ASA2_ORYSJ
ID ASA2_ORYSJ Reviewed; 606 AA.
AC Q9XJ29; A0A0P0VVQ9;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Anthranilate synthase alpha subunit 2, chloroplastic {ECO:0000303|PubMed:11500548};
DE Short=OsASA2 {ECO:0000303|PubMed:11500548};
DE EC=4.1.3.27 {ECO:0000269|PubMed:15159631};
DE Flags: Precursor;
GN Name=ASA2 {ECO:0000303|PubMed:11500548};
GN Synonyms=OASA2 {ECO:0000303|PubMed:11500548};
GN OrderedLocusNames=Os03g0264400, LOC_Os03g15780;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=cv. Nipponbare;
RX PubMed=11500548; DOI=10.1104/pp.126.4.1493;
RA Tozawa Y., Hasegawa H., Terakawa T., Wakasa K.;
RT "Characterization of rice anthranilate synthase alpha-subunit genes OASA1
RT and OASA2. Tryptophan accumulation in transgenic rice expressing a
RT feedback-insensitive mutant of OASA1.";
RL Plant Physiol. 126:1493-1506(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=15159631; DOI=10.1023/b:plan.0000028729.79034.07;
RA Kanno T., Kasai K., Ikejiri-Kanno Y., Wakasa K., Tozawa Y.;
RT "In vitro reconstitution of rice anthranilate synthase: distinct functional
RT properties of the alpha subunits OASA1 and OASA2.";
RL Plant Mol. Biol. 54:11-22(2004).
RN [7]
RP INDUCTION.
RX PubMed=18266919; DOI=10.1111/j.1365-313x.2008.03441.x;
RA Ishihara A., Hashimoto Y., Tanaka C., Dubouzet J.G., Nakao T., Matsuda F.,
RA Nishioka T., Miyagawa H., Wakasa K.;
RT "The tryptophan pathway is involved in the defense responses of rice
RT against pathogenic infection via serotonin production.";
RL Plant J. 54:481-495(2008).
CC -!- FUNCTION: Part of a heterotetrameric complex that catalyzes the two-
CC step biosynthesis of anthranilate, an intermediate in the biosynthesis
CC of L-tryptophan. In the first step, the glutamine-binding beta subunit
CC of anthranilate synthase (AS) provides the glutamine amidotransferase
CC activity which generates ammonia as a substrate that, along with
CC chorismate, is used in the second step, catalyzed by the large alpha
CC subunit of AS to produce anthranilate. {ECO:0000269|PubMed:15159631}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate +
CC pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:58359; EC=4.1.3.27;
CC Evidence={ECO:0000269|PubMed:15159631};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21733;
CC Evidence={ECO:0000269|PubMed:15159631};
CC -!- ACTIVITY REGULATION: Feedback inhibition by tryptophan. {ECO:0000250}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=178 uM for chorismate (for recombinant ASA2 and ASB1 proteins
CC synthesized with the wheat germ cell-free system)
CC {ECO:0000269|PubMed:15159631};
CC Vmax=231 nmol/min/mg enzyme toward chorismate (for recombinant ASA2
CC and ASB1 proteins synthesized with the wheat germ cell-free system)
CC {ECO:0000269|PubMed:15159631};
CC Note=kcat is 14.6 sec(-1) with chorismate as substrate (for
CC recombinant ASA2 and ASB1 proteins synthesized with the wheat germ
CC cell-free system). {ECO:0000269|PubMed:15159631};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5. {ECO:0000269|PubMed:15159631}.
CC -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: a
CC beta subunit and a large alpha subunit. {ECO:0000250|UniProtKB:P00897}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- INDUCTION: By chitin oligosaccharide elicitor and the phytopathogenic
CC fungus Bipolaris oryzae. {ECO:0000269|PubMed:11500548,
CC ECO:0000269|PubMed:18266919}.
CC -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC {ECO:0000305}.
