ID   A0A0G0XKC0_9BACT        Unreviewed;       356 AA.
AC   A0A0G0XKC0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Amidophosphoribosyltransferase {ECO:0000313|EMBL:KKR88097.1};
GN   ORFNames=UU34_C0001G0094 {ECO:0000313|EMBL:KKR88097.1};
OS   Candidatus Curtissbacteria bacterium GW2011_GWA1_41_11.
OC   Bacteria; Candidatus Curtissbacteria.
OX   NCBI_TaxID=1618409 {ECO:0000313|EMBL:KKR88097.1, ECO:0000313|Proteomes:UP000034854};
RN   [1] {ECO:0000313|EMBL:KKR88097.1, ECO:0000313|Proteomes:UP000034854}
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   -!- 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:KKR88097.1}.
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DR   EMBL; LCAG01000001; KKR88097.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0XKC0; -.
DR   PATRIC; fig|1618409.3.peg.96; -.
DR   Proteomes; UP000034854; Unassembled WGS sequence.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
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; PTHR11907; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR11907:SF0; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF13537; GATase_7; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   4: Predicted;
KW   Glycosyltransferase {ECO:0000313|EMBL:KKR88097.1};
KW   Transferase {ECO:0000313|EMBL:KKR88097.1}.
FT   DOMAIN          17..243
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51278"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   356 AA;  39756 MW;  56192E76DF3F1C31 CRC64;
     MISKSLIEND EKPHDHCGLA GSFTDTSDDV SAVVIEMGKA LQHRGQNGGG IAVKAKGKLI
     KVYKKSQAFN EIFKSVDLIE EQSLRGEVAI AHLRYPTEGA GRQNCDAQPF FASFGGWELA
     LGHNGSIVDV KKHKAKLRKF NIKTESDSDS EILAWLIATA PGITWKQKIA TALADVKGAY
     SLVMLTNDNK LMAIRDPWGI RPLVFAQDNG RVFVASETCA LDRIGIRHHE KLKAGQLLIA
     DSDGLSISQY AQPQKQSFCV FEKLYFSHET STWDGVIGEN RENLGKILAE EEIERVRKGK
     IKKETIEGID YVVAVPDTAR PGTFAFYQTL AENLKFKNKL RFLRGLVKER YDYKYF
//