N1MG01 · N1MG01_9SPHN

  • Protein
    Succinate--CoA ligase [ADP-forming] subunit beta
  • Gene
    sucC
  • 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 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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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
    • ORF names
      EBBID32_100

Organism names

  • Taxonomic identifier
  • Strain
    • BiD32
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Sphingomonadales > Sphingomonadaceae > Sphingobium

Accessions

  • Primary accession
    N1MG01

Proteomes

Subcellular Location

Interaction

Subunit

Heterotetramer of two alpha and two beta subunits.

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)
    41,962
  • Last updated
    2013-06-26 v1
  • MD5 Checksum
    810B108047F714A33C14872F200E48B1
MNIHEYQAKELLAKYGAPIAAGYAAFSVEEAVEAAKKLPGPLYVVKSQIHAGGRGKGKFKELPADAKGGVRLAFNLDEVKAHSTDMLGNTLVTIQTGDAGKQVNRLYITDGADIDKEFYLALLVDRGSSKVAFVVSTEGGMDIEEVAHSTPEKIHSFSVDPATGFMPHHGRSIAAALGLTGDLAKQASKVASSLYAAFLDTDAEQIEVNPLALTKQGNLLVLDAKVGFDGNAMFRHKDIAQLRDLTEEDAAEVEASKYDLAYIKLDGNIGCMVNGAGLAMATMDIIKLNGEFPANFLDVGGGATTEKVTAAFKIILQDPAVKGILVNIFGGIMKCDIIADGIVAAAKEVNLSVPLVVRLEGTNVQQGKDILAASGLAIVPADDLGDAARKIVAEVRKAA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CAVK010000002
EMBL· GenBank· DDBJ
CCW15684.1
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.
This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice.
Help