ID   PROB_MAGSA              Reviewed;         370 AA.
AC   Q2VZU1;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 100.
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=amb4080;
OS   Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Magnetospirillaceae; Paramagnetospirillum.
OX   NCBI_TaxID=342108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA   Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT   "Complete genome sequence of the facultative anaerobic magnetotactic
RT   bacterium Magnetospirillum sp. strain AMB-1.";
RL   DNA Res. 12:157-166(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}.
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DR   EMBL; AP007255; BAE52884.1; -; Genomic_DNA.
DR   RefSeq; WP_011386430.1; NC_007626.1.
DR   AlphaFoldDB; Q2VZU1; -.
DR   SMR; Q2VZU1; -.
DR   STRING; 342108.amb4080; -.
DR   KEGG; mag:amb4080; -.
DR   HOGENOM; CLU_025400_2_0_5; -.
DR   OrthoDB; 9804434at2; -.
DR   UniPathway; UPA00098; UER00359.
DR   Proteomes; UP000007058; 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; 2.
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..370
FT                   /note="Glutamate 5-kinase"
FT                   /id="PRO_0000252984"
FT   DOMAIN          278..355
FT                   /note="PUA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT   BINDING         13
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         140
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT   BINDING         172..173
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT   BINDING         214..220
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
SQ   SEQUENCE   370 AA;  39445 MW;  D0DD407A1BB7E11C CRC64;
     MSPLAAAKRL IVKIGSSLLV DDSTGQVRRG WLETLAADIA ACKARGQEVI VVSSGAVAVG
     RRKLGLVPPL KLEEKQAAAA TGQIRLAHAW QDALAHHQIT VAQVLLTLDD SENRRRYLNA
     RSTLETLLKL GAVPVINEND TVATAEIRVG DNDRLAARVA QMVSADALVL FSDIDGLYTA
     DPRKDPDARF IPEVHELTPE IEAMAGDPGS AYGSGGMVTK LVAARICLSA GCRMAITRGE
     PMHPLKTIED GGRCTWFLPN SEPRTARKQW IFGSMKPTGT LVLDAGAARA LAQGRSLLPA
     GITEVSGAFE RGDCVLVKDG SGKVLGRGLV AYSADDSRAI MGRKSGEIEA ILGFRGRDEL
     IHRDDLVMEG
//