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Protein

Succinate--CoA ligase [ADP-forming] subunit alpha-2, mitochondrial

Gene

At5g23250

Organism
Arabidopsis thaliana (Mouse-ear cress)
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 ATP 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 nucleotide specificity is provided by the beta subunit.UniRule annotation

Catalytic activityi

ATP + succinate + CoA = ADP + 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 (At2g20420), Succinate--CoA ligase [ADP-forming] subunit alpha-2, mitochondrial (At5g23250), Succinate--CoA ligase [ADP-forming] subunit alpha-1, mitochondrial (At5g08300)
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 sitei87Coenzyme AUniRule annotation1
Binding sitei204Substrate; shared with subunit betaUniRule annotation1
Active sitei293Tele-phosphohistidine intermediateUniRule annotation1

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

BioCyciARA:AT5G23250-MONOMER.
ReactomeiR-ATH-71403. Citric acid cycle (TCA cycle).
UniPathwayiUPA00223; UER00999.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinate--CoA ligase [ADP-forming] subunit alpha-2, mitochondrialUniRule annotation (EC:6.2.1.5UniRule annotation)
Alternative name(s):
Succinyl-CoA synthetase subunit alpha-2UniRule annotation
Short name:
SCS-alpha-2UniRule annotation
Gene namesi
Ordered Locus Names:At5g23250
ORF Names:MKD15.11
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G23250.

Subcellular locationi

  • Mitochondrion UniRule annotation1 Publication

GO - Cellular componenti

  • mitochondrial matrix Source: GO_Central
  • mitochondrion Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 44MitochondrionUniRule annotationAdd BLAST44
ChainiPRO_000003333645 – 341Succinate--CoA ligase [ADP-forming] subunit alpha-2, mitochondrialAdd BLAST297

Proteomic databases

PaxDbiQ8LAD2.
PRIDEiQ8LAD2.

PTM databases

iPTMnetiQ8LAD2.

Expressioni

Gene expression databases

ExpressionAtlasiQ8LAD2. baseline and differential.
GenevisibleiQ8LAD2. AT.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit.UniRule annotation

Protein-protein interaction databases

STRINGi3702.AT5G23250.1.

Structurei

3D structure databases

ProteinModelPortaliQ8LAD2.
SMRiQ8LAD2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni61 – 64Coenzyme A bindingUniRule annotation4
Regioni140 – 142Coenzyme A bindingUniRule annotation3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi41 – 44Poly-Pro4
Compositional biasi122 – 125Poly-Ala4

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.
InParanoidiQ8LAD2.
KOiK01899.
OMAiIMEMVAY.
OrthoDBiEOG09360EDA.
PhylomeDBiQ8LAD2.

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.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q8LAD2-1) [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
MSRQVTRLLG SLRHSGGGCS GSSKVCSLTS LVQSRSFGTT PPPPAAVFVD
60 70 80 90 100
KNTRVICQGI TGKNGTFHTE QAIEYGTKMV AGVTPKKGGT EHLGLPVFNT
110 120 130 140 150
VAEAKAETKA NASVIYVPAP FAAAAIMEGL AAELDLIVCI TEGIPQHDMV
160 170 180 190 200
RVKAALNSQS KTRLIGPNCP GIIKPGECKI GIMPGYIHKP GKIGIVSRSG
210 220 230 240 250
TLTYEAVFQT TAVGLGQSTC VGIGGDPFNG TNFVDCLEKF FVDPQTEGIV
260 270 280 290 300
LIGEIGGTAE EDAAALIKEN GTDKPVVAFI AGLTAPPGRR MGHAGAIVSG
310 320 330 340
GKGTAQDKIK SLRDAGVKVV ESPAKIGAAM FELFQERGLL K
Length:341
Mass (Da):35,317
Last modified:October 25, 2004 - v2
Checksum:i5BFA16519C429FE7
GO

Sequence cautioni

The sequence CAA48891 differs from that shown. Reason: Frameshift at position 46.Curated
The sequence CAA79188 differs from that shown. Reason: Frameshift at position 46.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti22S → T in CAA48891 (Ref. 1) Curated1
Sequence conflicti22S → T in CAA79188 (PubMed:8281187).Curated1
Sequence conflicti296A → R in CAA48891 (Ref. 1) Curated1
Sequence conflicti309I → T in AAM65450 (PubMed:14593172).Curated1
Sequence conflicti326I → L in CAA48891 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69138 mRNA. Translation: CAA48891.1. Frameshift.
AB007648 Genomic DNA. Translation: BAB11180.1.
CP002688 Genomic DNA. Translation: AED93141.1.
AY092994 mRNA. Translation: AAM12993.1.
AY114607 mRNA. Translation: AAM47926.1.
AY087899 mRNA. Translation: AAM65450.1.
Z18444 mRNA. Translation: CAA79188.1. Frameshift.
PIRiS30579.
RefSeqiNP_197716.1. NM_122231.4. [Q8LAD2-1]
UniGeneiAt.22464.

Genome annotation databases

EnsemblPlantsiAT5G23250.1; AT5G23250.1; AT5G23250. [Q8LAD2-1]
GeneIDi832389.
GrameneiAT5G23250.1; AT5G23250.1; AT5G23250.
KEGGiath:AT5G23250.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69138 mRNA. Translation: CAA48891.1. Frameshift.
AB007648 Genomic DNA. Translation: BAB11180.1.
CP002688 Genomic DNA. Translation: AED93141.1.
AY092994 mRNA. Translation: AAM12993.1.
AY114607 mRNA. Translation: AAM47926.1.
AY087899 mRNA. Translation: AAM65450.1.
Z18444 mRNA. Translation: CAA79188.1. Frameshift.
PIRiS30579.
RefSeqiNP_197716.1. NM_122231.4. [Q8LAD2-1]
UniGeneiAt.22464.

3D structure databases

ProteinModelPortaliQ8LAD2.
SMRiQ8LAD2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT5G23250.1.

PTM databases

iPTMnetiQ8LAD2.

Proteomic databases

PaxDbiQ8LAD2.
PRIDEiQ8LAD2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G23250.1; AT5G23250.1; AT5G23250. [Q8LAD2-1]
GeneIDi832389.
GrameneiAT5G23250.1; AT5G23250.1; AT5G23250.
KEGGiath:AT5G23250.

Organism-specific databases

TAIRiAT5G23250.

Phylogenomic databases

eggNOGiKOG1255. Eukaryota.
COG0074. LUCA.
HOGENOMiHOG000239685.
InParanoidiQ8LAD2.
KOiK01899.
OMAiIMEMVAY.
OrthoDBiEOG09360EDA.
PhylomeDBiQ8LAD2.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00999.
BioCyciARA:AT5G23250-MONOMER.
ReactomeiR-ATH-71403. Citric acid cycle (TCA cycle).

Miscellaneous databases

PROiQ8LAD2.

Gene expression databases

ExpressionAtlasiQ8LAD2. baseline and differential.
GenevisibleiQ8LAD2. AT.

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 nameiSUCA2_ARATH
AccessioniPrimary (citable) accession number: Q8LAD2
Secondary accession number(s): O82661, P53586, Q9FMX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2004
Last sequence update: October 25, 2004
Last modified: November 30, 2016
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.