Q9P7W3 (ACL1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable ATP-citrate synthase subunit 1
EC=2.3.3.8

Alternative name(s):
ATP-citrate (pro-S-)-lyase 1
Citrate cleavage enzyme subunit 1

Gene names

ORF Names:

SPBC1703.07

Organism

Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)

Taxonomic identifier

284812 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	615 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the formation of cytosolic acetyl-CoA, which is mainly used for the biosynthesis of fatty acids and sterols By similarity.
Catalytic activity	ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA.
Subunit structure	Composed of two subunits By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the succinate/malate CoA ligase alpha subunit family.

Ontologies

Keywords
Biological process	Lipid synthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	acetyl-CoA biosynthetic process Inferred from sequence or structural similarity. Source: GeneDB_Spombe cellular carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro citrate metabolic process Inferred by curator. Source: GeneDB_Spombe fatty acid biosynthetic process Inferred from sequence or structural similarity. Source: GeneDB_Spombe tricarboxylic acid cycle Inferred by curator. Source: GeneDB_Spombe
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_Spombe nucleus Inferred from direct assay. Source: GeneDB_Spombe
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP citrate synthase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 615	615	Probable ATP-citrate synthase subunit 1		PRO_0000102786
Regions
	Nucleotide binding	221 – 241	21	ATP By similarity
	Nucleotide binding	272 – 298	27	ATP By similarity
	Region	299 – 309	11	CoA-binding Potential
Sites
	Active site	280	1	Tele-phosphohistidine intermediate By similarity
	Metal binding	238	1	Magnesium By similarity
Amino acid modifications
	Modified residue	359	1	Phosphoserine Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9P7W3 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: D9998607127639C4	FASTA	615	67,204
	10 20 30 40 50 60 MAGSVDKPSY ELFSKDTRAF VYGMQTKAVQ GMLDFDYMCG RTVPSVAAII YTFGSQSISK 70 80 90 100 110 120 LYWGTKEILL PVYRTIEEAC TKHPEVDVVV NFASSRSAYA STMELMEFPQ IRCIAIIAEG 130 140 150 160 170 180 VPERRAREIL VTSKEKNVVI IGPATVGGIK PGCFKIGNTG GMMDNIVASK LYRPGSVAYV 190 200 210 220 230 240 SKSGGMSNEL NNIISHTTDG VYEGIAIGGD RYPGTTFIDH LIRFEADPAC KLMVLLGEVG 250 260 270 280 290 300 GVEEYRVIEA VKNGTIKKPI VAWAIGTCSS MFKTEVQFGH AGSFANSELE TAVAKNQAMR 310 320 330 340 350 360 EAGIYVPETF EKLPALLQEV YEGLVKKGVI VPQPEVAPPN IPLDYAWAKE LGLVRKPSSF 370 380 390 400 410 420 ICTISNDRGS ELTYNNVPIS KVFEEELGIG GVISLLWLRR RLPSYATKFL EMVLQLTADH 430 440 450 460 470 480 GPCVSGAMNT IITTRAGKDL ISSLVAGLLT IGTRFGGALD GAAQEFSKAY DAGLSPRAFV 490 500 510 520 530 540 DSCRKANKLI PGIGHRIKSR NNPDLRVELV KGYVKKNFPS TKLLDYALAV ENVTTSKKDN 550 560 570 580 590 600 LILNVDGCIA VCFVDLLRNC GAFTLEEANE YINLGILNGM FVLGRSIGLI GHHLDQKRLR 610 APLYRHPWDD FLYLS

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: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843.
[2]	"Identification of open reading frames in Schizosaccharomyces pombe cDNAs." Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H. DNA Res. 4:363-369(1997) [PubMed: 9501991] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 293-615. Strain: PR745.
[3]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329671 Genomic DNA. Translation: CAB66451.1. D89194 mRNA. Translation: BAA13855.1.
PIR	T42753. T50320.
RefSeq	NP_596202.1. NM_001022121.1.
3D structure databases
ProteinModelPortal	Q9P7W3.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9P7W3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	SPBC1703.07.1; SPBC1703.07.1:pep; SPBC1703.07.
GeneID	2539879.
KEGG	spo:SPBC1703.07.
NMPDR	fig|4896.1.peg.2068.
Organism-specific databases
GeneDB_Spombe	SPBC1703.07.
Phylogenomic databases
eggNOG	fuNOG06879.
GeneTree	EFGT00050000003524.
HOGENOM	HBG318254.
OMA	NVDGTIG.
OrthoDB	EOG4CC78H.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-004232-MONOMER.
Gene expression databases
ArrayExpress	Q9P7W3.
Family and domain databases
InterPro	IPR016142. Citrate_synth-like_lrg_a-sub. IPR016143. Citrate_synth-like_sm_a-sub. IPR002020. Citrate_synthase-like. IPR016141. Citrate_synthase-like_core. IPR003781. CoA-bd. IPR005810. CoA_lig_alpha. IPR005811. CoA_ligase. IPR016040. NAD(P)-bd_dom. IPR017866. Succ-CoA_synthase_bsu_CS. IPR016102. Succinyl-CoA_synth-like. [Graphical view]
Gene3D	G3DSA:1.10.580.10. Citrate_synthase_lrg_a-sub. 1 hit. G3DSA:1.10.230.10. Citrate_synthase_sm_a-sub. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:3.40.50.261. Succinyl-CoA_synth-like. 1 hit.
KO	K01648.
Pfam	PF00285. Citrate_synt. 1 hit. PF02629. CoA_binding. 1 hit. PF00549. Ligase_CoA. 1 hit. [Graphical view]
SUPFAM	SSF48256. Citrate_synthase_core. 1 hit.
PROSITE	PS01216. SUCCINYL_COA_LIG_1. 1 hit. PS00399. SUCCINYL_COA_LIG_2. False negative. PS01217. SUCCINYL_COA_LIG_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACL1_SCHPO

Accession

Primary (citable) accession number: Q9P7W3
Secondary accession number(s): P78844

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2003
Last sequence update:	October 1, 2000
Last modified:	December 14, 2011
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program