ID A0A1I1NUG8_9RHOB Unreviewed; 248 AA.
AC A0A1I1NUG8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=GMP synthase (Glutamine-hydrolysing) {ECO:0000313|EMBL:SFC98383.1};
GN ORFNames=SAMN04488094_112133 {ECO:0000313|EMBL:SFC98383.1};
OS Tropicimonas isoalkanivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Tropicimonas.
OX NCBI_TaxID=441112 {ECO:0000313|EMBL:SFC98383.1, ECO:0000313|Proteomes:UP000198728};
RN [1] {ECO:0000313|EMBL:SFC98383.1, ECO:0000313|Proteomes:UP000198728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19548 {ECO:0000313|EMBL:SFC98383.1,
RC ECO:0000313|Proteomes:UP000198728};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOLG01000012; SFC98383.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1NUG8; -.
DR STRING; 441112.SAMN04488094_112133; -.
DR OrthoDB; 9794816at2; -.
DR Proteomes; UP000198728; Unassembled WGS sequence.
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 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 Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Reference proteome {ECO:0000313|Proteomes:UP000198728}.
FT DOMAIN 50..196
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 101
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 191
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 193
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 248 AA; 27231 MW; E397B64700FC3310 CRC64;
MKPFLILQLR PEPEASDNEY EAFLSRGGLR PEETRRIRLE REEVPGDLDL TAFSGIIVGG
GPGCVSDPDD TKPVIEKAIE REILGMMPQI TEQDIPFLGC CYGIGILAHH LGAEVSKARY
GEPVGAVSCE VTPDGRNDPV LAGLPERFDA LVGHKEAVQT LPPGCVHLLA SDPCPFQMIR
YGRNVYATQF HPEADGAVFA LRIAIYKDKG YFPPEEADAL TETVLASKVD LAPRLLRNFV
QTYRQSRG
//
