2ODD_SINHE
ID 2ODD_SINHE Reviewed; 310 AA.
AC A0A0N9HQ36;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Deoxypodophyllotoxin synthase {ECO:0000303|PubMed:26359402};
DE EC=1.14.20.8 {ECO:0000269|PubMed:26359402};
DE AltName: Full=2-oxoglutarate dependent dioxygenase {ECO:0000303|PubMed:26359402};
GN Name=2-ODD {ECO:0000303|PubMed:26359402};
GN Synonyms=Phex30848 {ECO:0000303|PubMed:26359402};
OS Sinopodophyllum hexandrum (Himalayan may apple) (Podophyllum hexandrum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Berberidaceae; Podophylloideae;
OC Sinopodophyllum.
OX NCBI_TaxID=93608;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOTECHNOLOGY,
RP TISSUE SPECIFICITY, INDUCTION BY WOUNDING, AND PATHWAY.
RX PubMed=26359402; DOI=10.1126/science.aac7202;
RA Lau W., Sattely E.S.;
RT "Six enzymes from mayapple that complete the biosynthetic pathway to the
RT etoposide aglycone.";
RL Science 349:1224-1228(2015).
CC -!- FUNCTION: 2-oxoglutarate-dependent dioxygenase involved in the
CC biosynthesis of etoposide, a chemotherapeutic compound of the
CC topoisomerase inhibitor family (PubMed:26359402). Catalyzes the
CC conversion of yatein to deoxypodophyllotoxin (PubMed:26359402). Can
CC also use, to some extent, demethylyatein as substrate
CC (PubMed:26359402). {ECO:0000269|PubMed:26359402}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(-)-yatein + 2-oxoglutarate + O2 = (-)-deoxypodophyllotoxin +
CC CO2 + H2O + succinate; Xref=Rhea:RHEA:48744, ChEBI:CHEBI:4429,
CC ChEBI:CHEBI:4553, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031;
CC EC=1.14.20.8; Evidence={ECO:0000269|PubMed:26359402};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48745;
CC Evidence={ECO:0000269|PubMed:26359402};
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 -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC {ECO:0000269|PubMed:26359402}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in leaves and stems.
CC {ECO:0000269|PubMed:26359402}.
CC -!- INDUCTION: Transiently induced after wounding.
CC {ECO:0000269|PubMed:26359402}.
CC -!- BIOTECHNOLOGY: Combinatorially expression of Sinopodophyllum hexandrum
CC (mayapple) genes of the podophyllotoxin pathway (e.g. DIR, PLR, SDH,
CC CYP719A23, OMT3, CYP71CU1, OMT1, 2-ODD, CYP71BE54 and CYP82D61) in
CC Nicotiana benthamiana (tobacco) results in the production of the
CC chemotherapeutic compound etoposide. {ECO:0000305|PubMed:26359402}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; KT390173; ALG05135.1; -; mRNA.
DR PDB; 7E37; X-ray; 2.09 A; A/B=1-310.
DR PDB; 7E38; X-ray; 2.05 A; A/B=1-310.
DR PDBsum; 7E37; -.
DR PDBsum; 7E38; -.
DR AlphaFoldDB; A0A0N9HQ36; -.
DR SMR; A0A0N9HQ36; -.
DR KEGG; ag:ALG05135; -.
DR BRENDA; 1.14.20.8; 4928.
DR UniPathway; UPA00711; -.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019438; P:aromatic compound biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009699; P:phenylpropanoid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009611; P:response to wounding; IEP:UniProtKB.
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 3D-structure; Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT CHAIN 1..310
FT /note="Deoxypodophyllotoxin synthase"
FT /id="PRO_0000451906"
FT DOMAIN 159..258
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 184
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 186
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 239
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 249
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:7E38"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:7E38"
FT HELIX 24..39
FT /evidence="ECO:0007829|PDB:7E38"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:7E38"
FT HELIX 52..66
FT /evidence="ECO:0007829|PDB:7E38"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:7E38"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:7E38"
FT TURN 80..83
FT /evidence="ECO:0007829|PDB:7E38"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:7E38"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:7E38"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:7E38"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:7E38"
FT HELIX 119..146
FT /evidence="ECO:0007829|PDB:7E38"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:7E38"
FT HELIX 153..157
FT /evidence="ECO:0007829|PDB:7E38"
FT STRAND 161..169
FT /evidence="ECO:0007829|PDB:7E38"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:7E38"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:7E38"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:7E38"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:7E38"
FT STRAND 215..222
FT /evidence="ECO:0007829|PDB:7E38"
FT HELIX 224..229
FT /evidence="ECO:0007829|PDB:7E38"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:7E38"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:7E38"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:7E38"
FT STRAND 249..257
FT /evidence="ECO:0007829|PDB:7E38"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:7E38"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:7E38"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:7E38"
FT HELIX 282..289
FT /evidence="ECO:0007829|PDB:7E38"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:7E38"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:7E38"
SQ SEQUENCE 310 AA; 35028 MW; 9A4351E8D74AB74A CRC64;
MGSTAPLRLP VIDLSMKNLK PGTTSWNSVR TQVREALEEY GCFEAVIDAV SPELQKAVCN
KGHELLNLPL ETKMLNGNKP EYDGFTSIPN LNEGMGVGRI TDLEKVERFT NLMWPEGNKD
FCETVYSYGK RMAEVDHILK MMVFESFGME KHFDSFCEST NYLLHFMRYQ QPGKDGRSPA
LSLHKDKSIL TIVNQNDVKG LEFETKDGEW ILPTADNHIV LLGDCFMAWS NGRLHSPLHR
VTLVANQARL STSSFSFPKD IIETPAELVD EEHPLLFNPF EITELLAYCF TKEGAKAVCD
LKQYKAYTGA
