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UniProtKB - Q9P7W3 (ACL1_SCHPO)

Entry version 128 (16 Oct 2019)
Sequence version 1 (01 Oct 2000)
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Protein

Probable ATP-citrate synthase subunit 1

Gene

SPBC1703.07

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

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes the formation of cytosolic acetyl-CoA, which is mainly used for the biosynthesis of fatty acids and sterols.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi238MagnesiumBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei280Tele-phosphohistidine intermediateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi221 – 241ATPBy similarityAdd BLAST21
Nucleotide bindingi272 – 298ATPBy similarityAdd BLAST27

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionTransferase
Biological processLipid biosynthesis, Lipid metabolism
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-SPO-163765 ChREBP activates metabolic gene expression
R-SPO-6798695 Neutrophil degranulation
R-SPO-75105 Fatty acyl-CoA biosynthesis

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
ORF Names:SPBC1703.07
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri284812 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002485 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome II

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		FungiDB:SPBC1703.07

Schizosaccharomyces pombe database

More...PomBasei		SPBC1703.07

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001027861 – 615Probable ATP-citrate synthase subunit 1Add BLAST615

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei359Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q9P7W3

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q9P7W3

PRoteomics IDEntifications database

More...PRIDEi		Q9P7W3

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9P7W3

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Composed of two subunits.

By similarity

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		276425, 5 interactors

STRING: functional protein association networks

More...STRINGi		4896.SPBC1703.07.1

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q9P7W3

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni299 – 309CoA-bindingSequence analysisAdd BLAST11

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the succinate/malate CoA ligase alpha subunit family.Curated

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000151479

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9P7W3

KEGG Orthology (KO)

More...KOi		K01648

Identification of Orthologs from Complete Genome Data

More...OMAi		HAGAKEG

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9P7W3

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.230.10, 1 hit
1.10.580.10, 1 hit
3.40.50.261, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR016142 Citrate_synth-like_lrg_a-sub
IPR016143 Citrate_synth-like_sm_a-sub
IPR002020 Citrate_synthase
IPR036969 Citrate_synthase_sf
IPR033847 Citrt_syn/SCS-alpha_CS
IPR003781 CoA-bd
IPR005811 CoA_ligase
IPR036291 NAD(P)-bd_dom_sf
IPR017866 Succ-CoA_synthase_bsu_CS
IPR016102 Succinyl-CoA_synth-like

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00285 Citrate_synt, 1 hit
PF02629 CoA_binding, 1 hit
PF00549 Ligase_CoA, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00881 CoA_binding, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48256 SSF48256, 1 hit
SSF51735 SSF51735, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS01216 SUCCINYL_COA_LIG_1, 1 hit
PS01217 SUCCINYL_COA_LIG_3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q9P7W3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAGSVDKPSY ELFSKDTRAF VYGMQTKAVQ GMLDFDYMCG RTVPSVAAII 
        60         70         80         90        100
YTFGSQSISK LYWGTKEILL PVYRTIEEAC TKHPEVDVVV NFASSRSAYA 
       110        120        130        140        150
STMELMEFPQ IRCIAIIAEG VPERRAREIL VTSKEKNVVI IGPATVGGIK 
       160        170        180        190        200
PGCFKIGNTG GMMDNIVASK LYRPGSVAYV SKSGGMSNEL NNIISHTTDG 
       210        220        230        240        250
VYEGIAIGGD RYPGTTFIDH LIRFEADPAC KLMVLLGEVG GVEEYRVIEA 
       260        270        280        290        300
VKNGTIKKPI VAWAIGTCSS MFKTEVQFGH AGSFANSELE TAVAKNQAMR 
       310        320        330        340        350
EAGIYVPETF EKLPALLQEV YEGLVKKGVI VPQPEVAPPN IPLDYAWAKE 
       360        370        380        390        400
LGLVRKPSSF ICTISNDRGS ELTYNNVPIS KVFEEELGIG GVISLLWLRR 
       410        420        430        440        450
RLPSYATKFL EMVLQLTADH GPCVSGAMNT IITTRAGKDL ISSLVAGLLT 
       460        470        480        490        500
IGTRFGGALD GAAQEFSKAY DAGLSPRAFV DSCRKANKLI PGIGHRIKSR 
       510        520        530        540        550
NNPDLRVELV KGYVKKNFPS TKLLDYALAV ENVTTSKKDN LILNVDGCIA 
       560        570        580        590        600
VCFVDLLRNC GAFTLEEANE YINLGILNGM FVLGRSIGLI GHHLDQKRLR 
       610 
APLYRHPWDD FLYLS
Length:615
Mass (Da):67,204
Last modified:October 1, 2000 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iD9998607127639C4
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
CU329671 Genomic DNA Translation: CAB66451.1
D89194 mRNA Translation: BAA13855.1

