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Database: UniProt
Entry: A0A1G2DDW1_9BACT
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ID   A0A1G2DDW1_9BACT        Unreviewed;       595 AA.
AC   A0A1G2DDW1;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   13-SEP-2023, entry version 31.
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=A3D67_03220 {ECO:0000313|EMBL:OGZ11040.1};
OS   Candidatus Lloydbacteria bacterium RIFCSPHIGHO2_02_FULL_51_22.
OC   Bacteria; Candidatus Lloydbacteria.
OX   NCBI_TaxID=1798663 {ECO:0000313|EMBL:OGZ11040.1, ECO:0000313|Proteomes:UP000178099};
RN   [1] {ECO:0000313|EMBL:OGZ11040.1, ECO:0000313|Proteomes:UP000178099}
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:OGZ11040.1}.
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DR   EMBL; MHLN01000027; OGZ11040.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G2DDW1; -.
DR   Proteomes; UP000178099; 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..221
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   DOMAIN          283..422
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   DOMAIN          449..585
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
SQ   SEQUENCE   595 AA;  64263 MW;  5EA064D2A3DFBFFD CRC64;
     MCGIFSYRGE KEQNALVVLK GLRDLEYRGY DSWGFAVRNG DGTIVCKKAV GKISEAREED
     FARLFGISAI GHTRWATHGG VSEKNTHPHL SADGSIAVVH NGIIENYEVL KAELIKKYGA
     RLFRSETDTE VIPHLIADAV SGGATFEKAC SVVSKRLTGR FAFIALHGKT GALFAVRDGS
     PLVLGNGGES WYAASDIPAL LDYTTKIYFL ENGESAMLSP GASAVFQNFR TGKKIAKRAT
     TLTLTKQSAS KEGHAHYMLK EILDQKETLS ATLSVSKKEI ARAVRELRAA KKIFMTGCGT
     AGHMCMGGEY FFIAHAGRTA PFAASSEFGK LLPFVDRESV VIAVTQSGET ADLLEAIKGA
     KVRGAKIISL VNVRNSSVER ESDITLPIQV GVEKAVASTK AATSQLLLLI LLAYAVGGKE
     TAARRLLGDA AHGVSAWLTT ALFKKIKRAA RRFITREHVY VIGKSLYFPV ALEAALKIKE
     VSYMHAEGLA SGELKHGTLA LIEKGTPCMV FVANDAHTHD VLGSVSELKA RGAFLIGVSP
     EKHPSFDEWI KVPDLKDASP LTHMIAAQIF AYYLSVGRGH NPDMPRNLAK SVTVK
//
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