Q12680 · GLT1_YEAST

Function

function

Forms L-glutamate from L-glutamine and 2-oxoglutarate. Represents an alternative pathway to L-glutamate dehydrogenase for the biosynthesis of L-glutamate. Participates with glutamine synthetase in ammonia assimilation processes. The enzyme is specific for NADH, L-glutamine and 2-oxoglutarate.

Miscellaneous

Present with 18900 molecules/cell in log phase SD medium.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
[3Fe-4S] cluster (UniProtKB | Rhea| CHEBI:21137 )
Note: Binds 1 [3Fe-4S] cluster.
FAD (UniProtKB | Rhea| CHEBI:57692 )
FMN (UniProtKB | Rhea| CHEBI:58210 )

Activity regulation

Inhibited by homocysteine sulfonamide.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
280 μML-glutamine
40 μM2-oxoglutarate
7 μMNADH

pH Dependence

Optimum pH is 7-7.5. Active from pH 6 to 9.

Pathway

Amino-acid biosynthesis; L-glutamate biosynthesis via GLT pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NAD+ route): step 1/1.
Energy metabolism; nitrogen metabolism.

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site54For GATase activity
Binding site1132-1189FMN (UniProtKB | ChEBI)
Binding site1185[3Fe-4S] cluster (UniProtKB | ChEBI)
Binding site1191[3Fe-4S] cluster (UniProtKB | ChEBI)
Binding site1196[3Fe-4S] cluster (UniProtKB | ChEBI)
Binding site1928-1942NAD+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmitochondrion
Molecular Function3 iron, 4 sulfur cluster binding
Molecular Functionflavin adenine dinucleotide binding
Molecular FunctionFMN binding
Molecular Functionglutamate synthase (NADH) activity
Molecular Functioniron ion binding
Biological Processammonia assimilation cycle
Biological Processglutamate biosynthetic process
Biological ProcessL-glutamate biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glutamate synthase [NADH]
  • EC number
  • Alternative names
    • NADH-GOGAT

Gene names

    • Name
      GLT1
    • Ordered locus names
      YDL171C

Organism names

Accessions

  • Primary accession
    Q12680
  • Secondary accessions
    • D6VRI0
    • Q12290

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for propeptide, chain, modified residue.

TypeIDPosition(s)Description
PropeptidePRO_00000116121-53
ChainPRO_000001161354-2145Glutamate synthase [NADH]
Modified residue2070Phosphothreonine

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Homotrimer.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q12680YLR257W Q061462EBI-7727, EBI-36149

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, coiled coil.

TypeIDPosition(s)Description
Domain54-455Glutamine amidotransferase type-2
Coiled coil1551-1600

