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Protein

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

Gene

sucl-2

Organism
Caenorhabditis elegans
Status
Unreviewed-Annotation score: Annotation score: 3 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 (suca-1), Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (sucl-1), Succinate--CoA ligase [ADP/GDP-forming] subunit alpha, mitochondrial (sucl-2), Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial (sucg-1)
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 sitei69Coenzyme AUniRule annotation1
Binding sitei186Substrate; shared with subunit betaUniRule annotation1
Active sitei278Tele-phosphohistidine intermediateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigaseUniRule annotationImported
Biological processTricarboxylic acid cycleUniRule annotation
LigandNucleotide-bindingUniRule annotation

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:sucl-2Imported
ORF Names:CELE_F23H11.3Imported, F23H11.3Imported
OrganismiCaenorhabditis elegansImported
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome III

Organism-specific databases

WormBaseiF23H11.3; CE09611; WBGene00017759; sucl-2.

Subcellular locationi

  • Mitochondrion UniRule annotation

Keywords - Cellular componenti

MitochondrionUniRule annotation

PTM / Processingi

Proteomic databases

EPDiO02642.
PaxDbiO02642.
PeptideAtlasiO02642.

Expressioni

Gene expression databases

BgeeiWBGene00017759.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

DIPiDIP-25090N.
MINTiMINT-1087292.
STRINGi6239.F23H11.3.1.

Structurei

3D structure databases

ProteinModelPortaliO02642.
SMRiO02642.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini30 – 126CoA_bindingInterPro annotationAdd BLAST97

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni43 – 46Coenzyme A bindingUniRule annotation4
Regioni122 – 124Coenzyme A bindingUniRule annotation3

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG1255. Eukaryota.
COG0074. LUCA.
GeneTreeiENSGT00530000063275.
HOGENOMiHOG000239685.
InParanoidiO02642.
KOiK01899.
OMAiEAIECEM.
OrthoDBiEOG091G0D9C.
PhylomeDBiO02642.

Family and domain databases

Gene3Di3.40.50.261. 1 hit.
3.40.50.720. 1 hit.
HAMAPiMF_01988. Succ_CoA_alpha. 1 hit.
InterProiView protein in InterPro
IPR017440. 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.
PfamiView protein in Pfam
PF02629. CoA_binding. 1 hit.
PF00549. Ligase_CoA. 1 hit.
PIRSFiPIRSF001553. SucCS_alpha. 1 hit.
SMARTiView protein in SMART
SM00881. CoA_binding. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF52210. SSF52210. 1 hit.
TIGRFAMsiTIGR01019. sucCoAalpha. 1 hit.
PROSITEiView protein in PROSITE
PS01216. SUCCINYL_COA_LIG_1. 1 hit.
PS00399. SUCCINYL_COA_LIG_2. 1 hit.

Sequencei

Sequence statusi: Complete.

O02642-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASTLASAAR AATRAAVTRS VYNDTRNNLM INKSTKVIVQ GFTGRQGTFH
60 70 80 90 100
SKQMLEYNTN LVGGVSPNKA GQTHLGLPVF GSVAEAKDRT GADATVIYVP
110 120 130 140 150
AAGAARAIHE AMDAEIGLIV AITEGIPQQD MVRVKNRLLK QNKSRLLGPN
160 170 180 190 200
CPGIIASGDC KIGIMPGHIH KKGCIGIVSR SGTLTYEAVH QTTTVGLGQT
210 220 230 240 250
RCIGIGGDPF NGTNFIDCLE VFLEDEQTKG IILIGEIGGQ AEEQAAEFLK
260 270 280 290 300
SRNSGSNAKP VVSFIAGVTA PPGRRMGHAG AIIAGGKGTA GDKIEALRNA
310 320
NVVVTDSPAK LGVAMQKALL G
Length:321
Mass (Da):33,366
Last modified:July 1, 1997 - v1
Checksum:iFBE0AEEA412EF4F1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX284603 Genomic DNA. Translation: CCD69944.1.
PIRiT34065.
RefSeqiNP_497288.1. NM_064887.5.
UniGeneiCel.37553.

Genome annotation databases

EnsemblMetazoaiF23H11.3.1; F23H11.3.1; WBGene00017759.
F23H11.3.2; F23H11.3.2; WBGene00017759.
GeneIDi175252.
KEGGicel:CELE_F23H11.3.
UCSCiF23H11.3.1. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX284603 Genomic DNA. Translation: CCD69944.1.
PIRiT34065.
RefSeqiNP_497288.1. NM_064887.5.
UniGeneiCel.37553.

3D structure databases

ProteinModelPortaliO02642.
SMRiO02642.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-25090N.
MINTiMINT-1087292.
STRINGi6239.F23H11.3.1.

Proteomic databases

EPDiO02642.
PaxDbiO02642.
PeptideAtlasiO02642.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiF23H11.3.1; F23H11.3.1; WBGene00017759.
F23H11.3.2; F23H11.3.2; WBGene00017759.
GeneIDi175252.
KEGGicel:CELE_F23H11.3.
UCSCiF23H11.3.1. c. elegans.

Organism-specific databases

CTDi175252.
WormBaseiF23H11.3; CE09611; WBGene00017759; sucl-2.

Phylogenomic databases

eggNOGiKOG1255. Eukaryota.
COG0074. LUCA.
GeneTreeiENSGT00530000063275.
HOGENOMiHOG000239685.
InParanoidiO02642.
KOiK01899.
OMAiEAIECEM.
OrthoDBiEOG091G0D9C.
PhylomeDBiO02642.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00999.

Gene expression databases

BgeeiWBGene00017759.

Family and domain databases

Gene3Di3.40.50.261. 1 hit.
3.40.50.720. 1 hit.
HAMAPiMF_01988. Succ_CoA_alpha. 1 hit.
InterProiView protein in InterPro
IPR017440. 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.
PfamiView protein in Pfam
PF02629. CoA_binding. 1 hit.
PF00549. Ligase_CoA. 1 hit.
PIRSFiPIRSF001553. SucCS_alpha. 1 hit.
SMARTiView protein in SMART
SM00881. CoA_binding. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF52210. SSF52210. 1 hit.
TIGRFAMsiTIGR01019. sucCoAalpha. 1 hit.
PROSITEiView protein in PROSITE
PS01216. SUCCINYL_COA_LIG_1. 1 hit.
PS00399. SUCCINYL_COA_LIG_2. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiO02642_CAEEL
AccessioniPrimary (citable) accession number: O02642
Entry historyiIntegrated into UniProtKB/TrEMBL: July 1, 1997
Last sequence update: July 1, 1997
Last modified: April 12, 2017
This is version 129 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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.