ID A0A1J0A5H6_9ENTE Unreviewed; 489 AA.
AC A0A1J0A5H6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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:APB31190.1};
GN ORFNames=BHY08_04705 {ECO:0000313|EMBL:APB31190.1};
OS Vagococcus teuberi.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX NCBI_TaxID=519472 {ECO:0000313|EMBL:APB31190.1, ECO:0000313|Proteomes:UP000191200};
RN [1] {ECO:0000313|EMBL:APB31190.1, ECO:0000313|Proteomes:UP000191200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21459 {ECO:0000313|EMBL:APB31190.1,
RC ECO:0000313|Proteomes:UP000191200};
RA Wullschleger S., Seifert C., Baumgartner S., Lacroix C., Bonfoh B.,
RA Stevens M.J., Meile L.;
RT "Vagococcus teuberi sp. nov., isolated from the Malian artisanal sour milk
RT fene.";
RL Submitted (SEP-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|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}.
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DR EMBL; CP017267; APB31190.1; -; Genomic_DNA.
DR RefSeq; WP_071456776.1; NZ_CP017267.1.
DR AlphaFoldDB; A0A1J0A5H6; -.
DR STRING; 519472.BHY08_04705; -.
DR KEGG; vte:BHY08_04705; -.
DR OrthoDB; 9811471at2; -.
DR Proteomes; UP000191200; Chromosome.
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 InterPro; IPR006594; LisH.
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.
DR PROSITE; PS50896; LISH; 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:UP000191200};
KW Transferase {ECO:0000313|EMBL:APB31190.1}.
FT DOMAIN 25..463
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT ACT_SITE 78
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
FT ACT_SITE 153
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
FT ACT_SITE 177
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
SQ SEQUENCE 489 AA; 52789 MW; C684F70F828F6E94 CRC64;
MTELQQLTVK QLSEALNKKE LSSQEVVKSG FDYIKETEPT IDAFITLSEE KALAEAKKID
ESPRSDLTPL AGIPIGIKDN IVTKAVLTTA ASKMLYNFNP IYSATAVEKL ESAGLVSMGK
LNMDEFAMGS STETSYFKKT KNAWDQTKVP GGSSGGSAAS VAAGQVPASL GSDTGGSIRQ
PASFNGIVGM KPTYGRVSRY GLIAFSSSLD QIGPMTRTVE DNAMILNAIS GHDAKDSTSS
RRDTPDFTNL IGQDIKGMKI GVPKEFMGEG VHPDIRQAVK EAVKTFEALG ATVDEVSLPN
AVYGVEVYYI IASSEASSNL QRFDGIRYGY RSENISNLED VYVNSRSEGF GSEVKRRIML
GTFSLSAGFY DAYFRKAGQV RTLIVNDFKK VFENYDLILG PVSPTVAFEF GAAQDDPITA
YMRDILTIPV NLAGLPGMSV PGGFSEGLPI GIQLIGNHFD EEKMYQAAYA FEQATDFHKK
QPVILGGKA
//
