ID   HY6H_HYONI              Reviewed;         344 AA.
AC   P24397;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Hyoscyamine 6-dioxygenase;
DE            EC=1.14.11.11;
DE   AltName: Full=Hyoscyamine 6-beta-hydroxylase;
GN   Name=H6H;
OS   Hyoscyamus niger (Black henbane).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Hyoscyameae;
OC   Hyoscyamus.
OX   NCBI_TaxID=4079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE, AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Root;
RX   PubMed=2033047; DOI=10.1016/s0021-9258(18)92843-7;
RA   Matsuda J., Okabe S., Hashimoto T., Yamada Y.;
RT   "Molecular cloning of hyoscyamine 6 beta-hydroxylase, a 2-oxoglutarate-
RT   dependent dioxygenase, from cultured roots of Hyoscyamus niger.";
RL   J. Biol. Chem. 266:9460-9464(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8066129; DOI=10.1104/pp.105.2.483;
RA   Kanegae T., Kajiya H., Amano Y., Hashimoto T., Yamada Y.;
RT   "Species-dependent expression of the hyoscyamine 6 beta-hydroxylase gene in
RT   the pericycle.";
RL   Plant Physiol. 105:483-490(1994).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-hyoscyamine + O2 = (6S)-6-
CC         hydroxyhyoscyamine + CO2 + succinate; Xref=Rhea:RHEA:12629,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:57459, ChEBI:CHEBI:58164;
CC         EC=1.14.11.11;
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00805};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC   -!- PATHWAY: Alkaloid biosynthesis; scopolamine biosynthesis.
CC   -!- SUBUNIT: Monomer.
CC   -!- TISSUE SPECIFICITY: Root.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; M62719; AAA33387.1; -; mRNA.
DR   EMBL; D26583; BAA05630.1; -; Genomic_DNA.
DR   PIR; A40005; A40005.
DR   AlphaFoldDB; P24397; -.
DR   SMR; P24397; -.
DR   KEGG; ag:BAA05630; -.
DR   BRENDA; 1.14.11.11; 2740.
DR   BRENDA; 1.14.20.13; 2740.
DR   SABIO-RK; P24397; -.
DR   UniPathway; UPA00725; -.
DR   GO; GO:0047998; F:hyoscyamine (6S)-dioxygenase activity; IEA:UniProtKB-EC.
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:0009805; P:coumarin biosynthetic process; IEA:UniProt.
DR   GO; GO:0002238; P:response to molecule of fungal origin; IEA:UniProt.
DR   Gene3D; 2.60.120.330; -; 1.
DR   InterPro; IPR026992; DIOX_N.
DR   InterPro; IPR044861; IPNS-like_FE2OG_OXY.
DR   InterPro; IPR027443; IPNS-like_sf.
DR   InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   1: Evidence at protein level;
KW   Dioxygenase; Direct protein sequencing; Iron; Metal-binding;
KW   Oxidoreductase; Vitamin C.
FT   CHAIN           1..344
FT                   /note="Hyoscyamine 6-dioxygenase"
FT                   /id="PRO_0000067281"
FT   DOMAIN          193..293
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         217
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         219
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         274
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         284
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   344 AA;  39001 MW;  2618501AC1587F24 CRC64;
     MATFVSNWST KSVSESFIAP LQKRAEKDVP VGNDVPIIDL QQHHHLLVQQ ITKACQDFGL
     FQVINHGFPE ELMLETMEVC KEFFALPAEE KEKFKPKGEA AKFELPLEQK AKLYVEGEQL
     SNEEFLYWKD TLAHGCHPLD QDLVNSWPEK PAKYREVVAK YSVEVRKLTM RMLDYICEGL
     GLKLGYFDNE LSQIQMMLTN YYPPCPDPSS TLGSGGHYDG NLITLLQQDL PGLQQLIVKD
     ATWIAVQPIP TAFVVNLGLT LKVITNEKFE GSIHRVVTDP TRDRVSIATL IGPDYSCTIE
     PAKELLNQDN PPLYKPYSYS EFADIYLSDK SDYDSGVKPY KINV