C7A68_MEDTR
ID C7A68_MEDTR Reviewed; 520 AA.
AC Q2MJ19;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Cytochrome P450 72A68 {ECO:0000303|PubMed:17273868};
DE EC=1.14.14.- {ECO:0000269|PubMed:23378447};
GN Name=CYP72A68 {ECO:0000303|PubMed:17273868};
GN OrderedLocusNames=MTR_2g055470 {ECO:0000312|EMBL:KEH37987.1};
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, AND CATALYTIC ACTIVITY.
RC STRAIN=cv. Jemalong;
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 oleanolic acid at the C-23
CC position to form gypsogenic acid. Involved in the hemolytic saponin
CC biosynthetic pathway. {ECO:0000269|PubMed:23378447}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 O2 + oleanolate + 3 reduced [NADPH--hemoprotein reductase] =
CC gypsogenate + 4 H(+) + 4 H2O + 3 oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:56484, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:82828,
CC ChEBI:CHEBI:140468; Evidence={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 -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; DQ335782; ABC59077.1; -; mRNA.
DR EMBL; CM001218; KEH37987.1; -; Genomic_DNA.
DR RefSeq; XP_013463952.1; XM_013608498.1.
DR AlphaFoldDB; Q2MJ19; -.
DR SMR; Q2MJ19; -.
DR EnsemblPlants; KEH37987; KEH37987; MTR_2g055470.
DR GeneID; 25486777; -.
DR Gramene; KEH37987; KEH37987; MTR_2g055470.
DR KEGG; mtr:MTR_2g055470; -.
DR HOGENOM; CLU_001570_5_0_1; -.
DR OrthoDB; 1247045at2759; -.
DR Proteomes; UP000002051; Chromosome 2.
DR ExpressionAtlas; Q2MJ19; 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 1: Evidence at protein level;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..520
FT /note="Cytochrome P450 72A68"
FT /id="PRO_0000444126"
FT TRANSMEM 11..31
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; 59900 MW; A4885A53AF9377E7 CRC64;
MELSWETKSA IILITVTFGL VYAWRVLNWM WLKPKKIEKL LREQGLQGNP YRLLLGDAKD
YFVMQKKVQS KPMNLSDDIA PRVAPYIHHA VQTHGKKSFI WFGMKPWVIL NEPEQIREVF
NKMSEFPKVQ YKFMKLITRG LVKLEGEKWS KHRRIINPAF HMEKLKIMTP TFLKSCNDLI
SNWEKMLSSN GSCEMDVWPS LQSLTSDVIA RSSFGSSYEE GRKVFQLQIE QGELIMKNLM
KSLIPLWRFL PTADHRKINE NEKQIETTLK NIINKREKAI KAGEATENDL LGLLLESNHR
EIKEHGNVKN MGLSLEEVVG ECRLFHVAGQ ETTSDLLVWT MVLLSRYPDW QERARKEVLE
IFGNEKPDFD GLNKLKIMAM ILYEVLRLYP PVTGVARKVE NDIKLGDLTL YAGMEVYMPI
VLIHHDCELW GDDAKIFNPE RFSGGISKAT NGRFSYFPFG AGPRICIGQN FSLLEAKMAM
ALILKNFSFE LSQTYAHAPS VVLSVQPQHG AHVILRKIKT
