ID   PROB2_RHILO             Reviewed;         284 AA.
AC   Q989S7;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Glutamate 5-kinase 2 {ECO:0000255|HAMAP-Rule:MF_00456};
DE            EC=2.7.2.11 {ECO:0000255|HAMAP-Rule:MF_00456};
DE   AltName: Full=Gamma-glutamyl kinase 2 {ECO:0000255|HAMAP-Rule:MF_00456};
DE            Short=GK 2 {ECO:0000255|HAMAP-Rule:MF_00456};
GN   Name=proB2 {ECO:0000255|HAMAP-Rule:MF_00456}; OrderedLocusNames=mlr6298;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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; BA000012; BAB52617.1; -; Genomic_DNA.
DR   RefSeq; WP_010913936.1; NC_002678.2.
DR   AlphaFoldDB; Q989S7; -.
DR   SMR; Q989S7; -.
DR   STRING; 266835.14026018; -.
DR   EnsemblBacteria; BAB52617; BAB52617; BAB52617.
DR   KEGG; mlo:mlr6298; -.
DR   PATRIC; fig|266835.9.peg.5004; -.
DR   eggNOG; COG0263; Bacteria.
DR   HOGENOM; CLU_025400_0_2_5; -.
DR   OMA; QPHLMRI; -.
DR   OrthoDB; 1480250at2; -.
DR   UniPathway; UPA00098; UER00359.
DR   Proteomes; UP000000552; 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: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   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   Pfam; PF00696; AA_kinase; 1.
DR   PIRSF; PIRSF000729; GK; 1.
DR   PRINTS; PR00474; GLU5KINASE.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   TIGRFAMs; TIGR01027; proB; 1.
DR   PROSITE; PS00902; GLUTAMATE_5_KINASE; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; ATP-binding; Cytoplasm; Kinase;
KW   Nucleotide-binding; Proline biosynthesis; Transferase.
FT   CHAIN           1..284
FT                   /note="Glutamate 5-kinase 2"
FT                   /id="PRO_0000109714"
FT   BINDING         26
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT   BINDING         67
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         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT   BINDING         186..187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT   BINDING         228..234
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
SQ   SEQUENCE   284 AA;  30683 MW;  C7E8BB7D23C4FA54 CRC64;
     MQEKIRETCL ATKTVKLLSA RRLIVKIGSA VVADAETGEI RGPWLETLIK DVVRFFARGQ
     QVIIVTSGAV AAGSRHFKQL DRSLRIEEKQ AAAAIGQIRL MIAYEQSLKR HGFGLGQVLL
     TSADVDNQRC RLNARSAFQQ LLNVGAVPVI NENDATATPE VCLGDNDRLA ARVAQIAKAD
     LLILLSDVDG LFTEDPHDNP LARMIPEVRR ITPEIEIMAS LSPARHGSGG MVTKLMAARI
     AMEAGCNVVI AKGSKSYPLA AIENGAPSTW FIPPARETAT RGGR