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Protein

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

Gene

Suclg2

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

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 annotation

Catalytic activityi

GTP + succinate + CoA = GDP + 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 [GDP-forming] subunit beta, mitochondrial (Suclg2), Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial (Sucla2), Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (Suclg1), Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial (Suclg2)
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 sitei58GTPUniRule annotation1
Sitei80Important for substrate specificityUniRule annotation1
Binding sitei147GTP; via amide nitrogen and carbonyl oxygenUniRule annotation1
Sitei148Important for substrate specificityUniRule annotation1
Metal bindingi244MagnesiumUniRule annotation1
Metal bindingi258MagnesiumUniRule annotation1
Binding sitei309Substrate; shared with subunit alphaUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi91 – 93GTPUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

ReactomeiR-MMU-71403 Citric acid cycle (TCA cycle)
UniPathwayi
UPA00223;UER00999

Names & Taxonomyi

Protein namesi
Recommended name:
Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrialUniRule annotation (EC:6.2.1.4UniRule annotation)
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1306824 Suclg2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome 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 – 38MitochondrionBy similarityAdd BLAST38
ChainiPRO_000003335739 – 433Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrialAdd BLAST395

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei67N6-acetyllysine; alternateCombined sources1
Modified residuei67N6-succinyllysine; alternateCombined sources1
Modified residuei74N6-acetyllysineCombined sources1
Modified residuei79N6-succinyllysineCombined sources1
Modified residuei112N6-acetyllysineCombined sources1
Modified residuei133N6-acetyllysineCombined sources1
Modified residuei140N6-acetyllysineCombined sources1
Modified residuei162PhosphoserineCombined sources1
Modified residuei201N6-acetyllysineCombined sources1
Modified residuei217PhosphoserineCombined sources1
Modified residuei219N6-acetyllysineCombined sources1
Modified residuei228N6-acetyllysineCombined sources1
Modified residuei272N6-acetyllysineCombined sources1
Modified residuei339N6-succinyllysineCombined sources1
Modified residuei348N6-acetyllysineCombined sources1
Modified residuei387N6-acetyllysineCombined sources1
Modified residuei407N6-acetyllysineCombined sources1
Modified residuei424N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ9Z2I8
PeptideAtlasiQ9Z2I8
PRIDEiQ9Z2I8

2D gel databases

REPRODUCTION-2DPAGEiQ9Z2I8

PTM databases

iPTMnetiQ9Z2I8
PhosphoSitePlusiQ9Z2I8
SwissPalmiQ9Z2I8

Expressioni

Gene expression databases

BgeeiENSMUSG00000061838 Expressed in 82 organ(s), highest expression level in adult mammalian kidney
ExpressionAtlasiQ9Z2I8 baseline and differential
GenevisibleiQ9Z2I8 MM

Interactioni

Subunit structurei

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi203571, 2 interactors
CORUMiQ9Z2I8
IntActiQ9Z2I8, 6 interactors
MINTiQ9Z2I8
STRINGi10090.ENSMUSP00000078774

Structurei

3D structure databases

ProteinModelPortaliQ9Z2I8
SMRiQ9Z2I8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini47 – 275ATP-graspUniRule annotationAdd BLAST229

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni366 – 368Substrate binding; shared with subunit alphaUniRule annotation3

Sequence similaritiesi

Belongs to the succinate/malate CoA ligase beta subunit family. GTP-specific subunit beta subfamily.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2799 Eukaryota
COG0045 LUCA
GeneTreeiENSGT00390000010170
HOVERGENiHBG055555
InParanoidiQ9Z2I8
KOiK01900
OMAiVQIEINP
OrthoDBiEOG091G07T9
PhylomeDBiQ9Z2I8
TreeFamiTF300624

Family and domain databases

Gene3Di3.30.1490.20, 1 hit
3.40.50.261, 1 hit
HAMAPiMF_00558 Succ_CoA_beta, 1 hit
MF_03221 Succ_CoA_betaG_euk, 1 hit
InterProiView protein in InterPro
IPR011761 ATP-grasp
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
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
PS50975 ATP_GRASP, 1 hit
PS01217 SUCCINYL_COA_LIG_3, 1 hit

Sequences (2+)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: Q9Z2I8-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MASPVAIAAQ AGKLLRERAL RPLLAVRSQA GHLTPRRWLN LQEYQSKKLM
60 70 80 90 100
SEHGVRVQRF FVANTAKEAL EAAKRLNAKE IVLKAQILAG GRGKGVFNSG
110 120 130 140 150
LKGGVHLTKD PKVVGELAQQ MIGYNLATKQ TPKEGVKVNK VMVAEALDIS
160 170 180 190 200
RETYLAILMD RSHNGPVIVG SPQGGVDIEE VAASSPELIF KEQIDIFEGI
210 220 230 240 250
KDSQAQRMAE NLGFLGSLKN QAADQITKLY HLFLKIDATQ VEVNPFGETP
260 270 280 290 300
EGQVVCFDAK INFDDNAEFR QKDIFAMDDK SENEPIENEA ARYDLKYIGL
310 320 330 340 350
DGNIACFVNG AGLAMATCDI IFLNGGKPAN FLDLGGGVKE AQVYEAFKLL
360 370 380 390 400
TSDPKVEAIL VNIFGGIVNC AIIANGITKA CRELELKVPL VVRLEGTNVQ
410 420 430
EAQNILKSSG LPITSAVDLE DAAKKAVASV AKK
Length:433
Mass (Da):46,840
Last modified:January 10, 2006 - v3
Checksum:i8CA9C7998D2F2957
GO
Isoform 2 (identifier: Q9Z2I8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-49: Missing.

