Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutamine synthetase

Gene

gln1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine.

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • glutamate-ammonia ligase activity Source: PomBase

GO - Biological processi

  • ammonia assimilation cycle Source: PomBase
  • cellular response to nitrogen starvation Source: PomBase
  • glutamine biosynthetic process Source: PomBase
  • nitrogen utilization Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_296172. Amino acid synthesis and interconversion (transamination).
REACT_305937. Astrocytic Glutamate-Glutamine Uptake And Metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamine synthetase (EC:6.3.1.2)
Short name:
GS
Alternative name(s):
Glutamate--ammonia ligase
Gene namesi
Name:gln1
ORF Names:SPAC23H4.06
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC23H4.06.
PomBaseiSPAC23H4.06. gln1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 359359Glutamine synthetasePRO_0000153162Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei273 – 2731Phosphoserine1 Publication
Modified residuei303 – 3031Phosphothreonine1 Publication
Modified residuei305 – 3051Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ09179.
PaxDbiQ09179.

Interactioni

Subunit structurei

Homooctamer.By similarity

Protein-protein interaction databases

BioGridi278246. 1 interaction.
MINTiMINT-4693794.

Structurei

3D structure databases

ProteinModelPortaliQ09179.
SMRiQ09179. Positions 23-356.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glutamine synthetase family.Curated

Phylogenomic databases

eggNOGiCOG0174.
HOGENOMiHOG000061500.
InParanoidiQ09179.
KOiK01915.
OMAiLWEPSHS.
OrthoDBiEOG7GTTD8.
PhylomeDBiQ09179.

Family and domain databases

Gene3Di3.30.590.10. 1 hit.
InterProiIPR008147. Gln_synt_beta.
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR008146. Gln_synth_cat_dom.
IPR027303. Gln_synth_gly_rich_site.
IPR027302. Gln_synth_N_conserv_site.
[Graphical view]
PfamiPF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view]
SUPFAMiSSF54368. SSF54368. 1 hit.
PROSITEiPS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q09179-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQYDVEPLL SKAAILNKYA DLPQNGKVMA EYIWIDGFNH LRSKTMTLDA
60 70 80 90 100
KPSSIDQLRV WNFDGSSTGQ APGNNSDTLL KPVAMYNDPF RRGDNILVLA
110 120 130 140 150
ACYTADGSPN GFNHRDACAK LLEKHADKET WFGIEQEYTM LDYYDRPFGW
160 170 180 190 200
PKGGFPGPQG PFYCGVGTGR VFARDIVEAH YKACLYAGIN ISGINAEVMP
210 220 230 240 250
SQWEYQVGPC AGIEMGDQLW MSRFLLHRIA EDFGVKISFH PKPILGDWNG
260 270 280 290 300
AGCHTNVSTK DTRAEGGIKA IESYLEKFAK RHKEHIAVYG DDNDLRLTGR
310 320 330 340 350
HETGSIDKFT YGVADRGASV RIPRSVAMNG CGYFEDRRPA SSIDPYLVTG

IITETMFEH
Length:359
Mass (Da):40,018
Last modified:July 15, 1998 - v2
Checksum:i96AACB6A912B3D0E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB11660.1.
PIRiT38322.
RefSeqiNP_593400.1. NM_001018832.2.

Genome annotation databases

EnsemblFungiiSPAC23H4.06.1; SPAC23H4.06.1:pep; SPAC23H4.06.
GeneIDi2541752.
KEGGispo:SPAC23H4.06.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB11660.1.
PIRiT38322.
RefSeqiNP_593400.1. NM_001018832.2.

3D structure databases

ProteinModelPortaliQ09179.
SMRiQ09179. Positions 23-356.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278246. 1 interaction.
MINTiMINT-4693794.

Proteomic databases

MaxQBiQ09179.
PaxDbiQ09179.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC23H4.06.1; SPAC23H4.06.1:pep; SPAC23H4.06.
GeneIDi2541752.
KEGGispo:SPAC23H4.06.

Organism-specific databases

EuPathDBiFungiDB:SPAC23H4.06.
PomBaseiSPAC23H4.06. gln1.

Phylogenomic databases

eggNOGiCOG0174.
HOGENOMiHOG000061500.
InParanoidiQ09179.
KOiK01915.
OMAiLWEPSHS.
OrthoDBiEOG7GTTD8.
PhylomeDBiQ09179.

Enzyme and pathway databases

ReactomeiREACT_296172. Amino acid synthesis and interconversion (transamination).
REACT_305937. Astrocytic Glutamate-Glutamine Uptake And Metabolism.

Miscellaneous databases

NextBioi20802843.
PROiQ09179.

Family and domain databases

Gene3Di3.30.590.10. 1 hit.
InterProiIPR008147. Gln_synt_beta.
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR008146. Gln_synth_cat_dom.
IPR027303. Gln_synth_gly_rich_site.
IPR027302. Gln_synth_N_conserv_site.
[Graphical view]
PfamiPF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view]
SUPFAMiSSF54368. SSF54368. 1 hit.
PROSITEiPS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273; THR-303 AND SER-305, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiGLNA_SCHPO
AccessioniPrimary (citable) accession number: Q09179
Secondary accession number(s): O13949
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 15, 1998
Last modified: July 22, 2015
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.