ID GATA_PROMP Reviewed; 484 AA. AC Q7V1D0; DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 05-FEB-2008, entry version 22. DE Glutamyl-tRNA(Gln) amidotransferase subunit A (EC 6.3.5.-) (Glu-ADT DE subunit A). GN Name=gatA; OrderedLocusNames=PMM0946; OS Prochlorococcus marinus subsp. pastoris (strain CCMP 1378 / MED4). OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=59919; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22825698; PubMed=12917642; DOI=10.1038/nature01947; RA Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., RA Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., RA Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., RA Shaw S.L., Steglich C., Sullivan M.B., Ting C.S., Tolonen A., RA Webb E.A., Zinser E.R., Chisholm S.W.; RT "Genome divergence in two Prochlorococcus ecotypes reflects oceanic RT niche differentiation."; RL Nature 424:1042-1047(2003). CC -!- FUNCTION: Furnishes a means for formation of correctly charged CC Gln-tRNA(Gln) through the transamidation of misacylated Glu- CC tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The CC reaction takes place in the presence of glutamine and ATP through CC an activated gamma-phospho-Glu-tRNA(Gln) (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP CC + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate. CC -!- SUBUNIT: Heterotrimer of A, B and C subunits (By similarity). CC -!- SIMILARITY: Belongs to the amidase family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX572092; CAE19405.1; -; Genomic_DNA. DR RefSeq; NP_893064.1; -. DR GeneID; 1725620; -. DR GenomeReviews; BX548174_GR; PMM0946. DR KEGG; pmm:PMM0946; -. DR BioCyc; PMAR167540:PMM0946-MON; -. DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydroly...; IEA:HAMAP. DR GO; GO:0006412; P:translation; IEA:HAMAP. DR HAMAP; MF_00120; -; 1. DR InterPro; IPR000120; Amidase_sig_enz. DR InterPro; IPR004412; GatA. DR Gene3D; G3DSA:3.90.1300.10; Amidase_sig_enz; 1. DR PANTHER; PTHR11895; Amidase; 1. DR Pfam; PF01425; Amidase; 1. DR TIGRFAMs; TIGR00132; gatA; 1. DR PROSITE; PS00571; AMIDASES; 1. PE 3: Inferred from homology; KW Complete proteome; Ligase; Protein biosynthesis. FT CHAIN 1 484 Glutamyl-tRNA(Gln) amidotransferase FT subunit A. FT /FTId=PRO_0000105188. FT ACT_SITE 74 74 Charge relay system (By similarity). FT ACT_SITE 149 149 Charge relay system (By similarity). FT ACT_SITE 173 173 Acyl-ester intermediate (By similarity). SQ SEQUENCE 484 AA; 52186 MW; 1A473E5882F6FE6F CRC64; MNFNSFRKEI YSGNASVKEL VNEFFLKIDS LNPKINAYTC LTKKIANSQS ENIDKLITNN QKLPSLAGIP IAIKDNICTK GVVTSCSSKM LKDFVSPYES SASGKLWSLG GICLGKTNLD EFAMGSSTET SVFGTTSNPW DVNRVPGGSS GGSAASVAAG LCLAAIGSDT GGSIRQPASF CGVVGLKPTY GRVSRWGLIA FASSLDQIGP ITNTVSDAAE ILYSISGKDN LDSTCLDKPV PNYLSDLDKS IKGIKIGIIE ECFDHPGLDP EVKESVLSSV ERFRSLGAEI HDIKCPRFND GIATYYVIAP CEASANLARY DGVKYGYRSE GESNLLEMIC KSRAEGFGDE VQRRILIGTY ALSAGYSDAY YKKAQRVRTL IRSDFDNAFN EVDVLLTPTC PTTAFLKGDF VNDPLSMYLS DLLTVPVNLA GLPAISIPCG FDKKGLPIGL QLIGNVLEEH RILNVANIFE KDAEVMNTKP NIEI //