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Database: UniProt
Entry: G2J7F0_9BURK
LinkDB: G2J7F0_9BURK
Original site: G2J7F0_9BURK 
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
//
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