ID Q46BG4_METBF Unreviewed; 243 AA.
AC Q46BG4;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 24-JAN-2024, entry version 93.
DE SubName: Full=Glutamine amidotransferase (Class I) {ECO:0000313|EMBL:AAZ70778.1};
GN OrderedLocusNames=Mbar_A1837 {ECO:0000313|EMBL:AAZ70778.1};
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797 {ECO:0000313|EMBL:AAZ70778.1};
RN [1] {ECO:0000313|EMBL:AAZ70778.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Fusaro {ECO:0000313|EMBL:AAZ70778.1};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Goodwin L.A., Saunders E.H., Schmutz J.,
RA Larimer F., Land M., Anderson I., Richardson P.;
RT "Complete sequence of chromosome 1 of Methanosarcina barkeri str. fusaro.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000099; AAZ70778.1; -; Genomic_DNA.
DR AlphaFoldDB; Q46BG4; -.
DR STRING; 269797.Mbar_A1837; -.
DR PaxDb; 269797-Mbar_A1837; -.
DR KEGG; mba:Mbar_A1837; -.
DR eggNOG; arCOG00090; Archaea.
DR HOGENOM; CLU_054974_3_3_2; -.
DR OMA; TSMLHWH; -.
DR OrthoDB; 7388at2157; -.
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:AAZ70778.1}; Transferase {ECO:0000313|EMBL:AAZ70778.1}.
FT DOMAIN 43..184
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 87
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 180
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 182
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 243 AA; 27924 MW; AD07ED8730328690 CRC64;
MRIHCLQHLK NDTLGNIGIW IDEKGYKLTK TLLYENSLFP APEEFDILLI MGGTMSVYQE
KEYPWLKPEK KFVKKTMDAD KPVLGSCFGA QMIAEVLGGK VTKNQYKEIG WHTVRAVKGK
SPGEIKSSEL PSCMFPEFTG FMWHGDTFGI PAGAVKLFES EACPNQGFLY NEKVLGLQFH
PEANRQWVRN LIRDSGHELV QGKYIQSEKE IYVYESFFES SRNLAFSLMD WFEEKCKPEK
TKV
//