ASB2_ORYSJ
ID ASB2_ORYSJ Reviewed; 273 AA.
AC Q764B9; A0A0P0W2T5;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Anthranilate synthase beta subunit 2, chloroplastic {ECO:0000305};
DE Short=OsASB2 {ECO:0000303|PubMed:15159631};
DE EC=4.1.3.27 {ECO:0000269|PubMed:15159631};
DE AltName: Full=Anthranilate synthase, glutamine amidotransferase component 2-2 {ECO:0000305};
DE Flags: Precursor;
GN Name=ASB2 {ECO:0000305}; Synonyms=OASB2 {ECO:0000303|PubMed:15159631};
GN OrderedLocusNames=Os03g0718000 {ECO:0000312|EMBL:BAS86093.1},
GN LOC_Os03g50880 {ECO:0000312|EMBL:ABF98566.1};
GN ORFNames=OsJ_12361 {ECO:0000312|EMBL:EEE59817.1};
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, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Nipponbare;
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [8]
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 -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 1/5. {ECO:0000305}.
CC -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: a
CC beta subunit and a large alpha subunit. {ECO:0000250|UniProtKB:P00900}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and leaves.
CC {ECO:0000269|PubMed:15159631}.
CC -!- INDUCTION: By chitin oligosaccharide elicitor and the phytopathogenic
CC fungus Bipolaris oryzae. {ECO:0000269|PubMed:15159631,
CC ECO:0000269|PubMed:18266919}.
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DR EMBL; AB116722; BAD11024.1; -; mRNA.
DR EMBL; DP000009; ABF98566.1; -; Genomic_DNA.
DR EMBL; AP008209; BAF12999.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS86093.1; -; Genomic_DNA.
DR EMBL; CM000140; EEE59817.1; -; Genomic_DNA.
DR EMBL; AK105178; BAG97126.1; -; mRNA.
DR RefSeq; XP_015630317.1; XM_015774831.1.
DR AlphaFoldDB; Q764B9; -.
DR SMR; Q764B9; -.
DR STRING; 4530.OS03T0718000-01; -.
DR MEROPS; C26.A09; -.
DR PaxDb; Q764B9; -.
DR PRIDE; Q764B9; -.
DR EnsemblPlants; Os03t0718000-01; Os03t0718000-01; Os03g0718000.
DR GeneID; 4333918; -.
DR Gramene; Os03t0718000-01; Os03t0718000-01; Os03g0718000.
DR KEGG; osa:4333918; -.
DR eggNOG; KOG0026; Eukaryota.
DR HOGENOM; CLU_014340_1_3_1; -.
DR InParanoid; Q764B9; -.
DR OMA; HQVVIYR; -.
DR OrthoDB; 665558at2759; -.
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; Q764B9; 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:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IDA:UniProtKB.
DR CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR006221; TrpG/PapA_dom.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR TIGRFAMs; TIGR00566; trpG_papA; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Chloroplast;
KW Glutamine amidotransferase; Lyase; Plastid; Reference proteome;
KW Transit peptide; Tryptophan biosynthesis.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 48..273
FT /note="Anthranilate synthase beta subunit 2, chloroplastic"
FT /id="PRO_0000425668"
FT DOMAIN 70..269
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT REGION 15..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 148
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 243
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 245
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT BINDING 121..123
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT BINDING 152
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT BINDING 202..203
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
SQ SEQUENCE 273 AA; 29809 MW; BCF77B1A0B5A1A9E CRC64;
MATAARLLPK IQSPASPAVA EARRRRPSSL RLGVTSGPAR TLKQKLVAKS AVSVVEGENA
FDGVKQDTRP IIVIDNYDSF TYNLCQYMGE VGANFEVYRN DDITVEEIKK ISPRGILISP
GPGTPQDSGI SLQTVQDLGP STPLFGVCMG LQCIGEAFGG KVVRSPYGVV HGKGSLVHYE
EKLDGTLFSG LPNPFQAGRY HSLVIEKDSF PHDALEITAW TDDGLIMAAR HRKYKHIQGV
QFHPESIITT EGRLMVKNFI KIIEGYEALN CLP
