PROB_CAMJE
ID PROB_CAMJE Reviewed; 251 AA.
AC Q9PJ29; Q0PC40;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=Cj0097;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH ADP.
RA Gorman J., Shapiro L.;
RT "Crystal structure of glutamate 5-kinase from Campylobacter jejuni.";
RL Submitted (AUG-2005) to the PDB data bank.
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; AL111168; CAL34268.1; -; Genomic_DNA.
DR PIR; A81426; A81426.
DR RefSeq; WP_002851769.1; NC_002163.1.
DR RefSeq; YP_002343557.1; NC_002163.1.
DR PDB; 2AKO; X-ray; 2.20 A; A/B/C/D=1-251.
DR PDBsum; 2AKO; -.
DR AlphaFoldDB; Q9PJ29; -.
DR SMR; Q9PJ29; -.
DR IntAct; Q9PJ29; 9.
DR STRING; 192222.Cj0097; -.
DR PaxDb; Q9PJ29; -.
DR PRIDE; Q9PJ29; -.
DR EnsemblBacteria; CAL34268; CAL34268; Cj0097.
DR GeneID; 904426; -.
DR KEGG; cje:Cj0097; -.
DR PATRIC; fig|192222.6.peg.95; -.
DR eggNOG; COG0263; Bacteria.
DR HOGENOM; CLU_025400_0_0_7; -.
DR OMA; QPHLMRI; -.
DR UniPathway; UPA00098; UER00359.
DR EvolutionaryTrace; Q9PJ29; -.
DR Proteomes; UP000000799; 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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; ATP-binding; Cytoplasm; Kinase;
KW Nucleotide-binding; Proline biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..251
FT /note="Glutamate 5-kinase"
FT /id="PRO_0000109656"
FT BINDING 7
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT BINDING 130
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 162..163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 168..173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 204..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:2AKO"
FT HELIX 10..13
FT /evidence="ECO:0007829|PDB:2AKO"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:2AKO"
FT HELIX 21..37
FT /evidence="ECO:0007829|PDB:2AKO"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:2AKO"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:2AKO"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2AKO"
FT HELIX 62..84
FT /evidence="ECO:0007829|PDB:2AKO"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:2AKO"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:2AKO"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:2AKO"
FT HELIX 104..119
FT /evidence="ECO:0007829|PDB:2AKO"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:2AKO"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:2AKO"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:2AKO"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:2AKO"
FT HELIX 143..152
FT /evidence="ECO:0007829|PDB:2AKO"
FT STRAND 156..164
FT /evidence="ECO:0007829|PDB:2AKO"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:2AKO"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:2AKO"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:2AKO"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:2AKO"
FT HELIX 206..219
FT /evidence="ECO:0007829|PDB:2AKO"
FT STRAND 223..231
FT /evidence="ECO:0007829|PDB:2AKO"
FT HELIX 233..240
FT /evidence="ECO:0007829|PDB:2AKO"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:2AKO"
SQ SEQUENCE 251 AA; 27843 MW; D07802E92023A241 CRC64;
MKRIVVKVGS HVISEENTLS FERLKNLVAF LAKLMEKYEV ILVTSAAISA GHTKLDIDRK
NLINKQVLAA IGQPFLISVY NELLAKFNKL GGQILLTGKD FDSRKATKHA KNAIDMMINL
GILPIINEND ATAIEEIVFG DNDSLSAYAT HFFDADLLVI LSDIDGFYDK NPSEFSDAKR
LEKITHIKEE WLQATIKTGS EHGTGGIVTK LKAAKFLLEH NKKMFLASGF DLSVAKTFLL
EDKQIGGTLF E
