ASB2_ARATH
ID ASB2_ARATH Reviewed; 273 AA.
AC Q9FJM5; Q8L9I8;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Anthranilate synthase beta subunit 2, chloroplastic;
DE EC=4.1.3.27;
DE AltName: Full=Anthranilate synthase component 2-2;
DE AltName: Full=Anthranilate synthase, glutamine amidotransferase component 2-2;
DE Flags: Precursor;
GN Name=ASB2; OrderedLocusNames=At5g57890;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; AB013396; BAB08859.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96968.1; -; Genomic_DNA.
DR EMBL; BT024903; ABD91494.1; -; mRNA.
DR EMBL; AY088407; AAM65944.1; -; mRNA.
DR RefSeq; NP_200597.1; NM_125174.2.
DR AlphaFoldDB; Q9FJM5; -.
DR SMR; Q9FJM5; -.
DR BioGRID; 21144; 1.
DR STRING; 3702.AT5G57890.1; -.
DR MEROPS; C26.A09; -.
DR PaxDb; Q9FJM5; -.
DR PRIDE; Q9FJM5; -.
DR ProteomicsDB; 246501; -.
DR EnsemblPlants; AT5G57890.1; AT5G57890.1; AT5G57890.
DR GeneID; 835900; -.
DR Gramene; AT5G57890.1; AT5G57890.1; AT5G57890.
DR KEGG; ath:AT5G57890; -.
DR Araport; AT5G57890; -.
DR TAIR; locus:2174378; AT5G57890.
DR eggNOG; KOG0026; Eukaryota.
DR HOGENOM; CLU_014340_1_3_1; -.
DR InParanoid; Q9FJM5; -.
DR OMA; MHGIVDT; -.
DR OrthoDB; 665558at2759; -.
DR PhylomeDB; Q9FJM5; -.
DR BioCyc; ARA:AT5G57890-MON; -.
DR UniPathway; UPA00035; UER00040.
DR PRO; PR:Q9FJM5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FJM5; baseline and differential.
DR Genevisible; Q9FJM5; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
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 2: Evidence at transcript 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..36
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 37..273
FT /note="Anthranilate synthase beta subunit 2, chloroplastic"
FT /id="PRO_0000425666"
FT DOMAIN 71..270
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 149
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 244
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT CONFLICT 30
FT /note="S -> P (in Ref. 4; AAM65944)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 273 AA; 30321 MW; 5EB14AD6992480B1 CRC64;
MAATTLYNSC LLQPKYGFTT RRLNQSLVNS LTNPTRVSVL WKSRRDVIAK ASIEMAESNS
ISSVVVNSSG PIIVIDNYDS FTYNLCQYMG ELGCHFEVYR NDELTVEELK RKKPRGLLIS
PGPGTPQDSG ISLQTVLELG PLVPLFGVCM GLQCIGEAFG GKIVRSPFGV MHGKSSMVHY
DEKGEEGLFS GLSNPFLVGR YHSLVIEKDS FPSDELEVTA WTEDGLVMAA RHRKYKHIQG
VQFHPESIIT TEGKTIVRNF IKLVEKKESE KLA