Note: No experimental confirmation available.
Show »
Length:384
Mass (Da):41,349
Checksum:i4EB7A1CB5F5A5E82
GO

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0N4SWD1A0A0N4SWD1_MOUSE
Succinate--CoA ligase [GDP-forming]...
Suclg2
83Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti66A → T in BAE43106 (PubMed:16141072).Curated1
Sequence conflicti66A → T in BAE43068 (PubMed:16141072).Curated1
Sequence conflicti168I → L in AAC64399 (PubMed:9765291).Curated1
Sequence conflicti175 – 176GV → RS in AAC64399 (PubMed:9765291).Curated2
Sequence conflicti212L → P in AAH80781 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0169051 – 49Missing in isoform 2. 1 PublicationAdd BLAST49

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK167136 mRNA Translation: BAE39282.1
AK167339 mRNA Translation: BAE39440.1
AK172561 mRNA Translation: BAE43068.1
AK172633 mRNA Translation: BAE43106.1
BC030947 mRNA Translation: AAH30947.1
BC043312 mRNA Translation: AAH43312.1
BC054425 mRNA Translation: AAH54425.1
BC080781 mRNA Translation: AAH80781.1
AF058956 mRNA Translation: AAC64399.1
CCDSiCCDS20381.1 [Q9Z2I8-1]
CCDS85100.1 [Q9Z2I8-2]
RefSeqiNP_001313487.1, NM_001326558.1 [Q9Z2I8-2]
NP_035637.2, NM_011507.3 [Q9Z2I8-1]
UniGeneiMm.371585
Mm.426727

Genome annotation databases

EnsembliENSMUST00000079847; ENSMUSP00000078774; ENSMUSG00000061838 [Q9Z2I8-2]
ENSMUST00000204224; ENSMUSP00000144827; ENSMUSG00000061838 [Q9Z2I8-1]
GeneIDi20917
KEGGimmu:20917
UCSCiuc009daa.3 mouse [Q9Z2I8-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK167136 mRNA Translation: BAE39282.1
AK167339 mRNA Translation: BAE39440.1
AK172561 mRNA Translation: BAE43068.1
AK172633 mRNA Translation: BAE43106.1
BC030947 mRNA Translation: AAH30947.1
BC043312 mRNA Translation: AAH43312.1
BC054425 mRNA Translation: AAH54425.1
BC080781 mRNA Translation: AAH80781.1
AF058956 mRNA Translation: AAC64399.1
CCDSiCCDS20381.1 [Q9Z2I8-1]
CCDS85100.1 [Q9Z2I8-2]
RefSeqiNP_001313487.1, NM_001326558.1 [Q9Z2I8-2]
NP_035637.2, NM_011507.3 [Q9Z2I8-1]
UniGeneiMm.371585
Mm.426727

3D structure databases

ProteinModelPortaliQ9Z2I8
SMRiQ9Z2I8
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203571, 2 interactors
CORUMiQ9Z2I8
IntActiQ9Z2I8, 6 interactors
MINTiQ9Z2I8
STRINGi10090.ENSMUSP00000078774

PTM databases

iPTMnetiQ9Z2I8
PhosphoSitePlusiQ9Z2I8
SwissPalmiQ9Z2I8

2D gel databases

REPRODUCTION-2DPAGEiQ9Z2I8

Proteomic databases

PaxDbiQ9Z2I8
PeptideAtlasiQ9Z2I8
PRIDEiQ9Z2I8

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000079847; ENSMUSP00000078774; ENSMUSG00000061838 [Q9Z2I8-2]
ENSMUST00000204224; ENSMUSP00000144827; ENSMUSG00000061838 [Q9Z2I8-1]
GeneIDi20917
KEGGimmu:20917
UCSCiuc009daa.3 mouse [Q9Z2I8-1]

Organism-specific databases

CTDi8801
MGIiMGI:1306824 Suclg2

Phylogenomic databases

eggNOGiKOG2799 Eukaryota
COG0045 LUCA
GeneTreeiENSGT00390000010170
HOVERGENiHBG055555
InParanoidiQ9Z2I8
KOiK01900
OMAiVQIEINP
OrthoDBiEOG091G07T9
PhylomeDBiQ9Z2I8
TreeFamiTF300624

Enzyme and pathway databases

UniPathwayi
UPA00223;UER00999

ReactomeiR-MMU-71403 Citric acid cycle (TCA cycle)

Miscellaneous databases

PROiPR:Q9Z2I8
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000061838 Expressed in 82 organ(s), highest expression level in adult mammalian kidney
ExpressionAtlasiQ9Z2I8 baseline and differential
GenevisibleiQ9Z2I8 MM

Family and domain databases

Gene3Di3.30.1490.20, 1 hit
3.40.50.261, 1 hit
HAMAPiMF_00558 Succ_CoA_beta, 1 hit
MF_03221 Succ_CoA_betaG_euk, 1 hit
InterProiView protein in InterPro
IPR011761 ATP-grasp
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
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
PS50975 ATP_GRASP, 1 hit
PS01217 SUCCINYL_COA_LIG_3, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiSUCB2_MOUSE
AccessioniPrimary (citable) accession number: Q9Z2I8
Secondary accession number(s): Q3T9B8
, Q3TJQ5, Q3TK63, Q66JT3, Q7TMY3, Q80VV1, Q8K2K9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: January 10, 2006
Last modified: October 10, 2018
This is version 163 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

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