GATA_THEMA
ID GATA_THEMA Reviewed; 475 AA.
AC Q9X0Z9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 123.
DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A;
DE Short=Glu-ADT subunit A;
DE EC=6.3.5.7;
GN Name=gatA; OrderedLocusNames=TM_1272;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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) (By similarity). {ECO:0000250}.
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 -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the amidase family. GatA subfamily.
CC {ECO:0000305}.
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DR EMBL; AE000512; AAD36347.1; -; Genomic_DNA.
DR PIR; G72274; G72274.
DR RefSeq; NP_229077.1; NC_000853.1.
DR PDB; 2GI3; X-ray; 1.80 A; A=1-475.
DR PDB; 3AL0; X-ray; 3.37 A; A=1-475.
DR PDBsum; 2GI3; -.
DR PDBsum; 3AL0; -.
DR AlphaFoldDB; Q9X0Z9; -.
DR SMR; Q9X0Z9; -.
DR DIP; DIP-59228N; -.
DR IntAct; Q9X0Z9; 3.
DR STRING; 243274.THEMA_07975; -.
DR EnsemblBacteria; AAD36347; AAD36347; TM_1272.
DR KEGG; tma:TM1272; -.
DR PATRIC; fig|243274.18.peg.1542; -.
DR eggNOG; COG0154; Bacteria.
DR InParanoid; Q9X0Z9; -.
DR OMA; EVSCPHF; -.
DR BRENDA; 6.3.5.7; 6331.
DR EvolutionaryTrace; Q9X0Z9; -.
DR Proteomes; UP000008183; 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..475
FT /note="Glutamyl-tRNA(Gln) amidotransferase subunit A"
FT /id="PRO_0000105221"
FT ACT_SITE 66
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 141
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 165
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:2GI3"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:2GI3"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:2GI3"
FT HELIX 25..40
FT /evidence="ECO:0007829|PDB:2GI3"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:2GI3"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:2GI3"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:2GI3"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:2GI3"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:2GI3"
FT HELIX 93..101
FT /evidence="ECO:0007829|PDB:2GI3"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:2GI3"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:2GI3"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:2GI3"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:2GI3"
FT HELIX 143..150
FT /evidence="ECO:0007829|PDB:2GI3"
FT STRAND 153..164
FT /evidence="ECO:0007829|PDB:2GI3"
FT HELIX 167..173
FT /evidence="ECO:0007829|PDB:2GI3"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:2GI3"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:2GI3"
FT STRAND 199..206
FT /evidence="ECO:0007829|PDB:2GI3"
FT HELIX 207..217
FT /evidence="ECO:0007829|PDB:2GI3"
FT TURN 236..239
FT /evidence="ECO:0007829|PDB:2GI3"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:2GI3"
FT HELIX 251..255
FT /evidence="ECO:0007829|PDB:2GI3"
FT HELIX 260..275
FT /evidence="ECO:0007829|PDB:2GI3"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:2GI3"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:2GI3"
FT HELIX 291..304
FT /evidence="ECO:0007829|PDB:2GI3"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:3AL0"
FT HELIX 324..335
FT /evidence="ECO:0007829|PDB:3AL0"
FT HELIX 336..380
FT /evidence="ECO:0007829|PDB:2GI3"
FT STRAND 381..388
FT /evidence="ECO:0007829|PDB:2GI3"
FT STRAND 390..392
FT /evidence="ECO:0007829|PDB:3AL0"
FT TURN 396..398
FT /evidence="ECO:0007829|PDB:2GI3"
FT HELIX 402..406
FT /evidence="ECO:0007829|PDB:2GI3"
FT TURN 407..412
FT /evidence="ECO:0007829|PDB:2GI3"
FT HELIX 413..418
FT /evidence="ECO:0007829|PDB:2GI3"
FT STRAND 422..430
FT /evidence="ECO:0007829|PDB:2GI3"
FT STRAND 433..440
FT /evidence="ECO:0007829|PDB:2GI3"
FT HELIX 446..459
FT /evidence="ECO:0007829|PDB:2GI3"
SQ SEQUENCE 475 AA; 52529 MW; 4F01EA3A2DCBD9A0 CRC64;
MIDLDFRKLT IEECLKLSEE EREKLPQLSL ETIKRLDPHV KAFISVRENV SVEKKGKFWG
IPVAIKDNIL TLGMRTTCAS RILENYESVF DATVVKKMKE AGFVVVGKAN LDEFAMGSST
ERSAFFPTRN PWDLERVPGG SSGGSAAAVS AGMVVAALGS DTGGSVRQPA SLCGVVGYKP
TYGLVSRYGL VAFASSLDQI GPITKTVRDA AILMEIISGR DENDATTVNR KVDFLSEIEE
GVSGMKFAVP EEIYEHDIEE GVSERFEEAL KLLERLGAKV ERVKIPHIKY SVATYYVIAP
AEASSNLARF DGVKYGLRIK EKGLREMYMK TRNVGFGEEV RRRIMIGTFT LSAAYYEAYF
NKAMKVRRKI SDELNEVLSQ YDAILTPTSP VTAFKIGEIK DPLTYYLMDI FTIPANLAGL
PAISVPFGFS NNLPVGVQVI GRRFADGKVF RIARAIEKNS PYNENGMFPL PEVKA
