ID PROB_AFIC5 Reviewed; 397 AA. AC B6JD20; F8BTC0; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 16-DEC-2008, sequence version 1. DT 04-NOV-2026, entry version 92. 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=OCAR_4606, OCA5_c33380; OS Afipia carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5) OS (Oligotropha carboxidovorans). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Hyphomicrobiales; Nitrobacteraceae; Afipia. OX NCBI_TaxID=504832; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5; RX PubMed=18539730; DOI=10.1128/jb.00614-08; RA Paul D., Bridges S., Burgess S.C., Dandass Y., Lawrence M.L.; RT "Genome sequence of the chemolithoautotrophic bacterium Oligotropha RT carboxidovorans OM5T."; RL J. Bacteriol. 190:5531-5532(2008). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49405 / DSM 1227 / KCTC 32145 / OM5; RX PubMed=21742883; DOI=10.1128/jb.05619-11; RA Volland S., Rachinger M., Strittmatter A., Daniel R., Gottschalk G., RA Meyer O.; RT "Complete genome sequences of the chemolithoautotrophic Oligotropha RT carboxidovorans strains OM4 and OM5."; RL J. Bacteriol. 193:5043-5043(2011). 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=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: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; CP001196; ACI91750.1; -; Genomic_DNA. DR EMBL; CP002826; AEI08012.1; -; Genomic_DNA. DR RefSeq; WP_012561781.1; NC_011386.1. DR AlphaFoldDB; B6JD20; -. DR SMR; B6JD20; -. DR STRING; 504832.OCA5_c33380; -. DR KEGG; oca:OCAR_4606; -. DR KEGG; ocg:OCA5_c33380; -. DR PATRIC; fig|504832.7.peg.3509; -. DR eggNOG; COG0263; Bacteria. DR HOGENOM; CLU_025400_2_0_5; -. DR OMA; AACGQSH; -. DR OrthoDB; 9804434at2; -. DR UniPathway; UPA00098; UER00359. DR Proteomes; UP000007730; 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; 2.30.130.10:FF:000007; Glutamate 5-kinase; 1. DR FunFam; 3.40.1160.10:FF:000018; 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; ATP-binding; Cytoplasm; Kinase; KW Nucleotide-binding; Proline biosynthesis; Reference proteome; Transferase. FT CHAIN 1..397 FT /note="Glutamate 5-kinase" FT /id="PRO_1000206274" FT DOMAIN 283..360 FT /note="PUA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT REGION 374..397 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 17 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 58 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 145 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" SQ SEQUENCE 397 AA; 41633 MW; 278CF21B013A949E CRC64; MSHSDLRLTD FRRIVIKVGS SLLIDSAAGK VKSAWLAALA DDIAALHRAG KDVLVVSSGS IALGRSRLKL PSGTLKLEES QAAAAVGQIA LARIWAKVLD HHGIGAGQIL VTLRDTEERR RYLNARSTIS KLLEWRAVPV INENDTVATS EIRYGDNDRL AARVATMTSS DLLILLSDID GLYTAPPGIN PNAKLIPVVE SVTADIEAMA GAAGSELSRG GMRTKIEAAK IATSAGTHML IASGKIDHPL QAIIDGGPCT WFLTPANPVT ARKRWIAGSL EPKGVLVIDA GAVKALDAGR SLLAAGVTRI EGTFARGDAV VVRGPDGHEI GRGLVAYSAD NAERIKGKSS AAASKILGLT GRPEMIHRDD LVVSHHHDNG HNNGSHGVST PAPEPSA //