ASB1_ARATH
ID ASB1_ARATH Reviewed; 276 AA.
AC Q42565;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 156.
DE RecName: Full=Anthranilate synthase beta subunit 1, chloroplastic;
DE EC=4.1.3.27;
DE AltName: Full=Anthranilate synthase component 2-1;
DE AltName: Full=Anthranilate synthase, glutamine amidotransferase component 2-1;
DE AltName: Full=Protein TRYPTOPHAN BIOSYNTHESIS 4;
DE AltName: Full=Protein WEAK ETHYLENE INSENSITIVE 7;
DE Flags: Precursor;
GN Name=ASB1; Synonyms=TRP4, WEI7; OrderedLocusNames=At1g25220;
GN ORFNames=F4F7.39;
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 [MRNA], INDUCTION, MUTAGENESIS OF GLY-150, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=8400875; DOI=10.2307/3869623;
RA Niyogi K.K., Last R.L., Fink G.R., Keith B.;
RT "Suppressors of trp1 fluorescence identify a new arabidopsis gene, TRP4,
RT encoding the anthranilate synthase beta subunit.";
RL Plant Cell 5:1011-1027(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, INDUCTION BY ETHYLENE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP GLY-176.
RX PubMed=15980261; DOI=10.1105/tpc.105.033365;
RA Stepanova A.N., Hoyt J.M., Hamilton A.A., Alonso J.M.;
RT "A link between ethylene and auxin uncovered by the characterization of two
RT root-specific ethylene-insensitive mutants in Arabidopsis.";
RL Plant Cell 17:2230-2242(2005).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=18435826; DOI=10.1111/j.1365-313x.2008.03528.x;
RA Ivanchenko M.G., Muday G.K., Dubrovsky J.G.;
RT "Ethylene-auxin interactions regulate lateral root initiation and emergence
RT in Arabidopsis thaliana.";
RL Plant J. 55:335-347(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. Plays an important regulatory
CC role in auxin production via the tryptophan-dependent biosynthetic
CC pathway. {ECO:0000269|PubMed:15980261}.
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 -!- 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q42565-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in the central cylinder of mature primary
CC root zones, including pericycle and early lateral root primordia, and
CC vasculature of cotyledons. {ECO:0000269|PubMed:18435826}.
CC -!- INDUCTION: By ethylene and the bacterial pathogen P.syringae.
CC {ECO:0000269|PubMed:15980261, ECO:0000269|PubMed:8400875}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants are insensitive to inhibition of root
CC elongation by ethylene. {ECO:0000269|PubMed:15980261,
CC ECO:0000269|PubMed:8400875}.
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DR EMBL; L22585; AAA32742.1; -; mRNA.
DR EMBL; AC079374; AAG28813.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30589.1; -; Genomic_DNA.
DR EMBL; AY099834; AAM20685.1; -; mRNA.
DR EMBL; BT006303; AAP13411.1; -; mRNA.
DR EMBL; AK226500; BAE98642.1; -; mRNA.
DR PIR; JQ2340; JQ2340.
DR RefSeq; NP_173893.1; NM_102331.3. [Q42565-1]
DR AlphaFoldDB; Q42565; -.
DR SMR; Q42565; -.
DR BioGRID; 24340; 1.
DR IntAct; Q42565; 1.
DR STRING; 3702.AT1G25220.2; -.
DR MEROPS; C26.A09; -.
DR PaxDb; Q42565; -.
DR ProteomicsDB; 246500; -. [Q42565-1]
DR EnsemblPlants; AT1G25220.1; AT1G25220.1; AT1G25220. [Q42565-1]
DR GeneID; 839103; -.
DR Gramene; AT1G25220.1; AT1G25220.1; AT1G25220. [Q42565-1]
DR KEGG; ath:AT1G25220; -.
DR Araport; AT1G25220; -.
DR eggNOG; KOG0026; Eukaryota.
DR HOGENOM; CLU_014340_1_3_1; -.
DR OMA; HQVVIYR; -.
DR PhylomeDB; Q42565; -.
DR SABIO-RK; Q42565; -.
DR UniPathway; UPA00035; UER00040.
DR PRO; PR:Q42565; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q42565; baseline and differential.
DR Genevisible; Q42565; 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:0010600; P:regulation of auxin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IMP: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 Alternative splicing; Amino-acid biosynthesis;
KW Aromatic amino acid biosynthesis; Chloroplast; Glutamine amidotransferase;
KW Lyase; Plastid; Reference proteome; Transit peptide;
KW Tryptophan biosynthesis.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 51..276
FT /note="Anthranilate synthase beta subunit 1, chloroplastic"
FT /id="PRO_0000425665"
FT DOMAIN 74..273
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 152
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 247
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT ACT_SITE 249
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT MUTAGEN 150
FT /note="G->D: In trp4-1; no visible phenotype under normal
FT growth conditions."
FT /evidence="ECO:0000269|PubMed:8400875"
FT MUTAGEN 176
FT /note="G->E: In wei7-2; insensitive to inhibition of root
FT elongation by ethylene."
FT /evidence="ECO:0000269|PubMed:15980261"
SQ SEQUENCE 276 AA; 30460 MW; D79AE704B2704A78 CRC64;
MAASTLYKSC LLQPKSGSTT RRLNPSLVNP LTNPTRVSVL GKSRRDVFAK ASIEMAESNS
IPSVVVNSSK QHGPIIVIDN YDSFTYNLCQ YMGELGCHFE VYRNDELTVE ELKKKNPRGV
LISPGPGTPQ DSGISLQTVL ELGPLVPLFG VCMGLQCIGE AFGGKIVRSP FGVMHGKSSM
VHYDEKGEEG LFSGLSNPFI VGRYHSLVIE KDTFPSDELE VTAWTEDGLV MAARHRKYKH
IQGVQFHPES IITTEGKTIV RNFIKIVEKK ESEKLT
