Q9P2R7 · SUCB1_HUMAN
- ProteinSuccinate--CoA ligase [ADP-forming] subunit beta, mitochondrial
- GeneSUCLA2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids463 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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 (PubMed:15877282).
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 (By similarity).
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 (By similarity).
Catalytic activity
- ATP + CoA + succinate = ADP + phosphate + succinyl-CoA
Cofactor
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 site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 94 | Important for substrate specificity | ||||
Sequence: D | ||||||
Binding site | 98 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 105-107 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GRG | ||||||
Site | 162 | Important for substrate specificity | ||||
Sequence: Y | ||||||
Binding site | 258 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 272 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 323 | substrate; ligand shared with subunit alpha | ||||
Sequence: N | ||||||
Binding site | 380-382 | substrate; ligand shared with subunit alpha | ||||
Sequence: GIM |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular exosome | |
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrion | |
Cellular Component | succinate-CoA ligase complex | |
Cellular Component | succinate-CoA ligase complex (ADP-forming) | |
Molecular Function | ATP binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | succinate-CoA ligase (ADP-forming) activity | |
Biological Process | succinate metabolic process | |
Biological Process | succinyl-CoA catabolic process | |
Biological Process | succinyl-CoA metabolic process | |
Biological Process | succinyl-CoA pathway | |
Biological Process | tricarboxylic acid cycle |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSuccinate--CoA ligase [ADP-forming] subunit beta, mitochondrial
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9P2R7
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Mitochondrial DNA depletion syndrome 5 (MTDPS5)
- Note
- DescriptionA disorder due to mitochondrial dysfunction. It is characterized by infantile onset of hypotonia, neurologic deterioration, a hyperkinetic-dystonic movement disorder, external ophthalmoplegia, deafness, variable renal tubular dysfunction, and mild methylmalonic aciduria in some patients.
- See alsoMIM:612073
Natural variants in MTDPS5
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_046215 | 118 | G>R | in MTDPS5; dbSNP:rs121908537 | |
VAR_070123 | 251 | D>N | in MTDPS5; dbSNP:rs397515462 | |
VAR_046216 | 284 | R>C | in MTDPS5; dbSNP:rs121908538 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_046214 | 13 | in dbSNP:rs35201084 | |||
Sequence: V → M | ||||||
Natural variant | VAR_046215 | 118 | in MTDPS5; dbSNP:rs121908537 | |||
Sequence: G → R | ||||||
Natural variant | VAR_013459 | 199 | in dbSNP:rs7320366 | |||
Sequence: S → T | ||||||
Natural variant | VAR_070123 | 251 | in MTDPS5; dbSNP:rs397515462 | |||
Sequence: D → N | ||||||
Natural variant | VAR_046216 | 284 | in MTDPS5; dbSNP:rs121908538 | |||
Sequence: R → C |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 514 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Transit peptide | 1-52 | UniProt | Mitochondrion | ||||
Sequence: MAASMFYGRLVAVATLRNHRPRTAQRAAAQVLGSSGLFNNHGLQVQQQQQRN | |||||||
Chain | PRO_0000033352 | 53-463 | UniProt | Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial | |||
Sequence: LSLHEYMSMELLQEAGVSVPKGYVAKSPDEAYAIAKKLGSKDVVIKAQVLAGGRGKGTFESGLKGGVKIVFSPEEAKAVSSQMIGKKLFTKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSSHGGVNIEDVAAESPEAIIKEPIDIEEGIKKEQALQLAQKMGFPPNIVESAAENMVKLYSLFLKYDATMIEINPMVEDSDGAVLCMDAKINFDSNSAYRQKKIFDLQDWTQEDERDKDAAKANLNYIGLDGNIGCLVNGAGLAMATMDIIKLHGGTPANFLDVGGGATVHQVTEAFKLITSDKKVLAILVNIFGGIMRCDVIAQGIVMAVKDLEIKIPVVVRLQGTRVDDAKALIADSGLKILACDDLDEAARMVVKLSEIVTLAKQAHVDVKFQLPI | |||||||
Modified residue | 78 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 79 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 84 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 84 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 88 | UniProt | N6-acetyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 88 | UniProt | N6-succinyllysine; alternate | ||||
Sequence: K | |||||||
Modified residue | 129 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 139 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 143 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 216 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 279 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 279 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 341 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 368 | UniProt | N6-acetyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed. Not expressed in liver and lung.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Heterodimer of an alpha and a beta subunit. The beta subunit determines specificity for ATP (By similarity).
Interacts with ALAS2 (PubMed:14643893).
