ID   ICS2_ARATH              Reviewed;         562 AA.
AC   Q9M9V6; B2LWF5;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Isochorismate synthase 2, chloroplastic;
DE            Short=AtIcs2;
DE            EC=5.4.4.2 {ECO:0000305|PubMed:18451262};
DE   AltName: Full=Isochorismate mutase 2;
DE   AltName: Full=menF-like protein 2;
DE   Flags: Precursor;
GN   Name=ICS2; OrderedLocusNames=At1g18870; ORFNames=F6A14.3;
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], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP   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).
RN   [2]
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   [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   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).
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:16617180,
CC       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:0000305|PubMed:18451262};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Siderophore biosynthesis; salicylate biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:18451262}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q9M9V6-1; Sequence=Displayed;
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype; due to the redundancy with
CC       ICS1. Mutants are not impaired in salicylic acid accumulation upon
CC       induction. Ics1 and ics2 double mutant is seedling lethal due to
CC       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=AAF27094.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; EU589462; ACC60228.1; -; mRNA.
DR   EMBL; AC011809; AAF27094.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE29773.1; -; Genomic_DNA.
DR   PIR; F86322; F86322.
DR   RefSeq; NP_001154351.1; NM_001160879.1.
DR   RefSeq; NP_173321.4; NM_101744.7. [Q9M9V6-1]
DR   AlphaFoldDB; Q9M9V6; -.
DR   SMR; Q9M9V6; -.
DR   STRING; 3702.AT1G18870.1; -.
DR   PaxDb; Q9M9V6; -.
DR   PRIDE; Q9M9V6; -.
DR   ProteomicsDB; 228773; -. [Q9M9V6-1]
DR   EnsemblPlants; AT1G18870.1; AT1G18870.1; AT1G18870. [Q9M9V6-1]
DR   GeneID; 838468; -.
DR   Gramene; AT1G18870.1; AT1G18870.1; AT1G18870. [Q9M9V6-1]
DR   KEGG; ath:AT1G18870; -.
DR   Araport; AT1G18870; -.
DR   TAIR; locus:2034954; AT1G18870.
DR   eggNOG; KOG1223; Eukaryota.
DR   InParanoid; Q9M9V6; -.
DR   OrthoDB; 372295at2759; -.
DR   PhylomeDB; Q9M9V6; -.
DR   BRENDA; 5.4.4.2; 399.
DR   UniPathway; UPA00025; -.
DR   PRO; PR:Q9M9V6; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9M9V6; baseline and differential.
DR   Genevisible; Q9M9V6; 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:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0042372; P:phylloquinone biosynthetic process; IMP:TAIR.
DR   GO; GO:0009697; P:salicylic acid biosynthetic process; IEA:UniProtKB-UniPathway.
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..55
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           56..562
FT                   /note="Isochorismate synthase 2, chloroplastic"
FT                   /id="PRO_0000343792"
SQ   SEQUENCE   562 AA;  62386 MW;  05454B7F8124331C CRC64;
     MASLQCSFHF LGTNPKKYNP SSIFQSYSRT SFTKLSSRVS RQRFLRCTLS MNGCEADHKA
     PLGTVETRTL STVPSPAAAT ERLITAVSDL KSQPPPFSSG IVRLQVPIEQ KIGAIDWLHA
     QNEILPRSFF SRRSDSGRPD LLQDFSSDNG SSDHNPVSVA GIGSAVFFRD LDPFSHDDWR
     SIRRFLSSKS PLIRAYGGLR FDPTGKIAVE WEHFGSFYFT VPQVEFDEFG GSSMLAATVA
     WDNELSWTLE NAIEALQETM LQVSSVIMRL RRESLGVIVV SKNHVPSEGA YYPAVNNALE
     IIKDKHSPLS KVVLARSSRI ITDTDIDPIA WLARLQCEGQ DAYQFCLQPP GAPAFIGNTP
     ERLFHRKHLG VCSEALAATR PRGDSKVREM EIERDLLTSP KDDLEFSIVR ENIREKLKTI
     CDRVVVKPHK SVRKLARVQH LYSQLAGQLK REDDEFNILT ALHPTPAVCG CPVEEARLLI
     KQIESFDRGM YAGPIGFFGG GESEFSVGIR SALVEKGLGA LIYAGTGIVS GSNPSSEWNE
     LELKISQFTK SLEHESALQP IN