accept protostadienol as a substrate in vivo, the exact order of the two reactions has still to be established (PubMed:19415934). The remaining steps are probably performed by the monooxygenases cyp5180B1-D1, the acyltransferases encoded by AFUA_4G14820 and AFUA_4G14840, and the 3-ketosteroid 1-dehydrogenase encoded by AFUA_4G14850 (PubMed:19415934, PubMed:19216560).3 Publications

Catalytic activityi

(3S)-2,3-epoxy-2,3-dihydrosqualene = (17Z)-protosta-17(20),24-dien-3-beta-ol.3 Publications

Kineticsi

  1. KM=14.4 µM for 2,3-oxidosqualene1 Publication

    Pathwayi: Mycotoxin biosynthesis

    This protein is involved in Mycotoxin biosynthesis.2 Publications
    View all proteins of this organism that are known to be involved in Mycotoxin biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei240Proton acceptorCurated1
    Active sitei463Proton donorCurated1

    GO - Molecular functioni

    • lanosterol synthase activity Source: AspGD

    GO - Biological processi

    • (17Z)-protosta-17(20),24-dien-3beta-ol biosynthetic process Source: AspGD
    • pathogenesis Source: UniProtKB-KW
    • secondary metabolic process Source: AspGD

    Keywordsi

    Molecular functionIsomerase
    Biological processLipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Virulence

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16527

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protostadienol synthase A1 Publication (EC:5.4.99.323 Publications)
    Alternative name(s):
    Helvolic acid synthesis protein pdsA1 Publication
    Oxidosqualene cyclase1 Publication
    Oxidosqualene:protostadienol cyclase1 Publication
    Short name:
    OSPC1 Publication
    Gene namesi
    Name:pdsA1 Publication
    Synonyms:osc31 Publication
    ORF Names:AFUA_4G14770
    OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
    Taxonomic identifieri330879 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    Proteomesi
    • UP000002530 Componentsi: Chromosome 4, Unassembled WGS sequence

    Organism-specific databases

    EuPathDBiFungiDB:Afu4g14770

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi702 – 708APPGGMR → NKSCAIS: Changes its oxidosqualene:protostadienol cyclase (OSPC) activity to oxidosqualene:lanosterol cyclase (OSLC) activity. 1 Publication7
    Mutagenesisi703P → K: Impairs catalytic activity; when associated with S-704. 1 Publication1
    Mutagenesisi704P → S: Impairs catalytic activity; when associated with K-703. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004154951 – 735Protostadienol synthase AAdd BLAST735

    Expressioni

    Inductioni

    Expression is under the control of the secondary metabolism regulator laeA (PubMed:17432932). Expression is down-regulated when gliT is deleted and up-regulated upon exposure to exogenous gliotoxin (PubMed:25311525).2 Publications

    Interactioni

    Protein-protein interaction databases

    STRINGi5085.CADAFUBP00007020

    Structurei

    3D structure databases

    ProteinModelPortaliQ4WR16
    SMRiQ4WR16
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Repeati132 – 173PFTB 1Add BLAST42
    Repeati490 – 531PFTB 2Add BLAST42
    Repeati567 – 607PFTB 3Add BLAST41
    Repeati616 – 663PFTB 4Add BLAST48

    Sequence similaritiesi

    Belongs to the terpene cyclase/mutase family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    HOGENOMiHOG000234317
    InParanoidiQ4WR16
    KOiK15811
    OMAiEDGFWPG
    OrthoDBiEOG092C0KMX

    Family and domain databases

    CDDicd02892 SQCY_1, 1 hit
    InterProiView protein in InterPro
    IPR032696 SQ_cyclase_C
    IPR032697 SQ_cyclase_N
    IPR018333 Squalene_cyclase
    IPR008930 Terpenoid_cyclase/PrenylTrfase
    PfamiView protein in Pfam
    PF13243 SQHop_cyclase_C, 1 hit
    PF13249 SQHop_cyclase_N, 1 hit
    SUPFAMiSSF48239 SSF48239, 2 hits
    TIGRFAMsiTIGR01787 squalene_cyclas, 1 hit

    Sequencei

    Sequence statusi: Complete.

    Q4WR16-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MATDSSMPGT VIGKAEFSDT KAASEFGTDL SRWRLNVDNG RHMWEYLESE
    60 70 80 90 100
    DEARKRPQSF LEKYWLGLPY ELPARPRATC ALEAVENGWE FFKRLQTADG
    110 120 130 140 150
    HWGCNDDGPL FVTSGMVIAR YIVGIPIDSH MKQEMCRYLL NVVNEDGGWG
    160 170 180 190 200
    LFIQSPSTVF GTVMNYCMLR ILGLGPEHPA MAKARNTLHR LGSARATPTW
    210 220 230 240 250
    GKFWLCVLGV YEWEGMVPLP PEPLLVPASL PFNPGKWWVH TRNVYISMSY
    260 270 280 290 300
    LYGHRFSMPP NKLVQALRDE LYDIPYQQIN WPAQRTNVSA ADRLTDPTWI
    310 320 330 340 350
    QRSFTSALTM YETFKIPFLR RRALNEALFQ IETETRNTHY LCIAPVSFAS
    360 370 380 390 400
    NMLALYHAHG RDSHWIRGMR DRFIDPMWLC REGLAASGTN GTSLWDTALT
    410 420 430 440 450
    VQATIDAGLA ARPENQAILR KALEFIDNSQ IREDPLGVHH VYRQPTRGAW
    460 470 480 490 500
    PFSTRDQSYA VSDTTAEAVK VIVLLQRIEG FPSRISDERL QQAIDLILGM
    510 520 530 540 550
    ENAGGGFSAY EPVRGPKFLE LLNITELYEN VMTDNLYPEC TSSVIMCLTT
    560 570 580 590 600
    FAREYPTYRP RDIQACLSRS IDYLLRSQYP NGGWFASWGV CFTYATMFAL
    610 620 630 640 650
    QGLACMGWNE SNCAACQRAC SFLLQHQNPD GGWGESLDTV RFKQYLPHPD
    660 670 680 690 700
    GSQVTNTAYA VIGLLAARCG NHEAIRRGVA YLVKEQQDTG EWLPGPLEGV
    710 720 730
    FAPPGGMRYP NYKFHFTLMA LGRYVAIHGN ECLAI
    Length:735
    Mass (Da):83,091
    Last modified:July 5, 2005 - v1
    Checksum:iAA0AC92A8A6E36F8
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AAHF01000005 Genomic DNA Translation: EAL89318.1
    RefSeqiXP_751356.1, XM_746263.1

    Genome annotation databases

    EnsemblFungiiCADAFUAT00008356; CADAFUAP00008356; CADAFUAG00008356
    GeneIDi3509337
    KEGGiafm:AFUA_4G14770

    Similar proteinsi

    Entry informationi

    Entry nameiPDSA_ASPFU
    AccessioniPrimary (citable) accession number: Q4WR16
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 22, 2012
    Last sequence update: July 5, 2005
    Last modified: April 25, 2018
    This is version 74 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health