HAMAP rule MF_03220
General rule information
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Accession | MF_03220 |
Dates | 20-OCT-2016 (Created)
3-SEP-2024 (Last updated, Version 10) |
Name | Succ_CoA_betaA_euk |
Scope(s) |
Eukaryota |
Template(s) | Q9YI37 (SUCB1_COLLI); P0A836 (SUCC_ECOLI); P53590 (SUCB2_PIG); [ Recover all ] |
Triggered by |
case c? <OC:Metazoa> or <OC:Amoebozoa>
HAMAP; MF_03220 (Get profile general information and statistics) end case
|
Propagated annotation
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Identifier, protein and gene names
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Identifier | SUCB1 |
Protein name | RecName: Full=Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial; EC=6.2.1.5; AltName: Full=ATP-specific succinyl-CoA synthetase subunit beta; Short=A-SCS; AltName: Full=Succinyl-CoA synthetase beta-A chain; Short=SCS-betaA; |
case <OC:Vertebrata> | |
Gene name | Name=SUCLA2; |
end case |
Comments
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FUNCTION | ATP-specific 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 | Reaction=succinate + ATP + CoA = succinyl-CoA + ADP + phosphate; Xref=Rhea:RHEA:17661, ChEBI:CHEBI:30031, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:456216; EC=6.2.1.5; |
case <FTGroup:1> | |
COFACTOR | Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per subunit.; |
end case | |
PATHWAY | Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1. |
SUBUNIT | Heterodimer of an alpha and a beta subunit. The beta subunit determines specificity for ATP. |
SUBCELLULAR LOCATION | Mitochondrion. |
SIMILARITY | Belongs to the succinate/malate CoA ligase beta subunit family. ATP-specific subunit beta subfamily. |
case not <AnyFeature:TransitM> | |
MISCELLANEOUS | This protein may be expected to contain an N-terminal transit peptide but none has been predicted. |
end case |
Keywords
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ATP-binding | |
Ligase | |
case <FTGroup:1> | |
Magnesium | |
Metal-binding | |
end case | |
Mitochondrion | |
Nucleotide-binding | |
Tricarboxylic acid cycle |
Gene Ontology
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GO:0005524; Molecular function:ATP binding | |
case <FTGroup:1> | |
GO:0000287; Molecular function:magnesium ion binding | |
end case | |
GO:0004775; Molecular function:succinate-CoA ligase (ADP-forming) activity | |
GO:0006099; Biological process:tricarboxylic acid cycle |
Cross-references
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PROSITE | PS50975; ATP_GRASP; 1; |
PROSITE | PS01217; SUCCINYL_COA_LIG_3; 1; |
Pfam | PF08442; ATP-grasp_2; 1; |
Pfam | PF00549; Ligase_CoA; 1; |
NCBIfam | TIGR01016; sucCoAbeta; 1; |
PIRSF | PIRSF001554; SucCS_beta; 1; |
General | TransitM; -; 0-1; |
Features
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From: SUCB1_COLLI (Q9YI37) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
case <Feature:PS50975> | ||||||||||||
DOMAIN | 11 | 238 | /note="ATP-grasp" | |||||||||
end case | ||||||||||||
BINDING | 55 | 57 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
G-R-G | ||||||||
BINDING | 330 | 332 | /ligand="substrate" /ligand_note="ligand shared with subunit alpha" |
G-I-[VM] | ||||||||
BINDING | 208 | 208 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" |
N | 1 | |||||||
BINDING | 222 | 222 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" |
D | 1 | |||||||
BINDING | 48 | 48 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
K | ||||||||
BINDING | 273 | 273 | /ligand="substrate" /ligand_note="ligand shared with subunit alpha" |
N | ||||||||
SITE | 44 | 44 | /note="Important for substrate specificity" | [DN] | ||||||||
SITE | 112 | 112 | /note="Important for substrate specificity" | [YF] |
Additional information
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Size range | 405-503 amino acids |
Related rules |
MF_00558 MF_03221 |
Fusion | Nter: None Cter: None |
Comments | In animals, two different isoforms fo SCS exist, one specific for ATP and the other specific for GTP (PubMed:9765291). The two isoforms include the same alpha-subunit, but different beta-subunits (PubMed:9765290). This is the subfamily of ATP-specific beta subunits. |