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Database: UniProt
Entry: Q9HU65
LinkDB: Q9HU65
Original site: Q9HU65 
ID   GLN1B_PSEAE             Reviewed;         469 AA.
AC   Q9HU65;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   05-JUL-2017, entry version 90.
DE   RecName: Full=Glutamine synthetase {ECO:0000250|UniProtKB:P0A1P6};
DE            Short=GS {ECO:0000250|UniProtKB:P0A1P6};
DE            EC=6.3.1.2 {ECO:0000250|UniProtKB:P0A1P6};
DE   AltName: Full=Glutamate--ammonia ligase {ECO:0000305};
DE   AltName: Full=Glutamine synthetase I beta {ECO:0000250|UniProtKB:P0A1P6};
DE            Short=GSI beta {ECO:0000250|UniProtKB:P0A1P6};
GN   Name=glnA {ECO:0000250|UniProtKB:P0A1P6}; OrderedLocusNames=PA5119;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 /
OS   JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
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 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC   1C / PRS 101 / PAO1;
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   -!- FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine
CC       from glutamate and ammonia. {ECO:0000250|UniProtKB:P0A1P6}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate +
CC       L-glutamine. {ECO:0000250|UniProtKB:P0A1P6}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P9WN39};
CC       Note=Binds 2 Mg(2+) ions per subunit.
CC       {ECO:0000250|UniProtKB:P9WN39};
CC   -!- ENZYME REGULATION: The activity of this enzyme could be controlled
CC       by adenylation under conditions of abundant glutamine.
CC       {ECO:0000250|UniProtKB:Q3V5W6}.
CC   -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two
CC       hexameric ring. {ECO:0000250|UniProtKB:P0A1P6}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P9WN39}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000305}.
DR   EMBL; AE004091; AAG08504.1; -; Genomic_DNA.
DR   PIR; G83005; G83005.
DR   RefSeq; NP_253806.1; NC_002516.2.
DR   RefSeq; WP_003096016.1; NC_002516.2.
DR   ProteinModelPortal; Q9HU65; -.
DR   SMR; Q9HU65; -.
DR   STRING; 208964.PA5119; -.
DR   PaxDb; Q9HU65; -.
DR   PRIDE; Q9HU65; -.
DR   EnsemblBacteria; AAG08504; AAG08504; PA5119.
DR   GeneID; 877688; -.
DR   KEGG; pae:PA5119; -.
DR   PATRIC; fig|208964.12.peg.5365; -.
DR   PseudoCAP; PA5119; -.
DR   eggNOG; ENOG4105C5F; Bacteria.
DR   eggNOG; COG0174; LUCA.
DR   HOGENOM; HOG000005157; -.
DR   InParanoid; Q9HU65; -.
DR   KO; K01915; -.
DR   OMA; IEAAWNT; -.
DR   PhylomeDB; Q9HU65; -.
DR   Proteomes; UP000002438; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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_b-grasp.
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   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; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN         1    469       Glutamine synthetase.
FT                                /FTId=PRO_0000153251.
FT   NP_BIND     272    274       ATP. {ECO:0000250|UniProtKB:P0A1P6}.
FT   REGION      265    266       L-glutamate binding.
FT                                {ECO:0000250|UniProtKB:P0A1P6}.
FT   METAL       130    130       Magnesium 1.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   METAL       132    132       Magnesium 2.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   METAL       213    213       Magnesium 2.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   METAL       221    221       Magnesium 2.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   METAL       270    270       Magnesium 1; via pros nitrogen.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   METAL       358    358       Magnesium 1.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   BINDING     208    208       ATP. {ECO:0000250|UniProtKB:P0A1P6}.
FT   BINDING     266    266       L-glutamate; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P12425}.
FT   BINDING     274    274       ATP. {ECO:0000250|UniProtKB:P77961}.
FT   BINDING     322    322       L-glutamate.
FT                                {ECO:0000250|UniProtKB:P0A1P6}.
FT   BINDING     328    328       L-glutamate.
FT                                {ECO:0000250|UniProtKB:P0A1P6}.
FT   BINDING     340    340       ATP. {ECO:0000250|UniProtKB:P9WN39}.
FT   BINDING     340    340       L-glutamate.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
FT   BINDING     345    345       ATP. {ECO:0000250|UniProtKB:P9WN39}.
FT   BINDING     353    353       ATP. {ECO:0000250|UniProtKB:P77961}.
FT   BINDING     360    360       L-glutamate.
FT                                {ECO:0000250|UniProtKB:P0A1P6}.
FT   MOD_RES     398    398       O-AMP-tyrosine.
FT                                {ECO:0000250|UniProtKB:P9WN39}.
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
//
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