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 18-APR-2012, entry version 51. DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A; DE Short=Glu-ADT subunit A; DE EC=6.3.5.-; GN Name=gatA; OrderedLocusNames=PMM0946; OS Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4). OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae; OC Prochlorococcus. OX NCBI_TaxID=59919; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCMP1986 / MED4; 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: Allows the formation of correctly charged Gln-tRNA(Gln) CC through the transamidation of misacylated Glu-tRNA(Gln) in CC organisms which lack glutaminyl-tRNA synthetase. The reaction CC takes place in the presence of glutamine and ATP through an CC 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. GatA subfamily. 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; BX548174; CAE19405.1; -; Genomic_DNA. DR RefSeq; NP_893064.1; NC_005072.1. DR ProteinModelPortal; Q7V1D0; -. DR SMR; Q7V1D0; 4-480. DR STRING; Q7V1D0; -. DR GeneID; 1725620; -. DR GenomeReviews; BX548174_GR; PMM0946. DR KEGG; pmm:PMM0946; -. DR PATRIC; 23032814; VBIProMar68066_1071. DR eggNOG; COG0154; -. DR HOGENOM; HBG481888; -. DR KO; K02433; -. DR OMA; FDEETLF; -. DR ProtClustDB; PRK00012; -. DR BioCyc; PMAR167540:PMM0946-MONOMER; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016884; F:carbon-nitrogen ligase activity, with glutamine as amido-N-donor; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW. DR Gene3D; G3DSA:3.90.1300.10; Amidase_sig_enz; 1. DR HAMAP; MF_00120; GatA; 1; -. DR InterPro; IPR000120; Amidase. DR InterPro; IPR020556; Amidase_CS. DR InterPro; IPR023631; Amidase_dom. DR InterPro; IPR004412; GatA. DR PANTHER; PTHR11895; Amidase; 1. DR Pfam; PF01425; Amidase; 1. DR SUPFAM; SSF75304; Amidase_sig_enz; 1. DR TIGRFAMs; TIGR00132; GatA; 1. DR PROSITE; PS00571; AMIDASES; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding; KW 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 //