ID   GLMS_BACSH              Reviewed;         600 AA.
AC   E0U070; P39754;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   25-MAY-2022, entry version 58.
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=BSUW23_00920;
OS   Bacillus spizizenii (strain ATCC 23059 / NRRL B-14472 / W23) (Bacillus
OS   subtilis subsp. spizizenii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=655816;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX   PubMed=21527469; DOI=10.1099/mic.0.048520-0;
RA   Zeigler D.R.;
RT   "The genome sequence of Bacillus subtilis subsp. spizizenii W23: insights
RT   into speciation within the B. subtilis complex and into the history of B.
RT   subtilis genetics.";
RL   Microbiology 157:2033-2041(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 471-600.
RC   STRAIN=ATCC 23059 / NRRL B-14472 / W23;
RX   PubMed=8376346; DOI=10.1128/jb.175.18.6010-6017.1993;
RA   Morohoshi F., Hayashi K., Munakata N.;
RT   "Bacillus subtilis alkA gene encoding inducible 3-methyladenine DNA
RT   glycosylase is adjacent to the ada operon.";
RL   J. Bacteriol. 175:6010-6017(1993).
CC   -!- FUNCTION: Catalyzes the first step in hexosamine metabolism, converting
CC       fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-
CC         phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR   EMBL; CP002183; ADM36241.1; -; Genomic_DNA.
DR   EMBL; D21199; BAA04741.1; -; Genomic_DNA.
DR   RefSeq; WP_003223659.1; NC_014479.1.
DR   AlphaFoldDB; E0U070; -.
DR   SMR; E0U070; -.
DR   MEROPS; C44.A08; -.
DR   EnsemblBacteria; ADM36241; ADM36241; BSUW23_00920.
DR   GeneID; 64302037; -.
DR   KEGG; bss:BSUW23_00920; -.
DR   HOGENOM; CLU_012520_7_1_9; -.
DR   OMA; ASEYRYA; -.
DR   Proteomes; UP000002233; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:1901137; P:carbohydrate derivative biosynthetic process; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR   CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   HAMAP; MF_00164; GlmS; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR035466; GlmS/AgaS_SIS.
DR   InterPro; IPR035490; GlmS/FrlB_SIS.
DR   InterPro; IPR005855; GlmS_trans.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR001347; SIS_dom.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   PANTHER; PTHR10937:SF0; PTHR10937:SF0; 1.
DR   Pfam; PF01380; SIS; 2.
DR   SUPFAM; SSF53697; SSF53697; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   TIGRFAMs; TIGR01135; glmS; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
DR   PROSITE; PS51464; SIS; 2.
PE   3: Inferred from homology;
KW   Aminotransferase; Cytoplasm; Glutamine amidotransferase; Repeat;
KW   Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..600
FT                   /note="Glutamine--fructose-6-phosphate aminotransferase
FT                   [isomerizing]"
FT                   /id="PRO_0000403658"
FT   DOMAIN          2..217
FT                   /note="Glutamine amidotransferase type-2"
FT   DOMAIN          283..422
FT                   /note="SIS 1"
FT   DOMAIN          452..590
FT                   /note="SIS 2"
FT   ACT_SITE        2
FT                   /note="Nucleophile; for GATase activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        595
FT                   /note="For Fru-6P isomerization activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   600 AA;  65339 MW;  77E64F17C7E68919 CRC64;
     MCGIVGYIGQ LDAKEILLKG LEKLEYRGYD SAGIAVANEQ GIHVFKEKGR IADLREVVDA
     NIEAKAGIGH TRWATHGEPS YLNAHPHQSA LGRFTLVHNG VIENYVQLKQ EYLQDVELKS
     DTDTEVVVQV IEQFVNGGLD TEEAFRKTLT LLKGSYAIAL FDNENRETIF VAKNKSPLLV
     GLGDTFNVVA SDAMAMLQVT NEYVELMDKE MVIVTDDQVV IKNLDGDVIS RASYIAELDA
     SDIEKGTYPH YMLKETDEQP VVMRKIIQTY QDENGKLSVP GDIAAAVAEA DRIYIIGCGT
     SYHAGLVGKQ YIEMWANVPV EVHVASEFSY NMPLLSKKPL FIFLSQSGET ADSRAVLVQV
     KALGHKALTI TNVPGSTLSR EADYTLLLHA GPEIAVASTK AYTAQIAVLA VLASVAADKN
     GIDIGFDLVK ELGIAANAME ALCDQKDEME MIAREYLTVS RNAFFIGRGL DYFVCVEGAL
     KLKEISYIQA EGFAGGELKH GTIALIEQGT PVFALATQEH VNLSIRGNVK EVAARGANTC
     IISLKGLDDA DDRFVLPEVN PALAPLVSVV PLQLIAYYAA LHRGCDVDKP RNLAKSVTVE