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Protein

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

Gene

LSC2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + succinate + CoA = ADP + phosphate + succinyl-CoA.1 Publication

Pathwayi: tricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes succinate from succinyl-CoA (ligase route).
Proteins known to be involved in this subpathway in this organism are:
  1. Succinyl-CoA ligase [ADP-forming] subunit alpha, mitochondrial (LSC1), Succinyl-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.

GO - Molecular functioni

  • ATP 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
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

ATP-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:
Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial (EC:6.2.1.5)
Alternative name(s):
Succinyl-CoA synthetase beta chain
Short name:
SCS-beta
Gene namesi
Name:LSC2
Ordered Locus Names:YGR244C
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

GO - Cellular componenti

  • mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 427Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrialPRO_0000033365
Transit peptidei1 – ?MitochondrionSequence analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei102 – 1021PhosphoserineCombined sources
Modified residuei263 – 2631PhosphoserineCombined sources
Modified residuei276 – 2761PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53312.

2D gel databases

UCD-2DPAGEP53312.

PTM databases

iPTMnetiP53312.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit.By similarity

Protein-protein interaction databases

BioGridi33495. 70 interactions.
DIPiDIP-4003N.
IntActiP53312. 2 interactions.
MINTiMINT-520241.

Structurei

3D structure databases

ProteinModelPortaliP53312.
SMRiP53312. Positions 31-422.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 267229ATP-graspAdd
BLAST

Sequence similaritiesi

Contains 1 ATP-grasp domain.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00390000010170.
HOGENOMiHOG000007059.
InParanoidiP53312.
KOiK01900.
OMAiYIESGCD.
OrthoDBiEOG7DJSWM.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.261. 1 hit.
InterProiIPR013650. ATP-grasp_succ-CoA_synth-type.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR005811. CoA_ligase.
IPR017866. Succ-CoA_synthase_bsu_CS.
IPR005809. Succ_CoA_synthase_bsu.
IPR016102. Succinyl-CoA_synth-like.
[Graphical view]
PANTHERiPTHR11815. PTHR11815. 1 hit.
PfamiPF08442. ATP-grasp_2. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view]
PIRSFiPIRSF001554. SucCS_beta. 1 hit.
SUPFAMiSSF52210. SSF52210. 1 hit.
TIGRFAMsiTIGR01016. sucCoAbeta. 1 hit.
PROSITEiPS01217. SUCCINYL_COA_LIG_3. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP53312.
SMRiP53312. Positions 31-422.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33495. 70 interactions.
DIPiDIP-4003N.
IntActiP53312. 2 interactions.
MINTiMINT-520241.

PTM databases

iPTMnetiP53312.

2D gel databases

UCD-2DPAGEP53312.

Proteomic databases

MaxQBiP53312.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR244C; YGR244C; YGR244C.
GeneIDi853159.
KEGGisce:YGR244C.

Organism-specific databases

EuPathDBiFungiDB:YGR244C.
SGDiS000003476. LSC2.

Phylogenomic databases

GeneTreeiENSGT00390000010170.
HOGENOMiHOG000007059.
InParanoidiP53312.
KOiK01900.
OMAiYIESGCD.
OrthoDBiEOG7DJSWM.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP53312.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.261. 1 hit.
InterProiIPR013650. ATP-grasp_succ-CoA_synth-type.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR005811. CoA_ligase.
IPR017866. Succ-CoA_synthase_bsu_CS.
IPR005809. Succ_CoA_synthase_bsu.
IPR016102. Succinyl-CoA_synth-like.
[Graphical view]
PANTHERiPTHR11815. PTHR11815. 1 hit.
PfamiPF08442. ATP-grasp_2. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view]
PIRSFiPIRSF001554. SucCS_beta. 1 hit.
SUPFAMiSSF52210. SSF52210. 1 hit.
TIGRFAMsiTIGR01016. sucCoAbeta. 1 hit.
PROSITEiPS01217. SUCCINYL_COA_LIG_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequencing of a 9.9 kb segment on the right arm of yeast chromosome VII reveals four open reading frames, including PFK1, the gene coding for succinyl-CoA synthetase (beta-chain) and two ORFs sharing homology with ORFs of the yeast chromosome VIII."
    Guerreiro P., Azevedo D., Barreiros T., Rodrigues-Pousada C.
    Yeast 13:275-280(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: FUNCTION, CATALYTIC ACTIVITY.
  5. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  6. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; SER-263 AND SER-276, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSUCB_YEAST
AccessioniPrimary (citable) accession number: P53312
Secondary accession number(s): D6VV24
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 6, 2016
This is version 152 of the entry and version 1 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.