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Database: UniProt/TrEMBL
Entry: Q02DF9_PSEAB
LinkDB: Q02DF9_PSEAB
Original site: Q02DF9_PSEAB 
ID   Q02DF9_PSEAB            Unreviewed;       611 AA.
AC   Q02DF9;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   19-FEB-2014, entry version 57.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing];
DE            EC=2.6.1.16;
DE   AltName: Full=D-fructose-6-phosphate amidotransferase;
DE   AltName: Full=GFAT;
DE   AltName: Full=Glucosamine-6-phosphate synthase;
DE   AltName: Full=Hexosephosphate aminotransferase;
DE   AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase;
GN   Name=glmS; OrderedLocusNames=PA14_73170;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- FUNCTION: Catalyzes the first step in hexosamine metabolism,
CC       converting fructose-6P into glucosamine-6P using glutamine as a
CC       nitrogen source (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-glutamine + D-fructose 6-phosphate = L-
CC       glutamate + D-glucosamine 6-phosphate.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-2 domain.
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DR   EMBL; CP000438; ABJ14936.1; -; Genomic_DNA.
DR   RefSeq; YP_794027.1; NC_008463.1.
DR   ProteinModelPortal; Q02DF9; -.
DR   SMR; Q02DF9; 2-611.
DR   STRING; 208963.PA14_73170; -.
DR   EnsemblBacteria; ABJ14936; ABJ14936; PA14_73170.
DR   GeneID; 4385277; -.
DR   KEGG; pau:PA14_73170; -.
DR   PATRIC; 19858191; VBIPseAer79785_6001.
DR   eggNOG; COG0449; -.
DR   HOGENOM; HOG000258898; -.
DR   KO; K00820; -.
DR   OMA; LGIGENF; -.
DR   OrthoDB; EOG6KT2Q1; -.
DR   ProtClustDB; PRK00331; -.
DR   BioCyc; PAER208963:GI5K-5957-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_00164; GlmS; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR000583; GATase_dom.
DR   InterPro; IPR005855; GlmS_trans.
DR   InterPro; IPR001347; SIS.
DR   PANTHER; PTHR10937:SF0; PTHR10937:SF0; 1.
DR   Pfam; PF00310; GATase_2; 1.
DR   Pfam; PF01380; SIS; 2.
DR   TIGRFAMs; TIGR01135; glmS; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
DR   PROSITE; PS51464; SIS; 2.
PE   3: Inferred from homology;
KW   Aminotransferase; Complete proteome; Cytoplasm;
KW   Glutamine amidotransferase; Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   DOMAIN        2    219       Glutamine amidotransferase type-2 (By
FT                                similarity).
FT   ACT_SITE      2      2       Nucleophile; for GATase activity (By
FT                                similarity).
FT   ACT_SITE    606    606       For Fru-6P isomerization activity (By
FT                                similarity).
SQ   SEQUENCE   611 AA;  66327 MW;  B5B7F45CB5882E00 CRC64;
     MCGIVGAIAE RNITPILIEG LKRLEYRGYD SAGVAVFDNE GRLQRCRRVG KVASLEEGLA
     GTPLLGRLGI AHTRWATHGA PTEGNAHPHF SSDELAVVHN GIIENHEPLR ERLKGLGYVF
     TSQTDTEVIV HLLHHKLQSI GDLTLALKDA VKELHGAYGL AVISAAQPDR IVAARSGSPL
     VIGLGLGENF LASDQLALRQ VTDRFIYLEE GDIAEIRRDS VRLWDVQGND VQRETVQYHE
     GAEAADKGEY RHFMLKEIHE QPSVVQRTLE GRLGQNQVMV ESFGPQAAEL FAKVRNVQIV
     ACGTSYHAGM VARYWLESLT GIPCQVEVAS EFRYRKVAVQ PDCLFVTISQ SGETADTLAA
     LRNAKELGFL SSVAICNVAT SSLVRESDLT LLTQAGPEIG VASTKAFTTQ LVALLLLTLG
     IGQVQKRLAD GVEAELVDEL RRLPTRLGEA LAMNRTVEKV SELFAEKHHT LFLGRGAQFP
     VALEGALKLK EISYIHAEAY PAGELKHGPL ALVDSDMPVV TVAPNNELVE KLKSNLQEVR
     ARGGELVVFA DEGAGIEAGE GTHVVGMPHI GDVLSPILYT IPLQLLSYHV AVLKGTDVDQ
     PRNLAKSVTV E
//
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