GATA_THET8
ID GATA_THET8 Reviewed; 471 AA.
AC Q9LCX3; Q5SKS0;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 25-MAY-2022, entry version 108.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A {ECO:0000255|HAMAP-Rule:MF_00120};
DE Short=Glu-ADT subunit A {ECO:0000255|HAMAP-Rule:MF_00120};
DE EC=6.3.5.7 {ECO:0000255|HAMAP-Rule:MF_00120};
GN Name=gatA {ECO:0000255|HAMAP-Rule:MF_00120}; OrderedLocusNames=TTHA0573;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10913601; DOI=10.1016/s0014-5793(00)01697-5;
RA Becker H.D., Min B., Jacobi C., Raczniak G., Pelaschier J., Roy H.,
RA Klein S., Kern D., Soell D.;
RT "The heterotrimeric Thermus thermophilus Asp-tRNA(Asn) amidotransferase can
RT also generate Gln-tRNA(Gln).";
RL FEBS Lett. 476:140-144(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) 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). Also acts on Asp-tRNA(Asn).
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:0000255|HAMAP-Rule:MF_00120};
CC -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000255|HAMAP-
CC Rule:MF_00120}.
CC -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00120}.
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DR EMBL; AF202447; AAF91176.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD70396.1; -; Genomic_DNA.
DR RefSeq; WP_011228034.1; NC_006461.1.
DR RefSeq; YP_143839.1; NC_006461.1.
DR PDB; 3KFU; X-ray; 3.00 A; E/H=1-471.
DR PDBsum; 3KFU; -.
DR AlphaFoldDB; Q9LCX3; -.
DR SMR; Q9LCX3; -.
DR STRING; 300852.55771955; -.
DR EnsemblBacteria; BAD70396; BAD70396; BAD70396.
DR GeneID; 3168250; -.
DR KEGG; ttj:TTHA0573; -.
DR PATRIC; fig|300852.9.peg.572; -.
DR eggNOG; COG0154; Bacteria.
DR HOGENOM; CLU_009600_0_3_0; -.
DR OMA; EVSCPHF; -.
DR PhylomeDB; Q9LCX3; -.
DR EvolutionaryTrace; Q9LCX3; -.
DR Proteomes; UP000000532; 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:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.1300.10; -; 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 PANTHER; PTHR11895; PTHR11895; 1.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; SSF75304; 1.
DR TIGRFAMs; TIGR00132; gatA; 1.
DR PROSITE; PS00571; AMIDASES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..471
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT /id="PRO_0000105222"
FT ACT_SITE 66
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT ACT_SITE 141
FT /note="Charge relay system"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT ACT_SITE 165
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00120"
FT CONFLICT 217
FT /note="A -> V (in Ref. 1; AAF91176)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="V -> G (in Ref. 1; AAF91176)"
FT /evidence="ECO:0000305"
FT HELIX 3..11
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 17..35
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:3KFU"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:3KFU"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:3KFU"
FT TURN 82..85
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 93..99
FT /evidence="ECO:0007829|PDB:3KFU"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 143..150
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 155..164
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 167..172
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:3KFU"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 199..206
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 207..217
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:3KFU"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 259..273
FT /evidence="ECO:0007829|PDB:3KFU"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 290..305
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:3KFU"
FT TURN 311..314
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 324..331
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 336..349
FT /evidence="ECO:0007829|PDB:3KFU"
FT TURN 351..357
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 358..375
FT /evidence="ECO:0007829|PDB:3KFU"
FT TURN 376..378
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 380..386
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:3KFU"
FT TURN 394..397
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 400..404
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:3KFU"
FT TURN 408..410
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 411..416
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 420..428
FT /evidence="ECO:0007829|PDB:3KFU"
FT STRAND 431..438
FT /evidence="ECO:0007829|PDB:3KFU"
FT HELIX 444..457
FT /evidence="ECO:0007829|PDB:3KFU"
SQ SEQUENCE 471 AA; 50228 MW; 1D317E1EC961703E CRC64;
MLAHEIRARV ARGEVSPLEV AQAYLKRVQE LDPGLGAFLS LNERLLEEAE AVDPGLPLAG
LVVAVKDNIA TRGLRTTAGS RLLENFVPPY EATAVARLKA LGALVLGKTN LDEFGMGSST
EHSAFFPTKN PFDPDRVPGG SSGGSAAALA ADLAPLALGS DTGGSVRQPA AFCGVYGLKP
TYGRVSRFGL IAYASSLDQI GPMARSVRDL ALLMDAAAGP DPLDATSLDL PPRFQEALEG
PLPPLRLGVV REALAGNSPG VERALEEALK VFRELGLSVR EVSWPSLPQA LAAYYILAPA
EASSNLARYD GTLYGRRAAG EEVEGMMEAT RALFGLEVKR RVLVGTFVLS SGYYEAYYGR
AQAFRRRLKA EAQALFREVD LLLLPTTPHP AFPFGARRDP LAMYREDLYT VGANLTGLPA
LSFPAGFEGH LPVGLQLLAP WGEDERLLRA ALAFEEATAR AHLKAPLGEA L
