C7A44_SOLLC
ID C7A44_SOLLC Reviewed; 476 AA.
AC A0A3Q7HBJ5;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 10-APR-2019, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Beta-amyrin 28-monooxygenase {ECO:0000305};
DE EC=1.14.14.126 {ECO:0000269|PubMed:28194155};
DE AltName: Full=Beta-amyrin 28-oxidase {ECO:0000305};
DE AltName: Full=Cytochrome P450 716A44 {ECO:0000305};
GN Name=CYP716A44;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706;
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=20350329; DOI=10.1186/1471-2164-11-210;
RA Aoki K., Yano K., Suzuki A., Kawamura S., Sakurai N., Suda K.,
RA Kurabayashi A., Suzuki T., Tsugane T., Watanabe M., Ooga K., Torii M.,
RA Narita T., Shin-I T., Kohara Y., Yamamoto N., Takahashi H., Watanabe Y.,
RA Egusa M., Kodama M., Ichinose Y., Kikuchi M., Fukushima S., Okabe A.,
RA Arie T., Sato Y., Yazawa K., Satoh S., Omura T., Ezura H., Shibata D.;
RT "Large-scale analysis of full-length cDNAs from the tomato (Solanum
RT lycopersicum) cultivar Micro-Tom, a reference system for the Solanaceae
RT genomics.";
RL BMC Genomics 11:210-210(2010).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=28194155; DOI=10.3389/fpls.2017.00021;
RA Yasumoto S., Seki H., Shimizu Y., Fukushima E.O., Muranaka T.;
RT "Functional characterization of CYP716 family P450 enzymes in triterpenoid
RT biosynthesis in tomato.";
RL Front. Plant Sci. 8:21-21(2017).
CC -!- FUNCTION: Catalyzes the carboxylation of beta-amyrin at the C-28
CC position to form oleanolate (PubMed:28194155). Catalyzes the
CC carboxylation of alpha-amyrin at the C-28 position to form ursolate
CC (PubMed:28194155). {ECO:0000269|PubMed:28194155}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-amyrin + 3 O2 + 3 reduced [NADPH--hemoprotein reductase]
CC = 4 H(+) + 4 H2O + oleanolate + 3 oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:43068, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:10352, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:82828; EC=1.14.14.126;
CC Evidence={ECO:0000269|PubMed:28194155};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43069;
CC Evidence={ECO:0000269|PubMed:28194155};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q94IP1};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in roots.
CC {ECO:0000269|PubMed:28194155}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AK329870; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_004239296.1; XM_004239248.3.
DR AlphaFoldDB; A0A3Q7HBJ5; -.
DR SMR; A0A3Q7HBJ5; -.
DR STRING; 4081.Solyc05g021390.2.1; -.
DR EnsemblPlants; Solyc05g021390.3.1; Solyc05g021390.3.1; Solyc05g021390.3.
DR GeneID; 101251676; -.
DR Gramene; Solyc05g021390.3.1; Solyc05g021390.3.1; Solyc05g021390.3.
DR KEGG; sly:101251676; -.
DR OMA; IFNGFYI; -.
DR BRENDA; 1.14.14.126; 3101.
DR Proteomes; UP000004994; Chromosome 5.
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:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IDA:UniProtKB.
DR GO; GO:0102374; F:ursolic aldehyde 28-monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0102373; F:uvaol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..476
FT /note="Beta-amyrin 28-monooxygenase"
FT /id="PRO_0000451600"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 421
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:Q94IP1"
SQ SEQUENCE 476 AA; 54258 MW; 2C4FFB4644026527 CRC64;
MELLYVCLVC VFVFLVSLLL LYKKKSGEGL PPGKTGWPVF GESLEFLSSG WKGHPEKFIF
DRVAKYSSSV FKTHLLGEEA AVFCGASANK FLFSNENKLV QAWWPNSVNK VFPSSTQTSS
KEEAIKMRKM LPNFFKPEAL QRYVGIMDHI TQRHFATGWE NKEQVVVFPL TKRYTFWLAC
RLFLSVEDPK HVAKFADPFD VLASGLISIP IDLPGTPFNR AIKASNFIRK ELVRIIKQRK
IDLGEGKVSS TQDILSHMLL TCDENGKFLG DLDIADKILG LLIGGHDTAS SACSFIVKYL
AELPHIYQRV YTEQMEIAKS KGPGELLRWE DIQKMKYSWN VACEVLRLAP PLQGAFREAL
SDFMFNGFYI PKGWKIYWSA NSTHKREEFF PDPEKFDPSR FEGSGPAPYT FVPFGGGPRM
CPGKEYARLE ILVFMHHLVK RFKFEKIIPH EKIIVNPMPI PANGLPLRLY PHHHNP
