ID G2J7F0_9BURK Unreviewed; 661 AA.
AC G2J7F0;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 08-NOV-2023, entry version 58.
DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|ARBA:ARBA00016090, ECO:0000256|HAMAP-Rule:MF_00164};
DE EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916, ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=D-fructose-6-phosphate amidotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=GFAT {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=Glucosamine-6-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=Hexosephosphate aminotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
DE AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase {ECO:0000256|HAMAP-Rule:MF_00164};
GN Name=glmS {ECO:0000256|HAMAP-Rule:MF_00164,
GN ECO:0000313|EMBL:CCD28695.1};
GN ORFNames=CAGGBEG34_160003 {ECO:0000313|EMBL:CCD28695.1};
OS Candidatus Glomeribacter gigasporarum BEG34.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Candidatus Glomeribacter.
OX NCBI_TaxID=1070319 {ECO:0000313|EMBL:CCD28695.1, ECO:0000313|Proteomes:UP000054051};
RN [1] {ECO:0000313|EMBL:CCD28695.1, ECO:0000313|Proteomes:UP000054051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BEG34 {ECO:0000313|EMBL:CCD28695.1,
RC ECO:0000313|Proteomes:UP000054051};
RA Ghignone S., Salvioli A., Anca I., Lumini E., Ortu G., Petiti L.,
RA Cruveiller S., Bianciotto V., Piffanelli P., Lanfranco L., Bonfante P.;
RT "The genome of the obligate endobacterium of an arbuscular mycorrhizal
RT fungus reveals an interphylum network of nutritional interactions.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the first step in hexosamine metabolism, converting
CC fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
CC {ECO:0000256|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:0000256|ARBA:ARBA00001031, ECO:0000256|HAMAP-
CC Rule:MF_00164};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00164}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCD28695.1}.
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DR EMBL; CAFB01000032; CCD28695.1; -; Genomic_DNA.
DR RefSeq; WP_006681986.1; NZ_CAFB01000032.1.
DR AlphaFoldDB; G2J7F0; -.
DR STRING; 1070319.CAGGBEG34_160003; -.
DR eggNOG; COG0449; Bacteria.
DR OrthoDB; 9761808at2; -.
DR Proteomes; UP000054051; Unassembled WGS sequence.
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; cd00714; GFAT; 1.
DR CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR HAMAP; MF_00164; GlmS; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR005855; GFAT.
DR InterPro; IPR047084; GFAT_N.
DR InterPro; IPR035466; GlmS/AgaS_SIS.
DR InterPro; IPR035490; GlmS/FrlB_SIS.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR NCBIfam; TIGR01135; glmS; 1.
DR PANTHER; PTHR10937; GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE, ISOMERIZING; 1.
DR PANTHER; PTHR10937:SF0; GLUTAMINE--FRUCTOSE-6-PHOSPHATE TRANSAMINASE (ISOMERIZING); 1.
DR Pfam; PF13522; GATase_6; 1.
DR Pfam; PF01380; SIS; 2.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS51464; SIS; 2.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000256|HAMAP-
KW Rule:MF_00164}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00164};
KW Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW Reference proteome {ECO:0000313|Proteomes:UP000054051};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00164}.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT DOMAIN 2..272
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000259|PROSITE:PS51278"
FT DOMAIN 337..477
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT DOMAIN 510..651
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT REGION 162..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2
FT /note="Nucleophile; for GATase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
FT ACT_SITE 656
FT /note="For Fru-6P isomerization activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00164"
SQ SEQUENCE 661 AA; 71388 MW; 2AC3EC4CFD6A5DBB CRC64;
MCGIVSAIAR HNIVPVLIEG LRRLEYRGYD SCGIAVLTDG APRRVRSIAR VEDLAAQVEK
AGFASGIGLA HTRWATHGAP VPDNAHPIFS RETIALAHNG IIENHEALRK ALSAQGYTFV
SQTDSEVIAH LIHSLLPASS LEHFSARLLL ARARRQYGDR CGRSRSASLR DGGDPAAIPN
TRNDDVTQCK PLKNALADAV RAAVQQLRGA YAIAVFHSAE PHCIVGARRG SPLVVGIGEE
AHFLASDAIA LAGETERFIF LEDGDVVELT ADTVNITDSN GARAERELRV LTSLHQIGAL
GPYQHFMQKE IFEQPRALAE SIAQRDTFLP SCFGERARAV FERIDRALIL ACGSSYYAGL
TAKYWLESIA ALPTQVEIAS EYRYRSPVPH PDTLVVAISQ SGETADTLAA LKYAHALGQA
QSLAICNVAT SAMVRQTALS FLTRAGAEIG VASTKAFTAQ LAALFILTVT LGKVRARVAP
SAEDAYRQQL RHLPVALNRV LALEPHLIAW AETFAGKENA LFLGRGMHYP IALEGALKLK
EISYIHAEAY PAGELKHGPL ALVTDAMPVV AIAPNDALLE KLKSNLHEVR ARGGQLYALA
EPETRIDSDI GLRAIRMPEH EGPLSPLLHA VALQLLAYHT ARARGTDIDK PRNLAKSVTV
E
//