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DR EMBL; AB022603; BAA82095.1; -; mRNA.
DR EMBL; DP000009; ABF95122.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF11555.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS83390.1; -; Genomic_DNA.
DR RefSeq; XP_015631311.1; XM_015775825.1.
DR AlphaFoldDB; Q9XJ29; -.
DR SMR; Q9XJ29; -.
DR STRING; 4530.OS03T0264400-01; -.
DR PaxDb; Q9XJ29; -.
DR PRIDE; Q9XJ29; -.
DR EnsemblPlants; Os03t0264400-01; Os03t0264400-01; Os03g0264400.
DR GeneID; 4332341; -.
DR Gramene; Os03t0264400-01; Os03t0264400-01; Os03g0264400.
DR KEGG; osa:4332341; -.
DR eggNOG; KOG1223; Eukaryota.
DR InParanoid; Q9XJ29; -.
DR OMA; GCVGYLD; -.
DR OrthoDB; 1092460at2759; -.
DR PlantReactome; R-OSA-1119494; Tryptophan biosynthesis.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR ExpressionAtlas; Q9XJ29; baseline and differential.
DR Genevisible; Q9XJ29; OS.
DR GO; GO:0005950; C:anthranilate synthase complex; TAS:UniProtKB.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004049; F:anthranilate synthase activity; IDA:UniProtKB.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.60.120.10; -; 1.
DR InterPro; IPR005801; ADC_synthase.
DR InterPro; IPR019999; Anth_synth_I-like.
DR InterPro; IPR006805; Anth_synth_I_N.
DR InterPro; IPR005256; Anth_synth_I_PabB.
DR InterPro; IPR015890; Chorismate_C.
DR PANTHER; PTHR11236; PTHR11236; 1.
DR Pfam; PF04715; Anth_synt_I_N; 1.
DR Pfam; PF00425; Chorismate_bind; 1.
DR PRINTS; PR00095; ANTSNTHASEI.
DR SUPFAM; SSF56322; SSF56322; 1.
DR TIGRFAMs; TIGR00564; trpE_most; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Chloroplast;
KW Lyase; Plastid; Reference proteome; Transit peptide;
KW Tryptophan biosynthesis.
FT TRANSIT 1..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 50..606
FT /note="Anthranilate synthase alpha subunit 2,
FT chloroplastic"
FT /id="PRO_0000425664"
SQ SEQUENCE 606 AA; 66988 MW; A74AB7CE986F0608 CRC64;
MESIAAATFT PSRLAARPAT PAAAAAPVRA RAAVAAGGRR RTSRRGGVRC SAGKPEASAV
INGSAAARAA EEDRRRFFEA AERGSGKGNL VPMWECIVSD HLTPVLAYRC LVPEDNMETP
SFLFESVEQG PEGTTNVGRY SMVGAHPVME VVAKEHKVTI MDHEKGKVTE QVVDDPMQIP
RSMMEGWHPQ QIDQLPDSFT GGWVGFFSYD TVRYVEKKKL PFSGAPQDDR NLPDVHLGLY
DDVLVFDNVE KKVYVIHWVN LDRHATTEDA FQDGKSRLNL LLSKVHNSNV PKLSPGFVKL
HTRQFGTPLN KSTMTSDEYK NAVMQAKEHI MAGDIFQIVL SQRFERRTYA NPFEVYRALR
IVNPSPYMAY VQARGCVLVA SSPEILTRVR KGKIINRPLA GTVRRGKTEK EDEMQEQQLL
SDEKQCAEHI MLVDLGRNDV GKVSKPGSVK VEKLMNIERY SHVMHISSTV SGELDDHLQS
WDALRAALPV GTVSGAPKVK AMELIDELEV TRRGPYSGGL GGISFDGDML IALALRTIVF
STAPSHNTMY SYKDTERRRE WVAHLQAGAG IVADSSPDDE QRECENKAAA LARAIDLAES
AFVDKE
