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UniProtKB - Q12680 (GLT1_YEAST)

Entry version 196 (25 May 2022)
Sequence version 2 (05 Sep 2006)
Previous versions | rss
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Protein

Glutamate synthase [NADH]

Gene

GLT1

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

Forms L-glutamate from L-glutamine and 2-oxoglutarate. Represents an alternative pathway to L-glutamate dehydrogenase for the biosynthesis of L-glutamate. Participates with glutamine synthetase in ammonia assimilation processes. The enzyme is specific for NADH, L-glutamine and 2-oxoglutarate.

2 Publications

Miscellaneous

Present with 18900 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

Protein has several cofactor binding sites:

<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 homocysteine sulfonamide.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=280 µM for L-glutamine2 Publications
  2. KM=40 µM for 2-oxoglutarate2 Publications
  3. KM=7 µM for NADH2 Publications

pH dependencei

Optimum pH is 7-7.5. Active from pH 6 to 9.2 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: L-glutamate biosynthesis via GLT pathway

This protein is involved in step 1 of the subpathway that synthesizes L-glutamate from 2-oxoglutarate and L-glutamine (NAD(+) route). This subpathway is part of the pathway L-glutamate biosynthesis via GLT pathway, 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 from 2-oxoglutarate and L-glutamine (NAD(+) route), the pathway L-glutamate biosynthesis via GLT pathway and in Amino-acid biosynthesis.

Pathwayi: nitrogen metabolism

This protein is involved in the pathway nitrogen metabolism, which is part of Energy metabolism.
View all proteins of this organism that are known to be involved in the pathway nitrogen metabolism and in Energy 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 sitei54For GATase activityBy similarity1
<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 bindingi1185Iron-sulfur (3Fe-4S)By similarity1
Metal bindingi1191Iron-sulfur (3Fe-4S)By similarity1
Metal bindingi1196Iron-sulfur (3Fe-4S)By similarity1

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 bindingi1132 – 1189FMNBy similarityAdd BLAST58
Nucleotide bindingi1928 – 1942NADSequence analysisAdd BLAST15

<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 functionOxidoreductase
Biological processAmino-acid biosynthesis, Glutamate biosynthesis
Ligand3Fe-4S, FAD, Flavoprotein, FMN, Iron, Iron-sulfur, Metal-binding, NAD

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		Q12680

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

More...UniPathwayi		UPA00045
UPA00634;UER00690

<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:
Glutamate synthase [NADH] (EC:1.4.1.143 Publications)
Alternative name(s):
NADH-GOGAT
<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:GLT1
Ordered Locus Names:YDL171C
<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 IV

Organism-specific databases

Saccharomyces Genome Database

More...SGDi		S000002330, GLT1

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:YDL171C

<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

<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 describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_00000116121 – 531 PublicationAdd BLAST53
<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_000001161354 – 2145Glutamate synthase [NADH]Add BLAST2092

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 residuei2070PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein, Zymogen

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q12680

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

More...PaxDbi		Q12680

PRoteomics IDEntifications database

More...PRIDEi		Q12680

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q12680

<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

Homotrimer.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		31894, 178 interactors

Database of interacting proteins

More...DIPi		DIP-6490N

Protein interaction database and analysis system

More...IntActi		Q12680, 35 interactors

Molecular INTeraction database

More...MINTi		Q12680

STRING: functional protein association networks

More...STRINGi		4932.YDL171C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q12680, 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		Q12680

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

More...SMRi		Q12680

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%5Fand%5Fdomains%5Fsection">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>Domaini54 – 455Glutamine amidotransferase type-2PROSITE-ProRule annotationAdd BLAST402

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili1551 – 1600Sequence analysisAdd BLAST50

<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 synthase family.Curated

Keywords - Domaini

Coiled coil, Glutamine amidotransferase

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0399, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000172171

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000422_8_2_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q12680

