ID   PROB_BACTN              Reviewed;         360 AA.
AC   Q8A1E7;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
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}; OrderedLocusNames=BT_3719;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
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; AE015928; AAO78824.1; -; Genomic_DNA.
DR   RefSeq; NP_812630.1; NC_004663.1.
DR   RefSeq; WP_011108944.1; NC_004663.1.
DR   AlphaFoldDB; Q8A1E7; -.
DR   SMR; Q8A1E7; -.
DR   STRING; 226186.BT_3719; -.
DR   PaxDb; Q8A1E7; -.
DR   PRIDE; Q8A1E7; -.
DR   EnsemblBacteria; AAO78824; AAO78824; BT_3719.
DR   GeneID; 60924888; -.
DR   KEGG; bth:BT_3719; -.
DR   PATRIC; fig|226186.12.peg.3780; -.
DR   eggNOG; COG0263; Bacteria.
DR   HOGENOM; CLU_025400_2_0_10; -.
DR   InParanoid; Q8A1E7; -.
DR   OMA; TVIHRDN; -.
DR   UniPathway; UPA00098; UER00359.
DR   Proteomes; UP000001414; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006561; P:proline biosynthetic process; IBA:GO_Central.
DR   CDD; cd04242; AAK_G5K_ProB; 1.
DR   Gene3D; 2.30.130.10; -; 1.
DR   Gene3D; 3.40.1160.10; -; 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   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF01472; PUA; 1.
DR   PIRSF; PIRSF000729; GK; 1.
DR   PRINTS; PR00474; GLU5KINASE.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   SUPFAM; SSF88697; SSF88697; 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; ATP-binding; Cytoplasm; Kinase;
KW   Nucleotide-binding; Proline biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..360
FT                   /note="Glutamate 5-kinase"
FT                   /id="PRO_0000109643"
FT   DOMAIN          278..356
FT                   /note="PUA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT   BINDING         11
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT   BINDING         51
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT   BINDING         138
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT   BINDING         150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
SQ   SEQUENCE   360 AA;  39454 MW;  7DFF9BB6EB5CBC02 CRC64;
     MKQEFTRIAV KVGSNVLARR DGTLDVTRMS ALVDQIAELN KSGVEIILIS SGAVASGRSE
     IHPQKKLDSV DQRQLFSAVG QAKLINRYYE LFREHGIAVG QVLTTKENFS TRRHYLNQKN
     CMTVMLENGV IPIVNENDTI SVSELMFTDN DELSGLIASM MDAQALIILS NIDGIYNGSP
     SDPASAVIRE IEHGKDLSNY IQATKSSFGR GGMLTKTNIA RKVADEGITV IIANGKRDNI
     LVDLLQQPDD TVCTRFIPST EAVSSVKKWI AHSEGFAKGE IHINECATDI LSSEKAASIL
     PVGITHIEGE FEKDDIVRIM DFLGNQVGVG KANCDSAQAR EAMGKHGKKP VVHYDYLYIE