C92C6_MAIZE
ID C92C6_MAIZE Reviewed; 554 AA.
AC A0A1D6F9Y9; B4FSZ6; B8A110;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Trimethyltridecatetraene synthase {ECO:0000303|PubMed:27662898};
DE EC=1.14.14.58 {ECO:0000269|PubMed:27662898};
DE AltName: Full=Cytochrome P-450 20 {ECO:0000312|EMBL:ONM27923.1};
DE AltName: Full=Cytochrome P450 92C6 {ECO:0000303|PubMed:27662898};
GN Name=CYP92C6 {ECO:0000303|PubMed:27662898};
GN ORFNames=ZEAMMB73_Zm00001d007918 {ECO:0000312|EMBL:ONM27923.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73; TISSUE=Seedling;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-554.
RC STRAIN=cv. B73;
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION
RP BY HERBIVORES.
RC STRAIN=cv. B73;
RX PubMed=27662898; DOI=10.1105/tpc.15.00919;
RA Richter A., Schaff C., Zhang Z., Lipka A.E., Tian F., Koellner T.G.,
RA Schnee C., Preiss S., Irmisch S., Jander G., Boland W., Gershenzon J.,
RA Buckler E.S., Degenhardt J.;
RT "Characterization of biosynthetic pathways for the production of the
RT volatile homoterpenes DMNT and TMTT in Zea mays.";
RL Plant Cell 28:2651-2665(2016).
RN [4]
RP REVIEW.
RX PubMed=30187155; DOI=10.1007/s00425-018-2999-2;
RA Block A.K., Vaughan M.M., Schmelz E.A., Christensen S.A.;
RT "Biosynthesis and function of terpenoid defense compounds in maize (Zea
RT mays).";
RL Planta 249:21-30(2019).
CC -!- FUNCTION: Component of the volatile terpenes biosynthesis pathways
CC (PubMed:30187155). Converts mainly geranyllinalool to
CC trimethyltridecatetraene (TMTT) (PubMed:27662898).
CC {ECO:0000269|PubMed:27662898, ECO:0000303|PubMed:30187155}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6E,10E)-geranyllinalool + O2 + reduced [NADPH--hemoprotein
CC reductase] = (3E,7E)-4,8,12-trimethyltrideca 1,3,7,11-tetraene + but-
CC 3-en-2-one + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:13545, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:48058, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:74299, ChEBI:CHEBI:74322; EC=1.14.14.58;
CC Evidence={ECO:0000269|PubMed:27662898};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13546;
CC Evidence={ECO:0000269|PubMed:27662898};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q96242};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.4 uM for (6E,10E)-geranyllinalool
CC {ECO:0000269|PubMed:27662898};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305|PubMed:30187155}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Strongly induced in response to herbivory-mediated wounding.
CC {ECO:0000269|PubMed:27662898}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACF85239.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=ACL53859.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=ACR36247.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CM007648; ONM27923.1; -; Genomic_DNA.
DR EMBL; BT040234; ACF85239.1; ALT_INIT; mRNA.
DR EMBL; BT055252; ACL53859.1; ALT_INIT; mRNA.
DR EMBL; BT085894; ACR36247.1; ALT_INIT; mRNA.
DR RefSeq; NP_001146388.1; NM_001152916.1.
DR AlphaFoldDB; A0A1D6F9Y9; -.
DR SMR; A0A1D6F9Y9; -.
DR STRING; 4577.GRMZM2G139467_P01; -.
DR GeneID; 100279968; -.
DR KEGG; zma:100279968; -.
DR MaizeGDB; 9035643; -.
DR eggNOG; KOG0156; Eukaryota.
DR OMA; RRVCPAT; -.
DR OrthoDB; 702827at2759; -.
DR BRENDA; 1.14.14.58; 6752.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000007305; Chromosome 2.
DR ExpressionAtlas; A0A1D6F9Y9; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0097007; F:4,8,12-trimethyltrideca-1,3,7,11-tetraene synthase activity; IEA:RHEA.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR GO; GO:0080027; P:response to herbivore; IEP:UniProtKB.
DR GO; GO:0016114; P:terpenoid 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..554
FT /note="Trimethyltridecatetraene synthase"
FT /id="PRO_0000447525"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 464
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 554 AA; 60524 MW; FA8781D411252FA5 CRC64;
MSAAVALAVI LAVYVVLRYI SSPRGRSKPL NLPPGPRGWP VIGSLGALAG ALPPHRALAA
LAARHGPLMH LRLGSYHAVV ASSADTARLV LKVHDLAFAD RPRTAAGEVA SYGYLGIVHT
PYGAYWRMAR KLCATELFSA RRVDSFERVR AQEMRALARG LFECAGRGAV AVREHVAGAT
LRNILRMAVG EKWSGCYGSP EGEAFRRTLD EAFAVTGAVS NVGEWVPWLG WLDLQGCVRR
MKRLRAQYDR FFEQILDDHD HKKTRRERGR PGAGDSAADD DLVDVLLRLV EEDEDRPETT
EASRLTRDGV KAFVQDIVAG GTESSAVTIE WAMSELLRRP DALRAATAEL DRVIGHGRWV
TERDLPDLPY IDAVVKETMR LHPVGPLLVP HHAREHTVVA GYDVPAGARV LVNVWAIARD
PASWPDAPDA FRPERFLNGS SGASVDVRGA HFELLPFGAG RRMCPAHGLA MKLVTAGVAN
LVHGFAWRLP DGMAPEDVSM EELFGLSTRR KVPLVAVAEP RLPAHLYTNV TPPQQVAGST
IANLSTRPEY KLVF
