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Database: UniProt
Entry: A0A158F9T6_9BURK
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ID   A0A158F9T6_9BURK        Unreviewed;       524 AA.
AC   A0A158F9T6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=AWB69_00815 {ECO:0000313|EMBL:SAL16089.1};
OS   Caballeronia udeis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=1232866 {ECO:0000313|EMBL:SAL16089.1, ECO:0000313|Proteomes:UP000054683};
RN   [1] {ECO:0000313|EMBL:SAL16089.1, ECO:0000313|Proteomes:UP000054683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 27134 {ECO:0000313|EMBL:SAL16089.1};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) 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|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}.
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DR   EMBL; FCOK02000003; SAL16089.1; -; Genomic_DNA.
DR   RefSeq; WP_062082368.1; NZ_FCOK02000003.1.
DR   AlphaFoldDB; A0A158F9T6; -.
DR   OrthoDB; 9811471at2; -.
DR   Proteomes; UP000054683; 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:SAL16089.1}.
FT   DOMAIN          22..477
FT                   /note="Amidase"
FT                   /evidence="ECO:0000259|Pfam:PF01425"
FT   REGION          499..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   524 AA;  55813 MW;  3EABE53B453426C3 CRC64;
     MHQKSLTELR AALDAKTLSA VELAQLFLQR IDAAKDLNAF ISVDHDLTLE QAKAADALIA
     KGAAGALTGL PIAHKDVFVT RGWTSTAGSK MLANYASPFD ATVVERLKNA GVVTLGKTNM
     DEFAMGSSNE NSYFGPVKNP WDLKAVPGGS SGGSAAAVAA RLAPAATGTD TGGSIRQPAS
     FTGITGIKPT YGRVSRYGMI AFASSLDQGG PMARSASDCA LLLNAIASFD PRDSTSLQRE
     DEDYTRYLGQ NWSGTDAAKP LAGLRIGLPK EFFGEGLSAE VRGAVDAALK QYEALGATLV
     EVSLPKTELS IPVYYIIAPA EASSNLSRFD GVRYGHRAAE YTDLLDMYKK SRAEGFGPEV
     KRRILVGAYV LSHGYYDAYY LQAQKIRRII AQDFQEAFNH CDVIMGPVAP SVAWNLGEKA
     DDPVQMYLAD IYTLSISLAG LPGMSVPCGF GAAGSAHATR PVGLQIIGNY FNEARLLQVA
     DAFQRATDWH VQSPAGQIEL PPRSLNSLPP EGAHAPLEAA RRES
//
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