ID A0LSX2_ACIC1 Unreviewed; 393 AA. AC A0LSX2; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 02-SEP-2026, entry version 116. DE RecName: Full=Glutamate 5-kinase {ECO:0000256|HAMAP-Rule:MF_00456}; DE EC=2.7.2.11 {ECO:0000256|HAMAP-Rule:MF_00456}; DE AltName: Full=Gamma-glutamyl kinase {ECO:0000256|HAMAP-Rule:MF_00456}; DE Short=GK {ECO:0000256|HAMAP-Rule:MF_00456}; GN Name=proB {ECO:0000256|HAMAP-Rule:MF_00456}; GN OrderedLocusNames=Acel_0759 {ECO:0000313|EMBL:ABK52532.1}; OS Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Acidothermales; OC Acidothermaceae; Acidothermus. OX NCBI_TaxID=351607 {ECO:0000313|EMBL:ABK52532.1, ECO:0000313|Proteomes:UP000008221}; RN [1] {ECO:0000313|EMBL:ABK52532.1, ECO:0000313|Proteomes:UP000008221} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43068 / DSM 8971 / 11B RC {ECO:0000313|Proteomes:UP000008221}; RX PubMed=19270083; DOI=10.1101/gr.084848.108; RA Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V., RA Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C., RA Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.; RT "Complete genome of the cellulolytic thermophile Acidothermus RT cellulolyticus 11B provides insights into its ecophysiological and RT evolutionary adaptations."; RL Genome Res. 19:1033-1043(2009). CC -!- FUNCTION: Catalyzes the transfer of a phosphate group to glutamate to CC form L-glutamate 5-phosphate. {ECO:0000256|HAMAP-Rule:MF_00456}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-glutamate + ATP = L-glutamyl 5-phosphate + ADP; 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:0000256|HAMAP-Rule:MF_00456}; CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate CC 5-semialdehyde from L-glutamate: step 1/2. {ECO:0000256|HAMAP- CC Rule:MF_00456}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00456}. CC -!- SIMILARITY: Belongs to the glutamate 5-kinase family. CC {ECO:0000256|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; CP000481; ABK52532.1; -; Genomic_DNA. DR RefSeq; WP_011719595.1; NC_008578.1. DR AlphaFoldDB; A0LSX2; -. DR FunCoup; A0LSX2; 113. DR STRING; 351607.Acel_0759; -. DR KEGG; ace:Acel_0759; -. DR eggNOG; COG0263; Bacteria. DR HOGENOM; CLU_025400_2_0_11; -. DR InParanoid; A0LSX2; -. DR UniPathway; UPA00098; UER00359. DR Proteomes; UP000008221; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. 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-UniRule. DR CDD; cd04242; AAK_G5K_ProB; 1. DR CDD; cd21157; PUA_G5K; 1. DR FunFam; 3.40.1160.10:FF:000006; Glutamate 5-kinase; 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 {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_00456}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00456}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00456}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00456}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00456}; KW Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650, ECO:0000256|HAMAP- KW Rule:MF_00456}; Reference proteome {ECO:0000313|Proteomes:UP000008221}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00456}. FT DOMAIN 297..380 FT /note="PUA" FT /evidence="ECO:0000259|SMART:SM00359" FT BINDING 17 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456" FT BINDING 74 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456" FT BINDING 161 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456" FT BINDING 173 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456" FT BINDING 193..194 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456" FT BINDING 234..240 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456" SQ SEQUENCE 393 AA; 41332 MW; 8A69C4310B0B95F4 CRC64; MSGTRPEVTA AQTIVVKIGS SSVTSYPAAR AGSAAADDQP GGSASGLREE NIAALAAAVA ERVSRGAHCV IVSSGAIAAG LGPLGLVSRP RDLATQQAAA SVGQSLLVRA YARAFAVHRI TVGQILLTSD DMIRRAHYRN AERTLRRLFE LGVVPIVNEN DTVVTDEIRF GDNDRLAALV AHLIRADLLV LLSDVDALYT APPNRPGARR IEVVSSERDL DAIDLGGVGT AVGTGGMITK IEAARLATSA GIPVVLTAAT AVAAALRGDD VGTFFRPTGR RMSSRLLWLA HATAPRGRLV LDAGAVAAVV DRRLSLLPAG VVGVHGDFNA GDPVDLVDEH GRRVARGLVN YDAADLPNLI GRSTWELAQQ FGPDYQREVV HRDDLVVLVR RSR //