ID   M9SFG9_METAX            Unreviewed;       441 AA.
AC   M9SFG9;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Aspartyl-tRNA(Asn) amidotransferase subunit A/Glutamyl-tRNA(Gln) amidotransferase subunit A {ECO:0000313|EMBL:AGI86165.1};
DE            EC=6.3.5.6 {ECO:0000313|EMBL:AGI86165.1};
DE            EC=6.3.5.7 {ECO:0000313|EMBL:AGI86165.1};
GN   ORFNames=MMALV_14400 {ECO:0000313|EMBL:AGI86165.1};
OS   Methanomethylophilus alvi (strain Mx1201).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata;
OC   Methanomassiliicoccales; Methanomethylophilaceae; Methanomethylophilus.
OX   NCBI_TaxID=1236689 {ECO:0000313|EMBL:AGI86165.1, ECO:0000313|Proteomes:UP000012672};
RN   [1] {ECO:0000313|EMBL:AGI86165.1, ECO:0000313|Proteomes:UP000012672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mx1201 {ECO:0000313|EMBL:AGI86165.1,
RC   ECO:0000313|Proteomes:UP000012672};
RX   PubMed=23209209; DOI=10.1128/JB.01867-12;
RA   Borrel G., Harris H.M., Tottey W., Mihajlovski A., Parisot N.,
RA   Peyretaillade E., Peyret P., Gribaldo S., O'Toole P.W., Brugere J.F.;
RT   "Genome sequence of 'Candidatus Methanomethylophilus alvus' Mx1201, a
RT   methanogenic archaeon from the human gut belonging to a seventh order of
RT   methanogens.";
RL   J. Bacteriol. 194:6944-6945(2012).
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DR   EMBL; CP004049; AGI86165.1; -; Genomic_DNA.
DR   RefSeq; WP_015505311.1; NC_020913.1.
DR   AlphaFoldDB; M9SFG9; -.
DR   STRING; 1236689.MMALV_14400; -.
DR   GeneID; 41322196; -.
DR   KEGG; max:MMALV_14400; -.
DR   eggNOG; arCOG01717; Archaea.
DR   HOGENOM; CLU_009600_7_6_2; -.
DR   InParanoid; M9SFG9; -.
DR   OrthoDB; 7931at2157; -.
DR   Proteomes; UP000012672; Chromosome.
DR   GO; GO:0050566; F:asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR   InterPro; IPR000120; Amidase.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   PANTHER; PTHR11895:SF151; GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT A; 1.
DR   PANTHER; PTHR11895; TRANSAMIDASE; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   SUPFAM; SSF75304; Amidase signature (AS) enzymes; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:AGI86165.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012672};
KW   Transferase {ECO:0000313|EMBL:AGI86165.1}.
FT   DOMAIN          35..422
FT                   /note="Amidase"
FT                   /evidence="ECO:0000259|Pfam:PF01425"
SQ   SEQUENCE   441 AA;  48669 MW;  D98A9864A6A3F95B CRC64;
     MSDKDTLSRL KEINSVYGMF HDFGGEWTDD TKFLFSAKDN LTSIGFETCA GSKILEGYRP
     VFDATAIAKM KAAGGKLVGK TNMDEFGFGT FSANSAFEVP KNPFDLDRSC GGSSGGSACA
     AAVLEDHVSL GVSTGGSVCC PASFCGTYGI VPTYGRVSRY GLIDYGNSLD KIGLLAMDPH
     KLSEYLPVIS GRDPKDPTSC AQPDLKLEHR KMTSVAVPKE AVEGISDDVL RAFEDALERL
     KGMGIDVEYV DMPYLKYAMP AYYILATSEA STNLARYCGM RYGHQDGDLT LGFDEYFTSF
     RTEYFGDEAK RRILLGTYTR MEGFRDRYYA KALQVRLGVI DAYKTQFKDH DAVLTPTMPF
     VSPRFEDISA MSPVENYKAD FLTVPPNLAG TPHLNCPCGY DGNGMPIGMQ FVTDHWNEDQ
     LLTMAEEWDK QFDVRHAEVK A
//