GenomeNet

Database: UniProt
Entry: Q9HU65
LinkDB: Q9HU65
Original site: Q9HU65 
ID   GLNA_PSEAE              Reviewed;         469 AA.
AC   Q9HU65;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   29-OCT-2014, entry version 77.
DE   RecName: Full=Glutamine synthetase;
DE            EC=6.3.1.2;
DE   AltName: Full=Glutamate--ammonia ligase;
GN   Name=glnA {ECO:0000312|EMBL:AAG08504.1}; OrderedLocusNames=PA5119;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG
OS   12228).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T.,
RA   Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an
RT   opportunistic pathogen.";
RL   Nature 406:959-964(2000).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 37-59; 118-140; 142-150; 152-170; 178-193; 432-447
RP   AND 456-469.
RC   STRAIN=ATCC 33467 / type 1 smooth, and ATCC 33468 / type 2 mucoid;
RA   Liddor M.;
RT   "Biofouling in water treatment systems: effect of membrane properties
RT   on biofilm formation.";
RL   Thesis (2005), Ben-Gurion University, Israel.
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate +
CC       L-glutamine. {ECO:0000250|UniProtKB:P0A9C5}.
CC   -!- ENZYME REGULATION: The activity of this enzyme is controlled by
CC       adenylation under conditions of abundant glutamine. The fully
CC       adenylated enzyme complex is inactive (By similarity).
CC       {ECO:0000250|UniProtKB:P0A9C5}.
CC   -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two
CC       hexagons. {ECO:0000250|UniProtKB:P0A9C5}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000255}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE004091; AAG08504.1; -; Genomic_DNA.
DR   PIR; G83005; G83005.
DR   RefSeq; NP_253806.1; NC_002516.2.
DR   ProteinModelPortal; Q9HU65; -.
DR   SMR; Q9HU65; 8-469.
DR   STRING; 208964.PA5119; -.
DR   EnsemblBacteria; AAG08504; AAG08504; PA5119.
DR   GeneID; 877688; -.
DR   KEGG; pae:PA5119; -.
DR   PATRIC; 19845073; VBIPseAer58763_5365.
DR   PseudoCAP; PA5119; -.
DR   eggNOG; COG0174; -.
DR   HOGENOM; HOG000005157; -.
DR   InParanoid; Q9HU65; -.
DR   KO; K01915; -.
DR   OMA; DMLLMPI; -.
DR   OrthoDB; EOG6B360N; -.
DR   PhylomeDB; Q9HU65; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
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   GO; GO:0009399; P:nitrogen fixation; IEA:InterPro.
DR   Gene3D; 3.10.20.70; -; 1.
DR   Gene3D; 3.30.590.10; -; 1.
DR   InterPro; IPR008147; Gln_synt_beta.
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   SUPFAM; SSF54368; SSF54368; 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   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Ligase; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT   CHAIN         1    469       Glutamine synthetase.
FT                                /FTId=PRO_0000153251.
FT   MOD_RES     398    398       O-AMP-tyrosine. {ECO:0000250}.
SQ   SEQUENCE   469 AA;  51945 MW;  DED83E755B3CD225 CRC64;
     MSYKSHQLIK DHDVKWVDLR FTDTKGKQQH VTMPARDALD DEFFEAGKMF DGSSIAGWKG
     IEASDMILMP DDSTAVLDPF TEEPTLILVC DIIEPSTMQG YERDPRNIAK RAEEYLKSTG
     IGDTVFVGPE PEFFIFDEVK FKSDISGSMF KIFSEQASWN TDADIESGNK GHRPGVKGGY
     FPVPPVDHDH EIRTAMCNAL EEMGLVVEVH HHEVATAGQN EIGVKFNTLV AKADEVQTLK
     YCVHNVADAY GKTVTFMPKP LYGDNGSGMH VHMSISKDGK NTFAGEGYAG LSETALYFIG
     GIIKHGKALN GFTNPSTNSY KRLVPGFEAP VMLAYSARNR SASIRIPYVS SPKARRIEAR
     FPDPAANPYL AFAALLMAGL DGIQNKIHPG DAADKNLYDL PPEEAKEIPQ VCGSLKEALE
     ELDKGRAFLT KGGVFTDEFI DAYIELKSEE EIKVRTFVHP LEYDLYYSV
//
DBGET integrated database retrieval system