ID   C7A67_MEDTR             Reviewed;         520 AA.
AC   Q2MJ21;
DT   23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Cytochrome P450 716A67 {ECO:0000303|PubMed:17273868};
DE            EC=1.14.13.- {ECO:0000305};
GN   Name=CYP72A67 {ECO:0000303|PubMed:17273868};
GN   OrderedLocusNames=MTR_2g023680 {ECO:0000312|EMBL:KEH36885.1};
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 [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   [3]
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   [4]
RP   FUNCTION.
RC   STRAIN=cv. Jemalong;
RX   PubMed=26079384; DOI=10.1016/j.molp.2015.06.003;
RA   Biazzi E., Carelli M., Tava A., Abbruscato P., Losini I., Avato P.,
RA   Scotti C., Calderini O.;
RT   "CYP72A67 catalyzes a key oxidative step in Medicago truncatula hemolytic
RT   saponin biosynthesis.";
RL   Mol. Plant 8:1493-1506(2015).
CC   -!- FUNCTION: Catalyzes hydroxylation at the C-2 position of different
CC       intermediates of the hemolytic sapogenin biosynthetic pathway
CC       downstream of oleanolic acid synthesis. {ECO:0000269|PubMed:26079384}.
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   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; DQ335780; ABC59075.1; -; mRNA.
DR   EMBL; CM001218; KEH36885.1; -; Genomic_DNA.
DR   RefSeq; XP_013462851.1; XM_013607397.1.
DR   AlphaFoldDB; Q2MJ21; -.
DR   SMR; Q2MJ21; -.
DR   EnsemblPlants; KEH36885; KEH36885; MTR_2g023680.
DR   GeneID; 25486186; -.
DR   Gramene; KEH36885; KEH36885; MTR_2g023680.
DR   KEGG; ag:ABC59075; -.
DR   KEGG; mtr:MTR_2g023680; -.
DR   HOGENOM; CLU_001570_5_0_1; -.
DR   OrthoDB; 825914at2759; -.
DR   Proteomes; UP000002051; Chromosome 2.
DR   ExpressionAtlas; Q2MJ21; 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: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:0016135; P:saponin biosynthetic 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..520
FT                   /note="Cytochrome P450 716A67"
FT                   /id="PRO_0000444125"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         466
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"
SQ   SEQUENCE   520 AA;  59880 MW;  7DAF3A1C6CFE282D CRC64;
     MEASLAIYYG IILITVTLGL VYTWRVLNWI WLKPKRLEKL LREQGCNGNS YRLVLGDLKD
     SYKMGKKAKS KPMELSDDII PRVIPYIQQL VQIYGKNPFI WSGTTPRLIL TEPELIKDVL
     NRTSELQKPK YEIFKFLFSG LIIHEGEKWR KHRRLMNAAF QLEKLKIMAP SFLTSCIDMI
     SKWESTLSSD GSGEIDIWPS LQNLTSDVIS RNAFGSSYEE GKRIFDLQRE QGELVMKNLV
     KSLIPLWRFI PTATQRRMHE IEKDIDSSLR YIINKREKAM KAGEATENDL LGLLLESNHQ
     EIRDHGNNKN MGMSLEDVVG ECKLFYLAGQ ESTSTMLVWT MILLSRYPDW QERAREEVLQ
     IFGNKKPDYE GLNKLKILPM ILYEVLRLYP PAFGVTRYVG KDIKFGNMEV PAGVEVFLPI
     ILLQHNNELW GDDAKMFNPE RFAEGISKAT NGRFIYFPFG GGPRVCMGQN FSLLEAKMAV
     SMILQNFYFE LSPTYAHTPN LVMTIQPEKG AHVILRKVKA