ID PROB_XANAC Reviewed; 363 AA. AC Q8PK34; DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 27-MAR-2024, entry version 113. 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=XAC2343; OS Xanthomonas axonopodis pv. citri (strain 306). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=190486; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=306; RX PubMed=12024217; DOI=10.1038/417459a; RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B., RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.; RT "Comparison of the genomes of two Xanthomonas pathogens with differing host RT specificities."; RL Nature 417:459-463(2002). 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; AE008923; AAM37195.1; -; Genomic_DNA. DR AlphaFoldDB; Q8PK34; -. DR SMR; Q8PK34; -. DR KEGG; xac:XAC2343; -. DR eggNOG; COG0263; Bacteria. DR HOGENOM; CLU_025400_2_0_6; -. DR UniPathway; UPA00098; UER00359. DR Proteomes; UP000000576; 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; Transferase. FT CHAIN 1..363 FT /note="Glutamate 5-kinase" FT /id="PRO_0000109757" FT DOMAIN 267..349 FT /note="PUA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 3 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 43 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 128 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 140 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 160..161 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 202..208 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" SQ SEQUENCE 363 AA; 38134 MW; 733E98E7D6A73238 CRC64; MLKVGSSLLA ADGGGLSPRF ALGLAQFVSA NLAAGRELVI VSSGAVAAGR AILPKAMDVG APIAARQALA ALGQAQLIAL WQRFFERPVA QVLLTHDDLR NRRRYLNARA TLGELLRLGA LPVINENDTV SVDELKLGDN DNLAAIVAAL VDADALFIAT DIDGLYSADP RSNPLARPLD DVPELTPEVL AMAGGSGSNV GTGGMRTKLE AAAKAGAAGI ETYLFNGRSG EVVRALALDR LRGTRIHAAR TRIAARKYWL RHAPVEAGAI LIDDGAAAAL TGKGASLLPG GVAGAQGDFR RGDMVEIRRR DTTGDGQCLA RGVSQYSALD IRRIAGRHSR EIENVLGYSY GENVVHRDDL VVL //