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Protein

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

Gene

Suclg1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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/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 Publication1

GO - Molecular functioni

  • cofactor binding Source: InterPro
  • GDP binding Source: RGD
  • GTP binding Source: UniProtKB-KW
  • protein heterodimerization activity Source: RGD
  • succinate-CoA ligase (ADP-forming) activity Source: RGD
  • succinate-CoA ligase (GDP-forming) activity Source: RGD

GO - Biological processi

  • nucleoside triphosphate biosynthetic process Source: GO_Central
  • succinate metabolic process Source: RGD
  • succinyl-CoA metabolic process Source: RGD
  • tricarboxylic acid cycle Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

Nucleotide-binding

Enzyme and pathway databases

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi619821. Suclg1.

Subcellular locationi

  • Mitochondrion UniRule annotation

GO - Cellular componenti

  • mitochondrion Source: RGD
  • protein complex Source: RGD
  • succinate-CoA ligase complex (GDP-forming) Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 34MitochondrionUniRule annotationAdd BLAST34
ChainiPRO_000003334335 – 346Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrialUniRule annotationAdd BLAST312

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei54N6-acetyllysineBy similarity1
Modified residuei57N6-acetyllysine; alternateBy similarity1
Modified residuei57N6-succinyllysine; alternateBy similarity1
Modified residuei66N6-acetyllysine; alternateBy similarity1
Modified residuei66N6-succinyllysine; alternateBy similarity1
Modified residuei81N6-acetyllysineBy similarity1
Modified residuei94N6-acetyllysineBy similarity1
Modified residuei105N6-acetyllysineBy similarity1
Modified residuei338N6-succinyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP13086.
PRIDEiP13086.

PTM databases

iPTMnetiP13086.
PhosphoSitePlusiP13086.
SwissPalmiP13086.

Expressioni

Gene expression databases

BgeeiENSRNOG00000005587.
GenevisibleiP13086. RN.

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

GO - Molecular functioni

  • protein heterodimerization activity Source: RGD

Protein-protein interaction databases

BioGridi250390. 1 interactor.
IntActiP13086. 1 interactor.
STRINGi10116.ENSRNOP00000007624.

Structurei

3D structure databases

ProteinModelPortaliP13086.
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.
HOGENOMiHOG000239685.
HOVERGENiHBG000957.
InParanoidiP13086.
KOiK01899.
OrthoDBiEOG091G0D9C.
PhylomeDBiP13086.
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.

P13086-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAAVVAAAA TATMVSGSSG LAAARLLSRT FLLQQNGIRH GSYTASRKNI
60 70 80 90 100
YIDKNTKVIC QGFTGKQGTF HSQQALEYGT KLVGGTTPGK GGKKHLGLPV
110 120 130 140 150
FNTVKEAKEK TGATASVIYV PPPFAAAAIN EAIDAEIPLV VCITEGIPQQ
160 170 180 190 200
DMVRVKHKLT RQGKTRLIGP NCPGIINPGE CKIGIMPGHI HKKGRIGIVS
210 220 230 240 250
RSGTLTYEAV HQTTQVGLGQ SLCIGIGGDP FNGTNFIDCL DVFLKDPATE
260 270 280 290 300
GIVLIGEIGG HAEENAAEFL KEHNSGPKAK PVVSFIAGIT APPGRRMGHA
310 320 330 340
GAIIAGGKGG AKEKISALQS AGVIVSMSPA QLGTCMYKEF EKRKML
Length:346
Mass (Da):36,148
Last modified:February 10, 2009 - v2
Checksum:i2DDFC746C11B5B0C
GO

Sequence cautioni

The sequence AAA41233 differs from that shown. Chimeric cDNA.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti153V → L in AAA41233 (PubMed:3422742).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC061537 mRNA. Translation: AAH61537.2.
J03621 mRNA. Translation: AAA41233.1. Sequence problems.
PIRiA28962. SYRTSA.
RefSeqiNP_446204.2. NM_053752.2.
UniGeneiRn.3766.

Genome annotation databases

GeneIDi114597.
KEGGirno:114597.
UCSCiRGD:619821. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC061537 mRNA. Translation: AAH61537.2.
J03621 mRNA. Translation: AAA41233.1. Sequence problems.
PIRiA28962. SYRTSA.
RefSeqiNP_446204.2. NM_053752.2.
UniGeneiRn.3766.

3D structure databases

ProteinModelPortaliP13086.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250390. 1 interactor.
IntActiP13086. 1 interactor.
STRINGi10116.ENSRNOP00000007624.

PTM databases

iPTMnetiP13086.
PhosphoSitePlusiP13086.
SwissPalmiP13086.

Proteomic databases

PaxDbiP13086.
PRIDEiP13086.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi114597.
KEGGirno:114597.
UCSCiRGD:619821. rat.

Organism-specific databases

CTDi8802.
RGDi619821. Suclg1.

Phylogenomic databases

eggNOGiKOG1255. Eukaryota.
COG0074. LUCA.
HOGENOMiHOG000239685.
HOVERGENiHBG000957.
InParanoidiP13086.
KOiK01899.
OrthoDBiEOG091G0D9C.
PhylomeDBiP13086.
TreeFamiTF300666.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00999.

Miscellaneous databases

PROiP13086.

Gene expression databases

BgeeiENSRNOG00000005587.
GenevisibleiP13086. RN.

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_RAT
AccessioniPrimary (citable) accession number: P13086
Secondary accession number(s): Q6P7S4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: February 10, 2009
Last modified: November 30, 2016
This is version 145 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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.