ID A0A0B8N4H6_9NOCA Unreviewed; 489 AA.
AC A0A0B8N4H6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-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=NS07_v2contig00039-0054 {ECO:0000313|EMBL:GAM46899.1},
GN NS506_06630 {ECO:0000313|EMBL:APB00661.1};
OS Nocardia seriolae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=37332 {ECO:0000313|EMBL:GAM46899.1, ECO:0000313|Proteomes:UP000019401};
RN [1] {ECO:0000313|EMBL:GAM46899.1, ECO:0000313|Proteomes:UP000019401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N-2927 {ECO:0000313|EMBL:GAM46899.1,
RC ECO:0000313|Proteomes:UP000019401};
RA Imajoh M., Fukumoto Y., Yamane J., Sukeda M., Shimizu M., Ohnishi K.,
RA Oshima S.;
RT "Draft Genome Sequence of Nocardia seriolae Strain N-2927 (NBRC 110360),
RT Isolated as the Causal Agent of Nocardiosis of Yellowtail (Seriola
RT quinqueradiata) in Kochi Prefecture, Japan.";
RL Genome Announc. 3:e00082-15(2015).
RN [2] {ECO:0000313|EMBL:APB00661.1, ECO:0000313|Proteomes:UP000180166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EM150506 {ECO:0000313|EMBL:APB00661.1,
RC ECO:0000313|Proteomes:UP000180166};
RA Han H.-J.;
RT "Genome sequence of Nocardia seriolae strain EM150506, isolated from
RT Anguila japonica.";
RL Submitted (OCT-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; CP017839; APB00661.1; -; Genomic_DNA.
DR EMBL; BAWD02000039; GAM46899.1; -; Genomic_DNA.
DR RefSeq; WP_033087117.1; NZ_WMKH01000285.1.
DR STRING; 37332.NS506_06630; -.
DR GeneID; 61146878; -.
DR KEGG; nsr:NS506_06630; -.
DR PATRIC; fig|37332.12.peg.6812; -.
DR OrthoDB; 9811471at2; -.
DR Proteomes; UP000019401; Unassembled WGS sequence.
DR Proteomes; UP000180166; 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 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:UP000019401};
KW Transferase {ECO:0000313|EMBL:GAM46899.1}.
FT DOMAIN 25..474
FT /note="Amidase"
FT /evidence="ECO:0000259|Pfam:PF01425"
FT REGION 131..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 80
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
FT ACT_SITE 155
FT /note="Charge relay system"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
FT ACT_SITE 179
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00120"
SQ SEQUENCE 489 AA; 51144 MW; 4CD73788B7051452 CRC64;
MSDLTKLSAA DLADKIHTRA VSAVEVTEAH IQRIAEVDGE INAFLHVAGE QALLTAAEID
RQVAGGEIAS PLAGVPLALK DVFTTTDMPT TCGSKILEGW VSPYDATLTT KLRAAGIPIL
GKTNMDEFAM GSSTENSAYG PTRNPRDTDR IPGGSGGGSA AALASYQAPL AIGTDTGGSI
RQPAAVTATV GTKPTYGTVS RFGLVACASS LDQGGPCGRT VLDTALLHEV IAGYDPRDST
SRNVPVPPVV AAARAGAKGD LKGVKVGVVK ELHSDSYQPG VIASFDAAVA QLKDLGAEVI
EVSCPHFEYA LPAYYLILPS EVSSNLARFD AMRYGLRVGD DGTRSAEQVM SLTREAGLGP
EVKRRIMIGT YALSAGYYDA YYGQANKVRN LIAQDFDKAY ETVDVLVSPT SPFTPWKLGE
KVNDPLAMYL SDLCTLPTNL AGHCAMSVPS GLSAEDGMPV GLQIMAPALA DDRLYRVGAA
YEAARGPIA
//
