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Protein

Succinyl-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

Catalyzes the ATP- or GTP-dependent ligation of succinate and CoA to form succinyl-CoA. The nature of the beta subunit determines the nucleotide specificity (By similarity).By similarity

Catalytic activityi

GTP + succinate + CoA = GDP + phosphate + succinyl-CoA.
ATP + succinate + CoA = ADP + phosphate + succinyl-CoA.

Pathwayi: tricarboxylic acid cycle

This protein is involved in the pathway tricarboxylic acid cycle, which is part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei299 – 2991Tele-phosphohistidine intermediateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Succinyl-CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (EC:6.2.1.4, EC:6.2.1.5)
Alternative name(s):
Succinyl-CoA synthetase subunit alpha
Short name:
SCS-alpha
Gene namesi
Name:SUCLG1
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4040MitochondrionBy similarityAdd
BLAST
Chaini41 – 346306Succinyl-CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrialPRO_0000033342Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 541N6-acetyllysineBy similarity
Modified residuei57 – 571N6-acetyllysine; alternateBy similarity
Modified residuei57 – 571N6-succinyllysine; alternateBy similarity
Modified residuei66 – 661N6-acetyllysine; alternateBy similarity
Modified residuei66 – 661N6-succinyllysine; alternateBy similarity
Modified residuei105 – 1051N6-acetyllysineBy similarity
Cross-linki280 – 280Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei338 – 3381N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

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.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit.

Protein-protein interaction databases

BioGridi1149836. 1 interaction.

Structurei

Secondary structure

1
346
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi44 – 507Combined sources
Beta strandi57 – 615Combined sources
Turni62 – 643Combined sources
Helixi66 – 7813Combined sources
Beta strandi81 – 866Combined sources
Beta strandi93 – 953Combined sources
Beta strandi98 – 1036Combined sources
Helixi104 – 1118Combined sources
Beta strandi115 – 1184Combined sources
Helixi122 – 13413Combined sources
Beta strandi138 – 1425Combined sources
Helixi149 – 15911Combined sources
Beta strandi166 – 1683Combined sources
Beta strandi170 – 1723Combined sources
Beta strandi174 – 1774Combined sources
Turni178 – 1803Combined sources
Beta strandi181 – 1866Combined sources
Helixi188 – 1903Combined sources
Beta strandi193 – 2019Combined sources
Helixi204 – 21512Combined sources
Beta strandi220 – 2256Combined sources
Beta strandi228 – 2314Combined sources
Helixi236 – 24510Combined sources
Beta strandi251 – 26111Combined sources
Helixi262 – 27312Combined sources
Beta strandi274 – 2785Combined sources
Beta strandi282 – 2876Combined sources
Helixi311 – 32010Combined sources
Helixi329 – 3313Combined sources
Helixi332 – 34211Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliO19069.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO19069.

Family & Domainsi

Sequence similaritiesi

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.
InterProiIPR017440. Cit_synth/succinyl-CoA_lig_AS.
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.
PRINTSiPR01798. SCOASYNTHASE.
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 AAB94003.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAB94004.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 43TAA → PAG in AAB94003 (PubMed:9261120).Curated
Sequence conflicti2 – 43TAA → PAG in AAB94004 (PubMed:9261120).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei178 – 19619PGECK…KKGRI → RFLRFAVYITSRVFTCTQQE EYRKIPLLFGTRSIHM in isoform II. 1 PublicationVSP_036394Add
BLAST

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
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[»]
ProteinModelPortaliO19069.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1149836. 1 interaction.

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.
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.
InterProiIPR017440. Cit_synth/succinyl-CoA_lig_AS.
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.
PRINTSiPR01798. SCOASYNTHASE.
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...

Publicationsi

« Hide 'large scale' publications
  1. "PEDE (Pig EST Data Explorer): construction of a database for ESTs derived from porcine full-length cDNA libraries."
    Uenishi H., Eguchi T., Suzuki K., Sawazaki T., Toki D., Shinkai H., Okumura N., Hamasima N., Awata T.
    Nucleic Acids Res. 32:D484-D488(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-291 (ISOFORM I).
  2. "Mutually exclusive splicing generates two distinct isoforms of pig heart succinyl-CoA synthetase."
    Ryan D.G., Lin T., Brownie E., Bridger W.A., Wolodko W.T.
    J. Biol. Chem. 272:21151-21159(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-346 (ISOFORMS I AND II), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 133-234, ALTERNATIVE SPLICING.
    Tissue: Heart.

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: July 6, 2016
This is version 129 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.