ISPG_ARATH
ID ISPG_ARATH Reviewed; 741 AA.
AC F4K0E8; Q8GZR7; Q8LPQ4; Q8RXG8; Q9FF59;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (ferredoxin), chloroplastic;
DE EC=1.17.7.1 {ECO:0000269|PubMed:15650872};
DE AltName: Full=1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase;
DE AltName: Full=Protein CHLOROPLAST BIOGENESIS 4;
DE AltName: Full=Protein CONSTITUTIVE SUBTILISIN 3;
DE Flags: Precursor;
GN Name=ISPG; Synonyms=CLB4, CSB3, HDS; OrderedLocusNames=At5g60600;
GN ORFNames=MUP24.2;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11943178; DOI=10.1016/s0014-5793(02)02402-x;
RA Querol J., Campos N., Imperial S., Boronat A., Rodriguez-Concepcion M.;
RT "Functional analysis of the Arabidopsis thaliana GCPE protein involved in
RT plastid isoprenoid biosynthesis.";
RL FEBS Lett. 514:343-346(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=15133149; DOI=10.1104/pp.103.036996;
RA de la Luz Gutierrez-Nava M., Gillmor C.S., Jimenez L.F., Guevara-Garcia A.,
RA Leon P.;
RT "CHLOROPLAST BIOGENESIS genes act cell and noncell autonomously in early
RT chloroplast development.";
RL Plant Physiol. 135:471-482(2004).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=15650872; DOI=10.1007/s00775-004-0619-z;
RA Seemann M., Wegner P., Schuenemann V., Bui B.T., Wolff M., Marquet A.,
RA Trautwein A.X., Rohmer M.;
RT "Isoprenoid biosynthesis in chloroplasts via the methylerythritol phosphate
RT pathway: the (E)-4-hydroxy-3-methylbut-2-enyl diphosphate synthase (GcpE)
RT from Arabidopsis thaliana is a [4Fe-4S] protein.";
RL J. Biol. Inorg. Chem. 10:131-137(2005).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF GLY-696.
RX PubMed=16167903; DOI=10.1111/j.1365-313x.2005.02517.x;
RA Gil M.J., Coego A., Mauch-Mani B., Jorda L., Vera P.;
RT "The Arabidopsis csb3 mutant reveals a regulatory link between salicylic
RT acid-mediated disease resistance and the methyl-erythritol 4-phosphate
RT pathway.";
RL Plant J. 44:155-166(2005).
RN [8]
RP INDUCTION.
RX PubMed=15863698; DOI=10.1104/pp.104.058735;
RA Hsieh M.H., Goodman H.M.;
RT "The Arabidopsis IspH homolog is involved in the plastid nonmevalonate
RT pathway of isoprenoid biosynthesis.";
RL Plant Physiol. 138:641-653(2005).
RN [9]
RP FUNCTION.
RX PubMed=16480720; DOI=10.1016/j.febslet.2006.01.082;
RA Seemann M., Tse Sum Bui B., Wolff M., Miginiac-Maslow M., Rohmer M.;
RT "Isoprenoid biosynthesis in plant chloroplasts via the MEP pathway: direct
RT thylakoid/ferredoxin-dependent photoreduction of GcpE/IspG.";
RL FEBS Lett. 580:1547-1552(2006).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=18236010; DOI=10.1007/s11103-008-9297-5;
RA Hsieh M.H., Chang C.Y., Hsu S.J., Chen J.J.;
RT "Chloroplast localization of methylerythritol 4-phosphate pathway enzymes
RT and regulation of mitochondrial genes in ispD and ispE albino mutants in
RT Arabidopsis.";
RL Plant Mol. Biol. 66:663-673(2008).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=18948055; DOI=10.1016/j.tplants.2008.09.003;
RA Phillips M.A., Leon P., Boronat A., Rodriguez-Concepcion M.;
RT "The plastidial MEP pathway: unified nomenclature and resources.";
RL Trends Plant Sci. 13:619-623(2008).
