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P13086 (SUCA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Suclg1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length346 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

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

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

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle.

Subunit structure

Heterodimer of an alpha and a beta subunit.

Subcellular location

Mitochondrion.

Sequence similarities

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

Sequence caution

The sequence AAA41233.1 differs from that shown. Reason: Chimeric cDNA.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandGTP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
Isopeptide bond
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processsuccinate metabolic process

Inferred from direct assay PubMed 17403370. Source: RGD

succinyl-CoA metabolic process

Inferred from direct assay PubMed 17403370PubMed 7430155. Source: RGD

tricarboxylic acid cycle

Inferred from direct assay PubMed 17403370. Source: RGD

   Cellular_componentmitochondrial inner membrane

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from direct assay PubMed 17403370. Source: RGD

plasma membrane

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from direct assay PubMed 11831846. Source: RGD

succinate-CoA ligase complex (GDP-forming)

Inferred from direct assay PubMed 7430155. Source: RGD

   Molecular_functionATP citrate synthase activity

Inferred from electronic annotation. Source: InterPro

GDP binding

Inferred from direct assay PubMed 7430155. Source: RGD

GTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cofactor binding

Inferred from electronic annotation. Source: InterPro

protein heterodimerization activity

Inferred from direct assay PubMed 7430155. Source: RGD

succinate-CoA ligase (ADP-forming) activity

Inferred from direct assay PubMed 17403370. Source: RGD

succinate-CoA ligase (GDP-forming) activity

Inferred from direct assay PubMed 17403370PubMed 7430155. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4040Mitochondrion
Chain41 – 346306Succinyl-CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial
PRO_0000033343

Sites

Active site2991Tele-phosphohistidine intermediate Ref.2

Amino acid modifications

Modified residue541N6-acetyllysine By similarity
Modified residue571N6-acetyllysine; alternate By similarity
Modified residue571N6-succinyllysine; alternate By similarity
Modified residue661N6-acetyllysine; alternate By similarity
Modified residue661N6-succinyllysine; alternate By similarity
Modified residue811N6-acetyllysine By similarity
Modified residue941N6-acetyllysine By similarity
Modified residue1051N6-acetyllysine By similarity
Modified residue3381N6-succinyllysine By similarity
Cross-link280Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Sequence conflict1531V → L in AAA41233. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P13086 [UniParc].

Last modified February 10, 2009. Version 2.
Checksum: 2DDFC746C11B5B0C

FASTA34636,148
        10         20         30         40         50         60 
MTAAVVAAAA TATMVSGSSG LAAARLLSRT FLLQQNGIRH GSYTASRKNI YIDKNTKVIC 

        70         80         90        100        110        120 
QGFTGKQGTF HSQQALEYGT KLVGGTTPGK GGKKHLGLPV FNTVKEAKEK TGATASVIYV 

       130        140        150        160        170        180 
PPPFAAAAIN EAIDAEIPLV VCITEGIPQQ DMVRVKHKLT RQGKTRLIGP NCPGIINPGE 

       190        200        210        220        230        240 
CKIGIMPGHI HKKGRIGIVS RSGTLTYEAV HQTTQVGLGQ SLCIGIGGDP FNGTNFIDCL 

       250        260        270        280        290        300 
DVFLKDPATE GIVLIGEIGG HAEENAAEFL KEHNSGPKAK PVVSFIAGIT APPGRRMGHA 

       310        320        330        340 
GAIIAGGKGG AKEKISALQS AGVIVSMSPA QLGTCMYKEF EKRKML 

« Hide

References

« Hide 'large scale' references
[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pituitary.
[2]"Cloning and sequencing of the cytoplasmic precursor to the alpha subunit of rat liver mitochondrial succinyl-CoA synthetase."
Henning W.D., Upton C., McFadden G., Majumdar R., Bridger W.A.
Proc. Natl. Acad. Sci. U.S.A. 85:1432-1436(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-346.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC061537 mRNA. Translation: AAH61537.2.
J03621 mRNA. Translation: AAA41233.1. Sequence problems.
PIRSYRTSA. A28962.
RefSeqNP_446204.2. NM_053752.2.
UniGeneRn.3766.

3D structure databases

ProteinModelPortalP13086.
SMRP13086. Positions 42-346.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid250390. 1 interaction.
IntActP13086. 1 interaction.

PTM databases

PhosphoSiteP13086.

Proteomic databases

PaxDbP13086.
PRIDEP13086.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000007624; ENSRNOP00000007624; ENSRNOG00000005587.
GeneID114597.
KEGGrno:114597.
UCSCRGD:619821. rat.

Organism-specific databases

CTD8802.
RGD619821. Suclg1.

Phylogenomic databases

eggNOGCOG0074.
GeneTreeENSGT00530000063275.
HOGENOMHOG000239685.
HOVERGENHBG000957.
InParanoidQ6P7S4.
KOK01899.
OMAHNSGPKA.
OrthoDBEOG74BJSG.
PhylomeDBP13086.
TreeFamTF300666.

Enzyme and pathway databases

UniPathwayUPA00223.

Gene expression databases

GenevestigatorP13086.

Family and domain databases

Gene3D3.40.50.261. 1 hit.
3.40.50.720. 1 hit.
InterProIPR017440. 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]
PfamPF02629. CoA_binding. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view]
PIRSFPIRSF001553. SucCS_alpha. 1 hit.
PRINTSPR01798. SCOASYNTHASE.
SMARTSM00881. CoA_binding. 1 hit.
[Graphical view]
SUPFAMSSF52210. SSF52210. 1 hit.
TIGRFAMsTIGR01019. sucCoAalpha. 1 hit.
PROSITEPS01216. SUCCINYL_COA_LIG_1. 1 hit.
PS00399. SUCCINYL_COA_LIG_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio618767.
PROP13086.

Entry information

Entry nameSUCA_RAT
AccessionPrimary (citable) accession number: P13086
Secondary accession number(s): Q6P7S4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: February 10, 2009
Last modified: April 16, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways