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Protein

Pentalenolactone synthase

Gene

pntM

Organism
Streptomyces arenae
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the final step in the biosynthesis of the sesquiterpenoid antibiotic pentalenolactone by mediating the oxidative rearrangement of pentalenolactone F to pentalenolactone.1 Publication

Catalytic activityi

Pentalenolactone F + O2 + 2 reduced ferredoxin + 2 H+ = pentalenolactone + 2 oxidized ferredoxin + 2 H2O.1 Publication

Cofactori

heme1 Publication

Kineticsi

kcat is 8.8 min(-1) with pentalenolactone F as substrate.

  1. KM=430 µM for pentalenolactone F1 Publication

    Pathwayi: pentalenolactone biosynthesis

    This protein is involved in the pathway pentalenolactone biosynthesis, which is part of Antibiotic biosynthesis.1 Publication
    View all proteins of this organism that are known to be involved in the pathway pentalenolactone biosynthesis and in Antibiotic biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi347Iron (heme axial ligand)By similarity1

    GO - Molecular functioni

    GO - Biological processi

    • antibiotic biosynthetic process Source: UniProtKB-KW
    • oxidation-reduction process Source: UniProtKB
    • pentalenolactone biosynthetic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Biological processi

    Antibiotic biosynthesis

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00974.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pentalenolactone synthase (EC:1.14.19.8)
    Alternative name(s):
    Pentalenolactone biosynthesis protein M
    Gene namesi
    Name:pntM
    OrganismiStreptomyces arenae
    Taxonomic identifieri29301 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

    Pathology & Biotechi

    Disruption phenotypei

    Accumulation of the precursor pentalenolactone F and lack of production of pentalenolactone.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004220101 – 398Pentalenolactone synthaseAdd BLAST398

    Structurei

    Secondary structure

    1398
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi6 – 8Combined sources3
    Beta strandi12 – 16Combined sources5
    Helixi19 – 27Combined sources9
    Beta strandi29 – 34Combined sources6
    Beta strandi36 – 38Combined sources3
    Beta strandi40 – 43Combined sources4
    Helixi46 – 53Combined sources8
    Beta strandi58 – 61Combined sources4
    Helixi72 – 80Combined sources9
    Turni86 – 88Combined sources3
    Helixi89 – 100Combined sources12
    Helixi101 – 104Combined sources4
    Helixi106 – 129Combined sources24
    Beta strandi132 – 135Combined sources4
    Helixi136 – 139Combined sources4
    Turni140 – 142Combined sources3
    Helixi143 – 153Combined sources11
    Helixi157 – 159Combined sources3
    Helixi160 – 163Combined sources4
    Helixi166 – 170Combined sources5
    Helixi176 – 199Combined sources24
    Helixi205 – 211Combined sources7
    Helixi212 – 214Combined sources3
    Helixi219 – 232Combined sources14
    Helixi235 – 250Combined sources16
    Helixi252 – 260Combined sources9
    Helixi262 – 264Combined sources3
    Helixi265 – 275Combined sources11
    Helixi282 – 284Combined sources3
    Beta strandi286 – 292Combined sources7
    Beta strandi294 – 296Combined sources3
    Beta strandi299 – 301Combined sources3
    Beta strandi306 – 309Combined sources4
    Helixi311 – 315Combined sources5
    Turni318 – 320Combined sources3
    Turni322 – 325Combined sources4
    Helixi343 – 345Combined sources3
    Helixi350 – 367Combined sources18
    Beta strandi372 – 375Combined sources4
    Helixi377 – 379Combined sources3
    Beta strandi395 – 397Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    5L1OX-ray2.03A1-398[»]
    5L1PX-ray2.28A1-398[»]
    5L1QX-ray2.03A1-398[»]
    5L1RX-ray2.00A1-398[»]
    5L1SX-ray2.08A1-398[»]
    5L1TX-ray2.08A1-398[»]
    5L1UX-ray2.07A1-398[»]
    5L1VX-ray2.12A1-398[»]
    5L1WX-ray2.06A1-398[»]
    SMRiE3VWI3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.Curated

    Phylogenomic databases

    KOiK17476.

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    InterProiIPR001128. Cyt_P450.
    IPR002397. Cyt_P450_B.
    IPR017972. Cyt_P450_CS.
    [Graphical view]
    PfamiPF00067. p450. 1 hit.
    [Graphical view]
    PRINTSiPR00359. BP450.
    PR00385. P450.
    SUPFAMiSSF48264. SSF48264. 1 hit.
    PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    E3VWI3-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTDLPRLPFD NPDIMGIAPQ MLALQKEGPI ARVGTAGEDA WLVTRYDEVR
    60 70 80 90 100
    TLLADRRLRL SNPNPQPSAK SAARAFMVAL MAGDDHETEP ARHAQMRSLL
    110 120 130 140 150
    IPRFSTRRLR LMKTRIEHHV DELLDQLAAS APPVDLHRVL SFRLPTMVVC
    160 170 180 190 200
    DLLGVPLADR ERFGQWARGT FDQSDNEHSA NTFQQVVDYM LELVARKRVE
    210 220 230 240 250
    PGDDILSELI AEKDGALSDA DIAHLGNAVL LFGYETTIVR IDLGTLLLLR
    260 270 280 290 300
    NPVQRAQLAE DPGLAPAAVE EILRLGVGGK GSNALIPRYA HGDITVGETV
    310 320 330 340 350
    IRTGDAVMLA IGAANYDDRA FPDGGLFDLT RVRPRSHLAF GHGARHCIGR
    360 370 380 390
    TLARIELTAV FERLFRRLPD LRLAVPEESL RWQEHRITGG FDEIPVTF
    Length:398
    Mass (Da):44,164
    Last modified:January 11, 2011 - v1
    Checksum:i06DB17430F6ABBD0
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    HQ292065 Genomic DNA. Translation: ADO85571.1.

    Genome annotation databases

    KEGGiag:ADO85571.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    HQ292065 Genomic DNA. Translation: ADO85571.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    5L1OX-ray2.03A1-398[»]
    5L1PX-ray2.28A1-398[»]
    5L1QX-ray2.03A1-398[»]
    5L1RX-ray2.00A1-398[»]
    5L1SX-ray2.08A1-398[»]
    5L1TX-ray2.08A1-398[»]
    5L1UX-ray2.07A1-398[»]
    5L1VX-ray2.12A1-398[»]
    5L1WX-ray2.06A1-398[»]
    SMRiE3VWI3.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:ADO85571.

    Phylogenomic databases

    KOiK17476.

    Enzyme and pathway databases

    UniPathwayiUPA00974.

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    InterProiIPR001128. Cyt_P450.
    IPR002397. Cyt_P450_B.
    IPR017972. Cyt_P450_CS.
    [Graphical view]
    PfamiPF00067. p450. 1 hit.
    [Graphical view]
    PRINTSiPR00359. BP450.
    PR00385. P450.
    SUPFAMiSSF48264. SSF48264. 1 hit.
    PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiPNTM_STRAE
    AccessioniPrimary (citable) accession number: E3VWI3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2013
    Last sequence update: January 11, 2011
    Last modified: November 30, 2016
    This is version 20 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

    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.