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UniProtKB - P80210 (PURA_YEAST)

Entry version 188 (25 May 2022)
Sequence version 3 (23 Jan 2007)
Previous versions | rss
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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 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

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

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

Saccharomyces Genome Database

More...SGDi		S000005164, ADE12

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:YNL220W

<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

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P80210

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

AlphaFoldDBiP80210
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

SGDiS000005164, ADE12
VEuPathDBiFungiDB:YNL220W

Phylogenomic databases

eggNOGiKOG1355, Eukaryota
GeneTreeiENSGT00390000015553
HOGENOMiCLU_029848_3_2_1
InParanoidiP80210
OMAiFHHAKPI

Enzyme and pathway databases

UniPathwayiUPA00075;UER00335
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

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: May 25, 2022
This is version 188 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
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families
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