CC -!- FUNCTION: Enzyme of the plastid non-mevalonate pathway for isoprenoid
CC biosynthesis that converts 2-C-methyl-D-erythritol 2,4-cyclodiphosphate
CC (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate. Is
CC essential for chloroplast development and required for the salicylic
CC acid (SA)-mediated disease resistance to biotrophic pathogens.
CC {ECO:0000269|PubMed:11943178, ECO:0000269|PubMed:15133149,
CC ECO:0000269|PubMed:15650872, ECO:0000269|PubMed:16167903,
CC ECO:0000269|PubMed:16480720}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + H2O + 2
CC oxidized [2Fe-2S]-[ferredoxin] = 2-C-methyl-D-erythritol 2,4-cyclic
CC diphosphate + H(+) + 2 reduced [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:26119, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737,
CC ChEBI:CHEBI:33738, ChEBI:CHEBI:58483, ChEBI:CHEBI:128753;
CC EC=1.17.7.1; Evidence={ECO:0000269|PubMed:15650872};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:15650872};
CC Note=Binds 1 [4Fe-4S] cluster per subunit.
CC {ECO:0000269|PubMed:15650872};
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC phosphate: step 5/6.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000305|PubMed:11943178, ECO:0000305|PubMed:18236010}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4K0E8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4K0E8-2; Sequence=VSP_043826;
CC -!- TISSUE SPECIFICITY: Expressed in roots, shoots, leaves, flowers and
CC siliques (at protein level). {ECO:0000269|PubMed:15133149}.
CC -!- INDUCTION: Circadian-regulated with a peak in the late period of dark
CC phase and early period of the light phase.
CC {ECO:0000269|PubMed:15863698}.
CC -!- DISRUPTION PHENOTYPE: Albino phenotype and seedling lethal when
CC homozygous. The phenotype is caused by an early arrest in chloroplast
CC differentiation. {ECO:0000269|PubMed:15133149,
CC ECO:0000269|PubMed:18948055}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the IspG family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09833.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF434673; AAO15446.1; -; mRNA.
DR EMBL; AB005246; BAB09833.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED97353.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97354.1; -; Genomic_DNA.
DR EMBL; AY081261; AAL91150.1; -; mRNA.
DR EMBL; AY094472; AAM19840.1; -; mRNA.
DR EMBL; BT010473; AAQ65096.1; -; mRNA.
DR RefSeq; NP_200868.2; NM_125453.6. [F4K0E8-2]
DR RefSeq; NP_851233.1; NM_180902.5. [F4K0E8-1]
DR AlphaFoldDB; F4K0E8; -.
DR BioGRID; 21425; 2.
DR STRING; 3702.AT5G60600.1; -.
DR iPTMnet; F4K0E8; -.
DR MetOSite; F4K0E8; -.
DR PaxDb; F4K0E8; -.
DR PRIDE; F4K0E8; -.
DR ProteomicsDB; 250684; -. [F4K0E8-1]
DR EnsemblPlants; AT5G60600.1; AT5G60600.1; AT5G60600. [F4K0E8-1]
DR EnsemblPlants; AT5G60600.2; AT5G60600.2; AT5G60600. [F4K0E8-2]
DR GeneID; 836181; -.
DR Gramene; AT5G60600.1; AT5G60600.1; AT5G60600. [F4K0E8-1]
DR Gramene; AT5G60600.2; AT5G60600.2; AT5G60600. [F4K0E8-2]
DR KEGG; ath:AT5G60600; -.
DR Araport; AT5G60600; -.
DR TAIR; locus:2175851; AT5G60600.
DR eggNOG; ENOG502QSBY; Eukaryota.
DR HOGENOM; CLU_012689_0_0_1; -.
DR InParanoid; F4K0E8; -.
DR OMA; YGYVGAG; -.
DR BioCyc; MetaCyc:AT5G60600-MON; -.
DR BRENDA; 1.17.7.1; 399.
