Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Probable ATP-citrate synthase subunit 2

Gene

SPAC22A12.16

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA. Has a central role in de novo lipid synthesis (By similarity).By similarity

Catalytic activityi

ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Probable ATP-citrate synthase subunit 2 (EC:2.3.3.8)
Alternative name(s):
ATP-citrate (pro-S-)-lyase 2
Citrate cleavage enzyme subunit 2
Gene namesi
ORF Names:SPAC22A12.16
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC22A12.16.
PomBaseiSPAC22A12.16.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 492492Probable ATP-citrate synthase subunit 2PRO_0000340113Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO13907.
PRIDEiO13907.

PTM databases

iPTMnetiO13907.

Interactioni

Subunit structurei

Composed of two subunits.By similarity

Protein-protein interaction databases

BioGridi278302. 6 interactions.
MINTiMINT-4668878.

Structurei

3D structure databases

ProteinModelPortaliO13907.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

In the N-terminal section; belongs to the succinate/malate CoA ligase beta subunit family.Curated
In the C-terminal section; belongs to the succinate/malate CoA ligase alpha subunit family.Curated

Phylogenomic databases

HOGENOMiHOG000151490.
InParanoidiO13907.
KOiK01648.
OMAiVIMDPER.
OrthoDBiEOG7Z69NB.
PhylomeDBiO13907.

Family and domain databases

Gene3Di3.30.470.20. 1 hit.
3.40.50.261. 1 hit.
InterProiIPR013650. ATP-grasp_succ-CoA_synth-type.
IPR013816. ATP_grasp_subdomain_2.
IPR032263. Citrate-bd.
IPR017866. Succ-CoA_synthase_bsu_CS.
IPR016102. Succinyl-CoA_synth-like.
[Graphical view]
PfamiPF08442. ATP-grasp_2. 1 hit.
PF16114. Citrate_bind. 1 hit.
[Graphical view]
SUPFAMiSSF52210. SSF52210. 1 hit.
PROSITEiPS01217. SUCCINYL_COA_LIG_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O13907-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAKSIREYD GKAVLAYWLN RSPSISKEEY KTVSATPAVQ LAQIQFPLPT
60 70 80 90 100
LVIPAESTTY REVVEDVFAK VEQEHPWVKE TKLVAKPDQL IKRRGKSGLL
110 120 130 140 150
KLNATWDEAK EWIRERAGKN QKVQHAVGYL TTFLVEPFVP HPPNTEYYIN
160 170 180 190 200
INSVREGDWI LFCNEGGVDV GDVDAKARKL LVPVRLSEFP SRATIASTLL
210 220 230 240 250
SDIPVEQHES LVDFIIRLYS VYVDCQFTYL EINPLVVIPT AKGADVFYLD
260 270 280 290 300
LAAKLDQTAE FECGAKWAVA RAPESLGIKT SGEESGAINA DHGPPMVFPA
310 320 330 340 350
PFGRELSKEE AYVQGLDAKT GASLKLTILN AEGRVWNLVA GGGASVVYAD
360 370 380 390 400
AVAVNGAADE LANYGEYSGA PTDGQTYEYA KTVLDLMTRG EPRADGKVLF
410 420 430 440 450
IGGGIANFTS PAVTFRAIAR ALGDYKDKLH AHKVSIWVRR AGPNYQEGLR
460 470 480 490
VIREAGKKFD LPLKVYGPEC HISGIVPMGL GKAPVEAEWQ MA
Length:492
Mass (Da):53,943
Last modified:January 1, 1998 - v1
Checksum:i7B3FE2529B786CDA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB16586.1.
PIRiT38156.
RefSeqiNP_593246.1. NM_001018643.2.

Genome annotation databases

EnsemblFungiiSPAC22A12.16.1; SPAC22A12.16.1:pep; SPAC22A12.16.
GeneIDi2541811.
KEGGispo:SPAC22A12.16.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB16586.1.
PIRiT38156.
RefSeqiNP_593246.1. NM_001018643.2.

3D structure databases

ProteinModelPortaliO13907.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278302. 6 interactions.
MINTiMINT-4668878.

PTM databases

iPTMnetiO13907.

Proteomic databases

MaxQBiO13907.
PRIDEiO13907.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC22A12.16.1; SPAC22A12.16.1:pep; SPAC22A12.16.
GeneIDi2541811.
KEGGispo:SPAC22A12.16.

Organism-specific databases

EuPathDBiFungiDB:SPAC22A12.16.
PomBaseiSPAC22A12.16.

Phylogenomic databases

HOGENOMiHOG000151490.
InParanoidiO13907.
KOiK01648.
OMAiVIMDPER.
OrthoDBiEOG7Z69NB.
PhylomeDBiO13907.

Miscellaneous databases

NextBioi20802899.
PROiO13907.

Family and domain databases

Gene3Di3.30.470.20. 1 hit.
3.40.50.261. 1 hit.
InterProiIPR013650. ATP-grasp_succ-CoA_synth-type.
IPR013816. ATP_grasp_subdomain_2.
IPR032263. Citrate-bd.
IPR017866. Succ-CoA_synthase_bsu_CS.
IPR016102. Succinyl-CoA_synth-like.
[Graphical view]
PfamiPF08442. ATP-grasp_2. 1 hit.
PF16114. Citrate_bind. 1 hit.
[Graphical view]
SUPFAMiSSF52210. SSF52210. 1 hit.
PROSITEiPS01217. SUCCINYL_COA_LIG_3. 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.
  2. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiACL2_SCHPO
AccessioniPrimary (citable) accession number: O13907
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: January 1, 1998
Last modified: January 20, 2016
This is version 103 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. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. 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.