GA7_GIBF5
ID GA7_GIBF5 Reviewed; 527 AA.
AC S0E2Y2;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Cytochrome P450 monooygenase 3 {ECO:0000303|PubMed:9917370};
DE Short=P450-3 {ECO:0000303|PubMed:9917370};
DE EC=1.-.-.- {ECO:0000269|PubMed:12750377};
DE AltName: Full=Gibberellin 13-hydroxylase P450-3 {ECO:0000303|PubMed:12750377};
GN Name=P450-3 {ECO:0000303|PubMed:9917370}; ORFNames=FFUJ_14337;
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND FUNCTION.
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831;
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M.K., von Bargen K.W., Studt L., Niehaus E.-M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Muensterkoetter M., Freitag M., Humpf H.-U., Gueldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
RN [2]
RP FUNCTION.
RX PubMed=9745028; DOI=10.1007/s002940050392;
RA Tudzynski B., Kawaide H., Kamiya Y.;
RT "Gibberellin biosynthesis in Gibberella fujikuroi: cloning and
RT characterization of the copalyl diphosphate synthase gene.";
RL Curr. Genet. 34:234-240(1998).
RN [3]
RP FUNCTION, INDUCTION, AND PATHWAY.
RX PubMed=9917370; DOI=10.1006/fgbi.1998.1095;
RA Tudzynski B., Hoelter K.;
RT "Gibberellin biosynthetic pathway in Gibberella fujikuroi: evidence for a
RT gene cluster.";
RL Fungal Genet. Biol. 25:157-170(1998).
RN [4]
RP FUNCTION.
RX PubMed=10347043; DOI=10.1128/aem.65.6.2558-2564.1999;
RA Linnemannstoens P., Voss T., Hedden P., Gaskin P., Tudzynski B.;
RT "Deletions in the gibberellin biosynthesis gene cluster of Gibberella
RT fujikuroi by restriction enzyme-mediated integration and conventional
RT transformation-mediated mutagenesis.";
RL Appl. Environ. Microbiol. 65:2558-2564(1999).
RN [5]
RP FUNCTION.
RX PubMed=10803977; DOI=10.1271/bbb.64.660;
RA Toyomasu T., Kawaide H., Ishizaki A., Shinoda S., Otsuka M., Mitsuhashi W.,
RA Sassa T.;
RT "Cloning of a full-length cDNA encoding ent-kaurene synthase from
RT Gibberella fujikuroi: functional analysis of a bifunctional diterpene
RT cyclase.";
RL Biosci. Biotechnol. Biochem. 64:660-664(2000).
RN [6]
RP FUNCTION.
RX PubMed=11472927; DOI=10.1128/aem.67.8.3514-3522.2001;
RA Tudzynski B., Hedden P., Carrera E., Gaskin P.;
RT "The P450-4 gene of Gibberella fujikuroi encodes ent-kaurene oxidase in the
RT gibberellin biosynthesis pathway.";
RL Appl. Environ. Microbiol. 67:3514-3522(2001).
RN [7]
RP FUNCTION.
RX PubMed=11320210; DOI=10.1073/pnas.091096298;
RA Rojas M.C., Hedden P., Gaskin P., Tudzynski B.;
RT "The P450-1 gene of Gibberella fujikuroi encodes a multifunctional enzyme
RT in gibberellin biosynthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:5838-5843(2001).
RN [8]
RP FUNCTION.
RX PubMed=11943776; DOI=10.1074/jbc.m201651200;
RA Tudzynski B., Rojas M.C., Gaskin P., Hedden P.;
RT "The gibberellin 20-oxidase of Gibberella fujikuroi is a multifunctional
RT monooxygenase.";
RL J. Biol. Chem. 277:21246-21253(2002).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=12750377; DOI=10.1074/jbc.m301927200;
RA Tudzynski B., Mihlan M., Rojas M.C., Linnemannstons P., Gaskin P.,
RA Hedden P.;
RT "Characterization of the final two genes of the gibberellin biosynthesis
RT gene cluster of Gibberella fujikuroi: des and P450-3 encode GA4 desaturase
RT and the 13-hydroxylase, respectively.";
RL J. Biol. Chem. 278:28635-28643(2003).
RN [10]
RP FUNCTION.
RX PubMed=15925394; DOI=10.1016/j.phytochem.2005.04.012;
RA Malonek S., Boemke C., Bornberg-Bauer E., Rojas M.C., Hedden P.,
RA Hopkins P., Tudzynski B.;
RT "Distribution of gibberellin biosynthetic genes and gibberellin production
RT in the Gibberella fujikuroi species complex.";
RL Phytochemistry 66:1296-1311(2005).
