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UniProtKB - P09143 (SUCD_THETH)
Protein
Succinate--CoA ligase [GDP-forming] subunit alpha
Gene
sucD
Organism
Thermus thermophilus
Status
Functioni
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 alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit (By similarity).
Can use either ATP or GTP, but prefers GTP (PubMed:22751660).
UniRule annotation1 PublicationCatalytic activityi
- EC:6.2.1.41 Publication
Kineticsi
- KM=121 µM for ATP1 Publication
- KM=24 µM for GTP1 Publication
- KM=1.4 mM for succinate1 Publication
- KM=5.5 µM for CoA1 Publication
pH dependencei
Optimum pH is 8.0-8.4.1 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 | 42 | Coenzyme AUniRule annotation | 1 | |
Binding sitei | 158 | Substrate; shared with subunit betaUniRule annotation | 1 | |
Active sitei | 246 | Tele-phosphohistidine intermediateUniRule annotation1 Publication | 1 |
GO - Molecular functioni
- nucleotide binding Source: UniProtKB-KW
- succinate-CoA ligase (ADP-forming) activity Source: UniProtKB-UniRule
- succinate-CoA ligase (GDP-forming) activity Source: UniProtKB-EC
GO - Biological processi
- tricarboxylic acid cycle Source: UniProtKB-UniRule
Keywordsi
Molecular function | Ligase |
Biological process | Tricarboxylic acid cycle |
Ligand | Nucleotide-binding |
Enzyme and pathway databases
UniPathwayi | UPA00223;UER00999 |
Names & Taxonomyi
Protein namesi | Recommended name: Succinate--CoA ligase [GDP-forming] subunit alpha1 Publication (EC:6.2.1.41 Publication)Alternative name(s): Succinyl-CoA synthetase subunit alphaUniRule annotation Short name: SCS-alphaUniRule annotation |
Gene namesi | Name:sucDUniRule annotation Synonyms:scsA |
Organismi | Thermus thermophilus |
Taxonomic identifieri | 274 [NCBI] |
Taxonomic lineagei | Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000102807 | 1 – 288 | Succinate--CoA ligase [GDP-forming] subunit alphaAdd BLAST | 288 |
Interactioni
Subunit structurei
Heterotetramer of two alpha and two beta subunits.
UniRule annotation1 PublicationStructurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
AlphaFoldDBi | P09143 |
SMRi | P09143 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P09143 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 16 – 19 | Coenzyme A bindingUniRule annotation | 4 | |
Regioni | 95 – 97 | Coenzyme A bindingUniRule annotation | 3 |
Sequence similaritiesi
Belongs to the succinate/malate CoA ligase alpha subunit family.UniRule annotation
Family and domain databases
Gene3Di | 3.40.50.261, 1 hit |
HAMAPi | MF_01988, Succ_CoA_alpha, 1 hit |
InterProi | View protein in InterPro IPR017440, Cit_synth/succinyl-CoA_lig_AS IPR033847, Citrt_syn/SCS-alpha_CS IPR003781, CoA-bd IPR005810, CoA_lig_alpha IPR005811, CoA_ligase IPR036291, NAD(P)-bd_dom_sf IPR016102, Succinyl-CoA_synth-like |
Pfami | View protein in Pfam PF02629, CoA_binding, 1 hit PF00549, Ligase_CoA, 1 hit |
PIRSFi | PIRSF001553, SucCS_alpha, 1 hit |
SMARTi | View protein in SMART SM00881, CoA_binding, 1 hit |
SUPFAMi | SSF51735, SSF51735, 1 hit SSF52210, SSF52210, 1 hit |
TIGRFAMsi | TIGR01019, sucCoAalpha, 1 hit |
PROSITEi | View protein in PROSITE PS01216, SUCCINYL_COA_LIG_1, 1 hit PS00399, SUCCINYL_COA_LIG_2, 1 hit |
i Sequence
Sequence statusi: Complete.
P09143-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MILVNRETRV LVQGITGREG QFHTKQMLDY GTKIVAGVTP GKGGTEVLGV
60 70 80 90 100
PVYDTVKEAV AHHEVDASII FVPAPAAADA ALEAAHAGIP LIVLITEGIP
110 120 130 140 150
TLDMVRAVEE IKALGSRLIG GNCPGIISAE ETKIGIMPGH VFKRGRVGII
160 170 180 190 200
SRSGTLTYEA AAALSQAGLG TTTTVGIGGD PVIGTTFKDL LPLFNEDPET
210 220 230 240 250
EAVVLIGEIG GSDEEEAAAW VKDHMKKPVV GFIGGRSAPK GKRMGHAGAI
260 270 280
IMGNVGTPES KLRAFAEAGI PVADTIDEIV ELVKKALG
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 130 – 132 | EET → HLP in AAA27504 (PubMed:3186449).Curated | 3 | |
Sequence conflicti | 157 – 158 | TY → RH in AAA27504 (PubMed:3186449).Curated | 2 | |
Sequence conflicti | 183 – 185 | IGT → RRL in AAA27504 (PubMed:3186449).Curated | 3 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M35832 Genomic DNA Translation: AAA27504.2 X56033 Genomic DNA Translation: CAA39507.1 X54073 Genomic DNA Translation: CAA38007.1 |
RefSeqi | WP_014509987.1, NZ_LR027517.1 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M35832 Genomic DNA Translation: AAA27504.2 X56033 Genomic DNA Translation: CAA39507.1 X54073 Genomic DNA Translation: CAA38007.1 |
RefSeqi | WP_014509987.1, NZ_LR027517.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1OI7 | X-ray | 1.23 | A | 1-288 | [»] | |
3UFX | X-ray | 2.35 | A/D/F/H | 1-288 | [»] | |
AlphaFoldDBi | P09143 | |||||
SMRi | P09143 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Enzyme and pathway databases
UniPathwayi | UPA00223;UER00999 |
Miscellaneous databases
EvolutionaryTracei | P09143 |
Family and domain databases
Gene3Di | 3.40.50.261, 1 hit |
HAMAPi | MF_01988, Succ_CoA_alpha, 1 hit |
InterProi | View protein in InterPro IPR017440, Cit_synth/succinyl-CoA_lig_AS IPR033847, Citrt_syn/SCS-alpha_CS IPR003781, CoA-bd IPR005810, CoA_lig_alpha IPR005811, CoA_ligase IPR036291, NAD(P)-bd_dom_sf IPR016102, Succinyl-CoA_synth-like |
Pfami | View protein in Pfam PF02629, CoA_binding, 1 hit PF00549, Ligase_CoA, 1 hit |
PIRSFi | PIRSF001553, SucCS_alpha, 1 hit |
SMARTi | View protein in SMART SM00881, CoA_binding, 1 hit |
SUPFAMi | SSF51735, SSF51735, 1 hit SSF52210, SSF52210, 1 hit |
TIGRFAMsi | TIGR01019, sucCoAalpha, 1 hit |
PROSITEi | View protein in PROSITE PS01216, SUCCINYL_COA_LIG_1, 1 hit PS00399, SUCCINYL_COA_LIG_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | SUCD_THETH | |
Accessioni | P09143Primary (citable) accession number: P09143 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1989 |
Last sequence update: | July 1, 1989 | |
Last modified: | May 25, 2022 | |
This is version 129 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- 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