ASA1_ORYSI
ID ASA1_ORYSI Reviewed; 577 AA.
AC A2XNK3;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Anthranilate synthase alpha subunit 1, chloroplastic;
DE EC=4.1.3.27;
DE Flags: Precursor;
GN Name=ASA1; ORFNames=OsI_14147;
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
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).
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 (By similarity). {ECO:0000250}.
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 -!- ACTIVITY REGULATION: Feedback inhibition by tryptophan. {ECO:0000250}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5.
CC -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: a
CC beta subunit and a large alpha subunit. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC {ECO:0000305}.
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DR EMBL; CM000128; EAY92413.1; -; Genomic_DNA.
DR AlphaFoldDB; A2XNK3; -.
DR SMR; A2XNK3; -.
DR STRING; 39946.A2XNK3; -.
DR PRIDE; A2XNK3; -.
DR EnsemblPlants; BGIOSGA009526-TA; BGIOSGA009526-PA; BGIOSGA009526.
DR Gramene; BGIOSGA009526-TA; BGIOSGA009526-PA; BGIOSGA009526.
DR HOGENOM; CLU_006493_9_3_1; -.
DR OMA; HGRMDTS; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000007015; Chromosome 3.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway.
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 3: Inferred from homology;
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_0000425663"
SQ SEQUENCE 577 AA; 63938 MW; DAED13890844EB18 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 LLSDEKQCAE HIMLVDLGRN DVGKVSKPGS
VKVEKLMNVE RYSHVMHISS TVTGELRDDL TCWDALRAAL PVGTVSGAPK VRAMELIDQM
EGKMRGPYSG GFGGVSFRGD MDIALALRTI VFPTGSRFDT MYSYTDKNAR QEWVAHLQAG
AGIVADSKPD DEHQECLNKA AGLARAIDLA ESTFVDE
