Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 183 (29 Sep 2021)
Sequence version 2 (01 Oct 1996)
Previous versions | rss
Add a publicationFeedback
Protein

Glutamate 5-kinase

Gene

PRO1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's 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 transfer of a phosphate group to glutamate to form glutamate 5-phosphate which rapidly cyclizes to 5-oxoproline.

Miscellaneous

Present with 10400 molecules/cell in log phase SD medium.1 Publication

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-proline biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-glutamate 5-semialdehyde from L-glutamate. This subpathway is part of the pathway L-proline biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-glutamate 5-semialdehyde from L-glutamate, the pathway L-proline biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei56SubstrateBy similarity1
Binding sitei143SubstrateBy similarity1
Binding sitei155Substrate; via amide nitrogenBy 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 bindingi175 – 176ATPBy similarity2
Nucleotide bindingi219 – 225ATPBy similarity7

<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

GO - Biological processi

<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 functionKinase, Transferase
Biological processAmino-acid biosynthesis, Proline biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.2.11, 984

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

More...
UniPathwayi
UPA00098;UER00359

<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:
Glutamate 5-kinase (EC:2.7.2.11)
Short name:
GK
Alternative name(s):
Gamma-glutamyl kinase
<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
Name:PRO1
Ordered Locus Names:YDR300C
ORF Names:D9740.12
<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>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's 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 identifieri559292 [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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<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
  • UP000002311 <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 IV

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000002708, PRO1

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:YDR300C

<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 '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_00001097681 – 428Glutamate 5-kinaseAdd BLAST428

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P32264

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

More...
PaxDbi
P32264

PRoteomics IDEntifications database

More...
PRIDEi
P32264

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
P32264

<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 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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
32352, 34 interactors

Database of interacting proteins

More...
DIPi
DIP-5221N

Protein interaction database and analysis system

More...
IntActi
P32264, 12 interactors

Molecular INTeraction database

More...
MINTi
P32264

STRING: functional protein association networks

More...
STRINGi
4932.YDR300C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P32264, 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
P32264

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini321 – 412PUAAdd BLAST92

<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 glutamate 5-kinase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1154, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00500000044903

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_025400_1_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P32264

Identification of Orthologs from Complete Genome Data

More...
OMAi
GRAEMIH

Family and domain databases

Conserved Domains Database

More...
CDDi
cd04242, AAK_G5K_ProB, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.30.130.10, 1 hit
3.40.1160.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00456, ProB, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036393, AceGlu_kinase-like_sf
IPR001048, Asp/Glu/Uridylate_kinase
IPR041739, G5K_ProB
IPR001057, Glu/AcGlu_kinase
IPR011529, Glu_5kinase
IPR005715, Glu_5kinase/COase_Synthase
IPR019797, Glutamate_5-kinase_CS
IPR002478, PUA
IPR015947, PUA-like_sf
IPR036974, PUA_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00696, AA_kinase, 1 hit
PF01472, PUA, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000729, GK, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00474, GLU5KINASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00359, PUA, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53633, SSF53633, 1 hit
SSF88697, SSF88697, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01027, proB, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00902, GLUTAMATE_5_KINASE, 1 hit
PS50890, PUA, 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.

