ID   PROB_DICTD              Reviewed;         371 AA.
AC   B8E032;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   02-SEP-2026, entry version 87.
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=Dtur_0834;
OS   Dictyoglomus turgidum (strain DSM 6724 / Z-1310).
OC   Bacteria; Pseudomonadati; Dictyoglomota; Dictyoglomia; Dictyoglomales;
OC   Dictyoglomaceae; Dictyoglomus.
OX   NCBI_TaxID=515635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6724 / Z-1310;
RX   PubMed=28066333; DOI=10.3389/fmicb.2016.01979;
RA   Brumm P.J., Gowda K., Robb F.T., Mead D.A.;
RT   "The complete genome sequence of hyperthermophile Dictyoglomus turgidum DSM
RT   6724 reveals a specialized carbohydrate fermentor.";
RL   Front. Microbiol. 7:1979-1979(2016).
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=L-glutamate + ATP = L-glutamyl 5-phosphate + ADP;
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; CP001251; ACK42115.1; -; Genomic_DNA.
DR   RefSeq; WP_012583199.1; NC_011661.1.
DR   AlphaFoldDB; B8E032; -.
DR   SMR; B8E032; -.
DR   FunCoup; B8E032; 270.
DR   STRING; 515635.Dtur_0834; -.
DR   EnsemblBacteria; ACK42115; ACK42115; Dtur_0834.
DR   KEGG; dtu:Dtur_0834; -.
DR   PATRIC; fig|515635.4.peg.873; -.
DR   eggNOG; COG0263; Bacteria.
DR   HOGENOM; CLU_025400_2_0_0; -.
DR   InParanoid; B8E032; -.
DR   OrthoDB; 9804434at2; -.
DR   UniPathway; UPA00098; UER00359.
DR   Proteomes; UP000007719; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004349; F:glutamate 5-kinase activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IBA:GO_Central.
DR   CDD; cd04242; AAK_G5K_ProB; 1.
DR   CDD; cd21157; PUA_G5K; 1.
DR   FunFam; 2.30.130.10:FF:000007; Glutamate 5-kinase; 1.
DR   FunFam; 3.40.1160.10:FF:000018; Glutamate 5-kinase; 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; 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; 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..371
FT                   /note="Glutamate 5-kinase"
FT                   /id="PRO_1000125227"
FT   DOMAIN          274..352
FT                   /note="PUA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT   BINDING         10
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT   BINDING         50
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT   BINDING         137
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         169..170
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT   BINDING         208..214
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
SQ   SEQUENCE   371 AA;  41319 MW;  0BF754F7BA8D0E77 CRC64;
     MNNWKRIVVK VGTSSITDGR GSPSGEKILS LVKECVKLIR ADKELVLVSS GAIASGREII
     QKLSKRKDLP AKQALSAVGQ VRLMQYYSQL FSIFKQPIAQ ILLTAEDLRD RKRYINISQT
     FETLLEEKII PIVNENDTVA VEEIKIGDND TLSAKVACAI NADLLVILSD VEGLYSEDPN
     ISSNALLITD VYEIDESIEK IAGPGKGTGG MFTKVQAAKI VTEAGIPMIL ARADVENILE
     RIVLKKEKVG TFFYPSEKHL NKRKHWMLFM AKPEGRIYID DGAKDALLKR GKSLLPVGIK
     KVEGEFTRGD TVSIFDLRGE EIARGITNYD SLELDKIKGK NTEEIRNILG EDFYEEVIHR
     NNLVLTNRGD L
//