DR UniPathway; UPA00056; UER00096.
DR PRO; PR:F4K0E8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4K0E8; baseline and differential.
DR Genevisible; F4K0E8; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:TAIR.
DR GO; GO:0046429; F:4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase activity; IDA:TAIR.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IBA:GO_Central.
DR GO; GO:0009617; P:response to bacterium; IMP:TAIR.
DR GO; GO:0009862; P:systemic acquired resistance, salicylic acid mediated signaling pathway; IMP:TAIR.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.20.20.20; -; 1.
DR Gene3D; 3.30.413.10; -; 1.
DR HAMAP; MF_00159; IspG; 1.
DR InterPro; IPR011005; Dihydropteroate_synth-like.
DR InterPro; IPR017178; IspG_atypical.
DR InterPro; IPR004588; IspG_bac-typ.
DR InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR PANTHER; PTHR30454; PTHR30454; 1.
DR Pfam; PF04551; GcpE; 1.
DR PIRSF; PIRSF037336; IspG_like; 1.
DR SUPFAM; SSF56014; SSF56014; 1.
DR TIGRFAMs; TIGR00612; ispG_gcpE; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; Alternative splicing; Chloroplast; Iron; Iron-sulfur;
KW Isoprene biosynthesis; Metal-binding; Oxidoreductase; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..38
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 39..741
FT /note="4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
FT (ferredoxin), chloroplastic"
FT /id="PRO_0000417590"
FT BINDING 644
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 647
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 678
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 685
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT VAR_SEQ 373..374
FT /note="VA -> A (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11943178"
FT /id="VSP_043826"
FT MUTAGEN 696
FT /note="G->D: In clb4-3/csb3; semi-dwarf phenotype, elevated
FT levels of salicylic acid and enhanced resistance to
FT biotrophic pathogens."
FT /evidence="ECO:0000269|PubMed:16167903"
FT CONFLICT 94
FT /note="N -> D (in Ref. 4; AAM19840)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="R -> G (in Ref. 4; AAL91150/AAQ65096)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 741 AA; 82256 MW; E2E5615619D5D3E8 CRC64;
MATGVLPAPV SGIKIPDSKV GFGKSMNLVR ICDVRSLRSA RRRVSVIRNS NQGSDLAELQ
PASEGSPLLV PRQKYCESLH KTVRRKTRTV MVGNVALGSE HPIRIQTMTT SDTKDITGTV
DEVMRIADKG ADIVRITVQG KKEADACFEI KDKLVQLNYN IPLVADIHFA PTVALRVAEC
FDKIRVNPGN FADRRAQFET IDYTEDEYQK ELQHIEQVFT PLVEKCKKYG RAMRIGTNHG
SLSDRIMSYY GDSPRGMVES AFEFARICRK LDYHNFVFSM KASNPVIMVQ AYRLLVAEMY
VHGWDYPLHL GVTEAGEGED GRMKSAIGIG TLLQDGLGDT IRVSLTEPPE EEIDPCRRLA
NLGTKAAKLQ QGVAPFEEKH RHYFDFQRRT GDLPVQKEGE EVDYRNVLHR DGSVLMSISL
DQLKAPELLY RSLATKLVVG MPFKDLATVD SILLRELPPV DDQVARLALK RLIDVSMGVI
APLSEQLTKP LPNAMVLVNL KELSGGAYKL LPEGTRLVVS LRGDEPYEEL EILKNIDATM
ILHDVPFTED KVSRVHAARR LFEFLSENSV NFPVIHHINF PTGIHRDELV IHAGTYAGGL
LVDGLGDGVM LEAPDQDFDF LRNTSFNLLQ GCRMRNTKTE YVSCPSCGRT LFDLQEISAE
IREKTSHLPG VSIAIMGCIV NGPGEMADAD FGYVGGSPGK IDLYVGKTVV KRGIAMTEAT
DALIGLIKEH GRWVDPPVAD E