Identification of Orthologs from Complete Genome Data

More...OMAi		TVFRLQH

Family and domain databases

Conserved Domains Database

More...CDDi		cd00982, gltB_C, 1 hit
cd02808, GltS_FMN, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.1060.10, 1 hit
2.160.20.60, 1 hit
3.20.20.70, 2 hits
3.50.50.60, 2 hits
3.60.20.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR013785, Aldolase_TIM
IPR028261, DPD_II
IPR036188, FAD/NAD-bd_sf
IPR023753, FAD/NAD-binding_dom
IPR017932, GATase_2_dom
IPR002489, Glu_synth_asu_C
IPR036485, Glu_synth_asu_C_sf
IPR006982, Glu_synth_centr_N
IPR012220, Glu_synth_euk
IPR002932, Glu_synthdom
IPR006005, Glut_synth_ssu1
IPR009051, Helical_ferredxn
IPR029055, Ntn_hydrolases_N

Pfam protein domain database

More...Pfami		View protein in Pfam
PF14691, Fer4_20, 1 hit
PF00310, GATase_2, 1 hit
PF04898, Glu_syn_central, 1 hit
PF01645, Glu_synthase, 1 hit
PF01493, GXGXG, 1 hit
PF07992, Pyr_redox_2, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000187, GOGAT, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF56235, SSF56235, 1 hit
SSF69336, SSF69336, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01317, GOGAT_sm_gam, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51278, GATASE_TYPE_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.

