ID F4G2D9_METCR Unreviewed; 202 AA.
AC F4G2D9;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Glutamine amidotransferase class-I {ECO:0000313|EMBL:AEB94987.1};
GN OrderedLocusNames=Mcup_0882 {ECO:0000313|EMBL:AEB94987.1};
OS Metallosphaera cuprina (strain Ar-4).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Metallosphaera.
OX NCBI_TaxID=1006006 {ECO:0000313|EMBL:AEB94987.1, ECO:0000313|Proteomes:UP000007812};
RN [1] {ECO:0000313|EMBL:AEB94987.1, ECO:0000313|Proteomes:UP000007812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ar-4 {ECO:0000313|EMBL:AEB94987.1,
RC ECO:0000313|Proteomes:UP000007812};
RX PubMed=21551305; DOI=10.1128/JB.05038-11;
RA Liu L.J., You X.Y., Zheng H., Wang S., Jiang C.Y., Liu S.J.;
RT "Complete genome sequence of Metallosphaera cuprina, a metal sulfide-
RT oxidizing archaeon from a hot spring.";
RL J. Bacteriol. 193:3387-3388(2011).
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DR EMBL; CP002656; AEB94987.1; -; Genomic_DNA.
DR AlphaFoldDB; F4G2D9; -.
DR STRING; 1006006.Mcup_0882; -.
DR KEGG; mcn:Mcup_0882; -.
DR PATRIC; fig|1006006.8.peg.881; -.
DR eggNOG; arCOG00090; Archaea.
DR HOGENOM; CLU_054974_3_1_2; -.
DR OMA; FTIFEWH; -.
DR Proteomes; UP000007812; Chromosome.
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 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:AEB94987.1}; Transferase {ECO:0000313|EMBL:AEB94987.1}.
FT DOMAIN 24..160
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 74
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 156
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 158
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 202 AA; 22787 MW; FCA0F9779177D92E CRC64;
MEGPGSIKEV LEERGFKVLE RLATEIKGNE TFDGLIVMGG PMGVYESDRY PYLNVEMTLI
RRAITSGKPV LGVCLGSQLI SAALGGSVSR GEFGEELGVY KVYLLEDLRE VLGPSIEVFQ
MHGDTFTLPK GGKLLAYSEK YFQAFRVGTA LGLQFHLEVN RKIVSQWIEY YKINRQFDRE
VDDERLRRSS EKVISYWLSS VS
//