ID Q1LN14_CUPMC Unreviewed; 242 AA.
AC Q1LN14;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Glutamine amidotransferase {ECO:0000313|EMBL:ABF08462.1};
DE EC=6.3.5.2 {ECO:0000313|EMBL:ABF08462.1};
GN OrderedLocusNames=Rmet_1579 {ECO:0000313|EMBL:ABF08462.1};
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264 {ECO:0000313|EMBL:ABF08462.1, ECO:0000313|Proteomes:UP000002429};
RN [1] {ECO:0000313|Proteomes:UP000002429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34
RC {ECO:0000313|Proteomes:UP000002429};
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
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; CP000352; ABF08462.1; -; Genomic_DNA.
DR RefSeq; WP_011516314.1; NC_007973.1.
DR AlphaFoldDB; Q1LN14; -.
DR STRING; 266264.Rmet_1579; -.
DR KEGG; rme:Rmet_1579; -.
DR eggNOG; COG0518; Bacteria.
DR HOGENOM; CLU_054974_3_1_4; -.
DR Proteomes; UP000002429; Chromosome.
DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:ABF08462.1}; Ligase {ECO:0000313|EMBL:ABF08462.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002429}.
FT DOMAIN 26..193
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 98
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 185
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 187
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 242 AA; 26070 MW; DE7340C026647B5E CRC64;
MSDTHAPRGP RRTDVIQHVG FEHAGVIADA ARARGHEIRM YQAGVDDLAL VQDDPADLLV
VLGGPIGVYE TEAYPWLEAE IAVIRDRLHA QRPMIGACLG AQLIAAAAGA RVYPGTREIG
WAPITPTEAG RRSPLAALAE ADWQVLHWHG DTFDLPAGAE LLASTAATPH QAYAIGSHVL
ALQFHPEVKP GDIETWLIGH TVELGRAGID PRTIRRRTGE IGAVVANAGE RMFTRWMEEA
GV
//
