ANDA_EMEVA
ID ANDA_EMEVA Reviewed; 293 AA.
AC A0A097ZPD5;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-JAN-2015, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Dioxygenase andA {ECO:0000303|PubMed:25216349};
DE EC=1.14.11.- {ECO:0000269|PubMed:25216349};
DE AltName: Full=Anditomin synthesis protein A {ECO:0000303|PubMed:25216349};
GN Name=andA {ECO:0000303|PubMed:25216349};
OS Emericella variicolor (Aspergillus stellatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1549217;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE,
RP CATALYTIC ACTIVITY, AND COFACTOR.
RC STRAIN=ATCC 12069 / CBS 136.55 / IMI 60316 / NBRC 32302;
RX PubMed=25216349; DOI=10.1021/ja508127q;
RA Matsuda Y., Wakimoto T., Mori T., Awakawa T., Abe I.;
RT "Complete biosynthetic pathway of anditomin: nature's sophisticated
RT synthetic route to a complex fungal meroterpenoid.";
RL J. Am. Chem. Soc. 136:15326-15336(2014).
CC -!- FUNCTION: Dioxygenase; part of the gene cluster that mediates the
CC biosynthesis of anditomin, a fungal meroterpenoid (PubMed:25216349).
CC The first step of the pathway is the synthesis of 3,5-
CC dimethylorsellinic acid (DMOA) by the polyketide synthase andM
CC (PubMed:25216349). DMOA is then converted to the phthalide compound
CC 5,7-dihydroxy-4,6-dimethylphthalide (DHDMP) by the cytochrome P450
CC monooxygenase andK, which is further prenylated by the
CC prenyltransferase andD to yield farnesyl-DHDMP (PubMed:25216349).
CC Further epoxidation by the FAD-dependent monooxygenase andE leads to
CC epoxyfarnesyl-DHDMP (PubMed:25216349). The next step involves the
CC terpene cyclase andB that converts epoxyfarnesyl-DHDMP into preandiloid
CC A through opening of the epoxide ring followed by the cyclization of
CC the farnesyl moiety (PubMed:25216349). Preandiloid A is in turn
CC oxidized at the C-3 hydroxyl group to yield preandiloid B by the
CC dehydrogenase andC (PubMed:25216349). The dioxygenase andA is solely
CC responsible for the dehydrogenation of preandiloid B leading to the
CC enone preandiloid C, as well as for the intriguing structural
CC rearrangement to generate the bicyclo[2.2.2]octane core, transforming
CC preandiloid C into andiconin (PubMed:25216349). FAD-binding
CC monooxygenase andJ then produces andilesin D which is reduced by
CC dehydrogenase andI to yield andilesin A (PubMed:25216349). Action of
CC acetyltransferase andG followed by a spontaneous acetate elimination
CC leads then to andilesin B, which is in turn substrate of the short
CC chain dehydrogenase andH to yield andilesin C (PubMed:25216349).
CC Finally, the dioxygenase andF catalyzes the transformation of andilesin
CC C to anditomin (PubMed:25216349). {ECO:0000269|PubMed:25216349}.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:25216349};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:25216349}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q4WAW9}.
CC -!- DISRUPTION PHENOTYPE: Impairs the synthesis of anditomin but
CC accumulates preandiloid B (PubMed:25216349).
CC {ECO:0000269|PubMed:25216349}.
CC -!- SIMILARITY: Belongs to the PhyH family. {ECO:0000305}.
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DR EMBL; AB981314; BAP81855.1; -; Genomic_DNA.
DR PDB; 5ZM2; X-ray; 2.50 A; A/B/C/D=9-293.
DR PDB; 5ZM3; X-ray; 2.25 A; A/B/C/D=9-293.
DR PDB; 5ZM4; X-ray; 1.95 A; A/B/C/D=9-293.
DR PDBsum; 5ZM2; -.
DR PDBsum; 5ZM3; -.
DR PDBsum; 5ZM4; -.
DR AlphaFoldDB; A0A097ZPD5; -.
DR SMR; A0A097ZPD5; -.
DR BioCyc; MetaCyc:MON-19047; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR008775; Phytyl_CoA_dOase.
DR Pfam; PF05721; PhyH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT CHAIN 1..293
FT /note="Dioxygenase andA"
FT /id="PRO_0000436577"
FT BINDING 135
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 137
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT BINDING 213
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:O14832"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:5ZM4"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:5ZM4"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:5ZM4"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:5ZM4"
FT HELIX 41..54
FT /evidence="ECO:0007829|PDB:5ZM4"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:5ZM4"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:5ZM4"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:5ZM4"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:5ZM4"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:5ZM4"
FT HELIX 88..92
FT /evidence="ECO:0007829|PDB:5ZM4"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:5ZM4"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:5ZM4"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:5ZM4"
FT STRAND 115..125
FT /evidence="ECO:0007829|PDB:5ZM4"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:5ZM4"
FT HELIX 142..146
FT /evidence="ECO:0007829|PDB:5ZM4"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:5ZM4"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:5ZM4"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:5ZM3"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:5ZM4"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:5ZM4"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:5ZM4"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:5ZM3"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:5ZM4"
FT STRAND 224..233
FT /evidence="ECO:0007829|PDB:5ZM4"
FT HELIX 247..250
FT /evidence="ECO:0007829|PDB:5ZM4"
FT HELIX 255..260
FT /evidence="ECO:0007829|PDB:5ZM4"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:5ZM4"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:5ZM4"
FT HELIX 282..286
FT /evidence="ECO:0007829|PDB:5ZM4"
SQ SEQUENCE 293 AA; 32480 MW; 9438D81D45087ED3 CRC64;
MTIESKNYPP IRRVNASQGS DAAYQILQED GCVIVEQVIC PNIIAKISDD VNRVMDKATI
GAKKGEQTHI INMHNRTIHM GDLVLTSKTY RDELLNLPFA HEVLEKVFKK DSGDYWLNMG
NILNMLPGAE AQRPHRDDYL YPVSQHMDPA TSPDLMINIT FPLNEFRHDN GGTLLLPKSH
TGPNADFYAN AEDLPAAEMQ VGDALIFTGK CVHGGGANRS DKPRIGLALA AQPGYLTPRE
SNVNVPRDIV ETMTPLAQRM IGWGTVRTKD TYGLNMLQDK DFHEALGLKS KTA
