ATR2_STEAL
ID ATR2_STEAL Reviewed; 506 AA.
AC A0A8F4SN83;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2022, sequence version 1.
DT 03-AUG-2022, entry version 3.
DE RecName: Full=Cytochrome P450 monooxygenase atr2 {ECO:0000303|PubMed:34154413};
DE EC=1.-.-.- {ECO:0000269|PubMed:34154413};
DE AltName: Full=Atranorin biosynthesis cluster protein 2 {ECO:0000303|PubMed:34154413};
GN Name=atr2 {ECO:0000303|PubMed:34154413};
OS Stereocaulon alpinum (Alpine snow lichen) (Stereocaulon paschale var.
OS alpinum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC OSLEUM clade; Lecanoromycetidae; Lecanorales; Lecanorineae;
OC Stereocaulaceae; Stereocaulon.
OX NCBI_TaxID=350623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=34154413; DOI=10.1128/mbio.01111-21;
RA Kim W., Liu R., Woo S., Kang K.B., Park H., Yu Y.H., Ha H.H., Oh S.Y.,
RA Yang J.H., Kim H., Yun S.H., Hur J.S.;
RT "Linking a gene cluster to atranorin, a major cortical substance of
RT lichens, through genetic dereplication and heterologous expression.";
RL MBio 12:e0111121-e0111121(2021).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of atranorin, a depside of polyketide origin
CC that accumulates in the cortical or medullary layers of lichen thalli
CC (PubMed:34154413). Atr2 performs the oxidation at the C-9 position of
CC 4-O-demethylbarbatic acid to yield proatranorin III via proatranorin II
CC (PubMed:34154413). Atr2 is also able to oxidize the atr3 product
CC proatranorin I to produce the final compound atranorin
CC (PubMed:34154413). The first step in the pathway is performed by the
CC non-reducing polyketide synthase atr1 that produces 4-O-
CC demethylbarbatic acid composed of two 3-methylorsellinic acid (3MOA)
CC moieties. The pathway continues with the actions of the cytochrome P450
CC monooygenase atr2 that catalizes the oxidation of c-9 and the O-
CC methyltransferase atr3 that performs the methylation of the carboxyl
CC group to yield atranorin, via the proatranorin II and III intermediates
CC if atr2 acts first, or the proatranorin I intermediate if atr3 acts
CC first (PubMed:34154413). {ECO:0000269|PubMed:34154413}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:34154413}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; MZ277878; QXF68952.1; -; Genomic_DNA.
DR UniPathway; UPA00213; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
PE 1: Evidence at protein level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..506
FT /note="Cytochrome P450 monooxygenase atr2"
FT /id="PRO_0000455742"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 451
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
SQ SEQUENCE 506 AA; 57240 MW; 5936EBA93BCF5D60 CRC64;
MALLDTIELF SNFSLSGVFA GLVLASLLTT TYCIWNIFYN IYLHPLKGYP GPKFLTTSRL
PYLKWMFSGT LVPNFQRLHE QYGPVVRVAP NELSYINPEA LKTIYGHRQP GEGFRKNPAF
FQPATNGVHS ILTSEGDAHS SVRRKILPAF SDKALAEQQD ILQHFTDLLI RKLRERVEAS
KSSEPVDMFE WYIWTTFDLI GDLAFGEPFN CLEAASFTEW VALVFNAFKT FAFINISKQL
APLDKLVRLM IPKSMKARQD KVFSLNVAKV DRRIASKADR PDFLSYIIKG KDGVAMALPE
LYANSTLLVL AGSESTASGL AGITFELLKH REAQKKAVEE IRSAFKTEDE IVPESVKRLP
YLAAMVSEGL RMYPPFPEGL PRLTPRQGAQ ICGQWVPGGT YVQFSTHAAH RASANFTDPN
VFAPERWLGD TKFASDIKEA SQPFSIGPRS CIGRNLAYLE MRLILARMLW SFDMQLTPEC
EDWDDQNSWI QWDKKPLMVK LSLVKR
