Q2N695 · SUCC_ERYLH

Function

function

Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP 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 site46ATP (UniProtKB | ChEBI)
Binding site53-55ATP (UniProtKB | ChEBI)
Binding site112ATP (UniProtKB | ChEBI)
Binding site117ATP (UniProtKB | ChEBI)
Binding site209Mg2+ (UniProtKB | ChEBI)
Binding site223Mg2+ (UniProtKB | ChEBI)
Binding site274substrate; ligand shared with subunit alpha
Binding site331-333substrate; ligand shared with subunit alpha

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentsuccinate-CoA ligase complex
Molecular FunctionATP binding
Molecular Functionmagnesium ion binding
Molecular Functionsuccinate-CoA ligase (ADP-forming) activity
Molecular Functionsuccinate-CoA ligase (GDP-forming) activity
Biological Processsuccinyl-CoA metabolic process
Biological Processtricarboxylic acid cycle

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

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

Gene names

    • Name
      sucC
    • Ordered locus names
      ELI_13520

Organism names

Accessions

  • Primary accession
    Q2N695

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_10000820831-399Succinate--CoA ligase [ADP-forming] subunit beta

Interaction

Subunit

Heterotetramer of two alpha and two beta subunits.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain9-254ATP-grasp

Sequence similarities

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    399
  • Mass (Da)
    42,505
  • Last updated
    2006-02-07 v1
  • Checksum
    B0863FABF3D57293
MNLHEYQAKELLAKYGIGIPAGHAALTVEEAVAGAKQLPGPLYVVKAQIHAGGRGKGKFKELGPDAKGGVRLAKSIEDVEASAREMLGNTLVTVQTGEEGKQVNRLYVTDGVDIASEYYLSMVVDRASGRVGMIVSTEGGMDIEEVAHSTPEKITTITIDPAQGFMPHHGRAVAFALKLSGDLNKQAQKLAKQLYTAFMDLDCEMLEINPLVETEDGQLLVLDTKMSIDGNALYRHKDVEEMRDETEEDPAEVEASEYDLAYIKLDGNIGCMVNGAGLAMATMDIIKLNGAFPANFLDVGGGATTEKVTAAFKIILKDPAVEGILVNIFGGIMRCDTIAEGIVVAAKEVELDVPLVVRLEGTNVEKGKDILANSGLPIVPADDLGDAARKIVAEVKQAA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000157
EMBL· GenBank· DDBJ
ABC64796.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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.
Help