A0AA36GZN9 · A0AA36GZN9_CYLNA

Function

function

GTP-specific succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of 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 degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 1/4.
Carbohydrate metabolism; hexose metabolism.
Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.

Features

Showing features for binding site, site.

TypeIDPosition(s)Description
Binding site581GTP (UniProtKB | ChEBI)
Site608Important for substrate specificity
Binding site619-621GTP (UniProtKB | ChEBI)
Binding site677GTP (UniProtKB | ChEBI)
Binding site774Mg2+ (UniProtKB | ChEBI)
Binding site788Mg2+ (UniProtKB | ChEBI)
Binding site839substrate; ligand shared with subunit alpha
Binding site896-898substrate; ligand shared with subunit alpha

GO annotations

AspectTerm
Cellular Componentmitochondrion
Cellular Componentsuccinate-CoA ligase complex
Molecular FunctionATP binding
Molecular FunctionD-glucose binding
Molecular FunctionGTP binding
Molecular Functionhexokinase activity
Molecular Functionmagnesium ion binding
Molecular Functionsuccinate-CoA ligase (ADP-forming) activity
Molecular Functionsuccinate-CoA ligase (GDP-forming) activity
Biological Processintracellular glucose homeostasis
Biological Processsuccinyl-CoA metabolic process
Biological Processtricarboxylic acid cycle

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial
  • EC number
  • Alternative names
    • GTP-specific succinyl-CoA synthetase subunit beta
      (G-SCS
      ; GTPSCS
      )
    • Succinyl-CoA synthetase beta-G chain
      (SCS-betaG
      )

Gene names

    • ORF names
      CYNAS_LOCUS13215

Organism names

  • Taxonomic identifier
  • Strain
    • N/A
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Strongyloidea > Strongylidae > Cylicocyclus

Accessions

  • Primary accession
    A0AA36GZN9

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Heterodimer of an alpha and a beta subunit. The beta subunit determines specificity for GTP.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain9-202Hexokinase N-terminal
Domain212-447Hexokinase C-terminal
Domain563-778ATP-grasp fold succinyl-CoA synthetase-type
Domain837-957ATP-citrate synthase/succinyl-CoA ligase C-terminal

Sequence similarities

Belongs to the hexokinase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    961
  • Mass (Da)
    106,064
  • Last updated
    2024-01-24 v1
  • Checksum
    0F982073CB3935D1
MGMRLDRSEVQEILQKFVISEDDLHIISEKIELEMEAGLSSVDGSSIAMLPSYVPALPDGSEEGKYVAIDLSGKNLRIMLLTLNGKGREPTAVNNNYIVPNHVMKGTGDQLFTFIVNCLQRFLQEFGLVEANLPIGFVFSYPCELLSIRSARLLWWTKGFDIKDCLRKDVVQLLEEALEMNMSTKAQIKAVMNDTVGQLAAAGHKYGPECTIGVVIGYGCNSSYLEKTSRITKFDAEGVGYKHPNMVVVTEWEEFGSKGELDSILTQFDKEIDAASVHQGKQIIDKLTGALYLGELVRRVLSQLVLDRVLFDGQPCEKLDEADAFPTKYISEILAEEDGSYKACRRICDELDVPMHGSSDYHIIRDVCFAVSDRSAAIVAAAISALLRHLEVSRVKIGVGGALIQFHPIYHKLLHDKLVDLAPLCTEWELVPADEGSARGAALIAAVAEKMKLYTFAKTICLASIYRVGDIAIVARFVLSSFTVFGSFSSAASAFKRIRAMPHFARTSLDSWLFVWYIVARSNFSQQSNSQARQEDCSVMFRRATNLLARSSVGKVAQQRFLNLHEYQSKELLHKHGCTVQNFIVASDVEEAREKLKRFEMLFEGDIEYVVKAQILAGGRGKGHFIGGDDKIRGVFITLDRDECLKSIPRMLGKRLVTKQTTKNGVEVKKVMVAEGVPIKRETYVAVLMDRDSNGPVIVASPAGGVDIETVAHETPHLIFKEPIDIEVGITDEQAMKIAKNLQFSGEMAEKAAKEIKLLYKAFISSDATQVEINPFVETTDGRVFCMDAKMNFDDSAAFRQKEIFAMEDQSEQDVREVEAQKHNLNYVGMDGNIACLVNGAGLAMATMDIIKLKGGEPANFLDVGGTVTEEQVYQAFRIITEDAKVKCILVNIFGGIVNCATIAKGVIKACEKIKLKVPLVVRLQGTNVDEARRILKESGLPIISAGDLNDAAEKAVAALK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CATQJL010000305
EMBL· GenBank· DDBJ
CAJ0601232.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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