ID PROB_BURTA Reviewed; 372 AA. AC Q2SZF9; DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 27-MAR-2024, entry version 104. 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=BTH_I1143; OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 / OS CIP 106301 / E264). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=271848; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700388 / DSM 13276 / CCUG 48851 / CIP 106301 / E264; RX PubMed=16336651; DOI=10.1186/1471-2164-6-174; RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., RA DeShazer D.; RT "Bacterial genome adaptation to niches: divergence of the potential RT virulence genes in three Burkholderia species of different survival RT strategies."; RL BMC Genomics 6:174-174(2005). 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; CP000086; ABC38938.1; -; Genomic_DNA. DR RefSeq; WP_009888926.1; NZ_CP008785.1. DR PDB; 4Q1T; X-ray; 2.15 A; A/B/C/D=1-372. DR PDBsum; 4Q1T; -. DR AlphaFoldDB; Q2SZF9; -. DR SMR; Q2SZF9; -. DR GeneID; 66548400; -. DR KEGG; bte:BTH_I1143; -. DR HOGENOM; CLU_025400_2_0_4; -. DR UniPathway; UPA00098; UER00359. DR Proteomes; UP000001930; Chromosome I. 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 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; ATP-binding; Cytoplasm; Kinase; KW Nucleotide-binding; Proline biosynthesis; Transferase. FT CHAIN 1..372 FT /note="Glutamate 5-kinase" FT /id="PRO_0000252973" FT DOMAIN 280..358 FT /note="PUA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 14 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 54 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 141 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 153 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 173..174 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT HELIX 4..7 FT /evidence="ECO:0007829|PDB:4Q1T" FT STRAND 9..15 FT /evidence="ECO:0007829|PDB:4Q1T" FT HELIX 17..20 FT /evidence="ECO:0007829|PDB:4Q1T" FT HELIX 29..44 FT /evidence="ECO:0007829|PDB:4Q1T" FT STRAND 48..53 FT /evidence="ECO:0007829|PDB:4Q1T" FT HELIX 56..64 FT /evidence="ECO:0007829|PDB:4Q1T" FT HELIX 73..96 FT /evidence="ECO:0007829|PDB:4Q1T" FT TURN 97..99 FT /evidence="ECO:0007829|PDB:4Q1T" FT STRAND 102..107 FT /evidence="ECO:0007829|PDB:4Q1T" FT HELIX 109..113 FT /evidence="ECO:0007829|PDB:4Q1T" FT HELIX 115..130 FT /evidence="ECO:0007829|PDB:4Q1T" FT STRAND 134..139 FT /evidence="ECO:0007829|PDB:4Q1T" FT TURN 141..143 FT /evidence="ECO:0007829|PDB:4Q1T" FT TURN 146..148 FT /evidence="ECO:0007829|PDB:4Q1T" FT HELIX 154..164 FT /evidence="ECO:0007829|PDB:4Q1T" FT STRAND 167..175 FT /evidence="ECO:0007829|PDB:4Q1T" FT STRAND 193..196 FT /evidence="ECO:0007829|PDB:4Q1T" FT HELIX 219..229 FT /evidence="ECO:0007829|PDB:4Q1T" FT TURN 230..232 FT /evidence="ECO:0007829|PDB:4Q1T" FT STRAND 234..239 FT /evidence="ECO:0007829|PDB:4Q1T" FT HELIX 245..250 FT /evidence="ECO:0007829|PDB:4Q1T" FT STRAND 256..260 FT /evidence="ECO:0007829|PDB:4Q1T" FT HELIX 265..276 FT /evidence="ECO:0007829|PDB:4Q1T" FT STRAND 277..285 FT /evidence="ECO:0007829|PDB:4Q1T" FT HELIX 287..294 FT /evidence="ECO:0007829|PDB:4Q1T" FT HELIX 302..304 FT /evidence="ECO:0007829|PDB:4Q1T" FT STRAND 305..310 FT /evidence="ECO:0007829|PDB:4Q1T" FT STRAND 317..321 FT /evidence="ECO:0007829|PDB:4Q1T" FT STRAND 327..332 FT /evidence="ECO:0007829|PDB:4Q1T" FT HELIX 337..343 FT /evidence="ECO:0007829|PDB:4Q1T" FT HELIX 348..350 FT /evidence="ECO:0007829|PDB:4Q1T" FT HELIX 351..355 FT /evidence="ECO:0007829|PDB:4Q1T" FT HELIX 366..368 FT /evidence="ECO:0007829|PDB:4Q1T" FT STRAND 369..371 FT /evidence="ECO:0007829|PDB:4Q1T" SQ SEQUENCE 372 AA; 39330 MW; 777EE3DFCF77C4A6 CRC64; MRSIIADSKR LVVKVGSSLV TNDGRGLDHD AIGRWAAQIA ALRNEGKEVV LVSSGAIAEG MQRLGWSRRP REIDELQAAA AVGQMGLAQV YESRFAEHGI RTAQILLTHA DLADRERYLN ARSTLLTLLR LGVVPIINEN DTVVTDEIKF GDNDTLGALV ANLIEGDALI ILTDQQGLFT ADPRKDPGAT LVAEASAGAP ELEAMAGGAG SSIGRGGMLT KILAAKRAAH SGANTVIASG RERDVLLRLA SGEAIGTQLI ARTARMAARK QWMADHLQVR GHVVIDAGAV DKLTAGGKSL LPIGVVAVQG VFARGEVIAC VNDAGREVAR GITNYSSAEA KLIQRKPSGE IEAVLGYMLE PELIHRDNLV LV //