PAI1_ARATH
ID PAI1_ARATH Reviewed; 275 AA.
AC Q42440; Q3EDG7; Q7G9J9;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase 1, chloroplastic;
DE EC=5.3.1.24 {ECO:0000305|PubMed:7773017};
DE Flags: Precursor;
GN Name=PAI1; Synonyms=TRP6; OrderedLocusNames=At1g07780; ORFNames=F24B9.11;
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 [GENOMIC DNA].
RC STRAIN=cv. Wassilewskija;
RX PubMed=8521489; DOI=10.1016/0092-8674(95)90185-x;
RA Bender J., Fink G.R.;
RT "Epigenetic control of an endogenous gene family is revealed by a novel
RT blue fluorescent mutant of Arabidopsis.";
RL Cell 83:725-734(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=7773017; DOI=10.2307/3870082;
RA Li J., Zhao J., Rose A.B., Schmidt R., Last R.L.;
RT "Arabidopsis phosphoribosylanthranilate isomerase: molecular genetic
RT analysis of triplicate tryptophan pathway genes.";
RL Plant Cell 7:447-461(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10471722; DOI=10.1093/genetics/153.1.401;
RA Melquist S., Luff B., Bender J.;
RT "Arabidopsis PAI gene arrangements, cytosine methylation and expression.";
RL Genetics 153:401-413(1999).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [7]
RP TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=11346937; DOI=10.1007/s004250000452;
RA He Y., Li J.;
RT "Differential expression of triplicate phosphoribosylanthranilate isomerase
RT isogenes in the tryptophan biosynthetic pathway of Arabidopsis thaliana
RT (L.) Heynh.";
RL Planta 212:641-647(2001).
CC -!- FUNCTION: Catalyzes the conversion of 5-phosphoribosylanthranilate to
CC l-(O-carboxyphenylamino)-l-deoxyribulose-5-phosphate, which is the
CC third step of the tryptophan biosynthetic pathway.
CC {ECO:0000305|PubMed:7773017}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-
CC carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate;
CC Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613;
CC EC=5.3.1.24; Evidence={ECO:0000305|PubMed:7773017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21541;
CC Evidence={ECO:0000305|PubMed:7773017};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 3/5. {ECO:0000305|PubMed:7773017}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
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=Q42440-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots and shoots.
CC {ECO:0000269|PubMed:11346937}.
CC -!- INDUCTION: By silver nitrate and UV irradiation.
CC {ECO:0000269|PubMed:11346937}.
CC -!- DISRUPTION PHENOTYPE: Bushy morphology, reduced fertility, blue
CC fluorescence under UV light and resistance to the anthranilate analog
CC 6-methylanthranilate. {ECO:0000269|PubMed:11346937,
CC ECO:0000269|PubMed:7773017}.
CC -!- SIMILARITY: Belongs to the TrpF family. {ECO:0000305}.
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DR EMBL; U34756; AAB03498.1; -; Genomic_DNA.
DR EMBL; U18970; AAC49005.1; -; Genomic_DNA.
DR EMBL; AF130878; AAD38141.1; -; Genomic_DNA.
DR EMBL; AC007583; AAF75075.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28179.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28180.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28181.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28183.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60071.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60072.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60074.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM60075.1; -; Genomic_DNA.
DR EMBL; AY081274; AAL91163.1; -; mRNA.
DR EMBL; BT003351; AAO29969.1; -; mRNA.
DR PIR; C86213; C86213.
DR RefSeq; NP_001184931.1; NM_001198002.2. [Q42440-1]
DR RefSeq; NP_001322383.1; NM_001331736.1. [Q42440-1]
DR RefSeq; NP_001322384.1; NM_001331729.1. [Q42440-1]
DR RefSeq; NP_001322386.1; NM_001331731.1. [Q42440-1]
DR RefSeq; NP_001322387.1; NM_001331732.1. [Q42440-1]
DR RefSeq; NP_172257.1; NM_100652.5. [Q42440-1]
DR RefSeq; NP_849606.1; NM_179275.4. [Q42440-1]
DR RefSeq; NP_973784.2; NM_202055.4. [Q42440-1]
DR AlphaFoldDB; Q42440; -.
