Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial

Gene

Suclg1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 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 specificity for either ATP or GTP is provided by different beta subunits.UniRule annotation

Catalytic activityi

ATP + succinate + CoA = ADP + phosphate + succinyl-CoA.UniRule annotation
GTP + succinate + CoA = GDP + phosphate + succinyl-CoA.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
Binding sitei90Coenzyme AUniRule annotation1
Binding sitei207Substrate; shared with subunit betaUniRule annotation1
Active sitei299Tele-phosphohistidine intermediateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

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/GDP-forming] subunit alpha, mitochondrialUniRule annotation (EC:6.2.1.4UniRule annotation, EC:6.2.1.5UniRule annotation)
Alternative name(s):
Succinyl-CoA synthetase subunit alphaUniRule annotation
Short name:
SCS-alphaUniRule annotation
Gene namesi
Name:Suclg1UniRule annotation
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1927234. Suclg1.

Subcellular locationi

  • Mitochondrion UniRule annotation

GO - Cellular componenti

  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • mitochondrial inner membrane Source: MGI
  • mitochondrial matrix Source: GO_Central
  • mitochondrion Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 34MitochondrionUniRule annotationAdd BLAST34
ChainiPRO_000003334135 – 346Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrialUniRule annotationAdd BLAST312

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei54N6-acetyllysineCombined sources1
Modified residuei57N6-acetyllysine; alternateCombined sources1
Modified residuei57N6-succinyllysine; alternateCombined sources1
Modified residuei66N6-acetyllysine; alternateCombined sources1
Modified residuei66N6-succinyllysine; alternateCombined sources1
Modified residuei81N6-acetyllysineCombined sources1
Modified residuei94N6-acetyllysineCombined sources1
Modified residuei105N6-acetyllysineCombined sources1
Modified residuei338N6-succinyllysineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9WUM5.
MaxQBiQ9WUM5.
PaxDbiQ9WUM5.
PeptideAtlasiQ9WUM5.
PRIDEiQ9WUM5.

PTM databases

iPTMnetiQ9WUM5.
PhosphoSitePlusiQ9WUM5.
SwissPalmiQ9WUM5.

Expressioni

Gene expression databases

BgeeiENSMUSG00000052738.
CleanExiMM_SUCLG1.
ExpressionAtlasiQ9WUM5. baseline and differential.
GenevisibleiQ9WUM5. MM.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit. Different beta subunits determine nucleotide specificity. Together with the ATP-specific beta subunit SUCLA2, forms an ADP-forming succinyl-CoA synthetase (A-SCS). Together with the GTP-specific beta subunit SUCLG2 forms a GDP-forming succinyl-CoA synthetase (G-SCS).UniRule annotation

Protein-protein interaction databases

BioGridi207990. 1 interactor.
IntActiQ9WUM5. 5 interactors.
MINTiMINT-1841915.
STRINGi10090.ENSMUSP00000065113.

Structurei

3D structure databases

ProteinModelPortaliQ9WUM5.
SMRiQ9WUM5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni64 – 67Coenzyme A bindingUniRule annotation4
Regioni143 – 145Coenzyme A bindingUniRule annotation3

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1255. Eukaryota.
COG0074. LUCA.
GeneTreeiENSGT00530000063275.
HOGENOMiHOG000239685.
HOVERGENiHBG000957.
InParanoidiQ9WUM5.
KOiK01899.
OMAiVIICITE.
OrthoDBiEOG091G0D9C.
PhylomeDBiQ9WUM5.
TreeFamiTF300666.

Family and domain databases

Gene3Di3.40.50.261. 1 hit.
3.40.50.720. 1 hit.
HAMAPiMF_01988. Succ_CoA_alpha. 1 hit.
InterProiIPR017440. Cit_synth/succinyl-CoA_lig_AS.
IPR033847. Citrt_syn/SCS-alpha_CS.
IPR003781. CoA-bd.
IPR005810. CoA_lig_alpha.
IPR005811. CoA_ligase.
IPR016040. NAD(P)-bd_dom.
IPR016102. Succinyl-CoA_synth-like.
[Graphical view]
PfamiPF02629. CoA_binding. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view]
PIRSFiPIRSF001553. SucCS_alpha. 1 hit.
SMARTiSM00881. CoA_binding. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF52210. SSF52210. 1 hit.
TIGRFAMsiTIGR01019. sucCoAalpha. 1 hit.
PROSITEiPS01216. SUCCINYL_COA_LIG_1. 1 hit.
PS00399. SUCCINYL_COA_LIG_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9WUM5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTATVVAAAA TATMVSSSSG LAAARLLSRT FLLQQNGIRH GSYTASRKHI
60 70 80 90 100
YIDKNTKIIC QGFTGKQGTF HSQQALEYGT KLVGGTTPGK GGQKHLGLPV
110 120 130 140 150
FNTVKEAKEK TGATASVIYV PPPFAAAAIN EAIDAEIPLV VCITEGIPQQ
160 170 180 190 200
DMVRVKHRLT RQGTTRLIGP NCPGVINPGE CKIGIMPGHI HKKGRIGIVS
210 220 230 240 250
RSGTLTYEAV HQTTQVGLGQ SLCIGIGGDP FNGTDFIDCL EVFLNDPATE
260 270 280 290 300
GIILIGEIGG HAEENAAAFL KEHNSGPKAK PVVSFIAGIT APPGRRMGHA
310 320 330 340
GAIIAGGKGG AKEKISALQS AGVVVSMSPA QLGTTIYKEF EKRKML
Length:346
Mass (Da):36,155
Last modified:February 10, 2009 - v4
Checksum:i1EB7A444DFCE32FA
GO

