ID   A0A1G2DDK3_9BACT        Unreviewed;       601 AA.
AC   A0A1G2DDK3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   13-SEP-2023, entry version 19.
DE   RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] {ECO:0000256|ARBA:ARBA00016090};
DE            EC=2.6.1.16 {ECO:0000256|ARBA:ARBA00012916};
GN   ORFNames=A3C93_02210 {ECO:0000313|EMBL:OGZ11727.1};
OS   Candidatus Lloydbacteria bacterium RIFCSPHIGHO2_02_FULL_54_17.
OC   Bacteria; Candidatus Lloydbacteria.
OX   NCBI_TaxID=1798664 {ECO:0000313|EMBL:OGZ11727.1, ECO:0000313|Proteomes:UP000178636};
RN   [1] {ECO:0000313|EMBL:OGZ11727.1, ECO:0000313|Proteomes:UP000178636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGZ11727.1}.
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DR   EMBL; MHLO01000029; OGZ11727.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G2DDK3; -.
DR   STRING; 1798664.A3C93_02210; -.
DR   Proteomes; UP000178636; Unassembled WGS sequence.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IEA:UniProtKB-EC.
DR   GO; GO:1901137; P:carbohydrate derivative biosynthetic process; IEA:InterPro.
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   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   4: Predicted;
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          2..224
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          285..424
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          455..591
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
SQ   SEQUENCE   601 AA;  66045 MW;  C6DED8696BD6D202 CRC64;
     MCGIFGYVGV RERDVALMTY RALRDLEYRG YDSWGIAAMT PDGVFVRKSV GKISDTNEQE
     LKGISGKLAI GHSRWATHGG VSEVNSHPHF NRDRTIAVIH NGIVENHNEL RAFLYAKLGL
     VHADLFVSET DTEVIPHLID YFLRLGNTFE SAFVETGKML EGRYAVVVMK RGEPYLLAMR
     DGSPLVVGEG EDQYYLASDV PAFLDHTRTV CYPGDREYLK VSAEGIMMRS LDDGAKVEPK
     WSEILWDKAS ATKEGHPHYM LKEILEQPLS LDKAIRQEDG KLLEAAALMK EAEHCFFIGC
     GTAAKMAKLG ELYAASVGGR QTTAFVGSEF KPYEQFLDRK SVLFAVSQSG ETADVLEALS
     VGKKRGAKIV SLLNVVGSSM DRMSDKKLFI NTGPEIAVAS TKAATAQAAV LILLAHALAK
     DGKAKLAEGK HLLRRAVKEI KAWLTPDLSY EIRRVAERLK DTNDLYIIGR GLNAPIAHEA
     AIKIQEVSYI HAEGFPGGEL KHGPIALIQK GTPVIALIAN DETRRDMESN TMELKSRGAY
     IIGIAPTHSP LFDEWIPVPD LGIASTIANL IPIQLLAYHL AVLRGNDPDK PRNLAKSVTV
     K
//