ID RIMK_PSEPK Reviewed; 301 AA. AC Q88R85; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 111. DE RecName: Full=Probable alpha-L-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_01552}; DE EC=6.3.2.- {ECO:0000255|HAMAP-Rule:MF_01552}; GN Name=rimK {ECO:0000255|HAMAP-Rule:MF_01552}; GN OrderedLocusNames=PP_0248; OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 OS / KT2440). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=160488; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440; RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x; RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H., RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M., RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F., RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I., RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A., RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H., RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C., RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.; RT "Complete genome sequence and comparative analysis of the metabolically RT versatile Pseudomonas putida KT2440."; RL Environ. Microbiol. 4:799-808(2002). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01552}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01552}; CC Note=Binds 2 magnesium or manganese ions per subunit. CC {ECO:0000255|HAMAP-Rule:MF_01552}; CC -!- SIMILARITY: Belongs to the RimK family. {ECO:0000255|HAMAP- CC Rule:MF_01552}. 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; AE015451; AAN65880.1; -; Genomic_DNA. DR RefSeq; NP_742416.1; NC_002947.4. DR RefSeq; WP_003255817.1; NC_002947.4. DR AlphaFoldDB; Q88R85; -. DR SMR; Q88R85; -. DR STRING; 160488.PP_0248; -. DR PaxDb; 160488-PP_0248; -. DR DNASU; 1043821; -. DR GeneID; 83677509; -. DR KEGG; ppu:PP_0248; -. DR PATRIC; fig|160488.4.peg.265; -. DR eggNOG; COG0189; Bacteria. DR HOGENOM; CLU_054353_0_1_6; -. DR OrthoDB; 3865600at2; -. DR PhylomeDB; Q88R85; -. DR BioCyc; PPUT160488:G1G01-270-MONOMER; -. DR Proteomes; UP000000556; Chromosome. DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0036211; P:protein modification process; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.20; -; 1. DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1. DR HAMAP; MF_01552; RimK; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013651; ATP-grasp_RimK-type. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR023533; RimK. DR InterPro; IPR041107; Rimk_N. DR InterPro; IPR004666; Rp_bS6_RimK/Lys_biosynth_LsyX. DR NCBIfam; TIGR00768; rimK_fam; 1. DR PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1. DR PANTHER; PTHR21621:SF7; RIBOSOMAL PROTEIN S6--L-GLUTAMATE LIGASE; 1. DR Pfam; PF08443; RimK; 1. DR Pfam; PF18030; Rimk_N; 1. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1. DR PROSITE; PS50975; ATP_GRASP; 1. PE 3: Inferred from homology; KW ATP-binding; Ligase; Magnesium; Manganese; Metal-binding; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1..301 FT /note="Probable alpha-L-glutamate ligase" FT /id="PRO_0000205473" FT DOMAIN 104..287 FT /note="ATP-grasp" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01552" FT BINDING 141 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01552" FT BINDING 178..179 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01552" FT BINDING 187 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01552" FT BINDING 211..213 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01552" FT BINDING 248 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01552" FT BINDING 248 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01552" FT BINDING 260 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01552" FT BINDING 260 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01552" FT BINDING 260 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01552" FT BINDING 260 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01552" FT BINDING 262 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01552" FT BINDING 262 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01552" SQ SEQUENCE 301 AA; 32629 MW; 78894C76F30E69D7 CRC64; MKIAVLSRNP RLYSTRRLVE AGTQRGHEMV VIDTLRAYMN IASHKPQIHY RGKPLEGFDA VIPRIGASVT FYGCAVLRQF EMMGVYPLNE SVAIARSRDK LRSLQLLSRR GIGLPITGFA HSPDDIPDLI QMVNGAPLVI KVLEGTQGIG VVLCETPQAA ESVIEAFMGL KQNIMVQEYI KEAGGADIRC FVVGDKVIAS MKRQAKPGEF RSNLHRGGVA SLIKITPEER ITAIRAAKVM GLSVAGVDIL RSNHGPLVME VNSSPGLEGI EVTTGKNVAG MIIEHLEKNG GPNQTRTKGK G //