UniProtKB - P53590 (SUCB2_PIG)
Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial
SUCLG2
Functioni
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.
UniRule annotation2 PublicationsCatalytic activityi
- EC:6.2.1.4UniRule annotation2 Publications
Cofactori
Kineticsi
- KM=0.76 mM for succinate1 Publication
- Vmax=5.99 µmol/min/mg enzyme1 Publication
: tricarboxylic acid cycle Pathwayi
This protein is involved in step 1 of the subpathway that synthesizes succinate from succinyl-CoA (ligase route).UniRule annotation1 Publication This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.View all proteins of this organism that are known to be involved in the subpathway that synthesizes succinate from succinyl-CoA (ligase route), the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 58 | GTPUniRule annotation1 Publication | 1 | |
Sitei | 80 | Important for substrate specificityUniRule annotation | 1 | |
Binding sitei | 147 | GTP; via amide nitrogen and carbonyl oxygenUniRule annotation1 Publication | 1 | |
Sitei | 148 | Important for substrate specificityUniRule annotation | 1 | |
Metal bindingi | 244 | MagnesiumUniRule annotation1 Publication | 1 | |
Metal bindingi | 258 | MagnesiumUniRule annotation1 Publication | 1 | |
Binding sitei | 309 | Substrate; shared with subunit alphaUniRule annotation1 Publication | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 91 – 93 | GTPUniRule annotation1 Publication | 3 |
GO - Molecular functioni
- ATP binding Source: InterPro
- GTP binding Source: UniProtKB-KW
- metal ion binding Source: UniProtKB-KW
- succinate-CoA ligase (GDP-forming) activity Source: GO_Central
GO - Biological processi
- succinyl-CoA metabolic process Source: GO_Central
- tricarboxylic acid cycle Source: GO_Central
Keywordsi
Molecular function | Ligase |
Biological process | Tricarboxylic acid cycle |
Ligand | GTP-binding, Magnesium, Metal-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDAi | 6.2.1.4, 6170 |
SABIO-RKi | P53590 |
UniPathwayi | UPA00223;UER00999 |
Names & Taxonomyi
Protein namesi | Recommended name: Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrialUniRule annotation (EC:6.2.1.4UniRule annotation2 Publications)Alternative name(s): GTP-specific succinyl-CoA synthetase subunit betaUniRule annotation Short name: G-SCSUniRule annotation Short name: GTPSCSUniRule annotation Succinyl-CoA synthetase beta-G chainUniRule annotation Short name: SCS-betaGUniRule annotation |
Gene namesi | Name:SUCLG2UniRule annotation |
Organismi | Sus scrofa (Pig) |
Taxonomic identifieri | 9823 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Suina › Suidae › Sus |
Proteomesi |
|
Subcellular locationi
Mitochondrion
- Mitochondrion UniRule annotation
Mitochondrion
- mitochondrion Source: GO_Central
Other locations
- succinate-CoA ligase complex Source: GO_Central
Keywords - Cellular componenti
MitochondrionPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transit peptidei | ‹1 – 38 | MitochondrionAdd BLAST | ›38 | |
ChainiPRO_0000033358 | 39 – 433 | Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrialUniRule annotationAdd BLAST | 395 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 74 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 79 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 133 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 140 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 162 | PhosphoserineBy similarity | 1 | |
Modified residuei | 201 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 228 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 272 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 292 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 339 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 348 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 387 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 424 | N6-acetyllysineBy similarity | 1 |
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
PaxDbi | P53590 |
PeptideAtlasi | P53590 |
PRIDEi | P53590 |
Interactioni
Subunit structurei
Heterodimer of an alpha and a beta subunit. The beta subunit determines specificity for GTP.
UniRule annotation4 PublicationsBinary interactionsi
P53590
With | #Exp. | IntAct |
---|---|---|
SUCLG1 [O19069] | 2 | EBI-7317595,EBI-9024832 |
Protein-protein interaction databases
CORUMi | P53590 |
IntActi | P53590, 1 interactor |
MINTi | P53590 |
STRINGi | 9823.ENSSSCP00000012257 |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P53590 |
