C85A_PHAVU
ID C85A_PHAVU Reviewed; 466 AA.
AC Q69F95; V7B0S8;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 3.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Cytochrome P450 85A {ECO:0000303|PubMed:15221144};
DE Short=PvCYP85A {ECO:0000303|PubMed:15221144};
DE EC=1.14.14.- {ECO:0000250|UniProtKB:Q9FMA5};
DE AltName: Full=C6-oxidase {ECO:0000250|UniProtKB:Q9FMA5};
GN Name=CYP85A {ECO:0000303|PubMed:15221144};
GN OrderedLocusNames=PHAVU_008G028800g {ECO:0000312|EMBL:ESW11424.1};
GN ORFNames=BA13 {ECO:0000303|PubMed:15221144};
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15221144; DOI=10.1007/s00122-004-1697-6;
RA Melotto M., Coelho M.F., Pedrosa-Harand A., Kelly J.D., Camargo L.E.;
RT "The anthracnose resistance locus Co-4 of common bean is located on
RT chromosome 3 and contains putative disease resistance-related genes.";
RL Theor. Appl. Genet. 109:690-699(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. G19833;
RX PubMed=24908249; DOI=10.1038/ng.3008;
RA Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT "A reference genome for common bean and genome-wide analysis of dual
RT domestications.";
RL Nat. Genet. 46:707-713(2014).
CC -!- FUNCTION: Catalyzes the C6-oxidation step in brassinosteroids
CC biosynthesis. {ECO:0000250}.
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=AAR13307.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY341443; AAR13307.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM002295; ESW11424.1; -; Genomic_DNA.
DR RefSeq; XP_007139430.1; XM_007139368.1.
DR AlphaFoldDB; Q69F95; -.
DR SMR; Q69F95; -.
DR STRING; 3885.XP_007139430.1; -.
DR EnsemblPlants; ESW11424; ESW11424; PHAVU_008G028800g.
DR GeneID; 18621677; -.
DR Gramene; ESW11424; ESW11424; PHAVU_008G028800g.
DR KEGG; pvu:PHAVU_008G028800g; -.
DR eggNOG; KOG0157; Eukaryota.
DR OMA; PEDPIDC; -.
DR OrthoDB; 574756at2759; -.
DR Proteomes; UP000000226; Chromosome 8.
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.
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..466
FT /note="Cytochrome P450 85A"
FT /id="PRO_0000052173"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 414
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"
FT CONFLICT 17
FT /note="L -> F (in Ref. 1; AAR13307)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="R -> Q (in Ref. 1; AAR13307)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="N -> S (in Ref. 1; AAR13307)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 466 AA; 53541 MW; ABD38623A581ED42 CRC64;
MALFMAILGV LVLLLCLCSA LLKWNEVRFR RKGLPPGAMG WPVFGETTEF LKQGPNFMKN
KRARYGSFFK SHILGCPTIV SMDPELNRFI LMNEAKGLVP GYPQSMLDIL GTRNIAAVHG
STHKYMRGAL LSIISPTLIR DQLLPKIDEF MRTHLMDWDN KVINIQEKTK EMAFLSSLKQ
IAGMESSSIA QPFMTEFFKL VLGTLSLPIN LPRTNYRGGL QARKSIISIL SRLLEERKAS
QDVHVDMLGC LMKKDENRYK LNDEEIIDLV ITIMYSGYET VSTTSMMAVK YLHDHPKVLE
EIRKEHFAIR ERKKPEDPID CNDLKSMRFT RAVIFETSRL ATIVNGVLRK TTHDMELNGY
LIPKGWRIYV YTREINYDPF LYHDPLTFNP WRWLGNSLES QSHFLIFGGG TRQCPGKELG
IAEISTFLHY FVTRYRWEEV GGDKLMKFPR VVAPNGLHIR VSSFSN