CC -!- FUNCTION: Gibberellin 13-hydroxylase; part of the gene cluster that
CC mediates the biosynthesis of gibberellins (GAs), diterpenoids that may
CC provide a selective advantage during infection of the preferred host
CC plant, rice (PubMed:23825955, PubMed:9917370, PubMed:10347043,
CC PubMed:12750377, PubMed:15925394). Gibberellins (GAs) are diterpenoids
CC and are synthesized via the mevalonate pathway (PubMed:12750377).
CC Biosynthesis of the major metabolite GA3 (gibberellic acid) from
CC geranylgeranyl diphosphate (GGPP) requires 13 steps (PubMed:12750377).
CC The GGPP produced by the geranylgeranyl diphosphate synthase GGS2 is
CC converted to ent-kaurene via ent-copalyldiphosphate in a two-step
CC cyclization reaction performed by the bifunctional ent-copalyl
CC diphosphate synthase/ent-kaurene synthase enzyme (CPS/KS)
CC (PubMed:9745028, PubMed:10803977, PubMed:12750377). Ent-Kaurene is
CC metabolized to GAs by a series of oxidation reactions catalyzed by
CC cytochrome P450 monooxygenases (PubMed:9917370, PubMed:12750377).
CC Cytochrome P450 monooxygenase P450-4 is an ent-kaurene oxidase that
CC catalyzes the three oxidation steps between ent-kaurene and ent-
CC kaurenoic acid (PubMed:11472927). The highly multifunctional cytochrome
CC P450 monooxygenase P450-1 then catalyzes four steps involving oxidation
CC at two carbon atoms, in the main pathway from ent-kaurenoic acid to
CC GA14 via GA12-aldehyde as well as producing kaurenolides and fujenoic
CC acids as by-products (PubMed:11320210). The cytochrome P450
CC monooxygenase P450-2 then converts GA14 to GA4 by removal of C-20
CC (PubMed:11943776). GA4 is further converted to GA7 by the GA4
CC desaturase DES via 1,2-desaturation before cytochrome P450
CC monooxygenase P450-3, a 13-hydroxylase, hydroxylates GA7 to GA3, the
CC final product of the GA-biosynthetic pathway (PubMed:12750377).
CC {ECO:0000269|PubMed:10347043, ECO:0000269|PubMed:10803977,
CC ECO:0000269|PubMed:11320210, ECO:0000269|PubMed:11472927,
CC ECO:0000269|PubMed:11943776, ECO:0000269|PubMed:12750377,
CC ECO:0000269|PubMed:15925394, ECO:0000269|PubMed:23825955,
CC ECO:0000269|PubMed:9745028, ECO:0000269|PubMed:9917370}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC {ECO:0000269|PubMed:12750377, ECO:0000269|PubMed:9917370}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Expression is induced under gibberellin-producing conditions
CC (PubMed:9917370). {ECO:0000269|PubMed:9917370}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of GA3, although its
CC precursors, GA4 and GA7, are present (PubMed:12750377).
CC {ECO:0000269|PubMed:12750377}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; HF679027; CCT69171.1; -; Genomic_DNA.
DR AlphaFoldDB; S0E2Y2; -.
DR SMR; S0E2Y2; -.
DR STRING; 5127.CCT69171; -.
DR EnsemblFungi; CCT69171; CCT69171; FFUJ_14337.
DR VEuPathDB; FungiDB:FFUJ_14337; -.
DR HOGENOM; CLU_022195_0_2_1; -.
DR UniPathway; UPA00390; -.
DR Proteomes; UP000016800; 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; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0009686; P:gibberellin biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
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..527
FT /note="Cytochrome P450 monooygenase 3"
FT /id="PRO_0000442044"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 473
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:P04798"
SQ SEQUENCE 527 AA; 59898 MW; 3FF4CB8576BA17AE CRC64;
MSNFVTLIEP LELTGSRVLR IAVAFAALCG ATGLLAFSWW IYKQSSSKPT LPYPVVGDTH
AQSLEKNLIK GMQQYRDSPF FLAGSRPPLL ILPMSVFHEI HNMPNEYISI IVEHEDKFQG
KYTHITTIRP EIPATIRQDL TRNMPNIILE LQDELTYASD QWPRTSKWSS VSLYDMMLRT
VALLSGRAFV GLPLCRDEGW LQASIGYTVQ CVSIRDQLFT WSPVLRPIIG PFLPSVRSVR
RHLRFAAEIM APLISQALQD EKQHRADTLL ADQTEGRGTF ISWLLRHLPE ELRTPEQVGL
DQMLVSFAAI HTTTMALTKV VWELVKRPEY IEPLRTEMQD VFGPDAVSPD ICINKEALSR
LHKLDSFIRE VQRWCPSTFV TPSRRVMKSM TLSNGIKLQR GTSIAFPAHA IHMSEETPTF
SPDFSSDFEN PSPRIFDGFR YLNLRSIKGQ GSQHQAATTG PDYLIFNHGK HACPGRFFAI
SEIKMILIEL LAKYDFRLED GKPGPELMRV GTETRLDTKA GLEMRRR
