ID PROB_THET2 Reviewed; 370 AA. AC Q60050; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2004, sequence version 2. DT 27-MAR-2024, entry version 125. 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=TT_C1563; OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27). OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus. OX NCBI_TaxID=262724; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7988899; DOI=10.1111/j.1574-6968.1994.tb07201.x; RA Kosuge T., Tabata K., Hoshino T.; RT "Molecular cloning and sequence analysis of the proBA operon from an RT extremely thermophilic eubacterium Thermus thermophilus."; RL FEMS Microbiol. Lett. 123:55-61(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27; RX PubMed=15064768; DOI=10.1038/nbt956; RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H., RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C., RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P., RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.; RT "The genome sequence of the extreme thermophile Thermus thermophilus."; RL Nat. Biotechnol. 22:547-553(2004). 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; D29973; BAA06237.1; -; Genomic_DNA. DR EMBL; AE017221; AAS81905.1; -; Genomic_DNA. DR RefSeq; WP_008633899.1; NZ_CP133179.1. DR AlphaFoldDB; Q60050; -. DR SMR; Q60050; -. DR GeneID; 3169812; -. DR KEGG; tth:TT_C1563; -. DR eggNOG; COG0263; Bacteria. DR HOGENOM; CLU_025400_2_0_0; -. DR OrthoDB; 9804434at2; -. DR UniPathway; UPA00098; UER00359. DR Proteomes; UP000000592; 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..370 FT /note="Glutamate 5-kinase" FT /id="PRO_0000109747" FT DOMAIN 275..353 FT /note="PUA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 13 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 52 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 139 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 151 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 171..172 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 211..217 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT CONFLICT 1..32 FT /note="MRPGLSAKRLVVKVGSAVLTGERGLDLEAMAE -> MEFFGLPLRVEEGVLI FT PRPETEGLVELALGLPLPPAPR (in Ref. 1)" FT /evidence="ECO:0000305" SQ SEQUENCE 370 AA; 39890 MW; 8B67CD67D2A057BB CRC64; MRPGLSAKRL VVKVGSAVLT GERGLDLEAM AEIARQVAAL REEGREVVLV SSGAVAAGMR RLGLKERPKD MPKKQALAAL GQPLLMAFWQ EAFAPFGLPV AQVLLTAEDL SSRSRYLNAK ATLRALLDLG AIPVINENDT VAFEEIRFGD NDQLSARVAA LVEAGLLALL SDVDALYEED PKKNPQARPI PEVESVEAVL AHAGEENPLG SGGMKSKLLA ARIAGRVGIP TLLLPGKRPG VLLQALSGAP LGTYFHARRR YRGEKAWLFG LLRPKGELVL DRGAVRALKE RGASLLPAGV KEVRGRFSRG EAVRLLSEEG EEVGVGLANY ASEEIARIKG RRSAEIEAVL GYRYTEEVVH RDHLALKEEA //