ICS1_ARATH
ID ICS1_ARATH Reviewed; 569 AA.
AC Q9S7H8; O81522; Q3ECD2; Q9ASQ4;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Isochorismate synthase 1, chloroplastic;
DE Short=AtIcs1 {ECO:0000303|PubMed:17190832};
DE Short=IcsI;
DE EC=5.4.4.2 {ECO:0000269|PubMed:11734859, ECO:0000269|PubMed:17190832};
DE AltName: Full=Enhanced disease susceptibility 16;
DE Short=Eds16;
DE AltName: Full=Isochorismate mutase 1;
DE AltName: Full=Salicylic acid induction deficient 2;
DE Short=Sid2;
DE AltName: Full=menF-like protein 1;
DE Flags: Precursor;
GN Name=ICS1; OrderedLocusNames=At1g74710; ORFNames=F1M20.39, F25A4.31;
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 1).
RA Meng H., Pullman G.S., Peter G.F.;
RT "Cloning of a plant isochorismate synthase.";
RL (er) Plant Gene Register PGR98-214(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Leaf;
RX PubMed=11734859; DOI=10.1038/35107108;
RA Wildermuth M.C., Dewdney J., Wu G., Ausubel F.M.;
RT "Isochorismate synthase is required to synthesize salicylic acid for plant
RT defence.";
RL Nature 414:562-565(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
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 [5]
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 [6]
RP FUNCTION.
RX PubMed=10449575; DOI=10.2307/3870970;
RA Nawrath C., Metraux J.P.;
RT "Salicylic acid induction-deficient mutants of Arabidopsis express PR-2 and
RT PR-5 and accumulate high levels of camalexin after pathogen inoculation.";
RL Plant Cell 11:1393-1404(1999).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16617180; DOI=10.1074/jbc.m601754200;
RA Gross J., Cho W.K., Lezhneva L., Falk J., Krupinska K., Shinozaki K.,
RA Seki M., Herrmann R.G., Meurer J.;
RT "A plant locus essential for phylloquinone (vitamin K1) biosynthesis
RT originated from a fusion of four eubacterial genes.";
RL J. Biol. Chem. 281:17189-17196(2006).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, SUBUNIT,
RP BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND ACTIVITY REGULATION.
RX PubMed=17190832; DOI=10.1074/jbc.m605193200;
RA Strawn M.A., Marr S.K., Inoue K., Inada N., Zubieta C., Wildermuth M.C.;
RT "Arabidopsis isochorismate synthase functional in pathogen-induced
RT salicylate biosynthesis exhibits properties consistent with a role in
RT diverse stress responses.";
RL J. Biol. Chem. 282:5919-5933(2007).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=18451262; DOI=10.1104/pp.108.119420;
RA Garcion C., Lohmann A., Lamodiere E., Catinot J., Buchala A., Doermann P.,
RA Metraux J.-P.;
RT "Characterization and biological function of the ISOCHORISMATE SYNTHASE2
RT gene of Arabidopsis.";
RL Plant Physiol. 147:1279-1287(2008).
CC -!- FUNCTION: Isochorismate synthase involved in the synthesis of salicylic
CC acid (SA) required for both local and systemic acquired resistance (LAR
CC and SAR) while SA synthesized through the phenylalanine ammonium lyase
CC (PAL) pathway seems to potentiate plant cell death. Also involved in
CC phylloquinone (vitamin K1) synthesis. Has no isochorismate pyruvate
CC lyase (IPL) activity. {ECO:0000269|PubMed:10449575,
CC ECO:0000269|PubMed:11734859, ECO:0000269|PubMed:16617180,
CC ECO:0000269|PubMed:17190832, ECO:0000269|PubMed:18451262}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate = isochorismate; Xref=Rhea:RHEA:18985,
CC ChEBI:CHEBI:29748, ChEBI:CHEBI:29780; EC=5.4.4.2;
CC Evidence={ECO:0000269|PubMed:11734859, ECO:0000269|PubMed:17190832};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=41.5 uM for chorismate {ECO:0000269|PubMed:17190832};
CC KM=193 uM for magnesium {ECO:0000269|PubMed:17190832};
CC pH dependence:
CC Optimum pH is 7.5-8. {ECO:0000269|PubMed:17190832};
CC Temperature dependence:
CC Optimum temperature is 23 degrees Celsius. 90% of maximal activity
CC from 4 to 37 degrees Celsius. {ECO:0000269|PubMed:17190832};
CC -!- PATHWAY: Siderophore biosynthesis; salicylate biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17190832}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:17190832, ECO:0000269|PubMed:18451262}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9S7H8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9S7H8-2; Sequence=VSP_034699;
CC -!- TISSUE SPECIFICITY: Leaves.
CC -!- INDUCTION: By pathogen infection. Systemic induction during systemic
CC acquired resistance (SAR). Not induced by light.
CC {ECO:0000269|PubMed:17190832}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype; due to the redundancy with
CC ICS2. Nevertheless salicylic acid accumulation upon induction is
CC severely impaired. Ics1 and ics2 double mutant is seedling lethal due
CC to photosynthetic lesions induced by the lack of phylloquinone.
CC {ECO:0000269|PubMed:16617180, ECO:0000269|PubMed:18451262}.
CC -!- SIMILARITY: Belongs to the isochorismate synthase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC97926.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAD55272.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG52358.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF078080; AAC97926.1; ALT_INIT; mRNA.
DR EMBL; AY056055; AAL17715.1; -; mRNA.