Interacts with ALAS2 (PubMed:14643893).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9P2R7 | AGTRAP Q6RW13-2 | 6 | EBI-2269898, EBI-11522760 | |
BINARY | Q9P2R7 | ARL6IP1 Q15041 | 6 | EBI-2269898, EBI-714543 | |
BINARY | Q9P2R7 | CMTM5 Q96DZ9-2 | 6 | EBI-2269898, EBI-11522780 | |
BINARY | Q9P2R7 | FKBP7 Q9Y680 | 3 | EBI-2269898, EBI-3918971 | |
BINARY | Q9P2R7 | MAGEA11 P43364 | 3 | EBI-2269898, EBI-739552 | |
BINARY | Q9P2R7 | MAL2 Q969L2 | 3 | EBI-2269898, EBI-944295 | |
BINARY | Q9P2R7 | OPTN Q96CV9 | 3 | EBI-2269898, EBI-748974 | |
BINARY | Q9P2R7 | SEC23A Q15436 | 3 | EBI-2269898, EBI-81088 | |
BINARY | Q9P2R7 | TNFRSF10D Q9UBN6 | 3 | EBI-2269898, EBI-1044859 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 61-288 | ATP-grasp | ||||
Sequence: MELLQEAGVSVPKGYVAKSPDEAYAIAKKLGSKDVVIKAQVLAGGRGKGTFESGLKGGVKIVFSPEEAKAVSSQMIGKKLFTKQTGEKGRICNQVLVCERKYPRREYYFAITMERSFQGPVLIGSSHGGVNIEDVAAESPEAIIKEPIDIEEGIKKEQALQLAQKMGFPPNIVESAAENMVKLYSLFLKYDATMIEINPMVEDSDGAVLCMDAKINFDSNSAYRQKKI |
Sequence similarities
Belongs to the succinate/malate CoA ligase beta subunit family. ATP-specific subunit beta subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
Q9P2R7-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length463
- Mass (Da)50,317
- Last updated2006-05-02 v3
- Checksum1E1651728AF3B5CD
Q9P2R7-2
- Name2
- Differences from canonical
- 26-47: Missing
Computationally mapped potential isoform sequences
There are 12 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0U1RQL1 | A0A0U1RQL1_HUMAN | SUCLA2 | 80 | ||
A0A2R8Y6Y7 | A0A2R8Y6Y7_HUMAN | SUCLA2 | 484 | ||
A0A0U1RQU7 | A0A0U1RQU7_HUMAN | SUCLA2 | 136 | ||
A0A0U1RQF8 | A0A0U1RQF8_HUMAN | SUCLA2 | 191 | ||
A0A0U1RRI1 | A0A0U1RRI1_HUMAN | SUCLA2 | 104 | ||
A0A2R8Y6E6 | A0A2R8Y6E6_HUMAN | SUCLA2 | 224 | ||
A0A2R8Y5P4 | A0A2R8Y5P4_HUMAN | SUCLA2 | 159 | ||
A0A2R8Y5P6 | A0A2R8Y5P6_HUMAN | SUCLA2 | 221 | ||
A0A2R8YDQ9 | A0A2R8YDQ9_HUMAN | SUCLA2 | 405 | ||
A0A2R8YF84 | A0A2R8YF84_HUMAN | SUCLA2 | 9 | ||
Q5T9Q5 | Q5T9Q5_HUMAN | SUCLA2 | 298 | ||
Q5T9Q8 | Q5T9Q8_HUMAN | SUCLA2 | 154 |
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_006292 | 26-47 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 40 | in Ref. 2; BAA91939 | ||||
Sequence: N → D | ||||||
Sequence conflict | 203 | in Ref. 2; BAA91939 | ||||
Sequence: I → V | ||||||
Sequence conflict | 323 | in Ref. 2; BAA91703 | ||||
Sequence: N → S |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB035863 EMBL· GenBank· DDBJ | BAA92873.1 EMBL· GenBank· DDBJ | mRNA | ||
AK001458 EMBL· GenBank· DDBJ | BAA91703.1 EMBL· GenBank· DDBJ | mRNA | ||
AK001847 EMBL· GenBank· DDBJ | BAA91939.1 EMBL· GenBank· DDBJ | mRNA | ||
AK315513 EMBL· GenBank· DDBJ | BAG37894.1 EMBL· GenBank· DDBJ | mRNA | ||
AL157369 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471075 EMBL· GenBank· DDBJ | EAX08777.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC027587 EMBL· GenBank· DDBJ | AAH27587.1 EMBL· GenBank· DDBJ | mRNA | ||
AF058953 EMBL· GenBank· DDBJ | AAC64396.1 EMBL· GenBank· DDBJ | mRNA |