ID   A0A0G2AT72_9BACT        Unreviewed;       744 AA.
AC   A0A0G2AT72;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Putative Glutamine amidotransferase {ECO:0000313|EMBL:KKW44632.1};
DE   Flags: Fragment;
GN   ORFNames=UY95_C0023G0008 {ECO:0000313|EMBL:KKW44632.1};
OS   Parcubacteria group bacterium GW2011_GWA2_56_7.
OC   Bacteria.
OX   NCBI_TaxID=1618860 {ECO:0000313|EMBL:KKW44632.1, ECO:0000313|Proteomes:UP000033964};
RN   [1] {ECO:0000313|EMBL:KKW44632.1, ECO:0000313|Proteomes:UP000033964}
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:KKW44632.1}.
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DR   EMBL; LCSA01000023; KKW44632.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G2AT72; -.
DR   PATRIC; fig|1618860.3.peg.295; -.
DR   Proteomes; UP000033964; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01741; GATase1_1; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR044992; ChyE-like.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR42695; GLUTAMINE AMIDOTRANSFERASE YLR126C-RELATED; 1.
DR   PANTHER; PTHR42695:SF5; GLUTAMINE AMIDOTRANSFERASE YLR126C-RELATED; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF00117; GATase; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Glutamine amidotransferase {ECO:0000256|ARBA:ARBA00022962,
KW   ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000313|EMBL:KKW44632.1}.
FT   DOMAIN          430..486
FT                   /note="ClpA/ClpB AAA lid"
FT                   /evidence="ECO:0000259|Pfam:PF17871"
FT   DOMAIN          573..689
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   COILED          458..485
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        591
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        682
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        684
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KKW44632.1"
SQ   SEQUENCE   744 AA;  83232 MW;  0C5F889FAB16C41E CRC64;
     EEALAEGKVI WLMGMTHFRG LVEDEIHGLD NYGSRFFAVA RGLFICAAGV LSARKLQRYL
     RTLIAAGIEP PHYELVEGDN VIDGTLKNLC LRGQIADFVL NKGWKICFYV GGRDEERFLA
     ELGLDWTHTL NTPFHSDWGN KVTLRERMAT AGLRDRFPRH RIMRSELFVG SKRADLAQIA
     TSAGMIFAGW RKDGVLGAPS IGTFRHLTFV VKVEGGDGGS LCSGAINFCA FRNDPSGHAE
     ALLILHLIGL ARSKNRRVIV EAWLHHDEWM DVGVVFNVCP GLSTDAILPV YMNLQLVDTV
     HEKYHVGCFM GVGKSLIDPA LEARIIARLR PVLAVMCAGE HPLAGRFSVD VLVHRETGEV
     RVLEVNPRWT ASWVLYLHLL HIQARTGLPT FGAMENIECG VRSPARVARR LHEAGSALRG
     VEGAVVTAPR FLPDKAIDLI DEAAARIKME IDSKPEVMDK LDRRLIQLKI EREAVKKEKD
     EASQKRHAFF FMPPSPLSSL RVLLVQARPD EMKEHEYHCV LQTSGLRPDQ VVIHDALTQP
     YADTILDHLD AVLIGGSGDY CASKVEMPHQ LELEAFVRRV RERGVPLLGI CFGAHIMVRA
     FGGEVIHDVS RQESETTRIF VDDAGRRDPV FGPMPATFYA QTSHKDHQDV LPSGAVRLAS
     TPVSRNQAWT IPGEPVYAIQ FHVELDQKTL TERFDFYRAK YFPTEESYDA ALSRLKPSPV
     APRLLRIFLQ AVVCEKKTYP FRTS
//