ID PROB_BIFLS Reviewed; 377 AA. AC B7GNK0; E8MNT3; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 1. DT 27-MAR-2024, entry version 84. 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=Blon_2298, BLIJ_2372; OS Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM OS 1222 / NCTC 11817 / S12). OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=391904; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12; RX PubMed=19033196; DOI=10.1073/pnas.0809584105; RA Sela D.A., Chapman J., Adeuya A., Kim J.H., Chen F., Whitehead T.R., RA Lapidus A., Rokhsar D.S., Lebrilla C.B., German J.B., Price N.P., RA Richardson P.M., Mills D.A.; RT "The genome sequence of Bifidobacterium longum subsp. infantis reveals RT adaptations for milk utilization within the infant microbiome."; RL Proc. Natl. Acad. Sci. U.S.A. 105:18964-18969(2008). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12; RX PubMed=21270894; DOI=10.1038/nature09646; RA Fukuda S., Toh H., Hase K., Oshima K., Nakanishi Y., Yoshimura K., Tobe T., RA Clarke J.M., Topping D.L., Suzuki T., Taylor T.D., Itoh K., Kikuchi J., RA Morita H., Hattori M., Ohno H.; RT "Bifidobacteria can protect from enteropathogenic infection through RT production of acetate."; RL Nature 469:543-547(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=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; CP001095; ACJ53356.1; -; Genomic_DNA. DR EMBL; AP010889; BAJ69949.1; -; Genomic_DNA. DR RefSeq; WP_012578527.1; NZ_JDTT01000025.1. DR AlphaFoldDB; B7GNK0; -. DR SMR; B7GNK0; -. DR KEGG; bln:Blon_2298; -. DR KEGG; blon:BLIJ_2372; -. DR PATRIC; fig|391904.8.peg.2373; -. DR HOGENOM; CLU_025400_2_0_11; -. DR UniPathway; UPA00098; UER00359. DR Proteomes; UP000001360; 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: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 3: Inferred from homology; KW Amino-acid biosynthesis; ATP-binding; Cytoplasm; Kinase; KW Nucleotide-binding; Proline biosynthesis; Transferase. FT CHAIN 1..377 FT /note="Glutamate 5-kinase" FT /id="PRO_1000193688" FT DOMAIN 285..363 FT /note="PUA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 22 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 62 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 149 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 161 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 181..182 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" FT BINDING 223..229 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456" SQ SEQUENCE 377 AA; 39216 MW; 9AA9E115A5866A52 CRC64; MSTPSQAEVR RMVAAAGTIV VKVGSSSLTQ PSGHLDPDKL DALAAALAQI RLMGGRVVLV SSGAIAAGFG PLGFDERPAD VATQQATAAV GQGLLMARYE TAFGRFGIRV GQILITAEDT IRATQYRNVE RTLDRLLDLG VVPIINENDS LASNEIRFGD NDRLSALVAN LVRAEALVLL TDVDALYTAP PSQPGSRRVE YVPNVIDALG DIQVSGSGSK VGTGGMVTKL EAARVAAVSG IPTVLTCASN AGPAMMGDPV GTVFAPVKAR GSSRRLWIGF AADPRGAIVV DAGAGQAIRG GRASLLATGA LEVHGDFSAG DPVWIDAESG EHLARGLAGF DSEEIPQMLG RNTAQLKRFL GPQYAHPLIH RDNLVLV //