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Protein

Isochorismate synthase 1, chloroplastic

Gene

ICS1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the synthesis of salicylic acid (SA) required for both local and systemic acquired resistance (LAR and SAR) while SA synthesized through the phenylalanine ammonium lyase (PAL) pathway seems to potentiate plant cell death. Also involved in phylloquinone (vitamin K1) synthesis. Has no isochorismate pyruvate lyase (IPL) activity.4 Publications

Catalytic activityi

Chorismate = isochorismate.

Cofactori

Kineticsi

  1. KM=41.5 µM for chorismate1 Publication
  2. KM=193 µM for magnesium1 Publication

    pH dependencei

    Optimum pH is 7.5-8.1 Publication

    Temperature dependencei

    Optimum temperature is 23 degrees Celsius. 90% of maximal activity from 4 to 37 degrees Celsius.1 Publication

    Pathwayi: salicylate biosynthesis

    This protein is involved in the pathway salicylate biosynthesis, which is part of Siderophore biosynthesis.
    View all proteins of this organism that are known to be involved in the pathway salicylate biosynthesis and in Siderophore biosynthesis.

    GO - Molecular functioni

    • isochorismate synthase activity Source: TAIR

    GO - Biological processi

    • defense response Source: UniProtKB-KW
    • defense response to bacterium Source: TAIR
    • defense response to fungus Source: TAIR
    • negative regulation of defense response Source: TAIR
    • phylloquinone biosynthetic process Source: TAIR
    • response to bacterium Source: TAIR
    • response to cold Source: TAIR
    • salicylic acid biosynthetic process Source: TAIR
    • stomatal movement Source: TAIR
    • systemic acquired resistance Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Plant defense

    Keywords - Ligandi

    Magnesium

    Enzyme and pathway databases

    BioCyciARA:GQT-708-MONOMER.
    MetaCyc:AT1G74710-MONOMER.
    BRENDAi5.4.4.2. 399.
    SABIO-RKQ9S7H8.
    UniPathwayiUPA00025.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isochorismate synthase 1, chloroplastic (EC:5.4.4.2)
    Short name:
    AtIcs1
    Short name:
    IcsI
    Alternative name(s):
    Enhanced disease susceptibility 16
    Short name:
    Eds16
    Isochorismate mutase 1
    Salicylic acid induction deficient 2
    Short name:
    Sid2
    menF-like protein 1
    Gene namesi
    Name:ICS1
    Ordered Locus Names:At1g74710
    ORF Names:F1M20.39, F25A4.31
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 1

    Organism-specific databases

    TAIRiAT1G74710.

    Subcellular locationi

    GO - Cellular componenti

    • chloroplast Source: UniProtKB-SubCell
    • plastid Source: TAIR
    Complete GO annotation...

    Keywords - Cellular componenti

    Chloroplast, Plastid

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype; due to the redundancy with ICS2. Nevertheless salicylic acid accumulation upon induction is severely impaired. Ics1 and ics2 double mutant is seedling lethal due to photosynthetic lesions induced by the lack of phylloquinone.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4545ChloroplastSequence analysisAdd
    BLAST
    Chaini46 – 569524Isochorismate synthase 1, chloroplasticPRO_0000035791Add
    BLAST

    Proteomic databases

    PaxDbiQ9S7H8.
    PRIDEiQ9S7H8.

    Expressioni

    Tissue specificityi

    Leaves.

    Inductioni

    By pathogen infection. Systemic induction during systemic acquired resistance (SAR). Not induced by light.1 Publication

    Gene expression databases

    GenevisibleiQ9S7H8. AT.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    STRINGi3702.AT1G74710.2.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9S7H8.
    SMRiQ9S7H8. Positions 72-557.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the isochorismate synthase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiENOG410IMYR. Eukaryota.
    COG1169. LUCA.
    HOGENOMiHOG000006336.
    InParanoidiQ9S7H8.
    KOiK02552.
    OMAiNISSEWE.
    PhylomeDBiQ9S7H8.

