ICS_CATRO
ID ICS_CATRO Reviewed; 580 AA.
AC Q9ZPC0;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Isochorismate synthase, chloroplastic;
DE EC=5.4.4.2;
DE Flags: Precursor;
OS Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC Catharanthinae; Catharanthus.
OX NCBI_TaxID=4058;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 108-126; 191-204; 221-232;
RP 309-317 AND 509-530, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RC STRAIN=cv. G. Don;
RX PubMed=9952467; DOI=10.1104/pp.119.2.705;
RA van Tegelen L.J.P., Moreno P.R.H., Croes A.F., Verpoorte R., Wullems G.J.;
RT "Purification and cDNA cloning of isochorismate synthase from elicited cell
RT cultures of Catharanthus roseus.";
RL Plant Physiol. 119:705-712(1999).
RN [2]
RP FUNCTION, AND INDUCTION BY ELICITOR.
RX PubMed=24192892; DOI=10.1007/bf00233788;
RA Moreno P.R., van der Heijden R., Verpoorte R.;
RT "Elicitor-mediated induction of isochorismate synthase and accumulation of
RT 2,3-dihydroxy benzoic acid in Catharanthus roseus cell suspension and shoot
RT cultures.";
RL Plant Cell Rep. 14:188-191(1994).
RN [3]
RP FUNCTION.
RX PubMed=19251288; DOI=10.1016/j.phytochem.2009.01.009;
RA Mustafa N.R., Kim H.K., Choi Y.H., Erkelens C., Lefeber A.W., Spijksma G.,
RA van der Heijden R., Verpoorte R.;
RT "Biosynthesis of salicylic acid in fungus elicited Catharanthus roseus
RT cells.";
RL Phytochemistry 70:532-539(2009).
CC -!- FUNCTION: Involved in the synthesis of o-succinylbenzoic acid, 2,3-
CC dihydroxybenzoic acid and salicylic acid (SA).
CC {ECO:0000269|PubMed:19251288, ECO:0000269|PubMed:24192892,
CC ECO:0000269|PubMed:9952467}.
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:9952467};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9952467};
CC -!- ACTIVITY REGULATION: Not inhibited by Tyr, Phe or Trp.
CC {ECO:0000269|PubMed:9952467}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=319 uM for chorismate {ECO:0000269|PubMed:9952467};
CC KM=1.63 mM for Mg(2+) (in the presence of 2 mM chorismate)
CC {ECO:0000269|PubMed:9952467};
CC pH dependence:
CC Optimum pH is 7.0-9.0. {ECO:0000269|PubMed:9952467};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- INDUCTION: Up-regulated by fungal elicitor.
CC {ECO:0000269|PubMed:24192892}.
CC -!- MISCELLANEOUS: Two isoforms can be purified from cell cultures, but
CC they are probably encoded by a single gene and may arise by post-
CC transcriptional modifications. {ECO:0000305|PubMed:9952467}.
CC -!- SIMILARITY: Belongs to the isochorismate synthase family.
CC {ECO:0000305}.
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DR EMBL; AJ006065; CAA06837.1; -; mRNA.
DR AlphaFoldDB; Q9ZPC0; -.
DR SMR; Q9ZPC0; -.
DR KEGG; ag:CAA06837; -.
DR SABIO-RK; Q9ZPC0; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0008909; F:isochorismate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
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 Chloroplast; Direct protein sequencing; Isomerase; Magnesium;
KW Plant defense; Plastid; Transit peptide.
FT TRANSIT 1..91
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 92..580
FT /note="Isochorismate synthase, chloroplastic"
FT /id="PRO_0000035792"
SQ SEQUENCE 580 AA; 64073 MW; 83F9633B4067312D CRC64;
MASITGHCVA HFTDLSTRKS SFFSNSNNNS SLFRRKSTNI VTRKKYIFCS TSLSMNGCNG
DPRAPVGTIE TRTLPAVSTP ALAMERLSSA VANLKSTLPS AQSGIIRLEV PIEEHIEALD
WLHSQDQKNL LPRCYFSGRS QVTFSDFTSN DLTNRNGSAA NGHLQRISTS SDDKNLVSVA
GVGSAVLFRS PNPFSFDDWL SIKRFLSKNC PLIRAYGAIR FDARPHIAPE WKAFGSFYFV
VPQVEFDELH GSSMIAATVA WDNALSLTYQ QAIVALQTTM EQVSSTVSKL RQDVSHTSLV
SKANIPDRTS WDLTLNRVLE EIGNKYSPLT KVVLARRSQV ITTSDIDPLA WLSSFKADGK
DAYQFCLQPH EAPAFIGNTP EQLFGRDQLT VFSEALAATR ARGESDSLDL QMAHDLFSSP
KDNHEFAIVR ENIRQKLDAI CTSVETEPMK SVRKLKRIQH LYARFAGRLR SEDDEFKILS
SLHPTPAVCG FPMEDARKFI AENEMFDRGL YAGPVGFFGG AQSDFSVGIR SALIGKDAGA
LIYAGLGVVE GSDPALEWQE LELKASQFMK LMKLEAPALK