ID PROB_CAMJE Reviewed; 251 AA. AC Q9PJ29; Q0PC40; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 128. 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}; OrderedLocusNames=Cj0097; OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / OS NCTC 11168). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Campylobacteraceae; Campylobacter. OX NCBI_TaxID=192222; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700819 / NCTC 11168; RX PubMed=10688204; DOI=10.1038/35001088; RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S., RA Barrell B.G.; RT "The genome sequence of the food-borne pathogen Campylobacter jejuni RT reveals hypervariable sequences."; RL Nature 403:665-668(2000). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH ADP. RA Gorman J., Shapiro L.; RT "Crystal structure of glutamate 5-kinase from Campylobacter jejuni."; RL Submitted (AUG-2005) to the PDB data bank. 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; AL111168; CAL34268.1; -; Genomic_DNA. DR PIR; A81426; A81426. DR RefSeq; WP_002851769.1; NZ_SZUC01000005.1. DR RefSeq; YP_002343557.1; NC_002163.1. DR PDB; 2AKO; X-ray; 2.20 A; A/B/C/D=1-251. DR PDBsum; 2AKO; -. DR AlphaFoldDB; Q9PJ29; -. DR SMR; Q9PJ29; -. DR IntAct; Q9PJ29; 9. DR STRING; 192222.Cj0097; -. DR PaxDb; 192222-Cj0097; -. DR EnsemblBacteria; CAL34268; CAL34268; Cj0097. DR GeneID; 904426; -. DR KEGG; cje:Cj0097; -. DR PATRIC; fig|192222.6.peg.95; -. DR eggNOG; COG0263; Bacteria. DR HOGENOM; CLU_025400_0_0_7; -. DR OrthoDB; 9804434at2; -. DR UniPathway; UPA00098; UER00359. DR EvolutionaryTrace; Q9PJ29; -. DR Proteomes; UP000000799; 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: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 Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 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 NCBIfam; TIGR01027; proB; 1. DR PANTHER; PTHR43654; GLUTAMATE 5-KINASE; 1. DR PANTHER; PTHR43654:SF3; GLUTAMATE 5-KINASE; 1. DR Pfam; PF00696; AA_kinase; 1. DR PIRSF; PIRSF000729; GK; 1. DR PRINTS; PR00474; GLU5KINASE. DR SUPFAM; SSF53633; Carbamate kinase-like; 1. DR PROSITE; PS00902; GLUTAMATE_5_KINASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; ATP-binding; Cytoplasm; Kinase; KW Nucleotide-binding; Proline biosynthesis; Reference proteome; Transferase. FT CHAIN 1..251 FT /note="Glutamate 5-kinase" FT /id="PRO_0000109656" FT BINDING 7 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 45 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 130 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 162..163 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 168..173 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 204..210 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT STRAND 3..8 FT /evidence="ECO:0007829|PDB:2AKO" FT HELIX 10..13 FT /evidence="ECO:0007829|PDB:2AKO" FT STRAND 16..19 FT /evidence="ECO:0007829|PDB:2AKO" FT HELIX 21..37 FT /evidence="ECO:0007829|PDB:2AKO" FT STRAND 38..44 FT /evidence="ECO:0007829|PDB:2AKO" FT HELIX 47..54 FT /evidence="ECO:0007829|PDB:2AKO" FT STRAND 59..61 FT /evidence="ECO:0007829|PDB:2AKO" FT HELIX 62..84 FT /evidence="ECO:0007829|PDB:2AKO" FT HELIX 85..87 FT /evidence="ECO:0007829|PDB:2AKO" FT STRAND 91..96 FT /evidence="ECO:0007829|PDB:2AKO" FT HELIX 99..102 FT /evidence="ECO:0007829|PDB:2AKO" FT HELIX 104..119 FT /evidence="ECO:0007829|PDB:2AKO" FT STRAND 123..128 FT /evidence="ECO:0007829|PDB:2AKO" FT TURN 130..132 FT /evidence="ECO:0007829|PDB:2AKO" FT HELIX 135..138 FT /evidence="ECO:0007829|PDB:2AKO" FT TURN 140..142 FT /evidence="ECO:0007829|PDB:2AKO" FT HELIX 143..152 FT /evidence="ECO:0007829|PDB:2AKO" FT STRAND 156..164 FT /evidence="ECO:0007829|PDB:2AKO" FT STRAND 168..170 FT /evidence="ECO:0007829|PDB:2AKO" FT TURN 172..174 FT /evidence="ECO:0007829|PDB:2AKO" FT STRAND 183..185 FT /evidence="ECO:0007829|PDB:2AKO" FT HELIX 189..191 FT /evidence="ECO:0007829|PDB:2AKO" FT HELIX 206..219 FT /evidence="ECO:0007829|PDB:2AKO" FT STRAND 223..231 FT /evidence="ECO:0007829|PDB:2AKO" FT HELIX 233..240 FT /evidence="ECO:0007829|PDB:2AKO" FT STRAND 246..250 FT /evidence="ECO:0007829|PDB:2AKO" SQ SEQUENCE 251 AA; 27843 MW; D07802E92023A241 CRC64; MKRIVVKVGS HVISEENTLS FERLKNLVAF LAKLMEKYEV ILVTSAAISA GHTKLDIDRK NLINKQVLAA IGQPFLISVY NELLAKFNKL GGQILLTGKD FDSRKATKHA KNAIDMMINL GILPIINEND ATAIEEIVFG DNDSLSAYAT HFFDADLLVI LSDIDGFYDK NPSEFSDAKR LEKITHIKEE WLQATIKTGS EHGTGGIVTK LKAAKFLLEH NKKMFLASGF DLSVAKTFLL EDKQIGGTLF E //