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Protein

Anthranilate synthase beta subunit 1, chloroplastic

Gene

ASB1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS to produce anthranilate. Plays an important regulatory role in auxin production via the tryptophan-dependent biosynthetic pathway.1 Publication

Catalytic activityi

Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate.

Pathwayi: L-tryptophan biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-tryptophan from chorismate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Anthranilate synthase beta subunit 2, chloroplastic (ASB2), Anthranilate synthase beta subunit 1, chloroplastic (ASB1), Anthranilate synthase alpha subunit 1, chloroplastic (ASA1), Anthranilate synthase alpha subunit 2, chloroplastic (ASA2)
  2. Anthranilate phosphoribosyltransferase, chloroplastic (PAT1)
  3. N-(5'-phosphoribosyl)anthranilate isomerase 2, chloroplastic (PAI2), N-(5'-phosphoribosyl)anthranilate isomerase 3, chloroplastic (PAI3), N-(5'-phosphoribosyl)anthranilate isomerase 1, chloroplastic (PAI1)
  4. Indole-3-glycerol phosphate synthase, chloroplastic (IGPS)
  5. Tryptophan synthase alpha chain (TRPA1), Tryptophan synthase alpha chain, chloroplastic (TSA1), Tryptophan synthase beta chain 1, chloroplastic (TSB1), Tryptophan synthase beta chain 2, chloroplastic (TSB2)
This subpathway is part of the pathway L-tryptophan biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-tryptophan from chorismate, the pathway L-tryptophan biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei152 – 1521NucleophilePROSITE-ProRule annotation
Active sitei247 – 2471PROSITE-ProRule annotation
Active sitei249 – 2491PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • glutamine metabolic process Source: UniProtKB-KW
  • regulation of auxin biosynthetic process Source: UniProtKB
  • tryptophan biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis, Tryptophan biosynthesis

Enzyme and pathway databases

BioCyciARA:GQT-1090-MONOMER.
SABIO-RKQ42565.
UniPathwayiUPA00035; UER00040.

Protein family/group databases

MEROPSiC26.A09.

Names & Taxonomyi

Protein namesi
Recommended name:
Anthranilate synthase beta subunit 1, chloroplastic (EC:4.1.3.27)
Alternative name(s):
Anthranilate synthase component 2-1
Anthranilate synthase, glutamine amidotransferase component 2-1
Protein TRYPTOPHAN BIOSYNTHESIS 4
Protein WEAK ETHYLENE INSENSITIVE 7
Gene namesi
Name:ASB1
Synonyms:TRP4, WEI7
Ordered Locus Names:At1g25220
ORF Names:F4F7.39
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G25220.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Disruption phenotypei

No visible phenotype under normal growth conditions, but mutant plants are insensitive to inhibition of root elongation by ethylene.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi150 – 1501G → D in trp4-1; no visible phenotype under normal growth conditions. 1 Publication
Mutagenesisi176 – 1761G → E in wei7-2; insensitive to inhibition of root elongation by ethylene. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5050ChloroplastSequence analysisAdd
BLAST
Chaini51 – 276226Anthranilate synthase beta subunit 1, chloroplasticPRO_0000425665Add
BLAST

Proteomic databases

PaxDbiQ42565.
PRIDEiQ42565.

Expressioni

Tissue specificityi

Expressed in the central cylinder of mature primary root zones, including pericycle and early lateral root primordia, and vasculature of cotyledons.1 Publication

Inductioni

By ethylene and the bacterial pathogen P.syringae.2 Publications

Gene expression databases

ExpressionAtlasiQ42565. baseline and differential.
GenevisibleiQ42565. AT.

Interactioni

Subunit structurei

Heterotetramer consisting of two non-identical subunits: a beta subunit and a large alpha subunit.By similarity

Protein-protein interaction databases

BioGridi24340. 1 interaction.
IntActiQ42565. 1 interaction.
STRINGi3702.AT1G25220.2.

