ID   GLMS_GLUOX              Reviewed;         608 AA.
AC   Q5FUY5;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000255|HAMAP-Rule:MF_00164};
DE            EC=2.6.1.16 {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=D-fructose-6-phosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=GFAT {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=Glucosamine-6-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=Hexosephosphate aminotransferase {ECO:0000255|HAMAP-Rule:MF_00164};
DE   AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_00164};
GN   Name=glmS {ECO:0000255|HAMAP-Rule:MF_00164}; OrderedLocusNames=GOX0007;
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=621H;
RX   PubMed=15665824; DOI=10.1038/nbt1062;
RA   Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA   Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT   "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT   oxydans.";
RL   Nat. Biotechnol. 23:195-200(2005).
CC   -!- FUNCTION: Catalyzes the first step in hexosamine metabolism, converting
CC       fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
CC       {ECO:0000255|HAMAP-Rule:MF_00164}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00164};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00164}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00164}.
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DR   EMBL; CP000009; AAW59806.1; -; Genomic_DNA.
DR   RefSeq; WP_011251610.1; NZ_LT900338.1.
DR   AlphaFoldDB; Q5FUY5; -.
DR   SMR; Q5FUY5; -.
DR   STRING; 290633.GOX0007; -.
DR   PRIDE; Q5FUY5; -.
DR   EnsemblBacteria; AAW59806; AAW59806; GOX0007.
DR   KEGG; gox:GOX0007; -.
DR   eggNOG; COG0449; Bacteria.
DR   HOGENOM; CLU_012520_5_2_5; -.
DR   OMA; ASEYRYA; -.
DR   Proteomes; UP000006375; 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;
KW   Reference proteome; Repeat; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT   CHAIN           2..608
FT                   /note="Glutamine--fructose-6-phosphate aminotransferase
FT                   [isomerizing]"
FT                   /id="PRO_0000135337"
FT   DOMAIN          2..218
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT   DOMAIN          284..423
FT                   /note="SIS 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT   DOMAIN          456..598
FT                   /note="SIS 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT   ACT_SITE        2
FT                   /note="Nucleophile; for GATase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT   ACT_SITE        603
FT                   /note="For Fru-6P isomerization activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
SQ   SEQUENCE   608 AA;  65655 MW;  3EF138346B98E657 CRC64;
     MCGICGIVGH QPASPIAFEA LRRLEYRGYD SAGIATLTAS GDIERRRAAG KLDNLEHVLK
     EHPLPGTTGI GHTRWATHGA PTENNAHPHE AGRVAIVHNG IIENFAELKK ELEAKGRVFR
     TETDSETVAH LVDDYLGQGL EPREAAFAAI KRLEGAYAIA MIFKDHEGLL IGARHGAPLA
     VGYGNGEMFL GSDSIALAPM ARKMTYLEDG DWCELTPDHV TIFDMTGAEV SRPVQDLTFM
     AGQVGKDGYR HYMEKELHEH PVAIGQTLKR ITDPASKRIA LPEMPFDPAQ VPRITITACG
     SAYYAGMVGR YWLESLARIP VEIDVASEMR YREPPQPDKG VALLISQSGE TADTLGVLRS
     LKKAGQSIVS VLNVEHSTMG RESDLVLGMD AGPEISVAST KAFTAQLSVL AALAIDFARA
     RGTMDQAREE RLTASLLDLP SRAAEVFTRT KDIQAMAAVV AQARDVLYLG RGICTPIAFE
     GALKLKEISY IHAEAYAAGE LKHGPISLID QTVPVVAIAP STILFDKTLS NLQEAKARGG
     RILAFTDAEG AKRLEGVAEQ VVIMPDVDAF VAPILYAIPV QMLAYEVALL KGTDVDQPRN
     LAKSVTVE