ID PROB_PSESM Reviewed; 372 AA. AC Q889F0; DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 116. DE RecName: Full=Glutamate 5-kinase {ECO:0000255|HAMAP-Rule:MF_00456}; DE EC=2.7.2.11 {ECO:0000255|HAMAP-Rule:MF_00456}; DE AltName: Full=Gamma-glutamyl kinase {ECO:0000255|HAMAP-Rule:MF_00456}; DE Short=GK {ECO:0000255|HAMAP-Rule:MF_00456}; GN Name=proB {ECO:0000255|HAMAP-Rule:MF_00456}; GN OrderedLocusNames=PSPTO_0800; OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=223283; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-871 / DC3000; RX PubMed=12928499; DOI=10.1073/pnas.1731982100; RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T., RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C., RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M., RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R., RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R., RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G., RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M., RA Collmer A.; RT "The complete genome sequence of the Arabidopsis and tomato pathogen RT Pseudomonas syringae pv. tomato DC3000."; RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003). CC -!- FUNCTION: Catalyzes the transfer of a phosphate group to glutamate to CC form L-glutamate 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00456}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-glutamate = ADP + L-glutamyl 5-phosphate; CC Xref=Rhea:RHEA:14877, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:58274, ChEBI:CHEBI:456216; EC=2.7.2.11; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00456}; CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate CC 5-semialdehyde from L-glutamate: step 1/2. {ECO:0000255|HAMAP- CC Rule:MF_00456}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00456}. CC -!- SIMILARITY: Belongs to the glutamate 5-kinase family. CC {ECO:0000255|HAMAP-Rule:MF_00456}. 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; AE016853; AAO54342.1; -; Genomic_DNA. DR RefSeq; NP_790647.1; NC_004578.1. DR RefSeq; WP_003381304.1; NC_004578.1. DR AlphaFoldDB; Q889F0; -. DR SMR; Q889F0; -. DR STRING; 223283.PSPTO_0800; -. DR GeneID; 1182425; -. DR KEGG; pst:PSPTO_0800; -. DR PATRIC; fig|223283.9.peg.814; -. DR eggNOG; COG0263; Bacteria. DR HOGENOM; CLU_025400_2_0_6; -. DR OrthoDB; 9804434at2; -. DR PhylomeDB; Q889F0; -. DR UniPathway; UPA00098; UER00359. DR Proteomes; UP000002515; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004349; F:glutamate 5-kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd04242; AAK_G5K_ProB; 1. DR CDD; cd21157; PUA_G5K; 1. DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 2. DR Gene3D; 2.30.130.10; PUA domain; 1. DR HAMAP; MF_00456; ProB; 1. DR InterPro; IPR036393; AceGlu_kinase-like_sf. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR041739; G5K_ProB. DR InterPro; IPR001057; Glu/AcGlu_kinase. DR InterPro; IPR011529; Glu_5kinase. DR InterPro; IPR005715; Glu_5kinase/COase_Synthase. DR InterPro; IPR019797; Glutamate_5-kinase_CS. DR InterPro; IPR002478; PUA. DR InterPro; IPR015947; PUA-like_sf. DR InterPro; IPR036974; PUA_sf. DR NCBIfam; TIGR01027; proB; 1. DR PANTHER; PTHR43654; GLUTAMATE 5-KINASE; 1. DR PANTHER; PTHR43654:SF1; ISOPENTENYL PHOSPHATE KINASE; 1. DR Pfam; PF00696; AA_kinase; 1. DR Pfam; PF01472; PUA; 1. DR PIRSF; PIRSF000729; GK; 1. DR PRINTS; PR00474; GLU5KINASE. DR SMART; SM00359; PUA; 1. DR SUPFAM; SSF53633; Carbamate kinase-like; 1. DR SUPFAM; SSF88697; PUA domain-like; 1. DR PROSITE; PS00902; GLUTAMATE_5_KINASE; 1. DR PROSITE; PS50890; PUA; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; ATP-binding; Cytoplasm; Kinase; KW Nucleotide-binding; Proline biosynthesis; Reference proteome; Transferase. FT CHAIN 1..372 FT /note="Glutamate 5-kinase" FT /id="PRO_0000109711" FT DOMAIN 280..358 FT /note="PUA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 14 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 54 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 141 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 153 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 173..174 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" SQ SEQUENCE 372 AA; 39770 MW; 04F40B40451CDADE CRC64; MRSKVTGAQR WVVKIGSALL TADGKGLDRN AMGVWVEQMV ALHEAGVELV LVSSGAVAAG MSRLGWTARP SAMHELQAAA AIGQMGLVQA WESSFAEHGR HTAQILLTHD DLSDRKRYLN ARSTLRTLVE LGVVPVINEN DTVVTDEIRF GDNDTLAALV ANLVEADLLV ILTDRDGMFD ADPRNNPDAQ LIYEARADDP ALDAVAGGTG GALGRGGMQT KLRAARLAAR SGAHTVIVGG RIERVLARLK GGERLGTLLS PEREMLAARK QWLAGHLQTR GTLVLDDGAV SALASDHKSL LPVGVKLVQG SFRRGEMVVC VAPDGREIAR GLSNYSAIEA QKIIGHSSEA IVRELGYMAE PELIHRDNLI LV //