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Protein

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

Gene

Sucla2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. 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 annotation

Catalytic activityi

ATP + succinate + CoA = ADP + phosphate + succinyl-CoA.UniRule annotation

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 annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial (Sucla2), Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial (Suclg2), Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (Suclg1)
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
Sitei94Important for substrate specificityUniRule annotation1
Binding sitei98ATPUniRule annotation1
Sitei162Important for substrate specificityUniRule annotation1
Metal bindingi258MagnesiumUniRule annotation1
Metal bindingi272MagnesiumUniRule annotation1
Binding sitei323Substrate; shared with subunit alphaUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi105 – 107ATPUniRule annotation3

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-71403. Citric acid cycle (TCA cycle).
UniPathwayiUPA00223; UER00999.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrialUniRule annotation (EC:6.2.1.5UniRule annotation)
Alternative name(s):
ATP-specific succinyl-CoA synthetase subunit betaUniRule annotation
Short name:
A-SCSUniRule annotation
Succinyl-CoA synthetase beta-A chainUniRule annotation
Short name:
SCS-betaAUniRule annotation
Gene namesi
Name:Sucla2UniRule annotation
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1306775. Sucla2.

Subcellular locationi

  • Mitochondrion UniRule annotation

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • mitochondrion Source: MGI
  • myelin sheath Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 53MitochondrionUniRule annotationAdd BLAST53
ChainiPRO_000003335354 – 463Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrialUniRule annotationAdd BLAST410

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei78N6-acetyllysineCombined sources1
Modified residuei84PhosphotyrosineBy similarity1
Modified residuei88N6-acetyllysine; alternateCombined sources1
Modified residuei88N6-succinyllysine; alternateCombined sources1
Modified residuei129N6-acetyllysineCombined sources1
Modified residuei139N6-acetyllysineCombined sources1
Modified residuei143N6-acetyllysineBy similarity1
Modified residuei216N6-acetyllysineCombined sources1
Modified residuei279PhosphoserineCombined sources1
Modified residuei341PhosphothreonineCombined sources1
Modified residuei368N6-acetyllysineCombined sources1
Modified residuei438N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9Z2I9.
MaxQBiQ9Z2I9.
PaxDbiQ9Z2I9.
PeptideAtlasiQ9Z2I9.
PRIDEiQ9Z2I9.

2D gel databases

REPRODUCTION-2DPAGEIPI00261627.
Q9Z2I9.
UCD-2DPAGEQ9Z2I9.

PTM databases

iPTMnetiQ9Z2I9.
PhosphoSitePlusiQ9Z2I9.
SwissPalmiQ9Z2I9.

Expressioni

Gene expression databases

BgeeiENSMUSG00000022110.
GenevisibleiQ9Z2I9. MM.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit. The beta subunit determines specificity for ATP.UniRule annotation

Protein-protein interaction databases

BioGridi203570. 1 interactor.
IntActiQ9Z2I9. 11 interactors.
MINTiMINT-1843246.
STRINGi10090.ENSMUSP00000022706.

Structurei

3D structure databases

ProteinModelPortaliQ9Z2I9.
SMRiQ9Z2I9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini61 – 288ATP-graspUniRule annotationAdd BLAST228

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni380 – 382Substrate binding; shared with subunit alphaUniRule annotation3

