Q8GZ29 · GH315_ARATH

Function

function

Indole-3-acetic acid-amido (IAA) synthetase that catalyzes the conjugation of amino acids to auxin specifically using the auxin precursor indole-3-butyric acid (IBA) and glutamine and, possibly, cysteine as substrates (PubMed:29462792, PubMed:30315112).
Displays high catalytic activity with the auxinic phenoxyalkanoic acid herbicides 4-(2,4-dichlorophenoxy)butyric acid (2,4-DB) and to some extent 2,4-dichlorophenoxylacetic acid (2,4-D) as substrates, thus conferring resistance to herbicides (PubMed:30315112).

Catalytic activity

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
556 μMindole-3-acetic acidin the presence of ATP glutamine
3430 μMindole-3-propionic acidin the presence of ATP glutamine
527 μMindole-3-butyric acidin the presence of ATP glutamine
1120 μMjasmonic acidin the presence of ATP glutamine
1780 μMglutaminein the presence of ATP indole-3-butyric acid
2530 μMglutaminein the presence of ATP jasmonic acid
2080 μMcysteinein the presence of ATP indole-3-butyric acid
12300 μMhistidinein the presence of ATP indole-3-butyric acid
5670 μMmethioninein the presence of ATP indole-3-butyric acid
18600 μMtyrosinein the presence of ATP indole-3-butyric acid
84 μMATPin the presence of glutamine indole-3-butyric acid
590 μM4-(2,4-dichlorophenoxy)butyric acidin the presence of ATP glutamine
3790 μM2,4-dichlorophenoxylacetic acidin the presence of ATP glutamine
970 μMglutaminein the presence of ATP 4-(2,4-dichlorophenoxy)butyric acid
7240 μMcysteinein the presence of ATP 4-(2,4-dichlorophenoxy)butyric acid
9290 μMhistidinein the presence of ATP 4-(2,4-dichlorophenoxy)butyric acid
10600 μMmethioninein the presence of ATP 4-(2,4-dichlorophenoxy)butyric acid
18400 μMtyrosinein the presence of ATP 4-(2,4-dichlorophenoxy)butyric acid
23200 μM2,4,5-trichlorophenoxyacetic acidin the presence of ATP glutamine
1130 μM4-(4-chloro-2-methylphenoxy)butanoic acidin the presence of ATP glutamine
3550 μM4-(2-chlorophenoxy)butanoic acidin the presence of ATP glutamine
180 μM4-(2,6-dimethylphenoxy)butanoic acidin the presence of ATP glutamine
14800 μM4-(4-methoxyphenoxy)butanoic acidin the presence of ATP glutamine
2140 μM4-phenoxybutyric acidin the presence of ATP glutamine
6000 μM4-phenylbutryic acidin the presence of ATP glutamine
960 μM5-phenylvaleric acidin the presence of ATP glutamine
680 μM5-(4-fluorophenyl)valeric acidin the presence of ATP glutamine
kcat is 0.76 min-1 with indole-3-acetic acid as substrate (in the presence of ATP and glutamine) (PubMed:29462792, PubMed:30315112).
kcat is 10.2 min-1 with indole-3-propionic acid as substrate (in the presence of ATP and glutamine) (PubMed:29462792).
kcat is 9.9 min-1 with indole-3-butyric acid as substrate (in the presence of ATP and glutamine) (PubMed:29462792, PubMed:30315112).
kcat is 4.4 min-1 with jasmonic acid as substrate (in the presence of ATP and glutamine) (PubMed:29462792).
