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UniProtKB - P80210 (PURA_YEAST)

Entry version 185 (02 Dec 2020)
Sequence version 3 (23 Jan 2007)
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Protein

Adenylosuccinate synthetase

Gene

ADE12

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 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

Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.2 Publications

Miscellaneous

Present with 56800 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by GMP. Inhibited by chloride. Inhibited in a highly specific manner by the binding of a 44-base DNA oligonucleotide carrying the ARS core consensus sequence.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=1650 µM for L-aspartate2 Publications
  2. KM=200 µM for IMP2 Publications
  3. KM=1650 µM for GTP2 Publications

    pH dependencei

    Optimum pH is 8.0.2 Publications

    Temperature dependencei

    Optimum temperature is 35 degrees Celsius.2 Publications

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: AMP biosynthesis via de novo pathway

    This protein is involved in step 1 of the subpathway that synthesizes AMP from IMP.UniRule annotation
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Adenylosuccinate synthetase (ADE12)
    2. Adenylosuccinate lyase (ADE13)
    This subpathway is part of the pathway AMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes AMP from IMP, the pathway AMP biosynthesis via de novo pathway and in Purine metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei12Proton acceptorUniRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi12MagnesiumUniRule annotation1
    Metal bindingi39Magnesium; via carbonyl oxygenUniRule annotation1
    Active sitei40Proton donorUniRule annotation1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei134IMPUniRule annotation1
    Binding sitei148IMP; shared with dimeric partnerUniRule annotation1
    Binding sitei230IMPUniRule annotation1
    Binding sitei245IMPUniRule annotation1
    Binding sitei309IMPUniRule annotation1
    Binding sitei311GTPUniRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi11 – 17GTPUniRule annotation7
    Nucleotide bindingi39 – 41GTPUniRule annotation3
    Nucleotide bindingi337 – 339GTPUniRule annotation3
    Nucleotide bindingi419 – 421GTPUniRule annotation3

    <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

    • 'de novo' AMP biosynthetic process Source: GO_Central
    • IMP metabolic process Source: GO_Central
    • purine nucleotide biosynthetic process Source: SGD
    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 functionLigase
    Biological processPurine biosynthesis
    LigandGTP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...    BioCyci    		MetaCyc:YNL220W-MONOMER

    Reactome - a knowledgebase of biological pathways and processes

    More...    Reactomei    		R-SCE-73817, Purine ribonucleoside monophosphate biosynthesis

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...    UniPathwayi    		UPA00075;UER00335

    <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%5Fand%5Ftaxonomy%5Fsection">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:
    Adenylosuccinate synthetaseUniRule annotation (EC:6.3.4.4UniRule annotation)
    Short name:
    AMPSaseUniRule annotation
    Short name:
    AS-synthetase
    Short name:
    AdSSUniRule annotation
    Alternative name(s):
    IMP--aspartate ligaseUniRule annotation
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
    Name:ADE12UniRule annotation
    Ordered Locus Names:YNL220W
    ORF Names:N1290
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri559292 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
    • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 XIV

    Organism-specific databases

    Eukaryotic Pathogen and Host Database Resources

    More...    EuPathDBi    		FungiDB:YNL220W

    Saccharomyces Genome Database

    More...    SGDi    		S000005164, ADE12

    <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

    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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved2 Publications
    <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000951382 – 433Adenylosuccinate synthetaseAdd BLAST432

    Proteomic databases

    MaxQB - The MaxQuant DataBase

    More...    MaxQBi    		P80210

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

    More...    PaxDbi    		P80210

    PRoteomics IDEntifications database

    More...    PRIDEi    		P80210

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...    iPTMneti    		P80210

    <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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.

    UniRule annotation3 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Hide details

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...    BioGRIDi    		35616, 155 interactors

    Database of interacting proteins

    More...    DIPi    		DIP-4286N

    Protein interaction database and analysis system

    More...    IntActi    		P80210, 8 interactors

    Molecular INTeraction database

    More...    MINTi    		P80210

    STRING: functional protein association networks

    More...    STRINGi    		4932.YNL220W

    Miscellaneous databases

    RNAct, Protein-RNA interaction predictions for model organisms.

    More...    RNActi    		P80210, protein

    <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    		P80210

    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>Regioni12 – 15IMP bindingUniRule annotation4
    Regioni37 – 40IMP bindingUniRule annotation4
    Regioni305 – 311Substrate bindingUniRule annotation7

    <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 adenylosuccinate synthetase family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		KOG1355, Eukaryota

    Ensembl GeneTree

    More...    GeneTreei    		ENSGT00390000015553

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_029848_3_2_1

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P80210

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		FHHAKPI

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd03108, AdSS, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...    Gene3Di    		1.10.300.10, 1 hit
    3.40.440.10, 1 hit
    3.90.170.10, 1 hit

    HAMAP database of protein families

    More...    HAMAPi    		MF_00011, Adenylosucc_synth, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...    InterProi    		View protein in InterPro
    IPR018220, Adenylosuccin_syn_GTP-bd
    IPR033128, Adenylosuccin_syn_Lys_AS
    IPR042109, Adenylosuccinate_synth_dom1
    IPR042110, Adenylosuccinate_synth_dom2
    IPR042111, Adenylosuccinate_synth_dom3
    IPR001114, Adenylosuccinate_synthetase
    IPR027417, P-loop_NTPase

    The PANTHER Classification System

    More...    PANTHERi    		PTHR11846, PTHR11846, 1 hit

    Pfam protein domain database

    More...    Pfami    		View protein in Pfam
    PF00709, Adenylsucc_synt, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...    SMARTi    		View protein in SMART
    SM00788, Adenylsucc_synt, 1 hit

