O13750 (SUCA_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

ORF Names:

SPAC16E8.17c

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › Schizosaccharomyces pombe

Protein attributes

Sequence length	331 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	ATP + succinate + CoA = ADP + phosphate + succinyl-CoA.
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle.
Subunit structure	Heterodimer of an alpha and a beta subunit By similarity.
Subcellular location	Mitochondrion By similarity.
Sequence similarities	Belongs to the succinate/malate CoA ligase alpha subunit family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	GTP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	succinyl-CoA metabolic process Inferred from sequence or structural similarity. Source: PomBase tricarboxylic acid cycle Inferred from sequence or structural similarity. Source: PomBase
Cellular_component	mitochondrion Inferred from direct assay PubMed 16823372. Source: PomBase succinate-CoA ligase complex Inferred by curator. Source: PomBase
Molecular_function	ATP citrate synthase activity Inferred from electronic annotation. Source: InterPro GTP binding Inferred from electronic annotation. Source: UniProtKB-KW cofactor binding Inferred from electronic annotation. Source: InterPro succinate-CoA ligase (ADP-forming) activity Inferred from electronic annotation. Source: EC succinate-CoA ligase activity Inferred from sequence or structural similarity. Source: PomBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 331		Probable succinyl-CoA ligase [ADP-forming] subunit alpha, mitochondrial		PRO_0000033350
Regions
	Compositional bias	16 – 19	4	Poly-Ser
Sites
	Active site	285	1	Tele-phosphohistidine intermediate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O13750 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 1D22229C69CCC34E	FASTA	331	34,706
	10 20 30 40 50 60 MFKTQTTLLT SLRRFSSSSQ LKNSKSLYEQ TIPNLMINSD TKVIFQGFTG KQGTFHAQHA 70 80 90 100 110 120 MDYGTKVVGG TNPKKAGTTH LGKPVFGTIE EAMKETKADA SAVFVPPPLA AGAIEEAIAA 130 140 150 160 170 180 EVPLIVAITE GIPQHDMLRV SDILKTQSKS RLVGPNCPGI IRPGQCKIGI MPSHIHKPGC 190 200 210 220 230 240 IGIVSRSGTL TYEAVNQTTQ TDLGQSLVIG IGGDPFPGTN FIDALKLFLD DPNTQGIILI 250 260 270 280 290 300 GEIGGSAEED AAEFIRAANA SRSTPKPVVS FIAGATAPKG RRMGHAGAIV AGGKGTAAAK 310 320 330 FEALEAAGVR ISRSPATLGS LIVEELNKLK H

References

[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329670 Genomic DNA. Translation: CAB11045.1.
PIR	T37797.
RefSeq	NP_594230.1. NM_001019653.2.
3D structure databases
ProteinModelPortal	O13750.
SMR	O13750. Positions 28-330.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4667623.
STRING	4896.SPAC16E8.17c-1.
Proteomic databases
PaxDb	O13750.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPAC16E8.17c.1; SPAC16E8.17c.1:pep; SPAC16E8.17c.
GeneID	2542341.
KEGG	spo:SPAC16E8.17c.
Organism-specific databases
PomBase	SPAC16E8.17c.
Phylogenomic databases
eggNOG	COG0074.
HOGENOM	HOG000239685.
KO	K01899.
OMA	KGRKKPM.
OrthoDB	EOG4SBJ6V.
Enzyme and pathway databases
UniPathway	UPA00223.
Family and domain databases
Gene3D	3.40.50.261. 1 hit. 3.40.50.720. 1 hit.
InterPro	IPR017440. 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]
Pfam	PF02629. CoA_binding. 1 hit. PF00549. Ligase_CoA. 1 hit. [Graphical view]
PIRSF	PIRSF001553. SucCS_alpha. 1 hit.
PRINTS	PR01798. SCOASYNTHASE.
SMART	SM00881. CoA_binding. 1 hit. [Graphical view]
SUPFAM	SSF52210. CoA_ligase. 1 hit.
TIGRFAMs	TIGR01019. sucCoAalpha. 1 hit.
PROSITE	PS01216. SUCCINYL_COA_LIG_1. 1 hit. PS00399. SUCCINYL_COA_LIG_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20803402.

Entry information

Entry name

SUCA_SCHPO

Accession

Primary (citable) accession number: O13750

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	May 29, 2013
This is version 105 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program