DR SMR; Q42440; -.
DR BioGRID; 22533; 1.
DR STRING; 3702.AT1G07780.3; -.
DR PaxDb; Q42440; -.
DR PRIDE; Q42440; -.
DR ProteomicsDB; 248652; -. [Q42440-1]
DR EnsemblPlants; AT1G07780.1; AT1G07780.1; AT1G07780. [Q42440-1]
DR EnsemblPlants; AT1G07780.10; AT1G07780.10; AT1G07780. [Q42440-1]
DR EnsemblPlants; AT1G07780.12; AT1G07780.12; AT1G07780. [Q42440-1]
DR EnsemblPlants; AT1G07780.13; AT1G07780.13; AT1G07780. [Q42440-1]
DR EnsemblPlants; AT1G07780.2; AT1G07780.2; AT1G07780. [Q42440-1]
DR EnsemblPlants; AT1G07780.3; AT1G07780.3; AT1G07780. [Q42440-1]
DR EnsemblPlants; AT1G07780.5; AT1G07780.5; AT1G07780. [Q42440-1]
DR EnsemblPlants; AT1G07780.9; AT1G07780.9; AT1G07780. [Q42440-1]
DR GeneID; 837292; -.
DR Gramene; AT1G07780.1; AT1G07780.1; AT1G07780. [Q42440-1]
DR Gramene; AT1G07780.10; AT1G07780.10; AT1G07780. [Q42440-1]
DR Gramene; AT1G07780.12; AT1G07780.12; AT1G07780. [Q42440-1]
DR Gramene; AT1G07780.13; AT1G07780.13; AT1G07780. [Q42440-1]
DR Gramene; AT1G07780.2; AT1G07780.2; AT1G07780. [Q42440-1]
DR Gramene; AT1G07780.3; AT1G07780.3; AT1G07780. [Q42440-1]
DR Gramene; AT1G07780.5; AT1G07780.5; AT1G07780. [Q42440-1]
DR Gramene; AT1G07780.9; AT1G07780.9; AT1G07780. [Q42440-1]
DR KEGG; ath:AT1G07780; -.
DR Araport; AT1G07780; -.
DR TAIR; locus:2026509; AT1G07780.
DR eggNOG; KOG4202; Eukaryota.
DR HOGENOM; CLU_076364_0_0_1; -.
DR OMA; FYAKSPR; -.
DR PhylomeDB; Q42440; -.
DR BioCyc; ARA:AT1G07780-MON; -.
DR UniPathway; UPA00035; UER00042.
DR PRO; PR:Q42440; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q42440; baseline and differential.
DR Genevisible; Q42440; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IMP:TAIR.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IMP:TAIR.
DR CDD; cd00405; PRAI; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00135; PRAI; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001240; PRAI_dom.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR InterPro; IPR044643; TrpF_fam.
DR PANTHER; PTHR42894; PTHR42894; 1.
DR Pfam; PF00697; PRAI; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Amino-acid biosynthesis;
KW Aromatic amino acid biosynthesis; Chloroplast; Isomerase; Plastid;
KW Reference proteome; Transit peptide; Tryptophan biosynthesis.
FT TRANSIT 1..32
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 33..275
FT /note="N-(5'-phosphoribosyl)anthranilate isomerase 1,
FT chloroplastic"
FT /id="PRO_0000417453"
SQ SEQUENCE 275 AA; 29633 MW; 5F4417E94255F2C6 CRC64;
MSTGISTDLH VHFGALNFSK TYKSGLSNRT VSFSRVGYAQ NRKLSCSVSN TENVAPKDDE
RGKDRPLVKM CGITSARDAA MAVEAGADFI GMIIWPHSKR SISLSVAKDI SKVAREGGAK
PVGVFVEDDE NTILRAADSS DLELVQLHGN GSRAAFSRLV RKRRVIYVLN ANQDGKLLNE
VPEEDCHLAD WILVDSATGG SGHGFNWAQF KLPSVRSRNG WLLAGGINPT NVSEALSILQ
PDGIDVSSGI CGTDGIQKDK SKISSFITAV RSVHY
