ALS

UniProt ID: A0A292QBV7
Organism: Miscanthus sinensis
Review Status: INITIALIZED
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Gene Description

Acetolactate synthase, a thiamine-diphosphate- and magnesium-dependent enzyme catalyzing the first committed steps toward branched-chain amino acid biosynthesis.

Core Functions

Catalyzes pyruvate condensation to acetolactate as part of branched-chain amino acid biosynthesis.

Supporting Evidence:
  • file:MISSI/ALS/ALS-uniprot.txt
    Reaction=2 pyruvate + H(+) = (2S)-2-acetolactate + CO2
  • file:MISSI/ALS/ALS-uniprot.txt
    PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
  • file:MISSI/ALS/ALS-uniprot.txt
    COFACTOR: Name=thiamine diphosphate
  • file:interpro/panther/PTHR18968/PTHR18968-entries.csv
    Q41768,"Acetolactate synthase 1, chloroplastic",protein,4577,Zea mays
  • file:interpro/panther/PTHR18968/PTHR18968-entries.csv
    P17597,"Acetolactate synthase, chloroplastic",protein,3702,Arabidopsis thaliana

References

file:MISSI/ALS/ALS-uniprot.txt
UniProtKB entry for Miscanthus sinensis ALS
  • UniProt supports acetolactate synthase activity, branched-chain amino acid biosynthetic pathways, and the PANTHER assignment, but it has no explicit subcellular-location line for Miscanthus ALS.
file:interpro/panther/PTHR18968/PTHR18968-entries.csv
PANTHER PTHR18968 family entries for acetolactate synthase homologs
  • Several plant members of the same PANTHER acetolactate synthase subfamily are chloroplastic, while the subfamily label is mitochondrial and therefore not used directly for Miscanthus localization.

Suggested Questions for Experts

Q: Are Miscanthus ALS variants associated with herbicide sensitivity or altered branched-chain amino acid metabolism?

Suggested Experiments

Experiment: Assay ALS activity and herbicide inhibition in vitro using Miscanthus enzyme variants.

Type: targeted functional assay

📚 Additional Documentation

Notes

(ALS-notes.md)

Curation notes

  • QuickGO export is header-only; therefore no UniProt DR/InterPro-derived terms are listed as existing_annotations or proposed as NEW.
  • Core function focuses on acetolactate synthase activity in branched-chain amino acid biosynthesis; herbicide response is not treated as a core function.
  • Added chloroplast stroma localization after PR re-review. UniProt lacks a direct location line for this Miscanthus entry, but plant ALS homologs in PTHR18968 include chloroplastic Arabidopsis and maize enzymes; the PANTHER subfamily label says mitochondrial and is not used for localization.

📄 View Raw YAML

id: A0A292QBV7
gene_symbol: ALS
product_type: PROTEIN
status: INITIALIZED
taxon:
  id: NCBITaxon:62337
  label: Miscanthus sinensis
description: Acetolactate synthase, a thiamine-diphosphate- and magnesium-dependent enzyme catalyzing the first committed steps toward branched-chain amino acid biosynthesis.
existing_annotations: []
references:
- id: file:MISSI/ALS/ALS-uniprot.txt
  title: UniProtKB entry for Miscanthus sinensis ALS
  findings:
  - statement: UniProt supports acetolactate synthase activity, branched-chain amino acid biosynthetic pathways, and the PANTHER assignment, but it has no explicit subcellular-location line for Miscanthus ALS.
- id: file:interpro/panther/PTHR18968/PTHR18968-entries.csv
  title: PANTHER PTHR18968 family entries for acetolactate synthase homologs
  findings:
  - statement: >-
      Several plant members of the same PANTHER acetolactate synthase subfamily
      are chloroplastic, while the subfamily label is mitochondrial and therefore
      not used directly for Miscanthus localization.
core_functions:
- description: Catalyzes pyruvate condensation to acetolactate as part of branched-chain amino acid biosynthesis.
  molecular_function:
    id: GO:0003984
    label: acetolactate synthase activity
  directly_involved_in:
  - id: GO:1901705
    label: L-isoleucine biosynthetic process
  - id: GO:0009099
    label: L-valine biosynthetic process
  locations:
  - id: GO:0009570
    label: chloroplast stroma
  in_complex:
    id: GO:0005948
    label: acetolactate synthase complex
  supported_by:
  - reference_id: file:MISSI/ALS/ALS-uniprot.txt
    supporting_text: Reaction=2 pyruvate + H(+) = (2S)-2-acetolactate + CO2
  - reference_id: file:MISSI/ALS/ALS-uniprot.txt
    supporting_text: 'PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.'
  - reference_id: file:MISSI/ALS/ALS-uniprot.txt
    supporting_text: 'COFACTOR: Name=thiamine diphosphate'
  - reference_id: file:interpro/panther/PTHR18968/PTHR18968-entries.csv
    supporting_text: Q41768,"Acetolactate synthase 1, chloroplastic",protein,4577,Zea mays
  - reference_id: file:interpro/panther/PTHR18968/PTHR18968-entries.csv
    supporting_text: P17597,"Acetolactate synthase, chloroplastic",protein,3702,Arabidopsis thaliana
proposed_new_terms: []
suggested_questions:
- question: Are Miscanthus ALS variants associated with herbicide sensitivity or altered branched-chain amino acid metabolism?
suggested_experiments:
- description: Assay ALS activity and herbicide inhibition in vitro using Miscanthus enzyme variants.
  experiment_type: targeted functional assay