ID   PENH_STREX              Reviewed;         283 AA.
AC   E3VWK0;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 1.
DT   03-AUG-2022, entry version 15.
DE   RecName: Full=1-deoxypentalenic acid 11-beta-hydroxylase;
DE            EC=1.14.11.35;
DE   AltName: Full=Pentalenolactone biosynthesis protein H;
GN   Name=penH;
OS   Streptomyces exfoliatus (Streptomyces hydrogenans).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1905;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=UC5319;
RX   PubMed=21284395; DOI=10.1021/ja111279h;
RA   Zhu D., Seo M.J., Ikeda H., Cane D.E.;
RT   "Genome mining in streptomyces. Discovery of an unprecedented P450-
RT   catalyzed oxidative rearrangement that is the final step in the
RT   biosynthesis of pentalenolactone.";
RL   J. Am. Chem. Soc. 133:2128-2131(2011).
CC   -!- FUNCTION: Catalyzes the conversion of 1-deoxypentalenic acid to 11-
CC       beta-hydroxy-1-deoxypentalenic acid in the biosynthesis of
CC       pentalenolactone antibiotic. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-deoxypentalenate + 2-oxoglutarate + O2 = 1-deoxy-11beta-
CC         hydroxypentalenate + CO2 + succinate; Xref=Rhea:RHEA:34619,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:68650, ChEBI:CHEBI:70779;
CC         EC=1.14.11.35;
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
CC   -!- PATHWAY: Antibiotic biosynthesis; pentalenolactone biosynthesis.
CC   -!- SIMILARITY: Belongs to the PhyH family. {ECO:0000305}.
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DR   EMBL; HQ292066; ADO85588.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3VWK0; -.
DR   SMR; E3VWK0; -.
DR   UniPathway; UPA00974; -.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR008775; Phytyl_CoA_dOase.
DR   Pfam; PF05721; PhyH; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW   Vitamin C.
FT   CHAIN           1..283
FT                   /note="1-deoxypentalenic acid 11-beta-hydroxylase"
FT                   /id="PRO_0000422002"
FT   REGION          260..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         135..137
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250"
FT   BINDING         135
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         137
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         151
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         224
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         226
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250"
FT   BINDING         238
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   283 AA;  31325 MW;  2EFD6EAAAFE83414 CRC64;
     MTDTLSDYVD CTPLLDDREA LDRFYDEHGY VYLRGALDRE LVRTAAEQML EGLIALGHAD
     PATTLDTLTI DSFEAVDEVA MHDYVKYDDL WNHPSTLKVW EKVLGEPVFV FKSTTIRYYP
     SAAGSAEPSF LTPLHQDGFY IGPNKDFRTA WIPLLPTSHG IGGVAVADGS HKKGPREHVV
     TEQFRRFGHA VRGIPAEEFG TDEQLLFSPM EPGDVLIFHA FMCHKSIPNV SANPAGMRMS
     MDTRIQPASS HRGFNALTPW PESAKDASKG ILSKITGTPT TAE