Structurei

3D structure databases

ProteinModelPortaliQ42565.
SMRiQ42565. Positions 76-267.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini74 – 273200Glutamine amidotransferase type-1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 glutamine amidotransferase type-1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Glutamine amidotransferase, Transit peptide

Phylogenomic databases

eggNOGiKOG0026. Eukaryota.
COG0512. LUCA.
HOGENOMiHOG000025029.
KOiK01658.
PhylomeDBiQ42565.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR006221. TrpG/PapA_dom.
[Graphical view]
PfamiPF00117. GATase. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR00566. trpG_papA. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q42565-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAASTLYKSC LLQPKSGSTT RRLNPSLVNP LTNPTRVSVL GKSRRDVFAK
60 70 80 90 100
ASIEMAESNS IPSVVVNSSK QHGPIIVIDN YDSFTYNLCQ YMGELGCHFE
110 120 130 140 150
VYRNDELTVE ELKKKNPRGV LISPGPGTPQ DSGISLQTVL ELGPLVPLFG
160 170 180 190 200
VCMGLQCIGE AFGGKIVRSP FGVMHGKSSM VHYDEKGEEG LFSGLSNPFI
210 220 230 240 250
VGRYHSLVIE KDTFPSDELE VTAWTEDGLV MAARHRKYKH IQGVQFHPES
260 270
IITTEGKTIV RNFIKIVEKK ESEKLT
Length:276
Mass (Da):30,460
Last modified:November 1, 1996 - v1
Checksum:iD79AE704B2704A78
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L22585 mRNA. Translation: AAA32742.1.
AC079374 Genomic DNA. Translation: AAG28813.1.
CP002684 Genomic DNA. Translation: AEE30589.1.
AY099834 mRNA. Translation: AAM20685.1.
BT006303 mRNA. Translation: AAP13411.1.
AK226500 mRNA. Translation: BAE98642.1.
PIRiJQ2340.
RefSeqiNP_173893.1. NM_102331.2. [Q42565-1]
UniGeneiAt.51757.
At.7656.

Genome annotation databases

EnsemblPlantsiAT1G25220.1; AT1G25220.1; AT1G25220. [Q42565-1]
GeneIDi839103.
KEGGiath:AT1G25220.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L22585 mRNA. Translation: AAA32742.1.
AC079374 Genomic DNA. Translation: AAG28813.1.
CP002684 Genomic DNA. Translation: AEE30589.1.
AY099834 mRNA. Translation: AAM20685.1.
BT006303 mRNA. Translation: AAP13411.1.
AK226500 mRNA. Translation: BAE98642.1.
PIRiJQ2340.
RefSeqiNP_173893.1. NM_102331.2. [Q42565-1]
UniGeneiAt.51757.
At.7656.

3D structure databases

ProteinModelPortaliQ42565.
SMRiQ42565. Positions 76-267.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi24340. 1 interaction.
IntActiQ42565. 1 interaction.
STRINGi3702.AT1G25220.2.

Protein family/group databases

MEROPSiC26.A09.

Proteomic databases

PaxDbiQ42565.
PRIDEiQ42565.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G25220.1; AT1G25220.1; AT1G25220. [Q42565-1]
GeneIDi839103.
KEGGiath:AT1G25220.

Organism-specific databases

TAIRiAT1G25220.

Phylogenomic databases

eggNOGiKOG0026. Eukaryota.
COG0512. LUCA.
HOGENOMiHOG000025029.
KOiK01658.
PhylomeDBiQ42565.

Enzyme and pathway databases

UniPathwayiUPA00035; UER00040.
BioCyciARA:GQT-1090-MONOMER.
SABIO-RKQ42565.

Miscellaneous databases

PROiQ42565.

Gene expression databases

ExpressionAtlasiQ42565. baseline and differential.
GenevisibleiQ42565. AT.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR006221. TrpG/PapA_dom.
[Graphical view]
PfamiPF00117. GATase. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR00566. trpG_papA. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Suppressors of trp1 fluorescence identify a new arabidopsis gene, TRP4, encoding the anthranilate synthase beta subunit."
    Niyogi K.K., Last R.L., Fink G.R., Keith B.
    Plant Cell 5:1011-1027(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, MUTAGENESIS OF GLY-150, DISRUPTION PHENOTYPE.
    Strain: cv. Columbia.
  2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "A link between ethylene and auxin uncovered by the characterization of two root-specific ethylene-insensitive mutants in Arabidopsis."
    Stepanova A.N., Hoyt J.M., Hamilton A.A., Alonso J.M.
    Plant Cell 17:2230-2242(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION BY ETHYLENE, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLY-176.
  7. "Ethylene-auxin interactions regulate lateral root initiation and emergence in Arabidopsis thaliana."
    Ivanchenko M.G., Muday G.K., Dubrovsky J.G.
    Plant J. 55:335-347(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiASB1_ARATH
AccessioniPrimary (citable) accession number: Q42565
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 19, 2014
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.