P32264-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKDANESKSY TIVIKLGSSS LVDEKTKEPK LAIMSLIVET VVKLRRMGHK
60 70 80 90 100
VIIVSSGGIA VGLRTMRMNK RPKHLAEVQA IAAIGQGRLI GRWDLLFSQF
110 120 130 140 150
DQRIAQILLT RNDILDWTQY KNAQNTINEL LNMGVIPIVN ENDTLSVREI
160 170 180 190 200
KFGDNDTLSA ITSALIHADY LFLLTDVDCL YTDNPRTNPD AMPILVVPDL
210 220 230 240 250
SKGLPGVNTA GGSGSDVGTG GMETKLVAAD LATNAGVHTL IMKSDTPANI
260 270 280 290 300
GRIVEYMQTL ELDDENKVKQ AYNGDLTDLQ KREFEKLKAL NVPLHTKFIA
310 320 330 340 350
NDNKHHLKNR EFWILHGLVS KGAVVIDQGA YAALTRKNKA GLLPAGVIDV
360 370 380 390 400
QGTFHELECV DIKVGKKLPD GTLDPDFPLQ TVGKARCNYT SSELTKIKGL
410 420
HSDQIEEELG YNDSEYVAHR ENLAFPPR
Length:428
Mass (Da):47,162
Last modified:October 1, 1996 - v2
<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:i0DBAC7CA98051C80
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 conflicti332A → R in AAA34904 (PubMed:1350780).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
M85293 Genomic DNA Translation: AAA34904.1
U28374 Genomic DNA Translation: AAB64736.1
BK006938 Genomic DNA Translation: DAA12139.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S61186

NCBI Reference Sequences

More...
RefSeqi
NP_010586.3, NM_001180608.3

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YDR300C_mRNA; YDR300C; YDR300C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
851894

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YDR300C

<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
M85293 Genomic DNA Translation: AAA34904.1
U28374 Genomic DNA Translation: AAB64736.1
BK006938 Genomic DNA Translation: DAA12139.1
PIRiS61186
RefSeqiNP_010586.3, NM_001180608.3

3D structure databases

SMRiP32264
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi32352, 34 interactors
DIPiDIP-5221N
IntActiP32264, 12 interactors
MINTiP32264
STRINGi4932.YDR300C

Proteomic databases

MaxQBiP32264
PaxDbiP32264
PRIDEiP32264
TopDownProteomicsiP32264

Genome annotation databases

EnsemblFungiiYDR300C_mRNA; YDR300C; YDR300C
GeneIDi851894
KEGGisce:YDR300C

Organism-specific databases

SGDiS000002708, PRO1
VEuPathDBiFungiDB:YDR300C

Phylogenomic databases

eggNOGiKOG1154, Eukaryota
GeneTreeiENSGT00500000044903
HOGENOMiCLU_025400_1_1_1
InParanoidiP32264
OMAiGRAEMIH

Enzyme and pathway databases

UniPathwayiUPA00098;UER00359
BRENDAi2.7.2.11, 984

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P32264
RNActiP32264, protein

Family and domain databases

CDDicd04242, AAK_G5K_ProB, 1 hit
Gene3Di2.30.130.10, 1 hit
3.40.1160.10, 1 hit
HAMAPiMF_00456, ProB, 1 hit
InterProiView protein in InterPro
IPR036393, AceGlu_kinase-like_sf
IPR001048, Asp/Glu/Uridylate_kinase
IPR041739, G5K_ProB
IPR001057, Glu/AcGlu_kinase
IPR011529, Glu_5kinase
IPR005715, Glu_5kinase/COase_Synthase
IPR019797, Glutamate_5-kinase_CS
IPR002478, PUA
IPR015947, PUA-like_sf
IPR036974, PUA_sf
PfamiView protein in Pfam
PF00696, AA_kinase, 1 hit
PF01472, PUA, 1 hit
PIRSFiPIRSF000729, GK, 1 hit
PRINTSiPR00474, GLU5KINASE
SMARTiView protein in SMART
SM00359, PUA, 1 hit
SUPFAMiSSF53633, SSF53633, 1 hit
SSF88697, SSF88697, 1 hit
TIGRFAMsiTIGR01027, proB, 1 hit
PROSITEiView protein in PROSITE
PS00902, GLUTAMATE_5_KINASE, 1 hit
PS50890, PUA, 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 nameiPROB_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: P32264
Secondary accession number(s): D6VSS9
<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: October 1, 1993
Last sequence update: October 1, 1996
Last modified: September 29, 2021
This is version 183 of the entry and version 2 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

Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again