TRPD_ARATH
ID TRPD_ARATH Reviewed; 444 AA.
AC Q02166; Q42557;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Anthranilate phosphoribosyltransferase, chloroplastic;
DE EC=2.4.2.18;
DE Flags: Precursor;
GN Name=PAT1; OrderedLocusNames=At5g17990; ORFNames=MCM23.6;
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.
RC STRAIN=cv. Columbia;
RX PubMed=16653032; DOI=10.1104/pp.100.2.582;
RA Rose A.B., Casselman A.L., Last R.L.;
RT "A phosphoribosylanthranilate transferase gene is defective in blue
RT fluorescent Arabidopsis thaliana tryptophan mutants.";
RL Plant Physiol. 100:582-592(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Landsberg erecta;
RA Rose A.B., Li J., Last R.L.;
RT "Blue fluorescent trp1 mutants of Arabidopsis thaliana form a discontinuous
RT allelic series.";
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
RN [4]
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 [5]
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).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphosphate + N-(5-phospho-beta-D-ribosyl)anthranilate = 5-
CC phospho-alpha-D-ribose 1-diphosphate + anthranilate;
CC Xref=Rhea:RHEA:11768, ChEBI:CHEBI:16567, ChEBI:CHEBI:18277,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58017; EC=2.4.2.18;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P9WFX5};
CC Note=Binds 2 magnesium ions per monomer.
CC {ECO:0000250|UniProtKB:P9WFX5};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 2/5.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the anthranilate phosphoribosyltransferase
CC family. {ECO:0000305}.
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DR EMBL; M96073; AAA32835.1; -; Genomic_DNA.
DR EMBL; U58942; AAB02913.1; -; Genomic_DNA.
DR EMBL; AB015473; BAB08398.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92493.1; -; Genomic_DNA.
DR EMBL; AY054506; AAK96697.1; -; mRNA.
DR EMBL; AY093298; AAM13297.1; -; mRNA.
DR RefSeq; NP_197300.1; NM_121804.5.
DR AlphaFoldDB; Q02166; -.
DR SMR; Q02166; -.
DR BioGRID; 16942; 6.
DR IntAct; Q02166; 1.
DR STRING; 3702.AT5G17990.1; -.
DR PaxDb; Q02166; -.
DR PRIDE; Q02166; -.
DR ProteomicsDB; 232390; -.
DR EnsemblPlants; AT5G17990.1; AT5G17990.1; AT5G17990.
DR GeneID; 831666; -.
DR Gramene; AT5G17990.1; AT5G17990.1; AT5G17990.
DR KEGG; ath:AT5G17990; -.
DR Araport; AT5G17990; -.
DR TAIR; locus:2161528; AT5G17990.
DR eggNOG; KOG1438; Eukaryota.
DR HOGENOM; CLU_034315_4_0_1; -.
DR OMA; GPMTNPA; -.
DR OrthoDB; 1053815at2759; -.
DR PhylomeDB; Q02166; -.
DR BioCyc; ARA:AT5G17990-MON; -.
DR UniPathway; UPA00035; UER00041.
DR PRO; PR:Q02166; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q02166; baseline and differential.
DR Genevisible; Q02166; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0004048; F:anthranilate phosphoribosyltransferase activity; TAS:TAIR.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IMP:TAIR.
DR Gene3D; 3.40.1030.10; -; 1.
DR HAMAP; MF_00211; TrpD; 1.
DR InterPro; IPR005940; Anthranilate_Pribosyl_Tfrase.
DR InterPro; IPR000312; Glycosyl_Trfase_fam3.
DR InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom.
DR InterPro; IPR036320; Glycosyl_Trfase_fam3_N_dom_sf.
DR InterPro; IPR035902; Nuc_phospho_transferase.
DR PANTHER; PTHR43285; PTHR43285; 1.
DR Pfam; PF02885; Glycos_trans_3N; 1.
DR Pfam; PF00591; Glycos_transf_3; 1.
DR SUPFAM; SSF47648; SSF47648; 1.
DR SUPFAM; SSF52418; SSF52418; 1.
DR TIGRFAMs; TIGR01245; trpD; 1.
PE 2: Evidence at transcript level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Chloroplast;
KW Glycosyltransferase; Magnesium; Metal-binding; Plastid; Reference proteome;
KW Transferase; Transit peptide; Tryptophan biosynthesis.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..444
FT /note="Anthranilate phosphoribosyltransferase,
FT chloroplastic"
FT /id="PRO_0000035788"
FT BINDING 184
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250|UniProtKB:P9WFX5"
FT BINDING 184
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WFX5"
FT BINDING 187..188
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250|UniProtKB:P9WFX5"
FT BINDING 192
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250|UniProtKB:P9WFX5"
FT BINDING 194..197
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250|UniProtKB:P9WFX5"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WFX5"
FT BINDING 212..220
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250|UniProtKB:P9WFX5"
FT BINDING 215
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WFX5"
FT BINDING 224
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250|UniProtKB:P9WFX5"
FT BINDING 270
FT /ligand="anthranilate"
FT /ligand_id="ChEBI:CHEBI:16567"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WFX5"
FT BINDING 328
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WFX5"
FT BINDING 329
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WFX5"
FT BINDING 329
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P9WFX5"
FT CONFLICT 39..41
FT /note="Missing (in Ref. 2; AAB02913)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="D -> H (in Ref. 2; AAB02913)"
FT /evidence="ECO:0000305"
FT CONFLICT 76..78
FT /note="ACS -> VCP (in Ref. 2; AAB02913)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="A -> T (in Ref. 2; AAB02913)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="A -> E (in Ref. 2; AAB02913)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="T -> S (in Ref. 2; AAB02913)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="V -> A (in Ref. 2; AAB02913)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 444 AA; 46520 MW; 397DFD3141BED2C0 CRC64;
MVIAVATTSS IVSGIKLSGI LTSFNAVDDA SSSCGRSNLT GVRIFPTLSR RRFSSIGAVS
PIRGDAQSSF SRSSFACSQN LGLSGGFSAA EALPPACANA SPSSIKSFNQ LIETLIDRVD
LSETEAESSL EFLLNEANEA LISAFLVLLR AKGETYEEIV GLARAMMKHA RKVEGLVDAV
DIVGTGGDGA NTVNISTGSS ILAAACGAKV AKQGNRSSSS ACGSADVLEA LGVVLDLGPE
GIKRCVEEGG IGFMMSPMYH PAMKIVGPVR KKLKIKTVFN ILGPMLNPAR VSYAVVGVYH
KDLVVKMAKA LQRFGMKRAL VVHSCGLDEM SPLGGGLVYD VTPEKIEEFS FDPLDFGIPR
CTLEDLRGGG PDYNADVLRR VLSGESGAIA DSLILNAAAA LLVSNRVQTL AEGVTVAREV
QSSGKAIKTL DSWINISNLA QKSQ
