ID A7HME1_FERNB Unreviewed; 475 AA.
AC A7HME1;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 99.
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 OrderedLocusNames=Fnod_1227 {ECO:0000313|EMBL:ABS61074.1};
OS Fervidobacterium nodosum (strain ATCC 35602 / DSM 5306 / Rt17-B1).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Fervidobacteriaceae;
OC Fervidobacterium.
OX NCBI_TaxID=381764 {ECO:0000313|EMBL:ABS61074.1, ECO:0000313|Proteomes:UP000002415};
RN [1] {ECO:0000313|EMBL:ABS61074.1, ECO:0000313|Proteomes:UP000002415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1
RC {ECO:0000313|Proteomes:UP000002415};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Fervidobacterium nodosum Rt17-B1.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABS61074.1, ECO:0000313|Proteomes:UP000002415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35602 / DSM 5306 / Rt17-B1
RC {ECO:0000313|Proteomes:UP000002415};
RX PubMed=19307556; DOI=10.1073/pnas.0901260106;
RA Zhaxybayeva O., Swithers K.S., Lapierre P., Fournier G.P., Bickhart D.M.,
RA DeBoy R.T., Nelson K.E., Nesbo C.L., Doolittle W.F., Gogarten J.P.,
RA Noll K.M.;
RT "On the chimeric nature, thermophilic origin, and phylogenetic placement of
RT the Thermotogales.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5865-5870(2009).
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; CP000771; ABS61074.1; -; Genomic_DNA.
DR AlphaFoldDB; A7HME1; -.
DR STRING; 381764.Fnod_1227; -.
DR KEGG; fno:Fnod_1227; -.
DR eggNOG; COG0154; Bacteria.
DR HOGENOM; CLU_009600_0_3_0; -.
DR Proteomes; UP000002415; 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:UP000002415};
KW Transferase {ECO:0000313|EMBL:ABS61074.1}.
FT DOMAIN 71..462
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 475 AA; 52258 MW; 875BB9A373E141B4 CRC64;
MWYNFSEVEE VFELDKFIDK NNFKGMTLKA AIEYLNTHPE STELVERSLE VISDEEKRLN
AFITVKNEIE KGIPIGIKDN INVKGMKTTC ASKILEGYVA PYDATVIKKL RVCGYAFVGK
TNLDEFAMGA STEYSAFGPT RNPHDVERVA GGSSGGSAAA VASGEVIAAL GSDTGGSIRQ
PAAFCGVVGF KPTYGLVSRY GLVAFASSLD QIGPITKTVE DSAILMNIIA GKDENDATTV
DRNIDFTQFV GKQIPKMKIA VAKQSFGEGV EEGIKNRVNE FVQELSRHGH DVDVVDIDEI
KYSVATYYII APSEVSSNLS RFDGVKYGLR ISSDSLREMY EKTRGLGFGE EVRRRILIGT
FNLSAAYYDA YFEKAQKVRR VIANKLYSVF EKYDFIVTPT SPVVAFKVKS VNDPLVYYMM
DIFTIPANLA GIPAISIPYG KSENLPVGIQ IMGPRFSDAK LLGFADWVER NLGKS
//
