ASA1_ORYSJ
ID ASA1_ORYSJ Reviewed; 577 AA.
AC Q94GF1; A0A0P0W4Y1; Q10B97; Q9XJ30;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Anthranilate synthase alpha subunit 1, chloroplastic {ECO:0000303|PubMed:11500548};
DE Short=OsASA1 {ECO:0000303|PubMed:11500548};
DE EC=4.1.3.27 {ECO:0000269|PubMed:15159631};
DE Flags: Precursor;
GN Name=ASA1 {ECO:0000303|PubMed:11500548};
GN Synonyms=OASA1 {ECO:0000303|PubMed:11500548};
GN OrderedLocusNames=Os03g0826500, LOC_Os03g61120;
GN ORFNames=OJ1111_B11.9 {ECO:0000312|EMBL:AAK82452.1},
GN OsJ_13197 {ECO:0000312|EMBL:EAZ29134.1},
GN OSJNBa0010E04.11 {ECO:0000312|EMBL:AAL79757.1};
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], FUNCTION, ACTIVITY REGULATION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF ASP-323.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [7]
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).
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:11500548,
CC 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.
CC {ECO:0000269|PubMed:11500548}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=121 uM for chorismate (for recombinant ASA1 and ASB1 proteins
CC synthesized with the wheat germ cell-free system)
CC {ECO:0000269|PubMed:15159631};
CC Vmax=566 nmol/min/mg enzyme toward chorismate (for recombinant ASA1
CC and ASB1 proteins synthesized with the wheat germ cell-free system)
CC {ECO:0000269|PubMed:15159631};
CC Note=kcat is 34.7 sec(-1) with chorismate as substrate (for
CC recombinant ASA1 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 -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants are insensitive to feedback inhibition by
CC tryptophan. {ECO:0000269|PubMed:11500548}.
CC -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC {ECO:0000305}.
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DR EMBL; AB022602; BAA82094.1; -; mRNA.
DR EMBL; AC091247; AAK82452.1; -; Genomic_DNA.
DR EMBL; AC096687; AAL79757.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF99646.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF13678.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS87160.1; -; Genomic_DNA.
DR EMBL; CM000140; EAZ29134.1; -; Genomic_DNA.
DR RefSeq; XP_015628119.1; XM_015772633.1.
DR AlphaFoldDB; Q94GF1; -.
DR SMR; Q94GF1; -.
DR STRING; 4530.OS03T0826500-01; -.
DR PaxDb; Q94GF1; -.
DR PRIDE; Q94GF1; -.
DR EnsemblPlants; Os03t0826500-01; Os03t0826500-01; Os03g0826500.
DR GeneID; 4334640; -.
DR Gramene; Os03t0826500-01; Os03t0826500-01; Os03g0826500.
DR KEGG; osa:4334640; -.
DR eggNOG; KOG1223; Eukaryota.
DR HOGENOM; CLU_006493_9_3_1; -.
DR InParanoid; Q94GF1; -.
DR OMA; HGRMDTS; -.
DR OrthoDB; 1092460at2759; -.
DR PlantReactome; R-OSA-1119494; Tryptophan biosynthesis.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000007752; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR Genevisible; Q94GF1; 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; IMP: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..34
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 35..577
FT /note="Anthranilate synthase alpha subunit 1,
FT chloroplastic"
FT /id="PRO_0000425662"
FT MUTAGEN 323
FT /note="D->N: Insensitive to feedback inhibition by
FT tryptophan."
FT /evidence="ECO:0000269|PubMed:11500548"
FT CONFLICT 12
FT /note="P -> R (in Ref. 1; BAA82094)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="D -> H (in Ref. 1; BAA82094)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 577 AA; 63866 MW; 2B8E72EB0846EA95 CRC64;
MASLVLSLRI APSTPPLGLG GGRFRGRRGA VACRAATFQQ LDAVAVREEE SKFKAGAAEG
CNILPLKRCI FSDHLTPVLA YRCLVREDDR EAPSFLFESV EQGSEGTNVG RYSVVGAQPA
MEIVAKANHV TVMDHKMKSR REQFAPDPMK IPRSIMEQWN PQIVEGLPDA FCGGWVGFFS
YDTVRYVETK KLPFSNAPED DRNLPDIHLG LYNDIVVFDH VEKKTHVIHW VRVDCHESVD
EAYEDGKNQL EALLSRLHSV NVPTLTAGSV KLNVGQFGSA LQKSSMSRED YKKAVVQAKE
HILAGDIFQV VLSQRFERRT FADPFEVYRA LRIVNPSPYM AYLQARGCIL VASSPEILTR
VEKRTIVNRP LAGTIRRGKS KAEDKVLEQL LLSDGKQCAE HIMLVDLGRN DVGKVSKPGS
VKVEKLMNVE RYSHVMHISS TVTGELRDDL TCWDALRAAL PVGTVSGAPK VRAMELIDQM
EGKMRGPYSG GFGGVSFRGD MDIALALRTI VFPTGSRFDT MYSYTDKNAR QEWVAHLQAG
AGIVADSKPD DEHQECLNKA AGLARAIDLA ESTFVDE