DR EMBL; AC008263; AAD55272.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC011765; AAG52358.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35624.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35625.1; -; Genomic_DNA.
DR EMBL; AF367342; AAK32929.1; -; mRNA.
DR EMBL; AY124864; AAM70573.1; -; mRNA.
DR PIR; D96776; D96776.
DR PIR; T51711; T51711.
DR RefSeq; NP_565090.1; NM_106129.4. [Q9S7H8-1]
DR RefSeq; NP_974143.1; NM_202414.1. [Q9S7H8-2]
DR AlphaFoldDB; Q9S7H8; -.
DR SMR; Q9S7H8; -.
DR STRING; 3702.AT1G74710.2; -.
DR SwissLipids; SLP:000001506; -.
DR PaxDb; Q9S7H8; -.
DR PRIDE; Q9S7H8; -.
DR ProteomicsDB; 228772; -. [Q9S7H8-1]
DR EnsemblPlants; AT1G74710.1; AT1G74710.1; AT1G74710. [Q9S7H8-1]
DR EnsemblPlants; AT1G74710.2; AT1G74710.2; AT1G74710. [Q9S7H8-2]
DR GeneID; 843810; -.
DR Gramene; AT1G74710.1; AT1G74710.1; AT1G74710. [Q9S7H8-1]
DR Gramene; AT1G74710.2; AT1G74710.2; AT1G74710. [Q9S7H8-2]
DR KEGG; ath:AT1G74710; -.
DR Araport; AT1G74710; -.
DR TAIR; locus:2019245; AT1G74710.
DR eggNOG; KOG1223; Eukaryota.
DR HOGENOM; CLU_006493_8_3_1; -.
DR InParanoid; Q9S7H8; -.
DR OMA; AQDEIQP; -.
DR OrthoDB; 372295at2759; -.
DR PhylomeDB; Q9S7H8; -.
DR BioCyc; ARA:AT1G74710-MON; -.
DR BioCyc; MetaCyc:AT1G74710-MON; -.
DR BRENDA; 5.4.4.2; 399.
DR SABIO-RK; Q9S7H8; -.
DR UniPathway; UPA00025; -.
DR PRO; PR:Q9S7H8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9S7H8; baseline and differential.
DR Genevisible; Q9S7H8; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; IDA:TAIR.
DR GO; GO:0008909; F:isochorismate synthase activity; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:TAIR.
DR GO; GO:0060866; P:leaf abscission; IMP:TAIR.
DR GO; GO:0031348; P:negative regulation of defense response; IMP:TAIR.
DR GO; GO:0042372; P:phylloquinone biosynthetic process; IMP:TAIR.
DR GO; GO:0009617; P:response to bacterium; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IMP:TAIR.
DR GO; GO:0009697; P:salicylic acid biosynthetic process; TAS:TAIR.
DR GO; GO:0010118; P:stomatal movement; IMP:TAIR.
DR GO; GO:0009627; P:systemic acquired resistance; IEP:TAIR.
DR Gene3D; 3.60.120.10; -; 1.
DR InterPro; IPR005801; ADC_synthase.
DR InterPro; IPR015890; Chorismate_C.
DR InterPro; IPR004561; IsoChor_synthase.
DR InterPro; IPR044250; MenF-like.
DR PANTHER; PTHR47253; PTHR47253; 1.
DR Pfam; PF00425; Chorismate_bind; 1.
DR SUPFAM; SSF56322; SSF56322; 1.
DR TIGRFAMs; TIGR00543; isochor_syn; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Isomerase; Magnesium; Plant defense;
KW Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..45
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 46..569
FT /note="Isochorismate synthase 1, chloroplastic"
FT /id="PRO_0000035791"
FT VAR_SEQ 553..569
FT /note="FTKSIEYEATTSLQAIN -> VRAFVQKMFSDIMVLCYQNPNFYSLFCCCFC
FT SSPSQLNMKQQHLYRRLIEERVTFVFDCFVCMGDKGFSQ (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_034699"
FT CONFLICT 14
FT /note="N -> D (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="S -> P (in Ref. 1; AAC97926)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="Q -> R (in Ref. 1; AAC97926)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 569 AA; 62575 MW; E60963196FBBB81C CRC64;
MASLQFSSQF LGSNTKTHSS IISISRSYSP TPFTRFSRKK YESCSMSMNG CDGDFKTPLG
TVETRTMTAV LSPAAATERL ISAVSELKSQ PPSFSSGVVR LQVPIDQQIG AIDWLQAQNE
IQPRCFFSRR SDVGRPDLLL DLANENGNGN GNGTVSSDRN LVSVAGIGSA VFFRDLDPFS
HDDWRSIRRF LSSTSPLIRA YGGMRFDPNG KIAVEWEPFG AFYFSVPQVE FNEFGGSSML
AATIAWDDEL SWTLENAIEA LQETMLQVSS VVMKLRNRSL GVSVLSKNHV PTKGAYFPAV
EKALEMINQK SSPLNKVVLA RNSRIITDTD IDPIAWLAQL QREGHDAYQF CLQPPGAPAF
IGNTPERLFQ RTQLGVCSEA LAATRPRAAS SARDMEIERD LLTSPKDDLE FSIVRENIRE
KLNGICDRVV VKPQKTVRKL ARVQHLYSQL AGRLTKEDDE YKILAALHPT PAVCGLPAEE
ARLLIKEIES FDRGMYAGPI GFFGGEESEF AVGIRSALVE KGLGALIYAG TGIVAGSDPS
SEWNELDLKI SQFTKSIEYE ATTSLQAIN
