C7A12_MEDTR
ID C7A12_MEDTR Reviewed; 479 AA.
AC Q2MJ20; B7FI68; F8J4R7; I3T3X3;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Beta-amyrin 28-monooxygenase {ECO:0000305};
DE EC=1.14.14.126 {ECO:0000269|PubMed:21821776, ECO:0000269|PubMed:22039103, ECO:0000269|PubMed:23378447};
DE AltName: Full=Beta-amyrin 28-oxidase {ECO:0000305};
DE AltName: Full=Cytochrome P450 716A12 {ECO:0000303|PubMed:17273868};
DE Short=MtCYP716A12 {ECO:0000303|PubMed:17273868};
DE AltName: Full=Protein LACKING HEMOLYTIC ACTIVITY {ECO:0000303|PubMed:21821776};
GN Name=CYP716A12 {ECO:0000303|PubMed:17273868};
GN Synonyms=LAH {ECO:0000303|PubMed:21821776};
GN OrderedLocusNames=MTR_8g100135 {ECO:0000312|EMBL:KEH21305.1};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
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; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Jemalong;
RX PubMed=17273868; DOI=10.1007/s00425-006-0473-z;
RA Li L., Cheng H., Gai J., Yu D.;
RT "Genome-wide identification and characterization of putative cytochrome
RT P450 genes in the model legume Medicago truncatula.";
RL Planta 226:109-123(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF PRO-355.
RC STRAIN=cv. R108;
RX PubMed=21821776; DOI=10.1105/tpc.111.087312;
RA Carelli M., Biazzi E., Panara F., Tava A., Scaramelli L., Porceddu A.,
RA Graham N., Odoardi M., Piano E., Arcioni S., May S., Scotti C.,
RA Calderini O.;
RT "Medicago truncatula CYP716A12 is a multifunctional oxidase involved in the
RT biosynthesis of hemolytic saponins.";
RL Plant Cell 23:3070-3081(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Krishnakumar V., Cheung F., Xiao Y., Chan A., Moskal W.A., Town C.D.;
RT "Medicago truncatula cytochrome P450 monooxygenase CYP716A12 mRNA.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jemalong A17;
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B.,
RA Udvardi M.K., Benedito V.A., Mayer K.F.X., Gouzy J., Schoof H.,
RA Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., Cheung F.,
RA De Mita S., Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K.,
RA Murray J.D., Naoumkina M.A., Rosen B., Silverstein K.A.T., Tang H.,
RA Rombauts S., Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M.,
RA Bellec A., Berger A., Berges H., Bidwell S., Bisseling T., Choisne N.,
RA Couloux A., Denny R., Deshpande S., Dai X., Doyle J.J., Dudez A.-M.,
RA Farmer A.D., Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S.,
RA Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., Humphray S.J.,
RA Jeong D.-H., Jing Y., Jocker A., Kenton S.M., Kim D.-J., Klee K., Lai H.,
RA Lang C., Lin S., Macmil S.L., Magdelenat G., Matthews L., McCorrison J.,
RA Monaghan E.L., Mun J.-H., Najar F.Z., Nicholson C., Noirot C.,
RA O'Bleness M., Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F.,
RA Riddle C., Sallet E., Samain S., Samson N., Sanders I., Saurat O.,
RA Scarpelli C., Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R.,
RA Sims S., Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B.,
RA Wang K., Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D.,
RA White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F.,
RA Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D.,
RA Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Jemalong A17;
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Moskal W., Chan A., Cheung F., Xiao Y., Town C.D.;
RT "Medicago truncatula full length cDNA cloning project.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=22039103; DOI=10.1093/pcp/pcr146;
RA Fukushima E.O., Seki H., Ohyama K., Ono E., Umemoto N., Mizutani M.,
RA Saito K., Muranaka T.;
RT "CYP716A subfamily members are multifunctional oxidases in triterpenoid
RT biosynthesis.";
RL Plant Cell Physiol. 52:2050-2061(2011).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23378447; DOI=10.1093/pcp/pct015;
RA Fukushima E.O., Seki H., Sawai S., Suzuki M., Ohyama K., Saito K.,
RA Muranaka T.;
RT "Combinatorial biosynthesis of legume natural and rare triterpenoids in
RT engineered yeast.";
RL Plant Cell Physiol. 54:740-749(2013).