Sequence similarities

Belongs to the glutamate synthase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    2,145
  • Mass (Da)
    238,102
  • Last updated
    2006-09-05 v2
  • Checksum
    78184877D2167A0D
MPVLKSDNFDPLEEAYEGGTIQNYNDEHHLHKSWANVIPDKRGLYDPDYEHDACGVGFVANKHGEQSHKIVTDARYLLVNMTHRGAVSSDGNGDGAGILLGIPHEFMKREFKLDLDLDIPEMGKYAVGNVFFKKNEKNNKKNLIKCQKIFEDLAASFNLSVLGWRNVPVDSTILGDVALSREPTILQPLLVPLYDEKQPEFNETKFRTQLYLLRKEASLQIGLENWFYVCSLNNTTIVYKGQLTPAQVYNYYPDLTNAHFKSHMALVHSRFSTNTFPSWDRAQPLRWLAHNGEINTLRGNKNWMRSREGVMNSATFKDELDKLYPIIEEGGSDSAALDNVLELLTINGTLSLPEAVMMMVPEAYHKDMDSDLKAWYDWAACLMEPWDGPALLTFTDGRYCGAILDRNGLRPCRYYITSDDRVICASEVGVIPIENSLVVQKGKLKPGDLFLVDTQLGEMVDTKKLKSQISKRQDFKSWLSKVIKLDDLLSKTANLVPKEFISQDSLSLKVQSDPRLLANGYTFEQVTFLLTPMALTGKEALGSMGNDAPLACLNENPVLLYDYFRQLFAQVTNPPIDPIREANVMSLECYVGPQGNLLEMHSSQCDRLLLKSPILHWNEFQALKNIEAAYPSWSVAEIDITFDKSEGLLGYTDTIDKITKLASEAIDDGKKILIITDRKMGANRVSISSLIAISCIHHHLIRNKQRSQVALILETGEAREIHHFCVLLGYGCDGVYPYLAMETLVRMNREGLLRNVNNDNDTLEEGQILENYKHAIDAGILKVMSKMGISTLASYKGAQIFEALGLDNSIVDLCFTGTSSRIRGVTFEYLAQDAFSLHERGYPSRQTISKSVNLPESGEYHFRDGGYKHVNEPTAIASLQDTVRNKNDVSWQLYVKKEMEAIRDCTLRGLLELDFENSVSIPLEQVEPWTEIARRFASGAMSYGSISMEAHSTLAIAMNRLGAKSNCGEGGEDAERSAVQENGDTMRSAIKQVASARFGVTSYYLSDADEIQIKIAQGAKPGEGGELPAHKVSKDIAKTRHSTPNVGLISPPPHHDIYSIEDLKQLIYDLKCANPRAGISVKLVSEVGVGIVASGVAKAKADHILVSGHDGGTGAARWTSVKYAGLPWELGLAETHQTLVLNDLRRNVVVQTDGQLRTGFDIAVAVLLGAESFTLATVPLIAMGCVMLRRCHLNSCAVGIATQDPYLRSKFKGQPEHVINFFYYLIQDLRQIMAKLGFRTIDEMVGHSEKLKKRDDVNAKAINIDLSPILTPAHVIRPGVPTKFTKKQDHKLHTRLDNKLIDEAEVTLDRGLPVNIDASIINTDRALGSTLSYRVSKKFGEDGLPKDTVVVNIEGSAGQSFGAFLASGITFILNGDANDYVGKGLSGGIIVIKPPKDSKFKSDENVIVGNTCFYGATSGTAFISGSAGERFGVRNSGATIVVERIKGNNAFEYMTGGRAIVLSQMESLNAFSGATGGIAYCLTSDYDDFVGKINKDTVELESLCDPVEIAFVKNLIQEHWNYTQSDLAARILGNFNHYLKDFVKVIPTDYKKVLLKEKAEAAKAKAKATSEYLKKFRSNQEVDDEVNTLLIANQKAKEQEKKKSITISNKATLKEPKVVDLEDAVPDSKQLEKNSERIEKTRGFMIHKRRHETHRDPRTRVNDWKEFTNPITKKDAKYQTARCMDCGTPFCLSDTGCPLSNIIPKFNELLFKNQWKLALDKLLETNNFPEFTGRVCPAPCEGACTLGIIEDPVGIKSVERIIIDNAFKEGWIKPCPPSTRTGFTVGVIGSGPAGLACADMLNRAGHTVTVYERSDRCGGLLMYGIPNMKLDKAIVQRRIDLLSAEGIDFVTNTEIGKTISMDELKNKHNAVVYAIGSTIPRDLPIKGRELKNIDFAMQLLESNTKALLNKDLEIIREKIQGKKVIVVGGGDTGNDCLGTSVRHGAASVLNFELLPEPPVERAKDNPWPQWPRVMRVDYGHAEVKEHYGRDPREYCILSKEFIGNDEGEVTAIRTVRVEWKKSQSGVWQMVEIPNSEEIFEADIILLSMGFVGPELINGNDNEVKKTRRGTIATLDDSSYSIDGGKTFACGDCRRGQSLIVWAIQEGRKCAASVDKFLMDGTTYLPSNGGIVQRDYKLLKELASQV

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict166-173in Ref. 1; CAA61505
Sequence conflict450-452in Ref. 1; CAA61505
Sequence conflict1753in Ref. 1; CAA61505

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X89221
EMBL· GenBank· DDBJ
CAA61505.1
EMBL· GenBank· DDBJ
Genomic DNA
Z67750
EMBL· GenBank· DDBJ
CAA91574.1
EMBL· GenBank· DDBJ
Genomic DNA
Z74219
EMBL· GenBank· DDBJ
CAA98745.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006938
EMBL· GenBank· DDBJ
DAA11690.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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