C7162_ARATH
ID C7162_ARATH Reviewed; 473 AA.
AC A0A140JWM8; Q9LVY3; Q9LVY4;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 11-MAY-2016, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Cytochrome P450 716A2 {ECO:0000303|PubMed:26801524};
DE EC=1.14.-.- {ECO:0000305};
GN Name=CYP716A2 {ECO:0000303|PubMed:26801524};
GN OrderedLocusNames=At5g36130/At5g36140 {ECO:0000312|Araport:AT5G36130,
GN ECO:0000312|Araport:AT5G36140};
GN ORFNames=MAB16.8/MAB16.9 {ECO:0000312|EMBL:BAA96888.1,
GN ECO:0000312|EMBL:BAA96889.1};
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 [MRNA], AND FUNCTION.
RC STRAIN=cv. Columbia;
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).
RN [2]
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 [3]
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).
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. Possesses 22alpha-
CC hydroxylation activity against alpha- and beta-amaryn.
CC {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AED94047.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At5g36130 and At5g36140.; Evidence={ECO:0000305};
CC Sequence=AED94048.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At5g36130 and At5g36140.; Evidence={ECO:0000305};
CC Sequence=BAA96888.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At5g36130 and At5g36140.; Evidence={ECO:0000305};
CC Sequence=BAA96889.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At5g36130 and At5g36140.; Evidence={ECO:0000305};
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DR EMBL; LC106013; BAU61505.1; -; mRNA.
DR EMBL; AB018112; BAA96888.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AB018112; BAA96889.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED94047.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED94048.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_198462.1; NM_123004.2.
DR RefSeq; NP_198463.1; NM_123005.2.
DR AlphaFoldDB; A0A140JWM8; -.
DR SMR; A0A140JWM8; -.
DR STRING; 3702.AT5G36140.1; -.
DR PeptideAtlas; A0A140JWM8; -.
DR ProteomicsDB; 240305; -.
DR GeneID; 833610; -.
DR GeneID; 833611; -.
DR KEGG; ath:AT5G36130; -.
DR KEGG; ath:AT5G36140; -.
DR Araport; AT5G36130; -.
DR Araport; AT5G36140; -.
DR TAIR; locus:2158911; AT5G36130.
DR TAIR; locus:2158916; AT5G36140.
DR eggNOG; KOG0157; Eukaryota.
DR HOGENOM; CLU_001570_15_4_1; -.
DR OrthoDB; 871849at2759; -.
DR PRO; PR:A0A140JWM8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; A0A140JWM8; 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:UniProtKB.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR GO; GO:0006722; P:triterpenoid metabolic process; IDA:UniProtKB.
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 2: Evidence at transcript level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..473
FT /note="Cytochrome P450 716A2"
FT /id="PRO_0000444437"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 420
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 473 AA; 54323 MW; 6B462781B8E1C01F CRC64;
MYLTIIFLFI SSIIFPLLFF LGKHLSNFRY PNLPPGKIGF PLIGETLSFL SAGRQGHPEK
FVTDRVRHFS SGIFKTHLFG SPFAVVTGAS GNKFLFTNEN KLVISWWPDS VNKIFPSSTQ
TSSKEEAIKT RMLLMPSMKP EALRRYVGVM DEIAQKHFET EWANQDQLIV FPLTKKFTFS
IACRLFLSMD DLERVRKLEE PFTTVMTGVF SIPIDLPGTR FNRAIKASRL LSKEVSTIIR
QRKEELKAGK VSVEQDILSH MLMNIGETKD EDLADKIIAL LIGGHDTTSI VCTFVVNYLA
EFPHIYQRVL EEQKEILNNK DVNEKLTWED IEKMRYSWNV ACEVMRIVPP LAGTFREAID
HFSFKGFYIP KGWKLYWSAT ATHKNPEYFP EPEKFEPSRF EGSGPKPYTY VPFGGGSRIC
PGREYARLEI LIFMHNLVKR FKWEKVFPKE NKLVADPAPI PAKGLPIRIF PQS
