ISPH_ORYSJ
ID ISPH_ORYSJ Reviewed; 459 AA.
AC Q6AVG6; A0A0P0W2J7;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=4-hydroxy-3-methylbut-2-enyl diphosphate reductase, chloroplastic {ECO:0000305};
DE EC=1.17.7.4 {ECO:0000250|UniProtKB:Q94B35};
DE Flags: Precursor;
GN Name=ISPH {ECO:0000305};
GN OrderedLocusNames=Os03g0731900 {ECO:0000312|EMBL:BAS86228.1},
GN LOC_Os03g52170 {ECO:0000312|EMBL:ABF98702.1};
GN ORFNames=OSJNBa0079G12.18 {ECO:0000312|EMBL:AAT77894.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP INDUCTION.
RX PubMed=17634747; DOI=10.1007/s11103-007-9207-2;
RA Okada A., Shimizu T., Okada K., Kuzuyama T., Koga J., Shibuya N.,
RA Nojiri H., Yamane H.;
RT "Elicitor induced activation of the methylerythritol phosphate pathway
RT toward phytoalexins biosynthesis in rice.";
RL Plant Mol. Biol. 65:177-187(2007).
CC -!- FUNCTION: Enzyme of the plastid non-mevalonate pathway for isoprenoid
CC biosynthesis that converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-
CC diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl
CC diphosphate (DMAPP). Is essential for chloroplast development.
CC {ECO:0000250|UniProtKB:Q94B35}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + isopentenyl diphosphate + 2 oxidized [2Fe-2S]-
CC [ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+)
CC + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:24488, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:128753, ChEBI:CHEBI:128769; EC=1.17.7.4;
CC Evidence={ECO:0000250|UniProtKB:Q94B35};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dimethylallyl diphosphate + H2O + 2 oxidized [2Fe-2S]-
CC [ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+)
CC + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:24825, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC ChEBI:CHEBI:57623, ChEBI:CHEBI:128753; EC=1.17.7.4;
CC Evidence={ECO:0000250|UniProtKB:Q94B35};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P62623};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000250|UniProtKB:P62623};
CC -!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate
CC biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-
CC methylbutenyl diphosphate: step 1/1. {ECO:0000305}.
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC phosphate: step 6/6. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P62623}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000250|UniProtKB:Q94B35}.
CC -!- INDUCTION: Induced by jasmonate, copper, UV and chitin oligosaccharide
CC elicitor. {ECO:0000269|PubMed:17634747}.
CC -!- SIMILARITY: Belongs to the IspH family. {ECO:0000305}.
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DR EMBL; AC103550; AAT77894.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF98702.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF13081.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS86228.1; -; Genomic_DNA.
DR EMBL; AK064873; BAG89250.1; -; mRNA.
DR EMBL; AK121561; BAH00550.1; -; mRNA.
DR RefSeq; XP_015632597.1; XM_015777111.1.
DR AlphaFoldDB; Q6AVG6; -.
DR SMR; Q6AVG6; -.
DR STRING; 4530.OS03T0731900-01; -.
DR PaxDb; Q6AVG6; -.
DR PRIDE; Q6AVG6; -.
DR EnsemblPlants; Os03t0731900-01; Os03t0731900-01; Os03g0731900.
DR GeneID; 4334003; -.
DR Gramene; Os03t0731900-01; Os03t0731900-01; Os03g0731900.
DR KEGG; osa:4334003; -.
DR eggNOG; ENOG502QPIQ; Eukaryota.
DR HOGENOM; CLU_027486_4_1_1; -.
DR InParanoid; Q6AVG6; -.
DR OMA; DRIWLTN; -.
DR OrthoDB; 1067589at2759; -.
DR PlantReactome; R-OSA-1119464; Methylerythritol phosphate pathway.
DR UniPathway; UPA00056; UER00097.
DR UniPathway; UPA00059; UER00105.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR Genevisible; Q6AVG6; OS.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051745; F:4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050992; P:dimethylallyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
DR CDD; cd13944; lytB_ispH; 1.
DR HAMAP; MF_00191; IspH; 1.
DR InterPro; IPR003451; LytB/IspH.
DR Pfam; PF02401; LYTB; 1.
DR TIGRFAMs; TIGR00216; ispH_lytB; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Chloroplast; Iron; Iron-sulfur; Isoprene biosynthesis;
KW Metal-binding; Oxidoreductase; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..31
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 32..459
FT /note="4-hydroxy-3-methylbut-2-enyl diphosphate reductase,
FT chloroplastic"
FT /id="PRO_0000417593"
FT ACT_SITE 236
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P62623"
FT BINDING 115
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P62623"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P62623"
FT BINDING 206
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P62623"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P62623"
FT BINDING 305
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P62623"
FT BINDING 343
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P62623"
FT BINDING 372..374
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P62623"
FT BINDING 434
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P62617"
SQ SEQUENCE 459 AA; 51064 MW; 7134DF044F1814DD CRC64;
MATITTQLRS ALLSPAASPS RRARRAPSSV RCDSSAASSL SASASLDADF DKKQFRHNLT
RSDNYNRKGF GHKKETLELM SQEYTSDVIK TLKENGNQHT WGPVTVKLAE AYGFCWGVER
AVQIAYEARK QFPDDRIWLT NEIIHNPTVN KRLEDMGVQN IPVDAGIKDF DVVEQGDVVV
LPAFGAAVEE MYTLNEKKVQ IVDTTCPWVS KVWNMVEKHK KGDYTSIIHG KYSHEETVAT
ASFAGTYIIV KNIAEASYVC DYILGGQLDG SSSTKEEFLE KFKNAVSPGF DPDVDLVKVG
IANQTTMLKG ETEEIGKLVE KTMMRRFGVE NVNDHFIAFN TICDATQERQ DAMYQLVKEK
VDLILVVGGW NSSNTSHLQE IGELSGIPSY WIDSEQRIGP GNKISYKLNH GELVEKENWL
PEGPITIGVT SGASTPDKVV EDALQKVFEI KRQEVLQAA
