F4N2Q7 · F4N2Q7_YEREN

Function

function

Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate).

Catalytic activity

Cofactor

adenosylcob(III)alamin (UniProtKB | Rhea| CHEBI:18408 )

Pathway

Amino-acid degradation; L-glutamate degradation via mesaconate pathway; acetate and pyruvate from L-glutamate: step 1/4.

Features

Showing features for binding site.

114820406080100120140
TypeIDPosition(s)Description
Binding site13-17adenosylcob(III)alamin (UniProtKB | ChEBI)
Binding site16Co (UniProtKB | ChEBI) of adenosylcob(III)alamin (UniProtKB | ChEBI); axial binding residue
Binding site61-63adenosylcob(III)alamin (UniProtKB | ChEBI)
Binding site93-97adenosylcob(III)alamin (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Functioncobalamin binding
Molecular Functionmetal ion binding
Molecular Functionmethylaspartate mutase activity
Biological Processanaerobic glutamate catabolic process
Biological Processglutamate catabolic process via L-citramalate

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glutamate mutase sigma subunit
  • EC number
  • Alternative names
    • Glutamate mutase S chain
    • Glutamate mutase small subunit
    • Methylaspartate mutase

Gene names

    • Name
      glmS
    • ORF names
      YEW_DQ15660

Organism names

Accessions

  • Primary accession
    F4N2Q7

Interaction

Subunit

Heterotetramer composed of 2 epsilon subunits (GlmE) and 2 sigma subunits (GlmS). GlmE exists as a homodimer and GlmS as a monomer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain3-140B12-binding

Sequence similarities

Belongs to the methylaspartate mutase GlmS subunit family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    148
  • Mass (Da)
    16,197
  • Last updated
    2011-06-28 v1
  • MD5 Checksum
    0E0A1F2CFF7335611E87D489592DD7BF
MQNPTIVIGVIGADCHAVGNKVLDRVFTMHNFNVINLGVMVSQDEYIDAAIETGAQAIVVSSIYGHGEVDCIGMRENCVERGIGEILLYVGGNLVIGKHDFSEIETKFKGMGFNRVFAPDTDLELVCSLMKRDIERVMQSEEAAEGMQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FR718689
EMBL· GenBank· DDBJ
CBX72365.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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