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

Dual function macrocyclase-peptidase POPB

Gene

POPB

Organism
Galerina marginata (strain CBS 339.88)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Dual function macrocyclase-peptidase involved in the biosynthesis of the highly toxic amanitin toxin family of macrocycles (PubMed:22202811, PubMed:28866879, PubMed:29051530). Cleaves peptide bonds on the C-terminal side of prolyl residues (PubMed:29051530). The enzyme first removes 10 residues from the N-terminus of a 35-residue substrate (PubMed:29051530). Conformational trapping of the 25 amino-acid peptide forces the enzyme to release this intermediate rather than proceed to macrocyclization (PubMed:29051530). The enzyme rebinds the 25 amino-acid peptide in a different conformation and catalyzes macrocyclization of the N-terminal eight residues (PubMed:28866879, PubMed:29051530).3 Publications

Catalytic activityi

Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.2 Publications

Kineticsi

  1. KM=23 µM for the full alpha-amanitin 35mer proprotein1 Publication
  2. KM=51 µM for the 25mer IWGIGCNPWTAEHVDQTLASGNDIC1 Publication
  3. KM=19 µM for the 25mer LWGIGCNPWTAEHVDQTLASGNDIC1 Publication
  4. KM=8 µM for the 25mer IFGIGCNPWTAEHVDQTLASGNDIC1 Publication
  5. KM=28 µM for the 25mer IWGIGSNPWTAEHVDQTLASGNDIC1 Publication
  6. KM=10 µM for the 25mer IWGIGCNPWTAEHVDQTLASGNDIS1 Publication
  7. KM=25 µM for the 19mer IWGIGCNPDQTLASGNDIC1 Publication
  8. KM=380 µM for the 14mer IWGIGCNPWTAEHV1 Publication
  9. KM=24.4 µM for the 13mer IWGIGCNPWTAEH1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei577Charge relay systemPROSITE-ProRule annotation1 Publication1
    Active sitei661Charge relay systemPROSITE-ProRule annotation1 Publication1
    Active sitei698Charge relay systemPROSITE-ProRule annotation1 Publication1

    GO - Molecular functioni

    Keywordsi

    Molecular functionHydrolase, Protease, Serine protease

    Protein family/group databases

    ESTHERi9agar-h2e7q8 S9N_PPCE_Peptidase_S9

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual function macrocyclase-peptidase POPB1 Publication (EC:3.4.21.262 Publications)
    Alternative name(s):
    Prolyl oligopeptidase B1 Publication
    Short name:
    POP B1 Publication
    Toxin-processing prolyl oligopeptidase1 Publication
    Gene namesi
    Name:POPB1 Publication
    ORF Names:GALMADRAFT_78538
    OrganismiGalerina marginata (strain CBS 339.88)
    Taxonomic identifieri685588 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesStrophariaceaeGalerina
    Proteomesi
    • UP000027222 Componenti: Unassembled WGS sequence

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi577S → A: Impairs catalytic activity but still binds bith 35mer and 25mer substrates. 1 Publication1
    Mutagenesisi661D → A: Impairs catalytic activity but still binds bith 35mer and 25mer substrates. 1 Publication1
    Mutagenesisi663R → A, K or Q: Leads to diminished activities for both peptide bond hydrolysis and macrocyclization. 1 Publication1
    Mutagenesisi695Missing : Leads to diminished activities for both peptide bond hydrolysis and macrocyclization. 1 Publication1
    Mutagenesisi698H → A: Impairs catalytic activity but still binds bith 35mer and 25mer substrates. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004437171 – 730Dual function macrocyclase-peptidase POPBAdd BLAST730

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    Secondary structure

    1730
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi20 – 25Combined sources6
    Turni26 – 28Combined sources3
    Beta strandi29 – 34Combined sources6
    Helixi38 – 41Combined sources4
    Helixi45 – 63Combined sources19
    Helixi67 – 79Combined sources13
    Beta strandi95 – 100Combined sources6
    Beta strandi102 – 106Combined sources5
    Beta strandi108 – 116Combined sources9
    Helixi120 – 122Combined sources3
    Helixi124 – 127Combined sources4
    Beta strandi128 – 132Combined sources5
    Helixi134 – 136Combined sources3
    Beta strandi143 – 150Combined sources8
    Beta strandi154 – 163Combined sources10
    Beta strandi167 – 175Combined sources9
    Helixi182 – 187Combined sources6
    Beta strandi197 – 200Combined sources4
    Beta strandi211 – 218Combined sources8
    Beta strandi235 – 240Combined sources6
    Helixi245 – 247Combined sources3
    Beta strandi249 – 253Combined sources5
    Beta strandi261 – 266Combined sources6
    Beta strandi272 – 283Combined sources12
    Beta strandi286 – 291Combined sources6
    Beta strandi304 – 307Combined sources4
    Beta strandi309 – 312Combined sources4
    Beta strandi314 – 320Combined sources7
    Beta strandi323 – 328Combined sources6
    Beta strandi336 – 341Combined sources6
    Beta strandi344 – 346Combined sources3
    Beta strandi348 – 353Combined sources6
    Beta strandi359 – 367Combined sources9
    Turni368 – 370Combined sources3
    Beta strandi371 – 378Combined sources8
    Beta strandi381 – 387Combined sources7
    Beta strandi393 – 398Combined sources6
    Beta strandi403 – 408Combined sources6
    Beta strandi413 – 422Combined sources10
    Beta strandi425 – 433Combined sources9
    Helixi438 – 440Combined sources3
    Beta strandi442 – 447Combined sources6
    Helixi455 – 457Combined sources3
    Beta strandi458 – 466Combined sources9
    Beta strandi472 – 480Combined sources9
    Turni485 – 488Combined sources4
    Beta strandi491 – 494Combined sources4
    Helixi509 – 518Combined sources10
    Beta strandi521 – 525Combined sources5
    Helixi535 – 539Combined sources5
    Helixi543 – 546Combined sources4
    Helixi547 – 562Combined sources16
    Beta strandi571 – 576Combined sources6
    Helixi578 – 589Combined sources12
    Beta strandi596 – 602Combined sources7
    Turni607 – 609Combined sources3
    Helixi610 – 612Combined sources3
    Helixi616 – 619Combined sources4
    Helixi620 – 623Combined sources4
    Helixi629 – 635Combined sources7
    Turni636 – 638Combined sources3
    Helixi640 – 642Combined sources3
    Beta strandi646 – 648Combined sources3
    Beta strandi652 – 658Combined sources7
    Beta strandi662 – 664Combined sources3
    Helixi667 – 679Combined sources13
    Beta strandi687 – 692Combined sources6
    Helixi704 – 721Combined sources18