Sequence similaritiesi

Belongs to the succinate/malate CoA ligase beta subunit family. ATP-specific subunit beta subfamily.UniRule annotation
Contains 1 ATP-grasp domain.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2799. Eukaryota.
COG0045. LUCA.
GeneTreeiENSGT00390000010170.
HOVERGENiHBG055555.
InParanoidiQ9Z2I9.
KOiK01900.
OMAiYIESGCD.
OrthoDBiEOG091G07T9.
PhylomeDBiQ9Z2I9.
TreeFamiTF300624.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.261. 1 hit.
HAMAPiMF_00558. Succ_CoA_beta. 1 hit.
MF_03220. Succ_CoA_betaA_euk. 1 hit.
InterProiIPR011761. ATP-grasp.
IPR013650. 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.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS01217. SUCCINYL_COA_LIG_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9Z2I9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASMFYGRQ LAAAALRSHR PQTTLRAAAQ VLGNSGLFNK HGLQVQQQQQ
60 70 80 90 100
RTLSLHEYLS MELLQEAGVS VPKGFVAKSS DEAYAIAKKL GSKDVVIKAQ
110 120 130 140 150
VLAGGRGKGT FTSGLKGGVK IVFSPEEAKA VSSQMIGQKL ITKQTGEKGR
160 170 180 190 200
ICNQVLVCER KYPRREYYFA ITMERSFQGP VLIGSAQGGV NIEDVAAENP
210 220 230 240 250
EAIVKEPIDI VEGIKKEQAV TLAQKMGFPS NIVDSAAENM IKLYNLFLKY
260 270 280 290 300
DATMVEINPM VEDSDGKVLC MDAKINFDSN SAYRQKKIFD LQDWSQEDER
310 320 330 340 350
DKEAANADIN YIGLDGSIGC LVNGAGLAMA TMDIIKLHGG TPANFLDVGG
360 370 380 390 400
GATVQQVTEA FKLITSDKKV QAILVNIFGG IMRCDVIAQG IVMAVKDLEI
410 420 430 440 450
RIPVVVRLQG TRVDDAKALI ADSGLKILAC DDLDEAAKMV VKLSEIVTLA
460
KEAHVDVKFQ LPI
Length:463
Mass (Da):50,114
Last modified:September 27, 2004 - v2
Checksum:i74CE8E962BC0BB27
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK081965 mRNA. Translation: BAC38380.1.
AK088801 mRNA. Translation: BAC40580.1.
AK132762 mRNA. Translation: BAE21343.1.
AK160130 mRNA. Translation: BAE35647.1.
AK160652 mRNA. Translation: BAE35942.1.
BC056353 mRNA. Translation: AAH56353.1.
BC057605 mRNA. Translation: AAH57605.1.
AF058955 mRNA. Translation: AAC64398.1.
CCDSiCCDS27271.1.
RefSeqiNP_035636.1. NM_011506.3.
UniGeneiMm.38951.

Genome annotation databases

EnsembliENSMUST00000022706; ENSMUSP00000022706; ENSMUSG00000022110.
ENSMUST00000160507; ENSMUSP00000123765; ENSMUSG00000022110.
GeneIDi20916.
KEGGimmu:20916.
UCSCiuc007upx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK081965 mRNA. Translation: BAC38380.1.
AK088801 mRNA. Translation: BAC40580.1.
AK132762 mRNA. Translation: BAE21343.1.
AK160130 mRNA. Translation: BAE35647.1.
AK160652 mRNA. Translation: BAE35942.1.
BC056353 mRNA. Translation: AAH56353.1.
BC057605 mRNA. Translation: AAH57605.1.
AF058955 mRNA. Translation: AAC64398.1.
CCDSiCCDS27271.1.
RefSeqiNP_035636.1. NM_011506.3.
UniGeneiMm.38951.

3D structure databases

ProteinModelPortaliQ9Z2I9.
SMRiQ9Z2I9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203570. 1 interactor.
IntActiQ9Z2I9. 11 interactors.
MINTiMINT-1843246.
STRINGi10090.ENSMUSP00000022706.

PTM databases

iPTMnetiQ9Z2I9.
PhosphoSitePlusiQ9Z2I9.
SwissPalmiQ9Z2I9.

2D gel databases

REPRODUCTION-2DPAGEIPI00261627.
Q9Z2I9.
UCD-2DPAGEQ9Z2I9.

Proteomic databases

EPDiQ9Z2I9.
MaxQBiQ9Z2I9.
PaxDbiQ9Z2I9.
PeptideAtlasiQ9Z2I9.
PRIDEiQ9Z2I9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022706; ENSMUSP00000022706; ENSMUSG00000022110.
ENSMUST00000160507; ENSMUSP00000123765; ENSMUSG00000022110.
GeneIDi20916.
KEGGimmu:20916.
UCSCiuc007upx.1. mouse.

Organism-specific databases

CTDi8803.
MGIiMGI:1306775. Sucla2.

Phylogenomic databases

eggNOGiKOG2799. Eukaryota.
COG0045. LUCA.
GeneTreeiENSGT00390000010170.
HOVERGENiHBG055555.
InParanoidiQ9Z2I9.
KOiK01900.
OMAiYIESGCD.
OrthoDBiEOG091G07T9.
PhylomeDBiQ9Z2I9.
TreeFamiTF300624.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00999.
ReactomeiR-MMU-71403. Citric acid cycle (TCA cycle).

Miscellaneous databases

ChiTaRSiSucla2. mouse.
PROiQ9Z2I9.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000022110.
GenevisibleiQ9Z2I9. MM.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.261. 1 hit.
HAMAPiMF_00558. Succ_CoA_beta. 1 hit.
MF_03220. Succ_CoA_betaA_euk. 1 hit.
InterProiIPR011761. ATP-grasp.
IPR013650. 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.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS01217. SUCCINYL_COA_LIG_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSUCB1_MOUSE
AccessioniPrimary (citable) accession number: Q9Z2I9
Secondary accession number(s): Q3TVH1, Q8BGS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: September 27, 2004
Last modified: November 30, 2016
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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.