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A0A2I1EUC9 · A0A2I1EUC9_9GLOM

  • Protein
    Succinate--CoA ligase [ADP-forming] subunit alpha, mitochondrial
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit.

Caution

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

Catalytic activity

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.

Features

Showing features for binding site, active site.

Type
IDPosition(s)Description
Binding site55-58CoA (UniProtKB | ChEBI)
Binding site81CoA (UniProtKB | ChEBI)
Binding site134-136CoA (UniProtKB | ChEBI)
Binding site198substrate; ligand shared with subunit beta
Active site291Tele-phosphohistidine intermediate

GO annotations

AspectTerm
Cellular Componentmitochondrion
Cellular Componentsuccinate-CoA ligase complex (ADP-forming)
Molecular Functionnucleotide binding
Molecular Functionsuccinate-CoA ligase (ADP-forming) activity
Molecular Functionsuccinate-CoA ligase (GDP-forming) activity
Biological Processtricarboxylic acid cycle

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Succinate--CoA ligase [ADP-forming] subunit alpha, mitochondrial
  • EC number
  • Alternative names
    • Succinyl-CoA synthetase subunit alpha
      (SCS-alpha
      )

Gene names

    • ORF names
      CHRIB12_LOCUS14796
      , RhiirA1_424050

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • A1
    • CHB12
  • Taxonomic lineage
    Eukaryota > Fungi > Fungi incertae sedis > Mucoromycota > Glomeromycotina > Glomeromycetes > Glomerales > Glomeraceae > Rhizophagus

Accessions

  • Primary accession
    A0A2I1EUC9

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Interaction

Subunit

Heterodimer of an alpha and a beta subunit.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain43-138CoA-binding

Sequence similarities

Belongs to the succinate/malate CoA ligase alpha subunit family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    338
  • Mass (Da)
    35,776
  • Last updated
    2018-02-28 v1
  • MD5 Checksum
    4A62C003A6ACB26B6DED33DD76A0B163
MISFKNSFYRSLKPKAQFALCRGFSYSAIRSASYEDTVKNMRLTKDSRVICHGFTGKQGTFHSKQAIEYGTNMVGGVSPNKGGQTHLGLPVFRTTAEAAKELKPDATAIYVPPPAAAAAILDSIEAEIPLIVTITEGIPQQDMVKVVKVLKSQSKSRLIGPNCPGIIAPGACKIGIMPAHIHQKGKVGVVSRSGTLTYEAVNQTTQANLGQTLCVGIGGDPFNGTNFVDCLKLFLEDDSTEGIILIGEIGGSAEEEAAEYLKQHNLTRKQPKPVVSFIAGLTAPPGRRMGHAGAIIAGGKGGATDKIKALENAGVVVSRSPARLGIHLREEMEKLGLA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CAGKOT010000034
EMBL· GenBank· DDBJ
CAB5375266.1
EMBL· GenBank· DDBJ
Genomic DNA
LLXH01000885
EMBL· GenBank· DDBJ
PKC62231.1
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.
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