ID   GLMS_BUCAI              Reviewed;         609 AA.
AC   P57138;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 118.
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=BU026;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB12753.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000003; BAB12753.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_239867.2; NC_002528.1.
DR   RefSeq; WP_009873987.1; NC_002528.1.
DR   AlphaFoldDB; P57138; -.
DR   SMR; P57138; -.
DR   STRING; 107806.10038718; -.
DR   PRIDE; P57138; -.
DR   EnsemblBacteria; BAB12753; BAB12753; BAB12753.
DR   KEGG; buc:BU026; -.
DR   PATRIC; fig|107806.10.peg.38; -.
DR   eggNOG; COG0449; Bacteria.
DR   HOGENOM; CLU_012520_5_2_6; -.
DR   OMA; ASEYRYA; -.
DR   Proteomes; UP000001806; 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..609
FT                   /note="Glutamine--fructose-6-phosphate aminotransferase
FT                   [isomerizing]"
FT                   /id="PRO_0000135311"
FT   DOMAIN          2..219
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT   DOMAIN          288..428
FT                   /note="SIS 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
FT   DOMAIN          460..599
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        604
FT                   /note="For Fru-6P isomerization activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00164"
SQ   SEQUENCE   609 AA;  68682 MW;  5FF11730FEB2D715 CRC64;
     MCGIVAAVTQ RNIANFLIDG IKKLEYRGYD SSGLAVIDNK NNIVRIRCVG KVNELIKKTN
     KKKILGSIGV AHTRWATHGK VSKENTHPHI SSNIIVVHNG IIENNSTLRG FLKKQGYIFS
     SDTDTEVIAH LLHWEQNKKK DSLIKVIQNS IKKLDGNYSM VVIDQNNPSK LIAARSGSPL
     IIGLGTEENF IASDQIALLH VTKRFIYLEE GDIAIVARKE INIFNKNNSI IQREEVVSNI
     EYKSAKKGKY RYYMEKEIHE QPKSIRNTLK NRLTNSNKVH FSELGSKENN IFYNTEHIQI
     VACGTSYNAA MVSRYWFEEL ANIPCDVEIA SEFSSRKLVV RKKSLLITLS QSGETADTLS
     ALRYSKKLGY LGNLTICNMK SSSLVRESDF YILTKAGLEI GVASTKSFTT QLTVLLLLVA
     KIINSKKENN NTSKRIVQTL SILPVRIEEI LKKKQLIQDM ANTLANKKNM LFLGRGNQYP
     IAMEGALKLK EISYIHAEAY PSGELKHGPL ALIDKNIPVI MIAPENSLLE KNKKNIKEIC
     SRGGIVYVFS NQEFDYEENI NTIKLPYVEE LIAPIFYTIP LQLFAYYVAL KKGRDIDQPR
     HLAKSVTVE