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Protein

Probable ATP-citrate synthase subunit 2

Gene

SPAC22A12.16

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionAcyltransferase, Transferase
Biological processLipid biosynthesis, Lipid metabolism
LigandATP-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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003401131 – 492Probable ATP-citrate synthase subunit 2Add BLAST492

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei24Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO13907.
PaxDbiO13907.
PRIDEiO13907.

PTM databases

iPTMnetiO13907.

Interactioni

Subunit structurei

Composed of two subunits.By similarity

Protein-protein interaction databases

BioGridi278302. 6 interactors.
STRINGi4896.SPAC22A12.16.1.

Structurei

3D structure databases

ProteinModelPortaliO13907.
SMRiO13907.
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.
OMAiFECGVKW.
OrthoDBiEOG092C20LB.
PhylomeDBiO13907.

Family and domain databases

Gene3Di3.40.50.261. 1 hit.
InterProiView protein in InterPro
IPR013650. ATP-grasp_succ-CoA_synth-type.
IPR032263. Citrate-bd.
IPR017866. Succ-CoA_synthase_bsu_CS.
IPR016102. Succinyl-CoA_synth-like.
PfamiView protein in Pfam
PF08442. ATP-grasp_2. 1 hit.
PF16114. Citrate_bind. 1 hit.
SUPFAMiSSF52210. SSF52210. 1 hit.
PROSITEiView protein in PROSITE
PS01217. SUCCINYL_COA_LIG_3. 1 hit.

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.

Entry informationi

Entry nameiACL2_SCHPO
AccessioniPrimary (citable) accession number: O13907
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: January 1, 1998
Last modified: February 28, 2018
This is version 115 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome