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Database: UniProt
Entry: A0A0G0BIP9_9BACT
LinkDB: A0A0G0BIP9_9BACT
Original site: A0A0G0BIP9_9BACT 
ID   A0A0G0BIP9_9BACT        Unreviewed;       201 AA.
AC   A0A0G0BIP9;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|ARBA:ARBA00016090};
DE            EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
GN   Name=glmS {ECO:0000313|EMBL:KKP38685.1};
GN   ORFNames=UR28_C0014G0032 {ECO:0000313|EMBL:KKP38685.1};
OS   Candidatus Peregrinibacteria bacterium GW2011_GWF2_33_10.
OC   Bacteria; Candidatus Peregrinibacteria.
OX   NCBI_TaxID=1619065 {ECO:0000313|EMBL:KKP38685.1, ECO:0000313|Proteomes:UP000034183};
RN   [1] {ECO:0000313|EMBL:KKP38685.1, ECO:0000313|Proteomes:UP000034183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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};
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:KKP38685.1}.
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DR   EMBL; LBOP01000014; KKP38685.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0BIP9; -.
DR   PATRIC; fig|1619065.3.peg.698; -.
DR   Proteomes; UP000034183; Unassembled WGS sequence.
DR   GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
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   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   4: Predicted;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000313|EMBL:KKP38685.1};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KKP38685.1}.
FT   DOMAIN          2..201
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
SQ   SEQUENCE   201 AA;  22822 MW;  868CD39349A3370A CRC64;
     MCGIFAYFGP KDNALEIVIK GLKKLEYRGY DSWGVALKVA NDFVIHKELG KIGDFSFADI
     AKITQSGAVQ SKINTSKFSD RFKISIGHSR WATHGGVTEY NAHPQWSHDQ EIVLCHNGIF
     ENYLEIKKKL IDKGYTFRSE TDTEVLAHLI ADYLKNFDFE TATKKALAEM TGRYAVIVLF
     KNEDKIIAAR RGSPLRIFYC L
//
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