Protein sequence database of the Protein Information Resource

More...PIRi		T42753
T50320

NCBI Reference Sequences

More...RefSeqi		NP_596202.1, NM_001022121.2

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		SPBC1703.07.1; SPBC1703.07.1:pep; SPBC1703.07

Database of genes from NCBI RefSeq genomes

More...GeneIDi		2539879

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		spo:SPBC1703.07

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA Translation: CAB66451.1
D89194 mRNA Translation: BAA13855.1
PIRiT42753
T50320
RefSeqiNP_596202.1, NM_001022121.2

3D structure databases

SMRiQ9P7W3
ModBaseiSearch...

Protein-protein interaction databases

BioGridi276425, 5 interactors
STRINGi4896.SPBC1703.07.1

PTM databases

iPTMnetiQ9P7W3

Proteomic databases

MaxQBiQ9P7W3
PaxDbiQ9P7W3
PRIDEiQ9P7W3

Genome annotation databases

EnsemblFungiiSPBC1703.07.1; SPBC1703.07.1:pep; SPBC1703.07
GeneIDi2539879
KEGGispo:SPBC1703.07

Organism-specific databases

EuPathDBiFungiDB:SPBC1703.07
PomBaseiSPBC1703.07

Phylogenomic databases

HOGENOMiHOG000151479
InParanoidiQ9P7W3
KOiK01648
OMAiHAGAKEG
PhylomeDBiQ9P7W3

Enzyme and pathway databases

ReactomeiR-SPO-163765 ChREBP activates metabolic gene expression
R-SPO-6798695 Neutrophil degranulation
R-SPO-75105 Fatty acyl-CoA biosynthesis

Miscellaneous databases

Protein Ontology

More...PROi		PR:Q9P7W3

Family and domain databases

Gene3Di1.10.230.10, 1 hit
1.10.580.10, 1 hit
3.40.50.261, 1 hit
InterProiView protein in InterPro
IPR016142 Citrate_synth-like_lrg_a-sub
IPR016143 Citrate_synth-like_sm_a-sub
IPR002020 Citrate_synthase
IPR036969 Citrate_synthase_sf
IPR033847 Citrt_syn/SCS-alpha_CS
IPR003781 CoA-bd
IPR005811 CoA_ligase
IPR036291 NAD(P)-bd_dom_sf
IPR017866 Succ-CoA_synthase_bsu_CS
IPR016102 Succinyl-CoA_synth-like
PfamiView protein in Pfam
PF00285 Citrate_synt, 1 hit
PF02629 CoA_binding, 1 hit
PF00549 Ligase_CoA, 1 hit
SMARTiView protein in SMART
SM00881 CoA_binding, 1 hit
SUPFAMiSSF48256 SSF48256, 1 hit
SSF51735 SSF51735, 1 hit
PROSITEiView protein in PROSITE
PS01216 SUCCINYL_COA_LIG_1, 1 hit
PS01217 SUCCINYL_COA_LIG_3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiACL1_SCHPO
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9P7W3
Secondary accession number(s): P78844
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: October 1, 2000
Last modified: October 16, 2019
This is version 128 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
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