    Superfamily database of structural and functional annotation

    More...    SUPFAMi    		SSF52540, SSF52540, 1 hit

    TIGRFAMs; a protein family database

    More...    TIGRFAMsi    		TIGR00184, purA, 1 hit

    PROSITE; a protein domain and family database

    More...    PROSITEi    		View protein in PROSITE
    PS01266, ADENYLOSUCCIN_SYN_1, 1 hit
    PS00513, ADENYLOSUCCIN_SYN_2, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    P80210-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MVNVVLGSQW GDEGKGKLVD LLVGKYDIVA RCAGGNNAGH TIVVDGVKYD 
            60         70         80         90        100
    FHMLPSGLVN PNCQNLLGNG VVIHVPSFFK ELETLEAKGL KNARSRLFVS 
           110        120        130        140        150
    SRAHLVFDFH QVTDKLRELE LSGRSKDGKN IGTTGKGIGP TYSTKASRSG 
           160        170        180        190        200
    LRVHHLVNDQ PGAWEEFVAR YKRLLETRRQ RYGDFEYDFE AKLAEYKKLR 
           210        220        230        240        250
    EQLKPFVVDS VVFMHNAIEA KKKILVEGAN ALMLDIDFGT YPYVTSSNTG 
           260        270        280        290        300
    IGGVLTGLGI PPRTIDEIYG VVKAYTTRVG EGPFPTEQLN ENGEKLQTIG 
           310        320        330        340        350
    AEFGVTTGRK RRCGWLDLVV LKYSTLINGY TSLNITKLDV LDTFKEIPVG 
           360        370        380        390        400
    ISYSIQGKKL DLFPEDLNIL GKVEVEYKVL PGWDQDITKI TKYEDLPENA 
           410        420        430 
    KKYLKYIEDF VGVPVEWVGT GPARESMLHK EIK
    Length:433
    Mass (Da):48,279
    Last modified:January 23, 2007 - v3
    <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:i800E0F4062D9856F
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti237D → G AA sequence (PubMed:8376380).Curated1

    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
    		L22185 Genomic DNA Translation: AAA91338.1
    Z48671 Genomic DNA Translation: CAA88590.1
    Z71496 Genomic DNA Translation: CAA96123.1
    BK006947 Genomic DNA Translation: DAA10336.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		S48515

    NCBI Reference Sequences

    More...    RefSeqi    		NP_014179.1, NM_001183058.1

    Genome annotation databases

    Ensembl fungal genome annotation project

    More...    EnsemblFungii    		YNL220W_mRNA; YNL220W; YNL220W

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		855501

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		sce:YNL220W

    <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
    		L22185 Genomic DNA Translation: AAA91338.1
    Z48671 Genomic DNA Translation: CAA88590.1
    Z71496 Genomic DNA Translation: CAA96123.1
    BK006947 Genomic DNA Translation: DAA10336.1
    PIRiS48515
    RefSeqiNP_014179.1, NM_001183058.1

    3D structure databases

    SMRiP80210
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGRIDi35616, 155 interactors
    DIPiDIP-4286N
    IntActiP80210, 8 interactors
    MINTiP80210
    STRINGi4932.YNL220W

    PTM databases

    iPTMnetiP80210

    Proteomic databases

    MaxQBiP80210
    PaxDbiP80210
    PRIDEiP80210

    Genome annotation databases

    EnsemblFungiiYNL220W_mRNA; YNL220W; YNL220W
    GeneIDi855501
    KEGGisce:YNL220W

    Organism-specific databases

    EuPathDBiFungiDB:YNL220W
    SGDiS000005164, ADE12

    Phylogenomic databases

    eggNOGiKOG1355, Eukaryota
    GeneTreeiENSGT00390000015553
    HOGENOMiCLU_029848_3_2_1
    InParanoidiP80210
    OMAiFHHAKPI

    Enzyme and pathway databases

    UniPathwayiUPA00075;UER00335
    BioCyciMetaCyc:YNL220W-MONOMER
    ReactomeiR-SCE-73817, Purine ribonucleoside monophosphate biosynthesis

    Miscellaneous databases

    Protein Ontology

    More...    PROi    		PR:P80210
    RNActiP80210, protein

    Family and domain databases

    CDDicd03108, AdSS, 1 hit
    Gene3Di1.10.300.10, 1 hit
    3.40.440.10, 1 hit
    3.90.170.10, 1 hit
    HAMAPiMF_00011, Adenylosucc_synth, 1 hit
    InterProiView protein in InterPro
    IPR018220, Adenylosuccin_syn_GTP-bd
    IPR033128, Adenylosuccin_syn_Lys_AS
    IPR042109, Adenylosuccinate_synth_dom1
    IPR042110, Adenylosuccinate_synth_dom2
    IPR042111, Adenylosuccinate_synth_dom3
    IPR001114, Adenylosuccinate_synthetase
    IPR027417, P-loop_NTPase
    PANTHERiPTHR11846, PTHR11846, 1 hit
    PfamiView protein in Pfam
    PF00709, Adenylsucc_synt, 1 hit
    SMARTiView protein in SMART
    SM00788, Adenylsucc_synt, 1 hit
    SUPFAMiSSF52540, SSF52540, 1 hit
    TIGRFAMsiTIGR00184, purA, 1 hit
    PROSITEiView protein in PROSITE
    PS01266, ADENYLOSUCCIN_SYN_1, 1 hit
    PS00513, ADENYLOSUCCIN_SYN_2, 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 nameiPURA_YEAST
    <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: P80210
    Secondary accession number(s): D6W0X0
    <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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: January 23, 2007
    Last modified: December 2, 2020
    This is version 185 of the entry and version 3 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

    Direct protein sequencing, Reference proteome

    Documents

    1. Yeast chromosome XIV
      Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families
    4. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
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