ID A0A1F6M0W3_9BACT Unreviewed; 338 AA.
AC A0A1F6M0W3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Glutamine amidotransferase domain-containing protein {ECO:0000259|Pfam:PF00117};
GN ORFNames=A3J66_03835 {ECO:0000313|EMBL:OGH65259.1};
OS Candidatus Magasanikbacteria bacterium RIFCSPHIGHO2_02_FULL_47_14.
OC Bacteria; Candidatus Magasanikbacteria.
OX NCBI_TaxID=1798680 {ECO:0000313|EMBL:OGH65259.1, ECO:0000313|Proteomes:UP000176282};
RN [1] {ECO:0000313|EMBL:OGH65259.1, ECO:0000313|Proteomes:UP000176282}
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 -!- 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:OGH65259.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MFQB01000051; OGH65259.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6M0W3; -.
DR STRING; 1798680.A3J66_03835; -.
DR Proteomes; UP000176282; Unassembled WGS sequence.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR044992; ChyE-like.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR017926; GATASE.
DR PANTHER; PTHR42695; GLUTAMINE AMIDOTRANSFERASE YLR126C-RELATED; 1.
DR PANTHER; PTHR42695:SF5; GLUTAMINE AMIDOTRANSFERASE YLR126C-RELATED; 1.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605}.
FT DOMAIN 130..285
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT COILED 16..43
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 172
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 282
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 284
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 338 AA; 38265 MW; E9607D113D78BFEB CRC64;
MSRGPEQFIR PRAVQTEVWD RQLEALERER EGIEEHRLEA HRMVTDLLTE QARILVLDFS
QGSSGLDRLK DARMRDAVRE RQADGVMESH ADLFRAALGF DPGDSRIDIW KVYEDPERTG
IPYPDVWFAT GGPAMPSELH PGNETENTSW LERAVSAMKE LEKAKVPGMA VCLGHQLWEH
SQGANVGKRH PQREFGTVRL QGTPFAQELQ LLVGILDDQG GVEISASHSE AVITPPQGRN
MEVIALNRYS DYQGAIHGLG PAERPVREAV EEDEFVLSIQ NHPEVMAIFL AALRELRAPA
MRKEGLKPEE MIFHQTPEAR KLFLRFLEVA ARRMNKRT
//
