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Protein

Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial

Gene

LSC2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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:9874242). 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).UniRule annotation1 Publication

Catalytic activityi

ATP + succinate + CoA = ADP + phosphate + succinyl-CoA.UniRule annotation1 Publication

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Pathwayi: tricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes succinate from succinyl-CoA (ligase route).UniRule annotation1 Publication
Proteins known to be involved in this subpathway in this organism are:
  1. Succinate--CoA ligase [ADP-forming] subunit alpha, mitochondrial (LSC1), Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial (LSC2)
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 keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei76ATPUniRule annotation1
Binding sitei144ATPUniRule annotation1
Metal bindingi236MagnesiumUniRule annotation1
Metal bindingi253MagnesiumUniRule annotation1
Binding sitei304Substrate; shared with subunit alphaUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi83 – 85ATPUniRule annotation3

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • succinate-CoA ligase (ADP-forming) activity Source: SGD

GO - Biological processi

  • succinyl-CoA metabolic process Source: SGD
  • tricarboxylic acid cycle Source: SGD

Keywordsi

Molecular functionLigase
Biological processTricarboxylic acid cycle
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:YGR244C-MONOMER
ReactomeiR-SCE-71403 Citric acid cycle (TCA cycle)
UniPathwayiUPA00223; UER00999

Names & Taxonomyi

Protein namesi
Recommended name:
Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrialUniRule annotation1 Publication (EC:6.2.1.5UniRule annotation1 Publication)
Alternative name(s):
Succinyl-CoA synthetase beta chainUniRule annotation
Short name:
SCS-betaUniRule annotation
Gene namesi
Name:LSC21 Publication
Ordered Locus Names:YGR244CImported
ORF Names:G8625
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGR244C
SGDiS000003476 LSC2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 30MitochondrionUniRule annotationAdd BLAST30
ChainiPRO_000003336531 – 427Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrialUniRule annotationAdd BLAST397

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei102PhosphoserineCombined sources1
Modified residuei263PhosphoserineCombined sources1
Modified residuei276PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53312
PaxDbiP53312
PRIDEiP53312

2D gel databases

UCD-2DPAGEiP53312

PTM databases

iPTMnetiP53312

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit.UniRule annotation

Protein-protein interaction databases

BioGridi33495, 121 interactors
DIPiDIP-4003N
IntActiP53312, 2 interactors
MINTiP53312
STRINGi4932.YGR244C

Structurei

3D structure databases

ProteinModelPortaliP53312
SMRiP53312
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini39 – 284ATP-graspUniRule annotationAdd BLAST246

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni361 – 363Substrate binding; shared with subunit alphaUniRule annotation3

Sequence similaritiesi

Belongs to the succinate/malate CoA ligase beta subunit family.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00390000010170
HOGENOMiHOG000007059
InParanoidiP53312
KOiK01900
OMAiLCMDAKF
OrthoDBiEOG092C2IGW

Family and domain databases

Gene3Di3.30.1490.20, 1 hit
3.40.50.261, 1 hit
HAMAPiMF_00558 Succ_CoA_beta, 1 hit
InterProiView protein in InterPro
IPR013650 ATP-grasp_succ-CoA_synth-type
IPR013815 ATP_grasp_subdomain_1
IPR005811 CoA_ligase
IPR017866 Succ-CoA_synthase_bsu_CS
IPR005809 Succ_CoA_synthase_bsu
IPR016102 Succinyl-CoA_synth-like
PANTHERiPTHR11815 PTHR11815, 1 hit
PfamiView protein in Pfam
PF08442 ATP-grasp_2, 1 hit
PF00549 Ligase_CoA, 1 hit
PIRSFiPIRSF001554 SucCS_beta, 1 hit
SUPFAMiSSF52210 SSF52210, 1 hit
TIGRFAMsiTIGR01016 sucCoAbeta, 1 hit
PROSITEiView protein in PROSITE
PS01217 SUCCINYL_COA_LIG_3, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P53312-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYSRKSLSLI SKCGQLSRLN AQAALQARRH LSIHEYRSAQ LLREYGIGTP
60 70 80 90 100
EGFPAFTPEE AFEAAKKLNT NKLVIKAQAL TGGRGKGHFD TGYKSGVHMI
110 120 130 140 150
ESPQQAEDVA KEMLNHNLIT KQTGIAGKPV SAVYIVKRVD TKHEAYLSIL
160 170 180 190 200
MDRQTKKPMI IASSQGGMNI EEVAERTPDA IKKFSIETSK GLSPQMAKDV
210 220 230 240 250
AKSLGFSPDA QDEAAKAVSN LYKIFMERDA TQVEINPLSE IEHDPTHKIM
260 270 280 290 300
CTDAKFGFDD NASFRQEKIY SWRDLSQEDP DEVKAKKYDL NFVKLKGNIG
310 320 330 340 350
CLVNGAGLAM ATMDVIKLNG GDPANFLDCG GGATPETIKQ GFELILSNKN
360 370 380 390 400
VDAIFVNIFG GIVRCDYVAL GLVEAARELE VRVPIVARLQ GTKVEEGRDI
410 420
INKSGVKIYS FDELDPAAKK VVELTQN
Length:427
Mass (Da):46,901
Last modified:October 1, 1996 - v1
Checksum:i12DF242D4D148648
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z73029 Genomic DNA Translation: CAA97273.1
BK006941 Genomic DNA Translation: DAA08335.1
PIRiS64570
RefSeqiNP_011760.3, NM_001181373.3

Genome annotation databases

EnsemblFungiiYGR244C; YGR244C; YGR244C
GeneIDi853159
KEGGisce:YGR244C

Similar proteinsi

Entry informationi

Entry nameiSUCB_YEAST
AccessioniPrimary (citable) accession number: P53312
Secondary accession number(s): D6VV24
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 23, 2018
This is version 170 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

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