TRPC_ARATH
ID TRPC_ARATH Reviewed; 402 AA.
AC P49572; Q1EBW5; Q8GYM9; Q8LBV5; Q9SJC9;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Indole-3-glycerol phosphate synthase, chloroplastic {ECO:0000303|PubMed:7610197};
DE Short=IGPS {ECO:0000303|PubMed:7610197};
DE EC=4.1.1.48 {ECO:0000269|PubMed:7610197};
DE Flags: Precursor;
GN Name=IGPS {ECO:0000303|PubMed:7610197};
GN OrderedLocusNames=At2g04400 {ECO:0000312|Araport:AT2G04400};
GN ORFNames=T1O3.19 {ECO:0000312|EMBL:AAD25838.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-402, FUNCTION, CATALYTIC ACTIVITY, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=7610197; DOI=10.1104/pp.108.2.877;
RA Li J., Chen S., Zhu L., Last R.L.;
RT "Isolation of cDNAs encoding the tryptophan pathway enzyme indole-3-
RT glycerol phosphate synthase from Arabidopsis thaliana.";
RL Plant Physiol. 108:877-878(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 89-402.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
CC -!- FUNCTION: Indole-3-glycerol phosphate synthase required for tryptophan
CC biosynthesis. {ECO:0000269|PubMed:7610197}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+)
CC = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O;
CC Xref=Rhea:RHEA:23476, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:58613, ChEBI:CHEBI:58866; EC=4.1.1.48;
CC Evidence={ECO:0000269|PubMed:7610197};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 4/5.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000305|PubMed:7610197}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves. {ECO:0000269|PubMed:7610197}.
CC -!- SIMILARITY: Belongs to the TrpC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA60380.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC42166.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC006951; AAD25838.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05831.1; -; Genomic_DNA.
DR EMBL; AY086973; AAM64536.1; -; mRNA.
DR EMBL; BT025969; ABG25058.1; -; mRNA.
DR EMBL; U18770; AAA60380.1; ALT_INIT; mRNA.
DR EMBL; AK117503; BAC42166.1; ALT_INIT; mRNA.
DR PIR; B84457; B84457.
DR RefSeq; NP_178521.1; NM_126473.4.
DR AlphaFoldDB; P49572; -.
DR SMR; P49572; -.
DR IntAct; P49572; 1.
DR STRING; 3702.AT2G04400.1; -.
DR MetOSite; P49572; -.
DR PaxDb; P49572; -.
DR PRIDE; P49572; -.
DR ProteomicsDB; 232416; -.
DR EnsemblPlants; AT2G04400.1; AT2G04400.1; AT2G04400.
DR GeneID; 814980; -.
DR Gramene; AT2G04400.1; AT2G04400.1; AT2G04400.
DR KEGG; ath:AT2G04400; -.
DR Araport; AT2G04400; -.
DR TAIR; locus:2058294; AT2G04400.
DR eggNOG; KOG4201; Eukaryota.
DR HOGENOM; CLU_034247_1_0_1; -.
DR InParanoid; P49572; -.
DR OMA; EWEVEMY; -.
DR OrthoDB; 1404210at2759; -.
DR PhylomeDB; P49572; -.
DR BioCyc; ARA:AT2G04400-MON; -.
DR UniPathway; UPA00035; UER00043.
DR PRO; PR:P49572; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P49572; baseline and differential.
DR Genevisible; P49572; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IBA:GO_Central.
DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IBA:GO_Central.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
DR CDD; cd00331; IGPS; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00134_B; IGPS_B; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR045186; Indole-3-glycerol_P_synth.
DR InterPro; IPR013798; Indole-3-glycerol_P_synth_dom.
DR InterPro; IPR001468; Indole-3-GlycerolPSynthase_CS.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR22854; PTHR22854; 1.
DR Pfam; PF00218; IGPS; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR PROSITE; PS00614; IGPS; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Chloroplast;
KW Decarboxylase; Lyase; Plastid; Reference proteome; Transit peptide;
KW Tryptophan biosynthesis.
FT TRANSIT 1..65
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 66..402
FT /note="Indole-3-glycerol phosphate synthase, chloroplastic"
FT /id="PRO_0000035787"
FT CONFLICT 177
FT /note="T -> P (in Ref. 5; AAA60380)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="F -> Y (in Ref. 3; AAM64536)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="A -> T (in Ref. 3; AAM64536)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="L -> LAL (in Ref. 5; AAA60380)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 402 AA; 44577 MW; 288B4925BAD9E0DC CRC64;
MEGLVPVQRL PIKVASPSLY RCNNSVSIRR SISGFAMDRK INFRAPSQFS IRAQQSDLKE
SLAVSSSSVE DKGNVLRIKE WEVEMYQEEL AISQGIRIRR KPPSKAPLGY SGPFELRLHN
NDADSPRNIL EEITWYKDVE VSRMKELNPL DVLKKAVEDA PPTRDFVGAL RMAHKRTGFP
GLIAEVKKAS PSRGILKENF DPVEIAQAYE KGGAACLSVL TDQKYFQGGF ENLEAIRSAG
VKCPLLCKEF VVDPWQIYYA RTKGADAVLL IAAVLADLEI TFLLKICKKL SLAALVEVHD
EREMGRVLGI EGIELVGINN RSLETFEVDI SNTKKLLEGE HGRQIRERDM IVVGESGLFT
PDDIAYVQAA GVKAVLVGES IVKQNDPEKG IAGLFGRNIS HT
