A0A7G2C6Q3 · A0A7G2C6Q3_9TRYP

  • Protein
    Succinate--CoA ligase [ADP-forming] subunit beta, 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 beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 Mg2+ ion per subunit.

Pathway

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

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site66ATP (UniProtKB | ChEBI)
Binding site73-75ATP (UniProtKB | ChEBI)
Binding site135ATP (UniProtKB | ChEBI)
Binding site227Mg2+ (UniProtKB | ChEBI)
Binding site241Mg2+ (UniProtKB | ChEBI)
Binding site292substrate; ligand shared with subunit alpha
Binding site349-351substrate; ligand shared with subunit alpha

GO annotations

AspectTerm
Cellular Componentmitochondrion
Molecular FunctionATP binding
Molecular Functionmagnesium ion binding
Molecular Functionsuccinate-CoA ligase (ADP-forming) activity
Biological Processtricarboxylic acid cycle

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

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

Gene names

    • ORF names
      ADEAN_000188900

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Crithidia deanei Carvalho (ATCC PRA-265)
  • Taxonomic lineage
    Eukaryota > Discoba > Euglenozoa > Kinetoplastea > Metakinetoplastina > Trypanosomatida > Trypanosomatidae > Strigomonadinae > Angomonas

Accessions

  • Primary accession
    A0A7G2C6Q3

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
Domain22-230ATP-grasp fold succinyl-CoA synthetase-type
Domain290-407ATP-citrate synthase/succinyl-CoA ligase C-terminal

Sequence similarities

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    417
  • Mass (Da)
    44,779
  • Last updated
    2021-02-10 v1
  • Checksum
    394B7EA3D4FC3513
MQRFSRFVQPTSIALAQYRFFNIHEYQSKRILKDNGGKVEFGIPCTTIEEVEAACANIKTPQKVVKSQILAGGRGKGHFKDGYQGGVKVCKDAKEAVEVAKKMLGNTLITKQTGAKGQVVNTLFVTEAVAGIKRELYVSLILDRKSASPIFIGSAEGGTGIEELAKTHPEKIKTMKVNISEGIDHDACVAYAKELGFTGDSAEKAANQFKVIYNIGKSKDCTMVEINPFIELENGDVMEIDAKLSFDDNAAFRQKEIFALADDTQIDSKEVLAKKFDLNYIALDGNVGCLVNGAGLAMATMDLISLHGGSPANFLDVGGSAEEKQIVAAFRIITGDPNVKSILVNIFGGIMHCDVIAKGVVNAAKTLQTKVPIVVRLNGTNEEAGKQIIAESGMDVHTAEDFESGAKLAVELAVKGK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LR877147
EMBL· GenBank· DDBJ
CAD2214443.1
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