    3D structure databases

    SMRiH2E7Q8
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S9A family.Curated

    Family and domain databases

    Gene3Di3.40.50.1820, 2 hits
    InterProiView protein in InterPro
    IPR029058 AB_hydrolase
    IPR002471 Pept_S9_AS
    IPR023302 Pept_S9A_N
    IPR001375 Peptidase_S9
    IPR002470 Peptidase_S9A
    PfamiView protein in Pfam
    PF00326 Peptidase_S9, 1 hit
    PF02897 Peptidase_S9_N, 1 hit
    PRINTSiPR00862 PROLIGOPTASE
    SUPFAMiSSF53474 SSF53474, 1 hit
    PROSITEiView protein in PROSITE
    PS00708 PRO_ENDOPEP_SER, 1 hit

    Sequencei

    Sequence statusi: Complete.

    H2E7Q8-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSSVTWAPGN YPSTRRSDHV DTYQSASKGE VPVPDPYQWL EESTDEVDKW
    60 70 80 90 100
    TTAQADLAQS YLDQNADIQK LAEKFRASRN YAKFSAPTLL DDGHWYWFYN
    110 120 130 140 150
    RGLQSQSVLY RSKEPALPDF SKGDDNVGDV FFDPNVLAAD GSAGMVLCKF
    160 170 180 190 200
    SPDGKFFAYA VSHLGGDYST IYVRSTSSPL SQASVAQGVD GRLSDEVKWF
    210 220 230 240 250
    KFSTIIWTKD SKGFLYQRYP ARERHEGTRS DRNAMMCYHK VGTTQEEDII
    260 270 280 290 300
    VYQDNEHPEW IYGADTSEDG KYLYLYQFKD TSKKNLLWVA ELDEDGVKSG
    310 320 330 340 350
    IHWRKVVNEY AADYNIITNH GSLVYIKTNL NAPQYKVITI DLSKDEPEIR
    360 370 380 390 400
    DFIPEEKDAK LAQVNCANEE YFVAIYKRNV KDEIYLYSKA GVQLTRLAPD
    410 420 430 440 450
    FVGAASIANR QKQTHFFLTL SGFNTPGTIA RYDFTAPETQ RFSILRTTKV
    460 470 480 490 500
    NELDPDDFES TQVWYESKDG TKIPMFIVRH KSTKFDGTAA AIQYGYGGFA
    510 520 530 540 550
    TSADPFFSPI ILTFLQTYGA IFAVPSIRGG GEFGEEWHKG GRRETKVNTF
    560 570 580 590 600
    DDFIAAAQFL VKNKYAAPGK VAINGASNGG LLVMGSIVRA PEGTFGAAVP
    610 620 630 640 650
    EGGVADLLKF HKFTGGQAWI SEYGNPSIPE EFDYIYPLSP VHNVRTDKVM
    660 670 680 690 700
    PATLITVNIG DGRVVPMHSF KFIATLQHNV PQNPHPLLIK IDKSWLGHGM
    710 720 730
    GKPTDKNVKD AADKWGFIAR ALGLELKTVE
    Length:730
    Mass (Da):81,781
    Last modified:January 22, 2014 - v2
    Checksum:i354827749ED68A4B
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    JN827314 mRNA Translation: AEX26938.2
    KL142408 Genomic DNA Translation: KDR68475.1

    Genome annotation databases

    EnsemblFungiiKDR68475; KDR68475; GALMADRAFT_78538

    Similar proteinsi

    Entry informationi

    Entry nameiPOPB_GALM3
    AccessioniPrimary (citable) accession number: H2E7Q8
    Secondary accession number(s): A0A067SC43
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 28, 2018
    Last sequence update: January 22, 2014
    Last modified: July 18, 2018
    This is version 22 of the entry and version 2 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. Protein Spotlight
      Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
    4. SIMILARITY comments
      Index of protein domains and families

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health