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Database: UniProt
Entry: S2XE09_9BACL
LinkDB: S2XE09_9BACL
Original site: S2XE09_9BACL 
ID   S2XE09_9BACL            Unreviewed;       489 AA.
AC   S2XE09;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A {ECO:0000256|HAMAP-Rule:MF_00120};
DE            Short=Glu-ADT subunit A {ECO:0000256|HAMAP-Rule:MF_00120};
DE            EC=6.3.5.7 {ECO:0000256|HAMAP-Rule:MF_00120};
GN   Name=gatA {ECO:0000256|HAMAP-Rule:MF_00120};
GN   ORFNames=HMPREF1210_02924 {ECO:0000313|EMBL:EPD50353.1};
OS   Paenisporosarcina sp. HGH0030.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae;
OC   Paenisporosarcina.
OX   NCBI_TaxID=1078085 {ECO:0000313|EMBL:EPD50353.1, ECO:0000313|Proteomes:UP000014412};
RN   [1] {ECO:0000313|EMBL:EPD50353.1, ECO:0000313|Proteomes:UP000014412}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HGH0030 {ECO:0000313|EMBL:EPD50353.1,
RC   ECO:0000313|Proteomes:UP000014412};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA   Kim K., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Paenisporosarcina sp. HGH0030.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln)
CC       through the transamidation of misacylated Glu-tRNA(Gln) in organisms
CC       which lack glutaminyl-tRNA synthetase. The reaction takes place in the
CC       presence of glutamine and ATP through an activated gamma-phospho-Glu-
CC       tRNA(Gln). {ECO:0000256|ARBA:ARBA00025295, ECO:0000256|HAMAP-
CC       Rule:MF_00120}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + L-glutamine + L-glutamyl-tRNA(Gln) = ADP + H(+) +
CC         L-glutamate + L-glutaminyl-tRNA(Gln) + phosphate;
CC         Xref=Rhea:RHEA:17521, Rhea:RHEA-COMP:9681, Rhea:RHEA-COMP:9684,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:78520, ChEBI:CHEBI:78521, ChEBI:CHEBI:456216; EC=6.3.5.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00001243, ECO:0000256|HAMAP-
CC         Rule:MF_00120};
CC   -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000256|HAMAP-
CC       Rule:MF_00120}.
CC   -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC       {ECO:0000256|ARBA:ARBA00008069, ECO:0000256|HAMAP-Rule:MF_00120}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EPD50353.1}.
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DR   EMBL; AGEQ01000016; EPD50353.1; -; Genomic_DNA.
DR   RefSeq; WP_016429410.1; NZ_KE150422.1.
DR   AlphaFoldDB; S2XE09; -.
DR   STRING; 1078085.HMPREF1210_02924; -.
DR   PATRIC; fig|1078085.3.peg.2905; -.
DR   eggNOG; COG0154; Bacteria.
DR   HOGENOM; CLU_009600_0_3_9; -.
DR   Proteomes; UP000014412; Unassembled WGS sequence.
DR   GO; GO:0030956; C:glutamyl-tRNA(Gln) amidotransferase complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR   HAMAP; MF_00120; GatA; 1.
DR   InterPro; IPR000120; Amidase.
DR   InterPro; IPR020556; Amidase_CS.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   InterPro; IPR004412; GatA.
DR   NCBIfam; TIGR00132; gatA; 1.
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.
DR   PROSITE; PS00571; AMIDASES; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00120};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00120};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00120};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00120}; Reference proteome {ECO:0000313|Proteomes:UP000014412};
KW   Transferase {ECO:0000313|EMBL:EPD50353.1}.
FT   DOMAIN          24..463
FT                   /note="Amidase"
FT                   /evidence="ECO:0000259|Pfam:PF01425"
FT   ACT_SITE        77
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
FT   ACT_SITE        152
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
FT   ACT_SITE        176
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
SQ   SEQUENCE   489 AA;  52873 MW;  6B62F8B12C94D881 CRC64;
     MTLFNYSATD LQEMIHNKEL SIADLTAEAY TRIETLDGDV KAFLALNKEQ AMAQAKEMDE
     VPASKRGPLF GMPIGVKDNI VTEGIETTCS SKILQGFNPI YDATVVRKLR EAGMITIGKL
     NMDEFAMGSS TENSAYKITR NPWDLDRVPG GSSGGSAASV AAGEVPFSLG SDTGGSIRQP
     ASFCGVVGMK PTYGRVSRFG LVAFASSLDQ IGPITRNVRD NALLLEAISG VDENDTTSAN
     VDVPSFVESL TGDVKGLRIG VPKEYLGDGV GEAAKQSVLD ALKVLESLGA TWEEVSLPHS
     KYGLATYYLL ASSEASSNLA RFDGIRYGFR AENVESLMDL YKETRAQGFG DEVKRRIMLG
     TFALSAGSYD AYYKKAQQVR TLIKQDFDQV FEKYDVIIGP TTPTPAFKVG EKNDDPLTMY
     ANDILTIPVN LAGVPGISVP CGYSEGMPLG LQIIGKHFDE ATIYRVAHAY EQATSFHKET
     PQLWEGAKS
//
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