kcat is 17 min-1 with glutamine as substrate (in the presence of ATP and indole-3-butyric acid) (PubMed:29462792).
kcat is 4 min-1 with glutamine as substrate (in the presence of ATP and jasmonic acid) (PubMed:29462792).
kcat is 16 min-1 with cysteine as substrate (in the presence of ATP and indole-3-butyric acid) (PubMed:29462792).
kcat is 21 min-1 with histidine as substrate (in the presence of ATP and indole-3-butyric acid) (PubMed:29462792).
kcat is 13 min-1 with methionine as substrate (in the presence of ATP and indole-3-butyric acid) (PubMed:29462792).
kcat is 25 min-1 with tyrosine as substrate (in the presence of ATP and indole-3-butyric acid) (PubMed:29462792).
kcat is 13 min-1 with ATP as substrate (in the presence of indole-3-butyric acid and glutamine) (PubMed:29462792).
kcat is 11 min-1 with 4-(2,4-dichlorophenoxy)butyric acid as substrate (in the presence of ATP and glutamine) (PubMed:30315112).
kcat is 1.3 min-1 with 2,4-dichlorophenoxylacetic acid as substrate (in the presence of ATP and glutamine) (PubMed:30315112).
kcat is 52.3 min-1 with glutamine as substrate (in the presence of ATP and 4-(2,4-dichlorophenoxy)butyric acid) (PubMed:30315112).
kcat is 52.5 min-1 with cysteine as substrate (in the presence of ATP and 4-(2,4-dichlorophenoxy)butyric acid) (PubMed:30315112).
kcat is 43.1 min-1 with histidine as substrate (in the presence of ATP and 4-(2,4-dichlorophenoxy)butyric acid) (PubMed:30315112).
kcat is 27.5 min-1 with methionine as substrate (in the presence of ATP and 4-(2,4-dichlorophenoxy)butyric acid) (PubMed:30315112).
kcat is 12 min-1 with tyrosine as substrate (in the presence of ATP and 4-(2,4-dichlorophenoxy)butyric acid) (PubMed:30315112).
kcat is 4.3 min-1 with 2,4,5-trichlorophenoxyacetic acid as substrate (in the presence of ATP and glutamine) (PubMed:30315112).
kcat is 15.6 min-1 with 4-(4-chloro-2-methylphenoxy)butanoic acid as substrate (in the presence of ATP and glutamine) (PubMed:30315112).
kcat is 24 min-1 with 4-(2-chlorophenoxy)butanoic acid as substrate (in the presence of ATP and glutamine) (PubMed:30315112).
kcat is 5.4 min-1 with 4-(2,6-dimethylphenoxy)butanoic acid as substrate (in the presence of ATP and glutamine) (PubMed:30315112).
kcat is 29.8 min-1 with 4-(4-methoxyphenoxy)butanoic acid as substrate (in the presence of ATP and glutamine) (PubMed:30315112).
kcat is 16.2 min-1 with 4-phenoxybutyric acid as substrate (in the presence of ATP and glutamine) (PubMed:30315112).
kcat is 15 min-1 with 4-phenylbutryic acid as substrate (in the presence of ATP and glutamine) (PubMed:30315112).
kcat is 26.6 min-1 with 5-phenylvaleric acid as substrate (in the presence of ATP and glutamine) (PubMed:30315112).
kcat is 24 min-1 with 5-(4-fluorophenyl)valeric acid as substrate (in the presence of ATP and glutamine) (PubMed:30315112).

