PROB_ECOLI
ID PROB_ECOLI Reviewed; 367 AA.
AC P0A7B5; P07005; P78293;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 134.
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=b0242, JW0232;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-6 AND 8-12.
RX PubMed=6089111; DOI=10.1093/nar/12.15.6337;
RA Deutch A.H., Rushlow K.E., Smith C.J.;
RT "Analysis of the Escherichia coli proBA locus by DNA and protein
RT sequencing.";
RL Nucleic Acids Res. 12:6337-6355(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 143.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-62.
RC STRAIN=K12;
RX PubMed=6341601; DOI=10.1016/0022-2836(83)90110-9;
RA Overbeeke N., Bergmans H., van Mansfeld F., Lugtenberg B.;
RT "Complete nucleotide sequence of phoE, the structural gene for the
RT phosphate limitation inducible outer membrane pore protein of Escherichia
RT coli K12.";
RL J. Mol. Biol. 163:513-532(1983).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, AND SUBUNIT.
RX PubMed=6319365; DOI=10.1128/jb.157.2.545-551.1984;
RA Smith C.J., Deutch A.H., Rushlow K.E.;
RT "Purification and characteristics of a gamma-glutamyl kinase involved in
RT Escherichia coli proline biosynthesis.";
RL J. Bacteriol. 157:545-551(1984).
RN [8]
RP ACTIVITY REGULATION, SUBUNIT, AND DOMAIN.
RX PubMed=16337196; DOI=10.1016/j.febslet.2005.11.037;
RA Perez-Arellano I., Rubio V., Cervera J.;
RT "Dissection of Escherichia coli glutamate 5-kinase: functional impact of
RT the deletion of the PUA domain.";
RL FEBS Lett. 579:6903-6908(2005).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEXES WITH 5-OXOPROLINE AND
RP D-GAMMA-GLUTAMYL PHOSPHATE, AND SUBUNIT.
RX PubMed=17321544; DOI=10.1016/j.jmb.2007.01.073;
RA Marco-Marin C., Gil-Ortiz F., Perez-Arellano I., Cervera J., Fita I.,
RA Rubio V.;
RT "A novel two-domain architecture within the amino acid kinase enzyme family
RT revealed by the crystal structure of Escherichia coli glutamate 5-kinase.";
RL J. Mol. Biol. 367:1431-1446(2007).
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 ECO:0000269|PubMed:6319365}.
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 ECO:0000269|PubMed:6319365};
CC -!- ACTIVITY REGULATION: Interaction with gamma-glutamyl phosphate
CC reductase (proA) seems necessary for kinase activity. Requires free
CC Mg(2+). Inhibited by proline and ADP. {ECO:0000269|PubMed:16337196,
CC ECO:0000269|PubMed:6319365}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5-7.0. {ECO:0000269|PubMed:6319365};
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, ECO:0000269|PubMed:6319365}.
CC -!- SUBUNIT: Homotetramer. Dimer of dimers. May form a complex with gamma-
CC glutamyl phosphate reductase (proA). {ECO:0000269|PubMed:16337196,
CC ECO:0000269|PubMed:17321544, ECO:0000269|PubMed:6319365}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00456}.
CC -!- DOMAIN: Contains an N-terminal amino acid kinase (AAK) domain and a C-
CC terminal PUA domain. The AAK domain is responsible for catalyzing the
CC reaction and for proline and ADP inhibition. The PUA domain modulates
CC the catalytic and regulatory functions of the AAK domain.
CC {ECO:0000269|PubMed:16337196}.
CC -!- SIMILARITY: Belongs to the glutamate 5-kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00456}.
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DR EMBL; X00786; CAA25363.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08662.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73346.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77911.2; -; Genomic_DNA.
DR EMBL; V00316; CAA23604.1; -; Genomic_DNA.
DR PIR; C64749; KIECEG.
DR RefSeq; NP_414777.1; NC_000913.3.
DR RefSeq; WP_001285288.1; NZ_STEB01000020.1.
DR PDB; 2J5T; X-ray; 2.90 A; A/B/C/D/E/F/G/H=1-367.
DR PDB; 2J5V; X-ray; 2.50 A; A/B=1-367.
DR PDB; 2W21; X-ray; 2.95 A; A=1-259.
DR PDBsum; 2J5T; -.
DR PDBsum; 2J5V; -.
DR PDBsum; 2W21; -.
DR AlphaFoldDB; P0A7B5; -.
DR SMR; P0A7B5; -.
DR BioGRID; 4259767; 11.
DR IntAct; P0A7B5; 2.
DR STRING; 511145.b0242; -.
DR jPOST; P0A7B5; -.