SMRi | P53590 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P53590 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 47 – 275 | ATP-graspUniRule annotationAdd BLAST | 229 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 366 – 368 | Substrate binding; shared with subunit alphaUniRule annotation1 Publication | 3 |
Sequence similaritiesi
Keywords - Domaini
Transit peptidePhylogenomic databases
eggNOGi | KOG1447, Eukaryota |
InParanoidi | P53590 |
Family and domain databases
Gene3Di | 3.30.1490.20, 1 hit 3.40.50.261, 1 hit |
HAMAPi | MF_00558, Succ_CoA_beta, 1 hit MF_03221, Succ_CoA_betaG_euk, 1 hit |
InterProi | View protein in InterPro IPR013650, ATP-grasp_succ-CoA_synth-type IPR013815, ATP_grasp_subdomain_1 IPR005811, CoA_ligase IPR017866, Succ-CoA_synthase_bsu_CS IPR034722, Succ_CoA_betaG_euk IPR005809, Succ_CoA_synthase_bsu IPR016102, Succinyl-CoA_synth-like |
PANTHERi | PTHR11815, PTHR11815, 1 hit |
Pfami | View protein in Pfam PF08442, ATP-grasp_2, 1 hit PF00549, Ligase_CoA, 1 hit |
PIRSFi | PIRSF001554, SucCS_beta, 1 hit |
SUPFAMi | SSF52210, SSF52210, 1 hit |
TIGRFAMsi | TIGR01016, sucCoAbeta, 1 hit |
PROSITEi | View protein in PROSITE PS01217, SUCCINYL_COA_LIG_3, 1 hit |
i Sequence
Sequence statusi: Fragment.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
IPAAPVAAQA RKLLRDLAFR PPLLAARSQV VQLTPRRWLN LQEYQSKKLM
60 70 80 90 100
SDNGVKVQRF FVADTANEAL EAAKRLNAKE IVLKAQILAG GRGKGVFSSG
110 120 130 140 150
LKGGVHLTKD PEVVGQLAKQ MIGYNLATKQ TPKEGVKVNK VMVAEALDIS
160 170 180 190 200
RETYLAILMD RSCNGPVLVG SPQGGVDIEE VAASNPELIF KEQIDIIEGI
210 220 230 240 250
KDSQAQRMAE NLGFLGPLQN QAADQIKKLY NLFLKIDATQ VEVNPFGETP
260 270 280 290 300
EGQVVCFDAK INFDDNAEFR QKDIFAMDDK SENEPIENEA AKYDLKYIGL
310 320 330 340 350
DGNIACFVNG AGLAMATCDI IFLNGGKPAN FLDLGGGVKE SQVYQAFKLL
360 370 380 390 400
TADPKVEAIL VNIFGGIVNC AIIANGITKA CRELELKVPL VVRLEGTNVH
410 420 430
EAQNILTNSG LPITSAVDLE DAAKKAVASV TKK
Sequence cautioni
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Non-terminal residuei | 1 | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L06944 mRNA Translation: AAA31120.1 Different initiation. Z81187 mRNA Translation: CAB03559.1 |
PIRi | A44529 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L06944 mRNA Translation: AAA31120.1 Different initiation. Z81187 mRNA Translation: CAB03559.1 |
PIRi | A44529 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1EUC | X-ray | 2.10 | B | 39-433 | [»] | |
1EUD | X-ray | 2.10 | B | 39-433 | [»] | |
2FP4 | X-ray | 2.08 | B | 40-433 | [»] | |
2FPG | X-ray | 2.96 | B | 40-433 | [»] | |
2FPI | X-ray | 2.70 | B | 40-433 | [»] | |
2FPP | X-ray | 2.35 | B | 40-433 | [»] | |
4XX0 | X-ray | 2.10 | B | 40-433 | [»] | |
5CAE | X-ray | 2.20 | B | 40-433 | [»] | |
6XRU | X-ray | 1.40 | B | 39-433 | [»] | |
7JFP | X-ray | 2.55 | B | 39-433 | [»] | |
7JJ0 | X-ray | 2.25 | B/D | 39-433 | [»] | |
7JKR | X-ray | 2.64 | B | 39-433 | [»] | |
7JMK | X-ray | 2.50 | B/D | 39-433 | [»] | |
AlphaFoldDBi | P53590 | |||||
SMRi | P53590 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
CORUMi | P53590 |
IntActi | P53590, 1 interactor |
MINTi | P53590 |
STRINGi | 9823.ENSSSCP00000012257 |
Proteomic databases
PaxDbi | P53590 |
PeptideAtlasi | P53590 |
PRIDEi | P53590 |
Phylogenomic databases
eggNOGi | KOG1447, Eukaryota |
InParanoidi | P53590 |
Enzyme and pathway databases
UniPathwayi | UPA00223;UER00999 |
BRENDAi | 6.2.1.4, 6170 |
SABIO-RKi | P53590 |
Miscellaneous databases
EvolutionaryTracei | P53590 |
Family and domain databases
Gene3Di | 3.30.1490.20, 1 hit 3.40.50.261, 1 hit |
HAMAPi | MF_00558, Succ_CoA_beta, 1 hit MF_03221, Succ_CoA_betaG_euk, 1 hit |
InterProi | View protein in InterPro IPR013650, ATP-grasp_succ-CoA_synth-type IPR013815, ATP_grasp_subdomain_1 IPR005811, CoA_ligase IPR017866, Succ-CoA_synthase_bsu_CS IPR034722, Succ_CoA_betaG_euk IPR005809, Succ_CoA_synthase_bsu IPR016102, Succinyl-CoA_synth-like |
PANTHERi | PTHR11815, PTHR11815, 1 hit |
Pfami | View protein in Pfam PF08442, ATP-grasp_2, 1 hit PF00549, Ligase_CoA, 1 hit |
PIRSFi | PIRSF001554, SucCS_beta, 1 hit |
SUPFAMi | SSF52210, SSF52210, 1 hit |
TIGRFAMsi | TIGR01016, sucCoAbeta, 1 hit |
PROSITEi | View protein in PROSITE PS01217, SUCCINYL_COA_LIG_3, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | SUCB2_PIG | |
Accessioni | P53590Primary (citable) accession number: P53590 Secondary accession number(s): Q95279 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1996 |
Last sequence update: | May 27, 2002 | |
Last modified: | May 25, 2022 | |
This is version 159 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families