Q12680-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPVLKSDNFD PLEEAYEGGT IQNYNDEHHL HKSWANVIPD KRGLYDPDYE 
        60         70         80         90        100
HDACGVGFVA NKHGEQSHKI VTDARYLLVN MTHRGAVSSD GNGDGAGILL 
       110        120        130        140        150
GIPHEFMKRE FKLDLDLDIP EMGKYAVGNV FFKKNEKNNK KNLIKCQKIF 
       160        170        180        190        200
EDLAASFNLS VLGWRNVPVD STILGDVALS REPTILQPLL VPLYDEKQPE 
       210        220        230        240        250
FNETKFRTQL YLLRKEASLQ IGLENWFYVC SLNNTTIVYK GQLTPAQVYN 
       260        270        280        290        300
YYPDLTNAHF KSHMALVHSR FSTNTFPSWD RAQPLRWLAH NGEINTLRGN 
       310        320        330        340        350
KNWMRSREGV MNSATFKDEL DKLYPIIEEG GSDSAALDNV LELLTINGTL 
       360        370        380        390        400
SLPEAVMMMV PEAYHKDMDS DLKAWYDWAA CLMEPWDGPA LLTFTDGRYC 
       410        420        430        440        450
GAILDRNGLR PCRYYITSDD RVICASEVGV IPIENSLVVQ KGKLKPGDLF 
       460        470        480        490        500
LVDTQLGEMV DTKKLKSQIS KRQDFKSWLS KVIKLDDLLS KTANLVPKEF 
       510        520        530        540        550
ISQDSLSLKV QSDPRLLANG YTFEQVTFLL TPMALTGKEA LGSMGNDAPL 
       560        570        580        590        600
ACLNENPVLL YDYFRQLFAQ VTNPPIDPIR EANVMSLECY VGPQGNLLEM 
       610        620        630        640        650
HSSQCDRLLL KSPILHWNEF QALKNIEAAY PSWSVAEIDI TFDKSEGLLG 
       660        670        680        690        700
YTDTIDKITK LASEAIDDGK KILIITDRKM GANRVSISSL IAISCIHHHL 
       710        720        730        740        750
IRNKQRSQVA LILETGEARE IHHFCVLLGY GCDGVYPYLA METLVRMNRE 
       760        770        780        790        800
GLLRNVNNDN DTLEEGQILE NYKHAIDAGI LKVMSKMGIS TLASYKGAQI 
       810        820        830        840        850
FEALGLDNSI VDLCFTGTSS RIRGVTFEYL AQDAFSLHER GYPSRQTISK 
       860        870        880        890        900
SVNLPESGEY HFRDGGYKHV NEPTAIASLQ DTVRNKNDVS WQLYVKKEME 
       910        920        930        940        950
AIRDCTLRGL LELDFENSVS IPLEQVEPWT EIARRFASGA MSYGSISMEA 
       960        970        980        990       1000
HSTLAIAMNR LGAKSNCGEG GEDAERSAVQ ENGDTMRSAI KQVASARFGV 
      1010       1020       1030       1040       1050
TSYYLSDADE IQIKIAQGAK PGEGGELPAH KVSKDIAKTR HSTPNVGLIS 
      1060       1070       1080       1090       1100
PPPHHDIYSI EDLKQLIYDL KCANPRAGIS VKLVSEVGVG IVASGVAKAK 
      1110       1120       1130       1140       1150
ADHILVSGHD GGTGAARWTS VKYAGLPWEL GLAETHQTLV LNDLRRNVVV 
      1160       1170       1180       1190       1200
QTDGQLRTGF DIAVAVLLGA ESFTLATVPL IAMGCVMLRR CHLNSCAVGI 
      1210       1220       1230       1240       1250
ATQDPYLRSK FKGQPEHVIN FFYYLIQDLR QIMAKLGFRT IDEMVGHSEK 
      1260       1270       1280       1290       1300
LKKRDDVNAK AINIDLSPIL TPAHVIRPGV PTKFTKKQDH KLHTRLDNKL 
      1310       1320       1330       1340       1350
IDEAEVTLDR GLPVNIDASI INTDRALGST LSYRVSKKFG EDGLPKDTVV 
      1360       1370       1380       1390       1400
VNIEGSAGQS FGAFLASGIT FILNGDANDY VGKGLSGGII VIKPPKDSKF 
      1410       1420       1430       1440       1450
KSDENVIVGN TCFYGATSGT AFISGSAGER FGVRNSGATI VVERIKGNNA 
      1460       1470       1480       1490       1500
FEYMTGGRAI VLSQMESLNA FSGATGGIAY CLTSDYDDFV GKINKDTVEL 
      1510       1520       1530       1540       1550
ESLCDPVEIA FVKNLIQEHW NYTQSDLAAR ILGNFNHYLK DFVKVIPTDY 
      1560       1570       1580       1590       1600
KKVLLKEKAE AAKAKAKATS EYLKKFRSNQ EVDDEVNTLL IANQKAKEQE 
      1610       1620       1630       1640       1650
KKKSITISNK ATLKEPKVVD LEDAVPDSKQ LEKNSERIEK TRGFMIHKRR 
      1660       1670       1680       1690       1700
HETHRDPRTR VNDWKEFTNP ITKKDAKYQT ARCMDCGTPF CLSDTGCPLS 
      1710       1720       1730       1740       1750
NIIPKFNELL FKNQWKLALD KLLETNNFPE FTGRVCPAPC EGACTLGIIE 
      1760       1770       1780       1790       1800
DPVGIKSVER IIIDNAFKEG WIKPCPPSTR TGFTVGVIGS GPAGLACADM 
      1810       1820       1830       1840       1850
LNRAGHTVTV YERSDRCGGL LMYGIPNMKL DKAIVQRRID LLSAEGIDFV 
      1860       1870       1880       1890       1900
TNTEIGKTIS MDELKNKHNA VVYAIGSTIP RDLPIKGREL KNIDFAMQLL 
      1910       1920       1930       1940       1950
ESNTKALLNK DLEIIREKIQ GKKVIVVGGG DTGNDCLGTS VRHGAASVLN 
      1960       1970       1980       1990       2000
FELLPEPPVE RAKDNPWPQW PRVMRVDYGH AEVKEHYGRD PREYCILSKE 
      2010       2020       2030       2040       2050
FIGNDEGEVT AIRTVRVEWK KSQSGVWQMV EIPNSEEIFE ADIILLSMGF 
      2060       2070       2080       2090       2100
VGPELINGND NEVKKTRRGT IATLDDSSYS IDGGKTFACG DCRRGQSLIV 
      2110       2120       2130       2140 
WAIQEGRKCA ASVDKFLMDG TTYLPSNGGI VQRDYKLLKE LASQV
Length:2,145
Mass (Da):238,102
Last modified:September 5, 2006 - 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:i78184877D2167A0D
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 conflicti166 – 173NVPVDSTI → TSRRFYY in CAA61505 (PubMed:8923741).Curated8
Sequence conflicti450 – 452FLV → IPS in CAA61505 (PubMed:8923741).Curated3
Sequence conflicti1753V → L in CAA61505 (PubMed:8923741).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
X89221 Genomic DNA Translation: CAA61505.1
Z67750 Genomic DNA Translation: CAA91574.1
Z74219 Genomic DNA Translation: CAA98745.1
BK006938 Genomic DNA Translation: DAA11690.1