DR PaxDb; P0A7B5; -.
DR PRIDE; P0A7B5; -.
DR EnsemblBacteria; AAC73346; AAC73346; b0242.
DR EnsemblBacteria; BAA77911; BAA77911; BAA77911.
DR GeneID; 66671440; -.
DR GeneID; 946425; -.
DR KEGG; ecj:JW0232; -.
DR KEGG; eco:b0242; -.
DR PATRIC; fig|1411691.4.peg.2041; -.
DR EchoBASE; EB0761; -.
DR eggNOG; COG0263; Bacteria.
DR HOGENOM; CLU_025400_2_0_6; -.
DR InParanoid; P0A7B5; -.
DR OMA; TVIHRDN; -.
DR PhylomeDB; P0A7B5; -.
DR BioCyc; EcoCyc:GLUTKIN-MON; -.
DR BioCyc; MetaCyc:GLUTKIN-MON; -.
DR BRENDA; 2.7.2.11; 2026.
DR SABIO-RK; P0A7B5; -.
DR UniPathway; UPA00098; UER00359.
DR EvolutionaryTrace; P0A7B5; -.
DR PRO; PR:P0A7B5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004349; F:glutamate 5-kinase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:1901973; F:proline binding; IDA:EcoCyc.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0055129; P:L-proline biosynthetic process; IMP:EcoCyc.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006561; P:proline biosynthetic process; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Kinase; Nucleotide-binding;
KW Proline biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..367
FT /note="Glutamate 5-kinase"
FT /id="PRO_0000109669"
FT DOMAIN 275..353
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:0000305"
FT BINDING 50
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17321544,
FT ECO:0007744|PDB:2J5T, ECO:0007744|PDB:2J5V"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17321544,
FT ECO:0007744|PDB:2J5T, ECO:0007744|PDB:2J5V"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17321544,
FT ECO:0007744|PDB:2J5T, ECO:0007744|PDB:2J5V"
FT BINDING 169..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT BINDING 211..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="E -> A (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:2J5V"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:2J5V"
FT TURN 17..19
FT /evidence="ECO:0007829|PDB:2J5V"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:2J5V"
FT HELIX 25..40
FT /evidence="ECO:0007829|PDB:2J5V"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:2J5V"
FT HELIX 52..60
FT /evidence="ECO:0007829|PDB:2J5V"
FT HELIX 69..92
FT /evidence="ECO:0007829|PDB:2J5V"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:2J5V"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:2J5V"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:2J5V"
FT HELIX 111..126
FT /evidence="ECO:0007829|PDB:2J5V"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:2J5V"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:2W21"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:2J5V"
FT HELIX 149..160
FT /evidence="ECO:0007829|PDB:2J5V"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:2J5V"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:2J5T"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:2J5T"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:2J5T"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:2J5T"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:2J5T"
FT HELIX 215..226
FT /evidence="ECO:0007829|PDB:2J5V"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:2J5V"
FT HELIX 241..247
FT /evidence="ECO:0007829|PDB:2J5V"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:2J5V"
FT HELIX 264..270
FT /evidence="ECO:0007829|PDB:2J5V"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:2J5V"
FT HELIX 282..291
FT /evidence="ECO:0007829|PDB:2J5V"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:2J5V"
FT STRAND 300..305
FT /evidence="ECO:0007829|PDB:2J5V"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:2J5V"
FT STRAND 322..327
FT /evidence="ECO:0007829|PDB:2J5V"
FT HELIX 332..338
FT /evidence="ECO:0007829|PDB:2J5V"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:2J5V"
FT HELIX 346..350
FT /evidence="ECO:0007829|PDB:2J5V"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:2J5V"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:2J5V"
SQ SEQUENCE 367 AA; 39057 MW; 5541040202EBCCE8 CRC64;
MSDSQTLVVK LGTSVLTGGS RRLNRAHIVE LVRQCAQLHA AGHRIVIVTS GAIAAGREHL
GYPELPATIA SKQLLAAVGQ SRLIQLWEQL FSIYGIHVGQ MLLTRADMED RERFLNARDT
LRALLDNNIV PVINENDAVA TAEIKVGDND NLSALAAILA GADKLLLLTD QKGLYTADPR
SNPQAELIKD VYGIDDALRA IAGDSVSGLG TGGMSTKLQA ADVACRAGID TIIAAGSKPG
VIGDVMEGIS VGTLFHAQAT PLENRKRWIF GAPPAGEITV DEGATAAILE RGSSLLPKGI
KSVTGNFSRG EVIRICNLEG RDIAHGVSRY NSDALRRIAG HHSQEIDAIL GYEYGPVAVH
RDDMITR