    Family and domain databases

    Gene3Di3.60.120.10. 1 hit.
    InterProiIPR005801. ADC_synthase.
    IPR015890. Chorismate_C.
    IPR004561. IsoChor_synthase.
    [Graphical view]
    PfamiPF00425. Chorismate_bind. 1 hit.
    [Graphical view]
    SUPFAMiSSF56322. SSF56322. 1 hit.
    TIGRFAMsiTIGR00543. isochor_syn. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q9S7H8-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MASLQFSSQF LGSNTKTHSS IISISRSYSP TPFTRFSRKK YESCSMSMNG
    60 70 80 90 100
    CDGDFKTPLG TVETRTMTAV LSPAAATERL ISAVSELKSQ PPSFSSGVVR
    110 120 130 140 150
    LQVPIDQQIG AIDWLQAQNE IQPRCFFSRR SDVGRPDLLL DLANENGNGN
    160 170 180 190 200
    GNGTVSSDRN LVSVAGIGSA VFFRDLDPFS HDDWRSIRRF LSSTSPLIRA
    210 220 230 240 250
    YGGMRFDPNG KIAVEWEPFG AFYFSVPQVE FNEFGGSSML AATIAWDDEL
    260 270 280 290 300
    SWTLENAIEA LQETMLQVSS VVMKLRNRSL GVSVLSKNHV PTKGAYFPAV
    310 320 330 340 350
    EKALEMINQK SSPLNKVVLA RNSRIITDTD IDPIAWLAQL QREGHDAYQF
    360 370 380 390 400
    CLQPPGAPAF IGNTPERLFQ RTQLGVCSEA LAATRPRAAS SARDMEIERD
    410 420 430 440 450
    LLTSPKDDLE FSIVRENIRE KLNGICDRVV VKPQKTVRKL ARVQHLYSQL
    460 470 480 490 500
    AGRLTKEDDE YKILAALHPT PAVCGLPAEE ARLLIKEIES FDRGMYAGPI
    510 520 530 540 550
    GFFGGEESEF AVGIRSALVE KGLGALIYAG TGIVAGSDPS SEWNELDLKI
    560
    SQFTKSIEYE ATTSLQAIN
    Length:569
    Mass (Da):62,575
    Last modified:March 5, 2002 - v2
    Checksum:iE60963196FBBB81C
    GO
    Isoform 2 (identifier: Q9S7H8-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         553-569: FTKSIEYEATTSLQAIN → VRAFVQKMFS...VCMGDKGFSQ

    Note: Derived from EST data. No experimental confirmation available.
    Show »
    Length:622
    Mass (Da):68,989
    Checksum:i0C071AE78E7982D5
    GO

    Sequence cautioni

    The sequence AAC97926.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence AAD55272.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
    The sequence AAG52358.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti14 – 141N → D (Ref. 1) Curated
    Sequence conflicti195 – 1951S → P in AAC97926 (Ref. 1) Curated
    Sequence conflicti373 – 3731Q → R in AAC97926 (Ref. 1) Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei553 – 56917FTKSI…LQAIN → VRAFVQKMFSDIMVLCYQNP NFYSLFCCCFCSSPSQLNMK QQHLYRRLIEERVTFVFDCF VCMGDKGFSQ in isoform 2. CuratedVSP_034699Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF078080 mRNA. Translation: AAC97926.1. Different initiation.
    AY056055 mRNA. Translation: AAL17715.1.
    AC008263 Genomic DNA. Translation: AAD55272.1. Sequence problems.
    AC011765 Genomic DNA. Translation: AAG52358.1. Sequence problems.
    CP002684 Genomic DNA. Translation: AEE35624.1.
    CP002684 Genomic DNA. Translation: AEE35625.1.
    AF367342 mRNA. Translation: AAK32929.1.
    AY124864 mRNA. Translation: AAM70573.1.
    PIRiD96776.
    T51711.
    RefSeqiNP_565090.1. NM_106129.3. [Q9S7H8-1]
    NP_974143.1. NM_202414.1. [Q9S7H8-2]
    UniGeneiAt.22628.