Protein sequence database of the Protein Information Resource

More...PIRi		S61041

NCBI Reference Sequences

More...RefSeqi		NP_010110.1, NM_001180231.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YDL171C_mRNA; YDL171C; YDL171C

Database of genes from NCBI RefSeq genomes

More...GeneIDi		851383

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YDL171C

<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
X89221 Genomic DNA Translation: CAA61505.1
Z67750 Genomic DNA Translation: CAA91574.1
Z74219 Genomic DNA Translation: CAA98745.1
BK006938 Genomic DNA Translation: DAA11690.1
PIRiS61041
RefSeqiNP_010110.1, NM_001180231.1

3D structure databases

AlphaFoldDBiQ12680
SMRiQ12680
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi31894, 178 interactors
DIPiDIP-6490N
IntActiQ12680, 35 interactors
MINTiQ12680
STRINGi4932.YDL171C

PTM databases

iPTMnetiQ12680

Proteomic databases

MaxQBiQ12680
PaxDbiQ12680
PRIDEiQ12680

Genome annotation databases

EnsemblFungiiYDL171C_mRNA; YDL171C; YDL171C
GeneIDi851383
KEGGisce:YDL171C

Organism-specific databases

SGDiS000002330, GLT1
VEuPathDBiFungiDB:YDL171C

Phylogenomic databases

eggNOGiKOG0399, Eukaryota
GeneTreeiENSGT00940000172171
HOGENOMiCLU_000422_8_2_1
InParanoidiQ12680
OMAiTVFRLQH

Enzyme and pathway databases

UniPathwayiUPA00045
UPA00634;UER00690
SABIO-RKiQ12680

Miscellaneous databases

Protein Ontology

More...PROi		PR:Q12680
RNActiQ12680, protein

Family and domain databases

CDDicd00982, gltB_C, 1 hit
cd02808, GltS_FMN, 1 hit
Gene3Di1.10.1060.10, 1 hit
2.160.20.60, 1 hit
3.20.20.70, 2 hits
3.50.50.60, 2 hits
3.60.20.10, 1 hit
InterProiView protein in InterPro
IPR013785, Aldolase_TIM
IPR028261, DPD_II
IPR036188, FAD/NAD-bd_sf
IPR023753, FAD/NAD-binding_dom
IPR017932, GATase_2_dom
IPR002489, Glu_synth_asu_C
IPR036485, Glu_synth_asu_C_sf
IPR006982, Glu_synth_centr_N
IPR012220, Glu_synth_euk
IPR002932, Glu_synthdom
IPR006005, Glut_synth_ssu1
IPR009051, Helical_ferredxn
IPR029055, Ntn_hydrolases_N
PfamiView protein in Pfam
PF14691, Fer4_20, 1 hit
PF00310, GATase_2, 1 hit
PF04898, Glu_syn_central, 1 hit
PF01645, Glu_synthase, 1 hit
PF01493, GXGXG, 1 hit
PF07992, Pyr_redox_2, 1 hit
PIRSFiPIRSF000187, GOGAT, 1 hit
SUPFAMiSSF56235, SSF56235, 1 hit
SSF69336, SSF69336, 1 hit
TIGRFAMsiTIGR01317, GOGAT_sm_gam, 1 hit
PROSITEiView protein in PROSITE
PS51278, GATASE_TYPE_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 nameiGLT1_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: Q12680
Secondary accession number(s): D6VRI0, Q12290
<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: November 1, 1997
Last sequence update: September 5, 2006
Last modified: May 25, 2022
This is version 196 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

Direct protein sequencing, 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
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