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Protein

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

Gene

SUCLG1

Organism
Sus scrofa (Pig)
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 annotation1 Publication

Kineticsi

  1. KM=0.76 mM for succinate1 Publication
  1. Vmax=5.99 µmol/min/mg enzyme1 Publication

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), Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial (SUCLG2), Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial (SUCLA2)
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 Publication1
Binding sitei207Substrate; shared with subunit betaUniRule annotation1 Publication1
Active sitei299Tele-phosphohistidine intermediateUniRule annotation2 Publications1

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

BRENDAi6.2.1.4. 6170.
SABIO-RKO19069.
UniPathwayiUPA00223; UER00999.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrialUniRule annotation1 Publication (EC:6.2.1.4UniRule annotation, EC:6.2.1.5UniRule annotation)
Alternative name(s):
Succinyl-CoA synthetase subunit alpha1 PublicationUniRule annotation
Short name:
SCS-alphaUniRule annotation
Gene namesi
Name:SUCLG1UniRule annotation
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

  • Mitochondrion UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 34MitochondrionUniRule annotationAdd BLAST34
ChainiPRO_000003334235 – 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 residuei105N6-acetyllysineBy similarity1
Modified residuei338N6-succinyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PeptideAtlasiO19069.
PRIDEiO19069.

Expressioni

Tissue specificityi

Isoform I is expressed in all tissues examined: liver, brain, heart, and skeletal muscle. Isoform II is expressed only in heart and skeletal muscle.1 Publication

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 annotation4 Publications

Protein-protein interaction databases

BioGridi1149836. 1 interactor.

Structurei

Secondary structure

1346
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi44 – 50Combined sources7
Beta strandi57 – 61Combined sources5
Turni62 – 64Combined sources3
Helixi66 – 78Combined sources13
Beta strandi81 – 86Combined sources6
Beta strandi93 – 95Combined sources3
Beta strandi98 – 103Combined sources6
Helixi104 – 111Combined sources8
Beta strandi115 – 118Combined sources4
Helixi122 – 134Combined sources13
Beta strandi138 – 142Combined sources5
Helixi149 – 159Combined sources11
Beta strandi166 – 168Combined sources3
Beta strandi170 – 172Combined sources3
Beta strandi174 – 177Combined sources4
Turni178 – 180Combined sources3
Beta strandi181 – 186Combined sources6
Helixi188 – 190Combined sources3
Beta strandi193 – 201Combined sources9
Helixi204 – 215Combined sources12
Beta strandi220 – 225Combined sources6
Beta strandi228 – 231Combined sources4
Helixi236 – 245Combined sources10
Beta strandi251 – 261Combined sources11
Helixi262 – 273Combined sources12
Beta strandi274 – 278Combined sources5
Beta strandi282 – 287Combined sources6
Helixi311 – 320Combined sources10
Helixi329 – 331Combined sources3
Helixi332 – 342Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EUCX-ray2.10A38-346[»]
1EUDX-ray2.10A38-346[»]
2FP4X-ray2.08A43-346[»]
2FPGX-ray2.96A43-346[»]
2FPIX-ray2.70A43-346[»]
2FPPX-ray2.35A43-346[»]
4XX0X-ray2.10A42-346[»]
5CAEX-ray2.20A42-346[»]
ProteinModelPortaliO19069.
SMRiO19069.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO19069.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni64 – 67Coenzyme A bindingUniRule annotation1 Publication4
Regioni143 – 145Coenzyme A bindingUniRule annotation1 Publication3

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000239685.
HOVERGENiHBG000957.
InParanoidiO19069.
KOiK01899.

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]

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

Isoform I (identifier: O19069-2) [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
MTAALVAAPA AATMASGSSG LAAARLLSRS FLLQQNGIRH CSYTASRKHL
60 70 80 90 100
YVDKNTKVIC QGFTGKQGTF HSQQALEYGT NLVGGTTPGK GGKTHLGLPV
110 120 130 140 150
FNTVKEAKEQ TGATASVIYV PPPFAAAAIN EAIDAEVPLV VCITEGIPQQ
160 170 180 190 200
DMVRVKHRLL RQGKTRLIGP NCPGVINPGE CKIGIMPGHI HKKGRIGIVS
210 220 230 240 250
RSGTLTYEAV HQTTQVGLGQ SLCVGIGGDP FNGTDFTDCL EIFLNDPATE
260 270 280 290 300
GIILIGEIGG NAEENAAEFL KQHNSGPKSK PVVSFIAGLT APPGRRMGHA
310 320 330 340
GAIIAGGKGG AKEKITALQS AGVVVSMSPA QLGTTIYKEF EKRKML
Length:346
Mass (Da):36,117
Last modified:February 10, 2009 - v2
Checksum:iC5ACA670C214C2D4
GO
Isoform II (identifier: O19069-1) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     178-196: PGECKIGIMPGHIHKKGRI → RFLRFAVYITSRVFTCTQQEEYRKIPLLFGTRSIHM

Show »
Length:363
Mass (Da):38,454
Checksum:i537EAA9D870E9C01
GO

Sequence cautioni

The sequence AAB94003 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAB94004 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2 – 4TAA → PAG in AAB94003 (PubMed:9261120).Curated3
Sequence conflicti2 – 4TAA → PAG in AAB94004 (PubMed:9261120).Curated3

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_036394178 – 196PGECK…KKGRI → RFLRFAVYITSRVFTCTQQE EYRKIPLLFGTRSIHM in isoform II. 1 PublicationAdd BLAST19

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BP167826 mRNA. No translation available.
AF008432, AF008430 Genomic DNA. Translation: AAB94001.1.
AF008433, AF008430, AF008431 Genomic DNA. Translation: AAB94002.2.
AF008588 mRNA. Translation: AAB94003.1. Different initiation.
AF008589 mRNA. Translation: AAB94004.1. Different initiation.
RefSeqiNP_999574.1. NM_214409.2.
UniGeneiSsc.14502.

Genome annotation databases

GeneIDi399539.
KEGGissc:399539.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BP167826 mRNA. No translation available.
AF008432, AF008430 Genomic DNA. Translation: AAB94001.1.
AF008433, AF008430, AF008431 Genomic DNA. Translation: AAB94002.2.
AF008588 mRNA. Translation: AAB94003.1. Different initiation.
AF008589 mRNA. Translation: AAB94004.1. Different initiation.
RefSeqiNP_999574.1. NM_214409.2.
UniGeneiSsc.14502.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EUCX-ray2.10A38-346[»]
1EUDX-ray2.10A38-346[»]
2FP4X-ray2.08A43-346[»]
2FPGX-ray2.96A43-346[»]
2FPIX-ray2.70A43-346[»]
2FPPX-ray2.35A43-346[»]
4XX0X-ray2.10A42-346[»]
5CAEX-ray2.20A42-346[»]
ProteinModelPortaliO19069.
SMRiO19069.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1149836. 1 interactor.

Proteomic databases

PeptideAtlasiO19069.
PRIDEiO19069.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi399539.
KEGGissc:399539.

Organism-specific databases

CTDi8802.

Phylogenomic databases

HOGENOMiHOG000239685.
HOVERGENiHBG000957.
InParanoidiO19069.
KOiK01899.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00999.
BRENDAi6.2.1.4. 6170.
SABIO-RKO19069.

Miscellaneous databases

EvolutionaryTraceiO19069.

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_PIG
AccessioniPrimary (citable) accession number: O19069
Secondary accession number(s): O19068
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 10, 2009
Last modified: November 30, 2016
This is version 133 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.