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Database: UniProt
Entry: A0A1J4TV05_9BACT
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Original site: A0A1J4TV05_9BACT 
ID   A0A1J4TV05_9BACT        Unreviewed;       476 AA.
AC   A0A1J4TV05;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
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   ECO:0000313|EMBL:OIO13911.1};
GN   ORFNames=AUJ54_15345 {ECO:0000313|EMBL:OIO13911.1};
OS   Ignavibacteria bacterium CG1_02_37_35.
OC   Bacteria; Ignavibacteriota; Ignavibacteria.
OX   NCBI_TaxID=1805220 {ECO:0000313|EMBL:OIO13911.1, ECO:0000313|Proteomes:UP000182308};
RN   [1] {ECO:0000313|EMBL:OIO13911.1, ECO:0000313|Proteomes:UP000182308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CG1_02_37_35 {ECO:0000313|EMBL:OIO13911.1};
RX   PubMed=27112493;
RA   Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA   Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT   "Genomic resolution of a cold subsurface aquifer community provides
RT   metabolic insights for novel microbes adapted to high CO concentrations.";
RL   Environ. Microbiol. 0:0-0(2016).
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|HAMAP-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:OIO13911.1}.
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DR   EMBL; MNVA01000232; OIO13911.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J4TV05; -.
DR   STRING; 1805220.AUJ54_15345; -.
DR   Proteomes; UP000182308; 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}; Transferase {ECO:0000313|EMBL:OIO13911.1}.
FT   DOMAIN          22..463
FT                   /note="Amidase"
FT                   /evidence="ECO:0000259|Pfam:PF01425"
FT   ACT_SITE        75
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
FT   ACT_SITE        150
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
FT   ACT_SITE        174
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
SQ   SEQUENCE   476 AA;  52033 MW;  C783982BF0014D74 CRC64;
     MSYKNYTEKL RLLKEGKLSL VENVQNFLSR IEERKNLNAF TFLFAEEAIQ KATEVELKIA
     VGSFGKLAGM VIAVKDVLAI KDKPLTCSSR ILENFTSLYT ATAVQKLLDE DAIIIGKTNC
     DEFAMGSSNE NSAFGAVKNP LDETRVPGGS SGGSAVAVAA NLCDVALGTD TGGSIRQPAA
     FCGIYGLKPT YGLVSRFGLT AFASSFDCIG PFANSVEDIA LTLEVLAGQD KSDSTSINAE
     KKVYPNLLGN NKQKLKIGIP KEYFVEGLSL EIKEQIELVI HKLKELNFSI EEVSLPHTEF
     AIATYYILTT AEASSNLARF DGARYGYRSK QSSSLKEMYN ASRSEGFGSE VKRRIMLGTY
     VLSSGYYDAY YKKAQKVRRK IKEDFVKVFS KIDVLLTPTT PTTAFKLGEK TSDPLEMYLS
     DIFTTSANLA GIPGINIPIG KDKNNLPIGL QLLANQFEEE KLLQLGSTIT GEILII
//
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