ID ASB1_ORYSJ Reviewed; 288 AA.
AC Q7XUS2; A0A0P0WBC9;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 145.
DE RecName: Full=Anthranilate synthase beta subunit 1, chloroplastic {ECO:0000303|PubMed:15159631};
DE Short=OsASB1 {ECO:0000303|PubMed:15159631};
DE EC=4.1.3.27 {ECO:0000269|PubMed:15159631};
DE AltName: Full=Anthranilate synthase, glutamine amidotransferase component 2-1;
DE Flags: Precursor;
GN Name=ASB1 {ECO:0000303|PubMed:15159631};
GN Synonyms=OASB1 {ECO:0000303|PubMed:15159631};
GN OrderedLocusNames=Os04g0463500, LOC_Os04g38950;
GN ORFNames=B1358B12.20 {ECO:0000312|EMBL:CAE76011.1},
GN OSJNBa0060P14.1 {ECO:0000312|EMBL:CAD41042.1};
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,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND TISSUE SPECIFICITY.
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=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
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 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 -!- 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 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 ASA1
CC and ASB1 proteins synthesized with the wheat germ cell-free system)
CC {ECO:0000269|PubMed:15159631};
CC Vmax=75.6 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 34.7 sec(-1) with chorismate as substrate (for
CC recombinant ASA1 and ASB1 proteins synthesized with the wheat germ
CC cell-free system). kcat is 14.6 sec(-1) with chorismate as substrate
CC (for recombinant ASA2 and ASB1 proteins synthesized with the wheat
CC germ cell-free system).;
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:P00905}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and leaves.
CC {ECO:0000269|PubMed:15159631}.
CC -!- INDUCTION: By the phytopathogenic fungus Bipolaris oryzae.
CC {ECO:0000269|PubMed:18266919}.
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DR EMBL; AB116721; BAD11023.1; -; mRNA.
DR EMBL; AL663017; CAD41042.1; -; Genomic_DNA.
DR EMBL; BX842605; CAE76011.1; -; Genomic_DNA.
DR EMBL; AP008210; BAF14925.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS89576.1; -; Genomic_DNA.
DR RefSeq; XP_015636125.1; XM_015780639.1.
DR AlphaFoldDB; Q7XUS2; -.
DR SMR; Q7XUS2; -.
DR STRING; 39947.Q7XUS2; -.
DR MEROPS; C26.A09; -.
DR PaxDb; 39947-Q7XUS2; -.
DR EnsemblPlants; Os04t0463500-01; Os04t0463500-01; Os04g0463500.
DR GeneID; 4336076; -.
DR Gramene; Os04t0463500-01; Os04t0463500-01; Os04g0463500.
DR KEGG; osa:4336076; -.
DR eggNOG; KOG0026; Eukaryota.
DR HOGENOM; CLU_014340_1_3_1; -.
DR InParanoid; Q7XUS2; -.
DR OMA; IGLYHSW; -.
DR OrthoDB; 294181at2759; -.
DR PlantReactome; R-OSA-1119494; Tryptophan biosynthesis.
DR PlantReactome; R-OSA-9631623; Regulation of embryo development.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR Genevisible; Q7XUS2; 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 NCBIfam; TIGR00566; trpG_papA; 1.
DR PANTHER; PTHR43418:SF16; ANTHRANILATE SYNTHASE BETA SUBUNIT 1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43418; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-RELATED; 1.
DR Pfam; PF00117; GATase; 1.
DR PRINTS; PR00097; ANTSNTHASEII.
DR PRINTS; PR00099; CPSGATASE.
DR PRINTS; PR00096; GATASE.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 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..58
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 59..288
FT /note="Anthranilate synthase beta subunit 1, chloroplastic"
FT /id="PRO_0000425667"
FT DOMAIN 83..282
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 161
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 256
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 258
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT BINDING 134..136
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT BINDING 165
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
FT BINDING 215..216
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000250|UniProtKB:P00900"
SQ SEQUENCE 288 AA; 30722 MW; B4400C836A3FD366 CRC64;
MACSHLAAAA AAASPAAARS PAASSAATAS AFARLSATPR VASGGLAVRG QRGVAAVVAA
AAGAAAATPV ADIEERRATE KQPIIVIDNY DSFTYNLCQY MGELGLNFEV YRNDELTIED
VKRKNPRGIL ISPGPGEPQD SGISLQTVLE LGPTIPIFGV CMGLQCIGEA FGGKIIRAPS
GVMHGKSSPV RYDEELGKAL FNGLPNPFTA ARYHSLVIEQ ETFPHDALEA TAWTEDGLIM
AARHKKYRHI QGVQFHPESI ITPEGKRIIL NFVRFIEELE KQRAGEKN
//