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site97-98ATP (UniProtKB | ChEBI)
Binding site302ATP (UniProtKB | ChEBI)
Binding site325substrate
Binding site325-330ATP (UniProtKB | ChEBI)
Binding site332substrate
Binding site348ATP (UniProtKB | ChEBI)
Binding site408ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular FunctionATP binding
Molecular Functionglutamine binding
Molecular Functionligase activity
Biological Processauxin conjugate metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Indole-3-acetic acid-amido synthetase GH3.15
  • EC number
  • Alternative names
    • Auxin-responsive GH3-like protein 15
      (AtGH3-15
      )
    • Protein GRETCHEN HAGEN 3.15

Gene names

    • Name
      GH3.15
    • ORF names
      T22N19.20
    • Ordered locus names
      At5g13370

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q8GZ29
  • Secondary accessions
    • Q9LYR9

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Phenotypes & Variants

Disruption phenotype

No visible phenotype in normal conditions (PubMed:29462792).
Slight reduction in root length when grown on media containing indole-3-butyric acid (IBA) (PubMed:29462792).
Hypersensitivity to the auxinic phenoxyalkanoic acid herbicide 4-(2,4-dichlorophenoxy)butyric acid (2,4-DB) (PubMed:30315112).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis122Increased affinity and enhanced catalytic activity leading to improved efficiency toward indole-3-butyric acid. Reduced affinity but increased catalytic activity leading to almost unaffected efficiency toward indole-3-acetic acid.
Mutagenesis122Reduced affinity and altered catalytic activity leading to decreased efficiency toward indole-3-butyric acid.
Mutagenesis122Reduced affinity but enhanced catalytic activity leading to improved efficiency toward indole-3-butyric acid. Reduced affinity but increased catalytic activity leading to almost unaffected efficiency toward indole-3-acetic acid.
Mutagenesis162Increased affinity and enhanced catalytic activity leading to improved efficiency toward indole-3-butyric acid. Slightly increased affinity but normal catalytic activity leading to slightly improved efficiency toward indole-3-acetic acid.
Mutagenesis166Strongly reduced affinity but enhanced catalytic activity leading to reduced efficiency toward indole-3-butyric acid. Slightly increased affinity and slightly better catalytic activity leading to slightly improved efficiency toward indole-3-acetic acid.
Mutagenesis332Strongly reduced affinity but normal catalytic activity leading to reduced efficiency toward indole-3-butyric acid. Strongly reduced affinity and slightly better catalytic activity leading to reduced efficiency toward indole-3-acetic acid.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 72 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004472331-595Indole-3-acetic acid-amido synthetase GH3.15

Proteomic databases

Expression

Tissue specificity

Expressed in seedlings, roots, and parts of the siliques.

Developmental stage

Expressed widely in young seedling, including roots, shoots, and cotyledons. In older seedlings, present the primary root, shoots, and cotyledons, but not in the root epidermal cells or root hairs. Later observed in the cotyledons and the shoots, but not in the true leaves. In adult plants, accumulates in the primary root and lateral root tips and in the roots near the root/shoot junction. In mature siliques, confined to the tip of the silique in the style just below the stigma and at the base of the silique in the replum and abscission zone of siliques.

Gene expression databases

Interaction

Protein-protein interaction databases

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    595
  • Mass (Da)
    66,979
  • Last updated
    2003-03-01 v1
  • Checksum
    510294E9B2F5D1B1
MLPKFDPTNQKACLSLLEDLTTNVKQIQDSVLEAILSRNAQTEYLRGFLNGQVDKQNFKKNVPVVTYEDIRSYIDRIANGEPSDLICDRPISVLLTSSGTSGGVPKLIPLTTEDLEQRISFSSLYAPLLYKHIDGLSEGKSLIFYFVTRESKTANGLMVRTMVTSFLKSIKQTNSFLWDSLQVSPHAITTCADTTQSMYCQLLCGLLERDNVARLGAPFASSFLKVIKFLEDHWPELCSNIRTGRLSDWITDATCTSGIGKFLTAPNPELASLIEQECSKTSWEAILKRLWPKAKCIESIITGTMAQYIPLLEFYSGGLPLTSSFYGSSECFMGVNFNPLCKPSDVSYTIIPCMGYFEFLEVEKDHQEAGHDPTEKPVVVDLVDVKIGHDYEPVVTTFSGLYRYRVGDVLRATGFYNNAPHFCFVGRQKVVLSIDMDKTYEDDLLKAVTNAKLLLEPHDLMLMDFTSRVDSSSFPGHYVIYWELGSKVKDAKFEPNRDVMEECCFTVEESLDAVYRKGRKNDKNIGPLEIKVVKPGAFDELMNFFLSRGSSVSQYKTPRSVTNEEALKILEANVISEFLSRKIPSWELHELHSGR

Sequence caution

The sequence CAB87144.1 differs from that shown. Reason: Erroneous gene model prediction

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL163572
EMBL· GenBank· DDBJ
CAB87144.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
CP002688
EMBL· GenBank· DDBJ
AED91887.1
EMBL· GenBank· DDBJ
Genomic DNA
BT005922
EMBL· GenBank· DDBJ
AAO64857.1
EMBL· GenBank· DDBJ
mRNA
AK117242
EMBL· GenBank· DDBJ
BAC41918.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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