ID   GLMS_SPHYA              Reviewed;         156 AA.
AC   Q56206;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 85.
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;
DE   Flags: Fragment;
GN   Name=glmS;
OS   Sphingobium yanoikuyae (Sphingomonas yanoikuyae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=13690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 6900 / JCM 10274 / B1;
RX   PubMed=8626059; DOI=10.1016/0378-1119(95)00732-6;
RA   Wang Y., Lau P.C.K.;
RT   "Sequence and expression of an isocitrate dehydrogenase-encoding gene from
RT   a polycyclic aromatic hydrocarbon oxidizer, Sphingomonas yanoikuyae B1.";
RL   Gene 168:15-21(1996).
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; U37523; AAC43642.1; -; Genomic_DNA.
DR   PIR; PC4141; PC4141.
DR   AlphaFoldDB; Q56206; -.
DR   SMR; Q56206; -.
DR   STRING; 13690.CP98_01359; -.
DR   eggNOG; COG0449; Bacteria.
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-EC.
DR   GO; GO:1901137; P:carbohydrate derivative biosynthetic process; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR   InterPro; IPR035490; GlmS/FrlB_SIS.
DR   InterPro; IPR005855; GlmS_trans.
DR   InterPro; IPR001347; SIS_dom.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   PANTHER; PTHR10937:SF0; PTHR10937:SF0; 1.
DR   Pfam; PF01380; SIS; 1.
DR   SUPFAM; SSF53697; SSF53697; 1.
DR   PROSITE; PS51464; SIS; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Cytoplasm; Glutamine amidotransferase; Transferase.
FT   CHAIN           <1..156
FT                   /note="Glutamine--fructose-6-phosphate aminotransferase
FT                   [isomerizing]"
FT                   /id="PRO_0000135378"
FT   DOMAIN          4..146
FT                   /note="SIS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT   ACT_SITE        151
FT                   /note="For Fru-6P isomerization activity"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   156 AA;  16606 MW;  5D661DE8EEFD4EDD CRC64;
     IEAMAHHIVP ARDVLYLGRG TDYPLALEGA LKLKEISYIH AEGYAAGEMK HGPIALIDEL
     VPVICIAPSG PLFEKTVSNM QEVQARGGKV VLISAYDGVQ AAGEGCLATI TMPKVHPLIA
     PMVYAVPVQL LAYHVAVLKG TDVDQPRNLA KSVTVE