ID PROB_ESCF3 Reviewed; 367 AA. AC B7LNF8; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 1. DT 14-APR-2009, entry version 3. DE RecName: Full=Glutamate 5-kinase; DE EC=2.7.2.11; DE AltName: Full=Gamma-glutamyl kinase; DE Short=GK; GN Name=proB; OrderedLocusNames=EFER_2736; OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585054; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344; RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., RA Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., RA Dossat C., Karoui M.E., Frapy E., Garry L., Ghigo J.M., Gilles A.M., RA Johnson J., Le Bouguenec C., Lescat M., Mangenot S., RA Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A., RA Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B., RA Vallenet D., Medigue C., Rocha E.P.C., Denamur E.; RT "Organised genome dynamics in the Escherichia coli species results in RT highly diverse adaptive paths."; RL PLoS Genet. 5:E1000344-E1000344(2009). CC -!- FUNCTION: Catalyzes the transfer of a phosphate group to glutamate CC to form glutamate 5-phosphate which rapidly cyclizes to 5- CC oxoproline (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate = ADP + L-glutamate 5- CC phosphate. CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L- CC glutamate 5-semialdehyde from L-glutamate: step 1/2. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the glutamate 5-kinase family. CC -!- SIMILARITY: Contains 1 PUA domain. 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; CU928158; CAQ90231.1; -; Genomic_DNA. DR RefSeq; YP_002383842.1; -. DR GeneID; 7120132; -. DR HAMAP; MF_00456; -; 1. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR001057; Glu_5kinase. DR InterPro; IPR011529; Glu_5kinase_bact. DR InterPro; IPR005715; ProB. DR InterPro; IPR002478; PUA. DR Gene3D; G3DSA:3.40.1160.10; Aa_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 TIGRFAMs; TIGR01027; proB; 1. DR PROSITE; PS00902; GLUTAMATE_5_KINASE; 1. DR PROSITE; PS50890; PUA; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; Kinase; KW Proline biosynthesis; Transferase. FT CHAIN 1 367 Glutamate 5-kinase. FT /FTId=PRO_1000125237. FT DOMAIN 275 353 PUA. SQ SEQUENCE 367 AA; 39046 MW; 55410401CDEBCCE8 CRC64; MSDSQTLVVK LGTSVLTGGS RRLNRAHIVE LVRQCAQLHA AGHRIVIVTS GAIAAGREHL GYPELPATIA SKQLLAAVGQ SRLIQLWEQL FSIYGIHVGQ MLLTRADMED RERFLNARDT LRALLDNNIV PVINENDAVA TAEIKVGDND NLSALAAILA GADKLLLLTD QKGLYTADPR SNPQAELIKD VYGIDDALRA IAGDSVSGLG TGGMSTKLQA ADVACRAGID TIIAAGSKPG VIGDVMEGIS VGTLFHAQAT PLENRKRWIF GAPPAGEITV DEGATAAILE RGSSLLPKGI KSVTGNFSRG EVIRICNLEG RDIAHGVSRY NSDALRRIAG HHSQEIDAIL GYEYGSVAVH RDDMITR //