Sequence cautioni

The sequence AAD33927 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAH11087 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAB22331 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAB23804 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAC40634 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti6V → L in AAD33927 (Ref. 2) Curated1
Sequence conflicti175V → I in BAC40634 (PubMed:16141072).Curated1
Sequence conflicti188G → A in BAB22331 (PubMed:16141072).Curated1
Sequence conflicti201R → K in AAD33927 (Ref. 2) Curated1
Sequence conflicti220Q → H in AAD33927 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002754 mRNA. Translation: BAB22331.1. Different initiation.
AK005080 mRNA. Translation: BAB23804.1. Different initiation.
AK088888 mRNA. Translation: BAC40634.1. Different initiation.
AF144101 mRNA. Translation: AAD33927.2. Different initiation.
BC011087 mRNA. Translation: AAH11087.1. Different initiation.
CCDSiCCDS20246.2.
RefSeqiNP_063932.2. NM_019879.3.
UniGeneiMm.29845.

Genome annotation databases

EnsembliENSMUST00000064740; ENSMUSP00000065113; ENSMUSG00000052738.
GeneIDi56451.
KEGGimmu:56451.
UCSCiuc009cjm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002754 mRNA. Translation: BAB22331.1. Different initiation.
AK005080 mRNA. Translation: BAB23804.1. Different initiation.
AK088888 mRNA. Translation: BAC40634.1. Different initiation.
AF144101 mRNA. Translation: AAD33927.2. Different initiation.
BC011087 mRNA. Translation: AAH11087.1. Different initiation.
CCDSiCCDS20246.2.
RefSeqiNP_063932.2. NM_019879.3.
UniGeneiMm.29845.

3D structure databases

ProteinModelPortaliQ9WUM5.
SMRiQ9WUM5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207990. 1 interactor.
IntActiQ9WUM5. 5 interactors.
MINTiMINT-1841915.
STRINGi10090.ENSMUSP00000065113.

PTM databases

iPTMnetiQ9WUM5.
PhosphoSitePlusiQ9WUM5.
SwissPalmiQ9WUM5.

Proteomic databases

EPDiQ9WUM5.
MaxQBiQ9WUM5.
PaxDbiQ9WUM5.
PeptideAtlasiQ9WUM5.
PRIDEiQ9WUM5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000064740; ENSMUSP00000065113; ENSMUSG00000052738.
GeneIDi56451.
KEGGimmu:56451.
UCSCiuc009cjm.2. mouse.

Organism-specific databases

CTDi8802.
MGIiMGI:1927234. Suclg1.

Phylogenomic databases

eggNOGiKOG1255. Eukaryota.
COG0074. LUCA.
GeneTreeiENSGT00530000063275.
HOGENOMiHOG000239685.
HOVERGENiHBG000957.
InParanoidiQ9WUM5.
KOiK01899.
OMAiVIICITE.
OrthoDBiEOG091G0D9C.
PhylomeDBiQ9WUM5.
TreeFamiTF300666.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiSuclg1. mouse.
PROiQ9WUM5.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000052738.
CleanExiMM_SUCLG1.
ExpressionAtlasiQ9WUM5. baseline and differential.
GenevisibleiQ9WUM5. MM.

Family and domain databases

Gene3Di3.40.50.261. 1 hit.
3.40.50.720. 1 hit.
HAMAPiMF_01988. Succ_CoA_alpha. 1 hit.
InterProiIPR017440. Cit_synth/succinyl-CoA_lig_AS.
IPR033847. Citrt_syn/SCS-alpha_CS.
IPR003781. CoA-bd.
IPR005810. CoA_lig_alpha.
IPR005811. CoA_ligase.
IPR016040. NAD(P)-bd_dom.
IPR016102. Succinyl-CoA_synth-like.
[Graphical view]
PfamiPF02629. CoA_binding. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view]
PIRSFiPIRSF001553. SucCS_alpha. 1 hit.
SMARTiSM00881. CoA_binding. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF52210. SSF52210. 1 hit.
TIGRFAMsiTIGR01019. sucCoAalpha. 1 hit.
PROSITEiPS01216. SUCCINYL_COA_LIG_1. 1 hit.
PS00399. SUCCINYL_COA_LIG_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSUCA_MOUSE
AccessioniPrimary (citable) accession number: Q9WUM5
Secondary accession number(s): Q8C2C3, Q9DBA3, Q9DCI8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: February 10, 2009
Last modified: November 30, 2016
This is version 158 of the entry and version 4 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.