ID PROB_GEOSL Reviewed; 373 AA. AC Q747Q3; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 105. 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=GSU3212; OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA). OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=243231; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51573 / DSM 12127 / PCA; RX PubMed=14671304; DOI=10.1126/science.1088727; RA Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C., RA Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J., RA Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., RA Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J., RA Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A., RA Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E., RA Lovley D.R., Fraser C.M.; RT "Genome of Geobacter sulfurreducens: metal reduction in subsurface RT environments."; RL Science 302:1967-1969(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; AE017180; AAR36603.1; -; Genomic_DNA. DR RefSeq; NP_954253.1; NC_002939.5. DR RefSeq; WP_010943830.1; NC_002939.5. DR AlphaFoldDB; Q747Q3; -. DR SMR; Q747Q3; -. DR STRING; 243231.GSU3212; -. DR EnsemblBacteria; AAR36603; AAR36603; GSU3212. DR KEGG; gsu:GSU3212; -. DR PATRIC; fig|243231.5.peg.3236; -. DR eggNOG; COG0263; Bacteria. DR HOGENOM; CLU_025400_2_0_7; -. DR InParanoid; Q747Q3; -. DR OrthoDB; 9804434at2; -. DR UniPathway; UPA00098; UER00359. DR Proteomes; UP000000577; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004349; F:glutamate 5-kinase activity; IBA:GO_Central. 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 GO; GO:0006561; P:proline biosynthetic process; IBA:GO_Central. 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..373 FT /note="Glutamate 5-kinase" FT /id="PRO_0000109675" FT DOMAIN 281..359 FT /note="PUA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 15 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 55 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 142 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 154 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 174..175 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 216..222 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" SQ SEQUENCE 373 AA; 39997 MW; 8A8F25CD783F1BCD CRC64; MRSGILSKVK RIVIKIGSGV LTCGDNGLNK PLMGSIAAQV AELRASGRQV IIVSSGAVAA GRKELGIDGR PRSIPQKQAA AAIGQSRLMH AYEEAFEPFG HKVAQILLTR DDLAHRGRFL NARATLDTLL SFGVIPIINE NDTVVFDEIK FGDNDSLSAL VTNLAEANLL VILTDIDGFY EANPRTNPDA RLIPLVRQIT REMERAAGGS GSTVGTGGMV TKLAAAKKAG QFGVPTLMLN GRNPSLLAEA FAGREVGTLF LPGKESLNRR KHWIAHTLRP SGKIIVDDGA RTVLARQGKS LLPSGVVRVE GKFDRGACVR VCGTDGTEIA RGLVDYSHDE ITRILGHRSG EIEAILGYKY GDEIIHRDNL VVL //