    Genome annotation databases

    EnsemblPlantsiAT1G74710.1; AT1G74710.1; AT1G74710. [Q9S7H8-1]
    GeneIDi843810.
    KEGGiath:AT1G74710.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF078080 mRNA. Translation: AAC97926.1. Different initiation.
    AY056055 mRNA. Translation: AAL17715.1.
    AC008263 Genomic DNA. Translation: AAD55272.1. Sequence problems.
    AC011765 Genomic DNA. Translation: AAG52358.1. Sequence problems.
    CP002684 Genomic DNA. Translation: AEE35624.1.
    CP002684 Genomic DNA. Translation: AEE35625.1.
    AF367342 mRNA. Translation: AAK32929.1.
    AY124864 mRNA. Translation: AAM70573.1.
    PIRiD96776.
    T51711.
    RefSeqiNP_565090.1. NM_106129.3. [Q9S7H8-1]
    NP_974143.1. NM_202414.1. [Q9S7H8-2]
    UniGeneiAt.22628.

    3D structure databases

    ProteinModelPortaliQ9S7H8.
    SMRiQ9S7H8. Positions 72-557.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi3702.AT1G74710.2.

    Proteomic databases

    PaxDbiQ9S7H8.
    PRIDEiQ9S7H8.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT1G74710.1; AT1G74710.1; AT1G74710. [Q9S7H8-1]
    GeneIDi843810.
    KEGGiath:AT1G74710.

    Organism-specific databases

    TAIRiAT1G74710.

    Phylogenomic databases

    eggNOGiENOG410IMYR. Eukaryota.
    COG1169. LUCA.
    HOGENOMiHOG000006336.
    InParanoidiQ9S7H8.
    KOiK02552.
    OMAiNISSEWE.
    PhylomeDBiQ9S7H8.

    Enzyme and pathway databases

    UniPathwayiUPA00025.
    BioCyciARA:GQT-708-MONOMER.
    MetaCyc:AT1G74710-MONOMER.
    BRENDAi5.4.4.2. 399.
    SABIO-RKQ9S7H8.

    Miscellaneous databases

    PROiQ9S7H8.

    Gene expression databases

    GenevisibleiQ9S7H8. AT.

    Family and domain databases

    Gene3Di3.60.120.10. 1 hit.
    InterProiIPR005801. ADC_synthase.
    IPR015890. Chorismate_C.
    IPR004561. IsoChor_synthase.
    [Graphical view]
    PfamiPF00425. Chorismate_bind. 1 hit.
    [Graphical view]
    SUPFAMiSSF56322. SSF56322. 1 hit.
    TIGRFAMsiTIGR00543. isochor_syn. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning of a plant isochorismate synthase."
      Meng H., Pullman G.S., Peter G.F.
      Plant Gene Register PGR98-214
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Isochorismate synthase is required to synthesize salicylic acid for plant defence."
      Wildermuth M.C., Dewdney J., Wu G., Ausubel F.M.
      Nature 414:562-565(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Leaf.
    3. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    4. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: cv. Columbia.
    6. "Salicylic acid induction-deficient mutants of Arabidopsis express PR-2 and PR-5 and accumulate high levels of camalexin after pathogen inoculation."
      Nawrath C., Metraux J.P.
      Plant Cell 11:1393-1404(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "A plant locus essential for phylloquinone (vitamin K1) biosynthesis originated from a fusion of four eubacterial genes."
      Gross J., Cho W.K., Lezhneva L., Falk J., Krupinska K., Shinozaki K., Seki M., Herrmann R.G., Meurer J.
      J. Biol. Chem. 281:17189-17196(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    8. "Arabidopsis isochorismate synthase functional in pathogen-induced salicylate biosynthesis exhibits properties consistent with a role in diverse stress responses."
      Strawn M.A., Marr S.K., Inoue K., Inada N., Zubieta C., Wildermuth M.C.
      J. Biol. Chem. 282:5919-5933(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, ENZYME REGULATION.
    9. "Characterization and biological function of the ISOCHORISMATE SYNTHASE2 gene of Arabidopsis."
      Garcion C., Lohmann A., Lamodiere E., Catinot J., Buchala A., Doermann P., Metraux J.-P.
      Plant Physiol. 147:1279-1287(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiICS1_ARATH
    AccessioniPrimary (citable) accession number: Q9S7H8
    Secondary accession number(s): O81522, Q3ECD2, Q9ASQ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 5, 2002
    Last sequence update: March 5, 2002
    Last modified: November 11, 2015
    This is version 120 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.