ID PROB_XYLFT Reviewed; 384 AA. AC Q87EL0; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 108. 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=PD_0296; OS Xylella fastidiosa (strain Temecula1 / ATCC 700964). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xylella. OX NCBI_TaxID=183190; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Temecula1 / ATCC 700964; RX PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003; RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y., RA Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A., RA Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S., RA Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H., RA Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L., RA Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L., RA Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S., RA Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F., RA Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G., RA Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A., RA Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L., RA Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.; RT "Comparative analyses of the complete genome sequences of Pierce's disease RT and citrus variegated chlorosis strains of Xylella fastidiosa."; RL J. Bacteriol. 185:1018-1026(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; AE009442; AAO28181.1; -; Genomic_DNA. DR RefSeq; WP_011097579.1; NC_004556.1. DR AlphaFoldDB; Q87EL0; -. DR SMR; Q87EL0; -. DR GeneID; 58015851; -. DR KEGG; xft:PD_0296; -. DR HOGENOM; CLU_025400_2_0_6; -. DR UniPathway; UPA00098; UER00359. DR Proteomes; UP000002516; 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; 1. 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..384 FT /note="Glutamate 5-kinase" FT /id="PRO_0000109761" FT DOMAIN 288..370 FT /note="PUA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 24 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 64 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 149 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 161 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 181..182 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 223..229 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" SQ SEQUENCE 384 AA; 40872 MW; 03AE5E0240CA1304 CRC64; MTGIPPPSRF PEQPIPPWRR AVLKVGSSLL AADGGGLSPR FALDLAHFVS ANITAGRQLV IVSSGAVAAG RALIPPLPES GGALAARQAL AALGQAQLIA LWQRFFDRPV AQVLLTHDDL RNRRRYLNAR ATLRELLHLG TLPVVNENDT VSVDELKLGD NDNLAAIVAA LIDAQALFIA TDIDGLYTTD PRHHSDAQPL HEVRTLTPEN LAMAGDSSST VGTGGMRTKL EAALKAGAAG IDTYLFNGRS SDVVRGLAQH RLRGTRIHPT CTPIAARKYW LRHAPVEPGA ILIDAGAAAA LAQQGASLLP GGVLSAEGDF RRGDMIQIAT RSPDHPSHPL ARGLVQYSAA DVRRIAGCHS RDIQTLLGYT YGDTIVHRDD LVLL //