ID   C7161_ARATH             Reviewed;         477 AA.
AC   Q9LVY7;
DT   20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Cytochrome P450 716A1 {ECO:0000303|PubMed:26801524};
DE            EC=1.14.-.- {ECO:0000305};
GN   Name=CYP716A1 {ECO:0000303|PubMed:26801524};
GN   OrderedLocusNames=At5g36110 {ECO:0000312|Araport:AT5G36110};
GN   ORFNames=MAB16.5 {ECO:0000312|EMBL:BAA96885.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT   features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:31-63(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   FUNCTION.
RX   PubMed=26801524; DOI=10.1002/1873-3468.12074;
RA   Yasumoto S., Fukushima E.O., Seki H., Muranaka T.;
RT   "Novel triterpene oxidizing activity of Arabidopsis thaliana CYP716A
RT   subfamily enzymes.";
RL   FEBS Lett. 590:533-540(2016).
CC   -!- FUNCTION: Possesses triterpene oxidizing activity. Catalyzes the C28
CC       hydroxylation of alpha-amyrin, beta-amyrin, and lupeol, producing
CC       uvaol, erythrodiol, and betulin, respectively. Catalyzes the C28
CC       carboxylation of alpha- and beta-amyrin. {ECO:0000269|PubMed:26801524}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
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; AB018112; BAA96885.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94045.1; -; Genomic_DNA.
DR   RefSeq; NP_198460.1; NM_123002.2.
DR   AlphaFoldDB; Q9LVY7; -.
DR   SMR; Q9LVY7; -.
DR   IntAct; Q9LVY7; 2.
DR   STRING; 3702.AT5G36110.1; -.
DR   PaxDb; Q9LVY7; -.
DR   PRIDE; Q9LVY7; -.
DR   ProteomicsDB; 240304; -.
DR   EnsemblPlants; AT5G36110.1; AT5G36110.1; AT5G36110.
DR   GeneID; 833607; -.
DR   Gramene; AT5G36110.1; AT5G36110.1; AT5G36110.
DR   KEGG; ath:AT5G36110; -.
DR   Araport; AT5G36110; -.
DR   TAIR; locus:2158961; AT5G36110.
DR   eggNOG; KOG0157; Eukaryota.
DR   HOGENOM; CLU_001570_15_5_1; -.
DR   InParanoid; Q9LVY7; -.
DR   OMA; KNYTFWL; -.
DR   OrthoDB; 871849at2759; -.
DR   PhylomeDB; Q9LVY7; -.
DR   BioCyc; ARA:AT5G36110-MON; -.
DR   PRO; PR:Q9LVY7; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9LVY7; baseline and differential.
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; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IDA:TAIR.
DR   GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR   GO; GO:0006722; P:triterpenoid metabolic process; IDA:TAIR.
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.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..477
FT                   /note="Cytochrome P450 716A1"
FT                   /id="PRO_0000444436"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         424
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   477 AA;  54851 MW;  304B4B2C4970E405 CRC64;
     MYMAIMIILF LSSILLSLLL LLRKHLSHFS YPNLPPGNTG LPLIGESFSF LSAGRQGHPE
     KFITDRVRRF SSSSSCVFKT HLFGSPTAVV TGASGNKFLF TNENKLVVSW WPDSVNKIFP
     SSMQTSSKEE ARKLRMLLSQ FMKPEALRRY VGVMDEIAQR HFETEWANQD QVIVFPLTKK
     FTFSIACRSF LSMEDPARVR QLEEQFNTVA VGIFSIPIDL PGTRFNRAIK ASRLLRKEVS
     AIVRQRKEEL KAGKALEEHD ILSHMLMNIG ETKDEDLADK IIGLLIGGHD TASIVCTFVV
     NYLAEFPHVY QRVLQEQKEI LKEKKEKEGL RWEDIEKMRY SWNVACEVMR IVPPLSGTFR
     EAIDHFSFKG FYIPKGWKLY WSATATHMNP DYFPEPERFE PNRFEGSGPK PYTYVPFGGG
     PRMCPGKEYA RLEILIFMHN LVNRFKWEKV FPNENKIVVD PLPIPDKGLP IRIFPQS