PROB_PHOLL
ID PROB_PHOLL Reviewed; 368 AA.
AC Q7N7B2;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-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=plu1243;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(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; BX571863; CAE13537.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7N7B2; -.
DR SMR; Q7N7B2; -.
DR STRING; 243265.plu1243; -.
DR EnsemblBacteria; CAE13537; CAE13537; plu1243.
DR KEGG; plu:plu1243; -.
DR eggNOG; COG0263; Bacteria.
DR HOGENOM; CLU_025400_2_0_6; -.
DR OMA; TVIHRDN; -.
DR UniPathway; UPA00098; UER00359.
DR Proteomes; UP000002514; 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 Gene3D; 2.30.130.10; -; 1.
DR Gene3D; 3.40.1160.10; -; 2.
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 SMART; SM00359; PUA; 1.
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..368
FT /note="Glutamate 5-kinase"
FT /id="PRO_0000109703"
FT DOMAIN 276..354
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"
FT BINDING 170..171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT BINDING 212..218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
SQ SEQUENCE 368 AA; 39455 MW; 74587DB033C1A6EA CRC64;
MMNSSQTLVV KLGTSVLTGG SRRLNRAHIV ELVRQCAQQH EKGHRIIIVT SGAIAAGREH
LGYPDLPATI ASKQLLAAVG QSRLIQLWEQ FFSIYGIHVG QMLLTRADLE DRERFLNARD
TLQALLDNRI VPVINENDAV ATAEIKVGDN DNLSALAAIL GGADKLLLLT DIEGLYTADP
RNNPDAKLIP EVYDISDELR MVAGDSISGL GTGGMATKLQ AAGIAGRAGI DVIIAAGNKP
DVISDVIEGN PVGTRFHGLE SPMENRKRWI FGAPPAGEII VDHGAETAIC EKGSSLLPKG
IKNIKGDFSR GEVICIRSLS GKDLAHGVCR YNSDALRLIA GHHSQQISQI LGYEYGAVAV
HRDDMIVS