CC -!- FUNCTION: Catalyzes the carboxylation of beta-amyrin at the C-28
CC position to form oleanolic acid. Involved in an early step in the
CC hemolytic saponin biosynthetic pathway (PubMed:21821776,
CC PubMed:22039103, PubMed:23378447). Catalyzes the carboxylation of
CC alpha-amyrin and lupeol at the C-28 position to form ursolic acid and
CC betulinic acid respectively (PubMed:22039103).
CC {ECO:0000269|PubMed:21821776, ECO:0000269|PubMed:22039103,
CC ECO:0000269|PubMed:23378447}.
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:21821776, ECO:0000269|PubMed:22039103,
CC ECO:0000269|PubMed:23378447};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q96242};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, nodules and flowers.
CC {ECO:0000269|PubMed:21821776}.
CC -!- DISRUPTION PHENOTYPE: Severe reduction in root and shoot size.
CC {ECO:0000269|PubMed:21821776}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; DQ335781; ABC59076.1; -; mRNA.
DR EMBL; FN995112; CBN88268.1; -; Genomic_DNA.
DR EMBL; FN995113; CBN88269.1; -; mRNA.
DR EMBL; BT147421; AFK47215.1; -; mRNA.
DR EMBL; CM001224; KEH21305.1; -; Genomic_DNA.
DR EMBL; BT051785; ACJ84447.1; -; mRNA.
DR RefSeq; XP_013447278.1; XM_013591824.1.
DR AlphaFoldDB; Q2MJ20; -.
DR SMR; Q2MJ20; -.
DR EnsemblPlants; KEH21305; KEH21305; MTR_8g100135.
DR GeneID; 25502252; -.
DR Gramene; KEH21305; KEH21305; MTR_8g100135.
DR KEGG; ag:CBN88269; -.
DR KEGG; mtr:MTR_8g100135; -.
DR HOGENOM; CLU_001570_15_5_1; -.
DR OrthoDB; 871849at2759; -.
DR BioCyc; MetaCyc:MON-17480; -.
DR BRENDA; 1.14.14.126; 3201.
DR Proteomes; UP000002051; Chromosome 8.
DR ExpressionAtlas; Q2MJ20; 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:0102374; F:ursolic aldehyde 28-monooxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0102373; F:uvaol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0016135; P:saponin biosynthetic process; IDA:UniProtKB.
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..479
FT /note="Beta-amyrin 28-monooxygenase"
FT /id="PRO_0000444124"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 426
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:Q96242"
FT MUTAGEN 355
FT /note="P->L: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:21821776"
FT CONFLICT 15
FT /note="T -> S (in Ref. 2; CBN88268/CBN88269)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="I -> T (in Ref. 3; AFK47215 and 6; ACJ84447)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="V -> I (in Ref. 2; CBN88268/CBN88269)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="I -> T (in Ref. 6; ACJ84447)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="V -> A (in Ref. 3; AFK47215 and 6; ACJ84447)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 479 AA; 54713 MW; 2A0C52ADE1A7AC9D CRC64;
MEPNFYLSLL LLFVTFISLS LFFIFYKQKS PLNLPPGKMG YPIIGESLEF LSTGWKGHPE
KFIFDRMRKY SSELFKTSIV GESTVVCCGA ASNKFLFSNE NKLVTAWWPD SVNKIFPTTS
LDSNLKEESI KMRKLLPQFF KPEALQRYVG VMDVIAQRHF VTHWDNKNEI TVYPLAKRYT
FLLACRLFMS VEDENHVAKF SDPFQLIAAG IISLPIDLPG TPFNKAIKAS NFIRKELIKI
IKQRRVDLAE GTASPTQDIL SHMLLTSDEN GKSMNELNIA DKILGLLIGG HDTASVACTF
LVKYLGELPH IYDKVYQEQM EIAKSKPAGE LLNWDDLKKM KYSWNVACEV MRLSPPLQGG
FREAITDFMF NGFSIPKGWK LYWSANSTHK NAECFPMPEK FDPTRFEGNG PAPYTFVPFG
GGPRMCPGKE YARLEILVFM HNLVKRFKWE KVIPDEKIIV DPFPIPAKDL PIRLYPHKA
