ID   PROB_MEIRU              Reviewed;         377 AA.
AC   Q9ZG98;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 2.
DT   13-SEP-2023, entry version 91.
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};
OS   Meiothermus ruber.
OC   Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Meiothermus.
OX   NCBI_TaxID=277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=40;
RA   Yaklichkin S.Y., Zimina M.S., Yurchenko Y.V., Hromov I.S., Neumivakin L.V.;
RT   "Molecular cloning and sequence analysis of the proA gene from thermophilic
RT   eubacterium Thermus ruber.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAC72812.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF082661; AAC72812.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q9ZG98; -.
DR   SMR; Q9ZG98; -.
DR   UniPathway; UPA00098; UER00359.
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_0000109691"
FT   DOMAIN          281..359
FT                   /note="PUA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT   BINDING         18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT   BINDING         55
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         154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT   BINDING         174..175
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT   BINDING         216..222
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
SQ   SEQUENCE   377 AA;  40592 MW;  F637DFE9DD811155 CRC64;
     MHGRLPLTAQ THRRLVVKVG SAVLSGPQGR QHQLAIAAQV AALRAEGREV VLVSSGAQAT
     GMQKLGLTEK PKSMPGKQAL AAVGQPTLML LWEQAFSWYD LKVAQVLLTA EDLAHRHRYL
     NARQTLETLL EWGIVPIINE NDTVMVEEIK FGDNDQLSAL IASLVGADLL ILLSDIEALY
     EADPRTHPEA QPIPYVERVD AGVLRMAGDS PNRVGTGGMK SKLLAAEKAQ AAGIPHLLLP
     GTRPQSIAEA LQGAPVGTLF AGGQRRYSGR KLWLYQLPKP QGEVVVDAGA AKALRQGGAS
     LLPAGILEVR GQFGVGEAVR CLDEQGNLIG VGLVNYSAAE LARIKRRKTR EIEALLGYKN
     TDEAIHRDYF ALASELE
//