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Protein

Probable succinyl-CoA ligase [ADP-forming] subunit alpha, mitochondrial

Gene

SPAC16E8.17c

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

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

Pathway:itricarboxylic 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 sitei285 – 2851Tele-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

ReactomeiREACT_276964. Citric acid cycle (TCA cycle).
UniPathwayiUPA00223.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable succinyl-CoA ligase [ADP-forming] subunit alpha, mitochondrial (EC:6.2.1.5)
Alternative name(s):
Succinyl-CoA synthetase subunit alpha
Short name:
SCS-alpha
Gene namesi
ORF Names:SPAC16E8.17c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC16E8.17c.
PomBaseiSPAC16E8.17c.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: PomBase
  • succinate-CoA ligase complex Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 331Probable succinyl-CoA ligase [ADP-forming] subunit alpha, mitochondrialPRO_0000033350
Transit peptidei1 – ?MitochondrionSequence Analysis

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO13750.
PaxDbiO13750.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit.By similarity

Protein-protein interaction databases

BioGridi278807. 4 interactions.
MINTiMINT-4667623.

Structurei

3D structure databases

ProteinModelPortaliO13750.
SMRiO13750. Positions 28-330.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi16 – 194Poly-Ser

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0074.
HOGENOMiHOG000239685.
InParanoidiO13750.
KOiK01899.
OMAiVIICITE.
OrthoDBiEOG7XPZGS.
PhylomeDBiO13750.

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]
SUPFAMiSSF52210. 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.

O13750-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKTQTTLLT SLRRFSSSSQ LKNSKSLYEQ TIPNLMINSD TKVIFQGFTG
60 70 80 90 100
KQGTFHAQHA MDYGTKVVGG TNPKKAGTTH LGKPVFGTIE EAMKETKADA
110 120 130 140 150
SAVFVPPPLA AGAIEEAIAA EVPLIVAITE GIPQHDMLRV SDILKTQSKS
160 170 180 190 200
RLVGPNCPGI IRPGQCKIGI MPSHIHKPGC IGIVSRSGTL TYEAVNQTTQ
210 220 230 240 250
TDLGQSLVIG IGGDPFPGTN FIDALKLFLD DPNTQGIILI GEIGGSAEED
260 270 280 290 300
AAEFIRAANA SRSTPKPVVS FIAGATAPKG RRMGHAGAIV AGGKGTAAAK
310 320 330
FEALEAAGVR ISRSPATLGS LIVEELNKLK H
Length:331
Mass (Da):34,706
Last modified:January 1, 1998 - v1
Checksum:i1D22229C69CCC34E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB11045.1.
PIRiT37797.
RefSeqiNP_594230.1. NM_001019653.2.

Genome annotation databases

EnsemblFungiiSPAC16E8.17c.1; SPAC16E8.17c.1:pep; SPAC16E8.17c.
GeneIDi2542341.
KEGGispo:SPAC16E8.17c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB11045.1.
PIRiT37797.
RefSeqiNP_594230.1. NM_001019653.2.

3D structure databases

ProteinModelPortaliO13750.
SMRiO13750. Positions 28-330.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278807. 4 interactions.
MINTiMINT-4667623.

Proteomic databases

MaxQBiO13750.
PaxDbiO13750.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC16E8.17c.1; SPAC16E8.17c.1:pep; SPAC16E8.17c.
GeneIDi2542341.
KEGGispo:SPAC16E8.17c.

Organism-specific databases

EuPathDBiFungiDB:SPAC16E8.17c.
PomBaseiSPAC16E8.17c.

Phylogenomic databases

eggNOGiCOG0074.
HOGENOMiHOG000239685.
InParanoidiO13750.
KOiK01899.
OMAiVIICITE.
OrthoDBiEOG7XPZGS.
PhylomeDBiO13750.

Enzyme and pathway databases

UniPathwayiUPA00223.
ReactomeiREACT_276964. Citric acid cycle (TCA cycle).

Miscellaneous databases

NextBioi20803402.
PROiO13750.

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]
SUPFAMiSSF52210. 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

  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiSUCA_SCHPO
AccessioniPrimary (citable) accession number: O13750
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: July 22, 2015
This is version 119 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

External Data

Dasty 3

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 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.