A0A364KMN2 · A0A364KMN2_TALAM

Function

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.
thiamine diphosphate (UniProtKB | Rhea| CHEBI:58937 )

Note: Binds 1 thiamine pyrophosphate per subunit.

Pathway

Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 1/4.

GO annotations

AspectTerm
Cellular Componentacetolactate synthase complex
Cellular Componentmitochondrion
Molecular Functionacetolactate synthase activity
Molecular Functionflavin adenine dinucleotide binding
Molecular Functionmagnesium ion binding
Molecular Functionpyruvate decarboxylase activity
Molecular Functionthiamine pyrophosphate binding
Biological Processisoleucine biosynthetic process
Biological Processvaline biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Acetolactate synthase
  • EC number

Gene names

    • ORF names
      BHQ10_000804

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CIB
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Trichocomaceae > Talaromyces > Talaromyces sect. Talaromyces

Accessions

  • Primary accession
    A0A364KMN2

Proteomes

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region40-70Disordered
Compositional bias41-70Polar residues
Domain89-204Thiamine pyrophosphate enzyme N-terminal TPP-binding
Domain287-430Thiamine pyrophosphate enzyme central
Domain495-642Thiamine pyrophosphate enzyme TPP-binding

Sequence similarities

Belongs to the TPP enzyme family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    688
  • Mass (Da)
    75,295
  • Last updated
    2018-11-07 v1
  • Checksum
    427A79D156F93B67
MMPIRSSRSALRTLPSQRQLVSNRRHFSTTLVAGAVSPHRTFKRGQSTATASSEARPVPSPAFNQETRNVSPLENRKLPELDDSFVGLSGGEIFHEMMLRLDVKHIFGYPGGAILPVFDAIYNSKHFDFILPRHEQGAGHMAEGYARASGKPGVVLVTSGPGATNVITPMQDALSDGTPMVVFCGQVPTSAIGTDAFQEADVVGISRPCTKWNVLVKSVAELPRRIKEAFEIATSGRPGPVLVDLPKDITAGILRKSIPMNSTLPFYPTTASEAARALGRHNLENTLDRVADLIGVAQKPVLYVGQGLLARPDGPKLLKEFTDKTSIPVTTTLQGLGGFDELDPKSLHMLGMHGSAYANMAMQEADLIIALGARFDDRVTLNVARFAPQAKAAALEGRGGIVHFEVMPKNINKVVEATEAVEGDCADNLALLIPKVKAVPERPEWFAQINDWKKRFPLTLYEEQTTDGPIKPQALIQKLSDLTAHMKDRTVITTGVGQHQMWAAQHFRWRHPRTMITSGGLGTMGFGLPAAIGAKVARPEALVIDIDGDASFNMTLTELSTAAQFNIGVKVLVLNNEEQGMVTQWQNLFYEDRYAHTHQQNPDFVKLSEAMGVQAQRCSKPEEVEEKLKWLIESEGPALLEVFTDKKVPVLPMVPAGSALHEFLVYDEAKNKERKALMKKRGVTQMLN

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias41-70Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MIKG01000001
EMBL· GenBank· DDBJ
RAO64792.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp