ID   A6T3N6_JANMA            Unreviewed;       605 AA.
AC   A6T3N6;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   01-MAY-2013, entry version 48.
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=mma_3443;
OS   Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Janthinobacterium.
OX   NCBI_TaxID=375286;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marseille;
RX   PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA   Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M.,
RA   Raoult D., Drancourt M.;
RT   "Genome analysis of Minibacterium massiliensis highlights the
RT   convergent evolution of water-living bacteria.";
RL   PLoS Genet. 3:1454-1463(2007).
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; CP000269; ABR88336.1; -; Genomic_DNA.
DR   RefSeq; YP_001355133.1; NC_009659.1.
DR   ProteinModelPortal; A6T3N6; -.
DR   SMR; A6T3N6; 2-605.
DR   STRING; 375286.mma_3443; -.
DR   EnsemblBacteria; ABR88336; ABR88336; mma_3443.
DR   GeneID; 5350408; -.
DR   KEGG; mms:mma_3443; -.
DR   PATRIC; 22159415; VBIJanSp106498_3464.
DR   eggNOG; COG0449; -.
DR   HOGENOM; HOG000258896; -.
DR   KO; K00820; -.
DR   OMA; IRLPEHY; -.
DR   ProtClustDB; PRK00331; -.
DR   BioCyc; JSP375286:GJ8U-3494-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    216       Glutamine amidotransferase type-2 (By
FT                                similarity).
FT   ACT_SITE      2      2       Nucleophile; for GATase activity (By
FT                                similarity).
FT   ACT_SITE    600    600       For Fru-6P isomerization activity (By
FT                                similarity).
SQ   SEQUENCE   605 AA;  66248 MW;  5104BFCFD2AD0AE8 CRC64;
     MCGIVGAVAQ RNITPILVEG LKRLEYRGYD SCGIALHVDG KLERARSTAR VAELEKQIAK
     EHLSGFTGIA HTRWATHGAP ASHNAHPHFS RERIALVHNG IIENHDELRD ELKTLGYVFE
     SQTDTEVIAH LVDHLYTGDL FETVQTATKR LTGAFAIAVF SRDEPHRVVG ARRGSPLIVG
     VGDGENFLAS DALALAGTTD QIIYLEEGDV VDLQLQRVWI VDENGKRVER EVKTVHAHTG
     AVELGPYRHY MQKEIFEQPR AISDTLEGIT AITPDIFGDK AYGIFKKIDS VLILACGTSY
     YSGMTAKYWI EAVAGVTCNV EIASEYRYRD SVPNPNSLVV TISQSGETAD TLAALRHAQA
     QNMRHTLTIC NAATSAMVRE CELAYITRAG VEVGVASTKA FTTQLAALFL LTLSLAQVKG
     RLNDEQEAAQ LKAMRHLPSA ITAVLALEPQ IIAWAEAFAR KENALFLGRG LHYPIALEGA
     LKLKEISYIH AEAYPAGELK HGPLALVTEE MPVVTVAPND PMIEKLKSNM QEVRARGGEL
     YVFADADSRI TSSEGIHVIR LPEHYGLLSP ILHVVPLQLL AYHTALARGT DVDKPRNLAK
     SVTVE
//