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Database: UniProt
Entry: A4YGB5_METS5
LinkDB: A4YGB5_METS5
Original site: A4YGB5_METS5 
ID   A4YGB5_METS5            Unreviewed;       222 AA.
AC   A4YGB5;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   24-JAN-2024, entry version 70.
DE   SubName: Full=Glutamine amidotransferase class-I {ECO:0000313|EMBL:ABP95467.1};
GN   OrderedLocusNames=Msed_1309 {ECO:0000313|EMBL:ABP95467.1};
OS   Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS   / TH2).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Metallosphaera.
OX   NCBI_TaxID=399549 {ECO:0000313|EMBL:ABP95467.1, ECO:0000313|Proteomes:UP000000242};
RN   [1] {ECO:0000313|EMBL:ABP95467.1, ECO:0000313|Proteomes:UP000000242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2
RC   {ECO:0000313|Proteomes:UP000000242};
RX   PubMed=18083856; DOI=10.1128/AEM.02019-07;
RA   Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT   "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT   archaeon Metallosphaera sedula provides insights into bioleaching-
RT   associated metabolism.";
RL   Appl. Environ. Microbiol. 74:682-692(2008).
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DR   EMBL; CP000682; ABP95467.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4YGB5; -.
DR   STRING; 399549.Msed_1309; -.
DR   KEGG; mse:Msed_1309; -.
DR   eggNOG; arCOG00090; Archaea.
DR   HOGENOM; CLU_054974_3_1_2; -.
DR   OMA; FTIFEWH; -.
DR   Proteomes; UP000000242; 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:ABP95467.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000242};
KW   Transferase {ECO:0000313|EMBL:ABP95467.1}.
FT   DOMAIN          46..182
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   ACT_SITE        97
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        177
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        179
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   222 AA;  25126 MW;  95EE7BE7BDAD65F4 CRC64;
     MREEDIKPKV LLEIMFLVIQ NYPIEGLGTL KQVLDSKGIR TLTVSAEDLT GKEEFEGLIV
     LGGPMGVYEM EKYPHLRREV DLIQKAIAED KRVLGICLGA QLLSYALGGK VVKGAFGPEL
     GIGKVKFMGK LANLGEVEVF QWHGDTFSLP EGSELLAYSE KYFQAFSFSH ALGLQFHVEV
     DGKMVEEWIR EYGGNQDWVK EVEIRQNSLL RIASYLVEWW LR
//
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