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Protein

Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial

Gene

SPCC1620.08

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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 beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.UniRule annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.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 (SPCC1620.08), Succinate--CoA ligase [ADP-forming] subunit alpha, mitochondrial (SPAC16E8.17c)
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 sitei68ATPUniRule annotation1
Binding sitei136ATPUniRule annotation1
Metal bindingi228MagnesiumUniRule annotation1
Metal bindingi242MagnesiumUniRule annotation1
Binding sitei293Substrate; shared with subunit alphaUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi75 – 77ATPUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-71403. Citric acid cycle (TCA cycle).
UniPathwayiUPA00223; UER00999.

Names & Taxonomyi

Protein namesi
Recommended name:
Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrialUniRule annotation (EC:6.2.1.5UniRule annotation)
Alternative name(s):
Succinyl-CoA synthetase beta chainUniRule annotation
Short name:
SCS-betaUniRule annotation
Gene namesi
ORF Names:SPCC1620.08Imported
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC1620.08.
PomBaseiSPCC1620.08.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 23MitochondrionUniRule annotationAdd BLAST23
ChainiPRO_000003336424 – 433Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrialUniRule annotationAdd BLAST410

Proteomic databases

MaxQBiO94415.
PRIDEiO94415.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit.UniRule annotation

Protein-protein interaction databases

BioGridi275739. 10 interactors.
MINTiMINT-4683958.

Structurei

3D structure databases

ProteinModelPortaliO94415.
SMRiO94415.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 273ATP-graspUniRule annotationAdd BLAST243

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni350 – 352Substrate binding; shared with subunit alphaUniRule annotation3

Sequence similaritiesi

Belongs to the succinate/malate CoA ligase beta subunit family.UniRule annotation
Contains 1 ATP-grasp domain.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000007059.
InParanoidiO94415.
KOiK01900.
OMAiYIESGCD.
OrthoDBiEOG092C2IGW.
PhylomeDBiO94415.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.261. 1 hit.
HAMAPiMF_00558. Succ_CoA_beta. 1 hit.
InterProiIPR013650. ATP-grasp_succ-CoA_synth-type.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR005811. CoA_ligase.
IPR017866. Succ-CoA_synthase_bsu_CS.
IPR005809. Succ_CoA_synthase_bsu.
IPR016102. Succinyl-CoA_synth-like.
[Graphical view]
PANTHERiPTHR11815. PTHR11815. 1 hit.
PfamiPF08442. ATP-grasp_2. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view]
PIRSFiPIRSF001554. SucCS_beta. 1 hit.
SUPFAMiSSF52210. SSF52210. 1 hit.
TIGRFAMsiTIGR01016. sucCoAbeta. 1 hit.
PROSITEiPS01217. SUCCINYL_COA_LIG_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O94415-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTRSVLRKA PRAFSPFLQK RNLALHEYIS HDILRKFGVD VPRGAPARSG
60 70 80 90 100
EEAEKVARDL KVTDLVVKAQ VLAGGRGKGQ FDSGLRGGVR PVYDATEARM
110 120 130 140 150
FAEQMIGHKL ITRQTGPAGK ICNVVYVCER KFIRKEYYFA ILMDRENQCP
160 170 180 190 200
MIVASDQGGV DIETVAAENP SAIIKRSLPN SPNLDPHIAE ELVDKLGFSS
210 220 230 240 250
SSKPKAVDAI VKLYKVFNDC DATQVEINPL AETTDHKVLC MDAKLNFDDN
260 270 280 290 300
AEFRHSNIFV LRDISQEDPD EARAAKVGLN FIKLDGNIGC LVNGAGLAMA
310 320 330 340 350
TMDIIKLHGG EPANFLDVGG NANAEAIREA FSLITNDPKT TAIFVNIFGG
360 370 380 390 400
IVRCDVIAKG LISVVSALNL NIPIICRLQG TNQGAAKEVI NNSGLRIFSF
410 420 430
DDLDEAAKKA CRFSRVVEMA READVNVSFE LPL
Length:433
Mass (Da):47,287
Last modified:May 1, 1999 - v1
Checksum:iB2357DBDFA0A430F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA22492.1.
PIRiT41038.
RefSeqiNP_588466.1. NM_001023457.2.

Genome annotation databases

EnsemblFungiiSPCC1620.08.1; SPCC1620.08.1:pep; SPCC1620.08.
GeneIDi2539168.
KEGGispo:SPCC1620.08.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA. Translation: CAA22492.1.
PIRiT41038.
RefSeqiNP_588466.1. NM_001023457.2.

3D structure databases

ProteinModelPortaliO94415.
SMRiO94415.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275739. 10 interactors.
MINTiMINT-4683958.

Proteomic databases

MaxQBiO94415.
PRIDEiO94415.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC1620.08.1; SPCC1620.08.1:pep; SPCC1620.08.
GeneIDi2539168.
KEGGispo:SPCC1620.08.

Organism-specific databases

EuPathDBiFungiDB:SPCC1620.08.
PomBaseiSPCC1620.08.

Phylogenomic databases

HOGENOMiHOG000007059.
InParanoidiO94415.
KOiK01900.
OMAiYIESGCD.
OrthoDBiEOG092C2IGW.
PhylomeDBiO94415.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00999.
ReactomeiR-SPO-71403. Citric acid cycle (TCA cycle).

Miscellaneous databases

PROiO94415.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.261. 1 hit.
HAMAPiMF_00558. Succ_CoA_beta. 1 hit.
InterProiIPR013650. ATP-grasp_succ-CoA_synth-type.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR005811. CoA_ligase.
IPR017866. Succ-CoA_synthase_bsu_CS.
IPR005809. Succ_CoA_synthase_bsu.
IPR016102. Succinyl-CoA_synth-like.
[Graphical view]
PANTHERiPTHR11815. PTHR11815. 1 hit.
PfamiPF08442. ATP-grasp_2. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view]
PIRSFiPIRSF001554. SucCS_beta. 1 hit.
SUPFAMiSSF52210. SSF52210. 1 hit.
TIGRFAMsiTIGR01016. sucCoAbeta. 1 hit.
PROSITEiPS01217. SUCCINYL_COA_LIG_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSUCB_SCHPO
AccessioniPrimary (citable) accession number: O94415
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: May 1, 1999
Last modified: November 30, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  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.