ID   Q4UQG9_XANC8            Unreviewed;       609 AA.
AC   Q4UQG9;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   29-MAY-2013, entry version 61.
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=XC_3663;
OS   Xanthomonas campestris pv. campestris (strain 8004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=314565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8004;
RX   PubMed=15899963; DOI=10.1101/gr.3378705;
RA   Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q.,
RA   Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L.,
RA   Zeng S., Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B.,
RA   Fang R., Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.;
RT   "Comparative and functional genomic analyses of the pathogenicity of
RT   phytopathogen Xanthomonas campestris pv. campestris.";
RL   Genome Res. 15:757-767(2005).
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; CP000050; AAY50704.1; -; Genomic_DNA.
DR   RefSeq; YP_244724.1; NC_007086.1.
DR   ProteinModelPortal; Q4UQG9; -.
DR   SMR; Q4UQG9; 2-609.
DR   STRING; 314565.XC_3663; -.
DR   EnsemblBacteria; AAY50704; AAY50704; XC_3663.
DR   GeneID; 3379277; -.
DR   KEGG; xcb:XC_3663; -.
DR   PATRIC; 24069039; VBIXanCam24967_3881.
DR   eggNOG; COG0449; -.
DR   HOGENOM; HOG000258896; -.
DR   KO; K00820; -.
DR   OMA; IRLPEHY; -.
DR   ProtClustDB; PRK00331; -.
DR   BioCyc; XCAM314565:GCQG-3688-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:HAMAP.
DR   GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA: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    217       Glutamine amidotransferase type-2 (By
FT                                similarity).
FT   ACT_SITE      2      2       Nucleophile; for GATase activity (By
FT                                similarity).
FT   ACT_SITE    604    604       For Fru-6P isomerization activity (By
FT                                similarity).
SQ   SEQUENCE   609 AA;  66094 MW;  9E88C6881020F490 CRC64;
     MCGIVGAIAG RDVVPVLIEG LKRLEYRGYD SSGIAVLDGT QVRRVRRTGR VAEMAQAAQA
     EQFGATLGIG HTRWATHGGV TEANAHPHIS AGVALVHNGI IENHEEQREK LRALGYTFES
     QTDTEVIAHL IHHHLADAGD LLSALQRTVK ELTGAYALAV MSQAEQERFV CARMGCPLLI
     GVGEGENFVA SDVSAIVQAT RQVIFLEEGD TAELRRDGVR VFDASDAAVE RPLHLSDVSL
     ASLELGPFRH FMQKEIHEQP RALADTIEAA IDAKGFPASL FGPTADAVLR DIEGVQILAC
     GTSYYAGLTA RYWIEAIAGL PCSVEIASEY RYRAAYANPK HLIVTISQSG ETLDTMEALK
     YAKSLGHLHT LSICNVPESA IPRASELVCY TRAGAEIGVA STKAFTTQLA VLFQLTMVLG
     KLQGRISDSE EADYLEQLRF LPGSVQHALN LEPQIMAWAE RFSPKENALF LGRGLHYPIA
     LEGALKLKEI SYIHAEAYPA GELKHGPLAL VDATMPVVVI APNDRLLEKV KSNMQEVRAR
     GGELFVFADQ DSHFSESDGV HVIRTPRHAG VLSPVIHTIP VQLLAYHTAL ARGTDVDKPR
     NLAKSVTVE
//