ID PROB_LISMO Reviewed; 276 AA. AC Q93Q56; DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 121. 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=lmo1260; OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e). OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria. OX NCBI_TaxID=169963; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=11375165; DOI=10.1128/aem.67.6.2571-2577.2001; RA Sleator R.D., Gahan C.G.M., Hill C.; RT "Identification and disruption of the proBA Locus in Listeria RT monocytogenes: role of proline biosynthesis in salt tolerance and murine RT infection."; RL Appl. Environ. Microbiol. 67:2571-2577(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-679 / EGD-e; RX PubMed=11679669; DOI=10.1126/science.1063447; RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D., RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.; RT "Comparative genomics of Listeria species."; RL Science 294:849-852(2001). 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; AF282880; AAK62254.1; -; Genomic_DNA. DR EMBL; AL591978; CAC99338.1; -; Genomic_DNA. DR PIR; AD1232; AD1232. DR RefSeq; NP_464785.1; NC_003210.1. DR RefSeq; WP_003723561.1; NZ_CP023861.1. DR AlphaFoldDB; Q93Q56; -. DR SMR; Q93Q56; -. DR STRING; 169963.gene:17593917; -. DR PaxDb; 169963-lmo1260; -. DR EnsemblBacteria; CAC99338; CAC99338; CAC99338. DR GeneID; 985996; -. DR KEGG; lmo:lmo1260; -. DR PATRIC; fig|169963.11.peg.1295; -. DR eggNOG; COG0263; Bacteria. DR HOGENOM; CLU_025400_0_2_9; -. DR OrthoDB; 9804434at2; -. DR PhylomeDB; Q93Q56; -. DR BioCyc; LMON169963:LMO1260-MONOMER; -. DR UniPathway; UPA00098; UER00359. DR Proteomes; UP000000817; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004349; F:glutamate 5-kinase activity; IBA:GO_Central. DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0006561; P:proline biosynthetic process; IBA:GO_Central. DR CDD; cd04242; AAK_G5K_ProB; 1. DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 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 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 PIRSF; PIRSF000729; GK; 1. DR PRINTS; PR00474; GLU5KINASE. DR SUPFAM; SSF53633; Carbamate kinase-like; 1. DR PROSITE; PS00902; GLUTAMATE_5_KINASE; 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..276 FT /note="Glutamate 5-kinase" FT /id="PRO_0000109689" 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 157 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 177..178 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 219..225 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" SQ SEQUENCE 276 AA; 30034 MW; F9A94811AFC5AD06 CRC64; MRESLKNSKR LVIKVGTSTL MYGNGHINLR TIEKLAMVLS DLRNEGKEVI LVSSGAIGVG CHKLQLPVRP TSIPEQQAVA SVGQSELMHI YSKFFGEYGQ VVGQVLLTRD VTDFPISREN VMNTLESLLE RGIIPIVNEN DTVAVEELEH VTKYGDNDLL SAIVAKLVQA DLLIMLSDID GFYGSNPSTD PDAVMFSEIN QITPEIEALA GGKGSKFGTG GMLTKLSAAS YCMNANQKMI LTNGKNPTII FDIMQGEQIG TLFASKKEEF SHDGTH //