(data stored in SCRATCH zone)

SWISSPROT: Q3KJG8_PSEPF

ID   Q3KJG8_PSEPF            Unreviewed;       468 AA.
AC   Q3KJG8;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 101.
DE   RecName: Full=Glutamine synthetase {ECO:0000256|RuleBase:RU004356};
DE            EC=6.3.1.2 {ECO:0000256|RuleBase:RU004356};
GN   OrderedLocusNames=Pfl01_0344 {ECO:0000313|EMBL:ABA72088.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA72088.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA72088.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA72088.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine +
CC         phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216;
CC         EC=6.3.1.2; Evidence={ECO:0000256|RuleBase:RU004356};
CC   -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two
CC       hexagons. {ECO:0000256|RuleBase:RU000387}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU000387}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000256|RuleBase:RU000384}.
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DR   EMBL; CP000094; ABA72088.1; -; Genomic_DNA.
DR   RefSeq; WP_011332032.1; NC_007492.2.
DR   STRING; 205922.Pfl01_0344; -.
DR   PRIDE; Q3KJG8; -.
DR   EnsemblBacteria; ABA72088; ABA72088; Pfl01_0344.
DR   KEGG; pfo:Pfl01_0344; -.
DR   eggNOG; ENOG4105C5F; Bacteria.
DR   eggNOG; COG0174; LUCA.
DR   HOGENOM; HOG000005157; -.
DR   KO; K01915; -.
DR   OMA; IEAAWNT; -.
DR   BioCyc; PFLU205922:G1G4S-348-MONOMER; -.
DR   Proteomes; UP000002704; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.10.20.70; -; 1.
DR   InterPro; IPR008147; Gln_synt_b-grasp.
DR   InterPro; IPR036651; Gln_synt_N.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR008146; Gln_synth_cat_dom.
DR   InterPro; IPR027303; Gln_synth_gly_rich_site.
DR   InterPro; IPR004809; Gln_synth_I.
DR   InterPro; IPR001637; Gln_synth_I_adenylation_site.
DR   InterPro; IPR027302; Gln_synth_N_conserv_site.
DR   Pfam; PF00120; Gln-synt_C; 1.
DR   Pfam; PF03951; Gln-synt_N; 1.
DR   SMART; SM01230; Gln-synt_C; 1.
DR   SUPFAM; SSF54368; SSF54368; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   TIGRFAMs; TIGR00653; GlnA; 1.
DR   PROSITE; PS00180; GLNA_1; 1.
DR   PROSITE; PS00182; GLNA_ADENYLATION; 1.
DR   PROSITE; PS00181; GLNA_ATP; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3KJG8.
DR   SWISS-2DPAGE; Q3KJG8.
KW   ATP-binding {ECO:0000256|RuleBase:RU004356};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002704};
KW   Cytoplasm {ECO:0000256|RuleBase:RU000387};
KW   Ligase {ECO:0000256|RuleBase:RU004356, ECO:0000313|EMBL:ABA72088.1};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU004356};
KW   Phosphoprotein {ECO:0000256|PIRSR:PIRSR604809-50}.
FT   DOMAIN      101    378       Gln-synt_C. {ECO:0000259|SMART:SM01230}.
FT   MOD_RES     397    397       O-AMP-tyrosine. {ECO:0000256|PIRSR:
FT                                PIRSR604809-50}.
SQ   SEQUENCE   468 AA;  51803 MW;  EDF27561BCFF029E CRC64;
     MSKSVQLIKD HDVKWIDLRF TDTKGTQHHV TMPARDALED DFFEVGKMFD GSSIAGWKGI
     EASDMILLPD DETAVLDPFT EEPTLILVCD IIEPSTMQGY DRDPRAIARR AEEYLKTTGI
     GDTVFAGPEP EFFIFDEVKF KSDISGSMFK IYSEQGSWMS DQDVEGGNKG HRPGVKGGYF
     PVPPFDHDHE IRTSMCNALE EMGLTVEVHH HEVATAGQNE IGVKFNTLVK KADETQTLKY
     VVHNVADAYG RTATFMPKPL YGDNGSGMHV HMSISKDGKN TFAGEGYAGL SDTALYFIGG
     IIKHGKALNG FTNPATNSYK RLVPGFEAPV MLAYSARNRS ASIRIPYVNS PKGRRIEARF
     PDPAANPYLA FAALLMAGLD GIQNKIHPGD AADKNLYDLP PEEAKEIPQV CGSLKEALEE
     LDKGRAFLTK GGVFSDDFID AYIALKSEEE IKVRTFVHPL EYELYYSC
//

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