(data stored in ACNUC10821 zone)

SWISSPROT: C8U1X3_ECO10

ID   C8U1X3_ECO10            Unreviewed;       367 AA.
AC   C8U1X3;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 69.
DE   RecName: Full=Glutamate 5-kinase {ECO:0000256|HAMAP-Rule:MF_00456};
DE            EC=2.7.2.11 {ECO:0000256|HAMAP-Rule:MF_00456};
DE   AltName: Full=Gamma-glutamyl kinase {ECO:0000256|HAMAP-Rule:MF_00456};
DE            Short=GK {ECO:0000256|HAMAP-Rule:MF_00456};
GN   Name=proB {ECO:0000256|HAMAP-Rule:MF_00456,
GN   ECO:0000313|EMBL:BAI29131.1};
GN   OrderedLocusNames=ECO103_0257 {ECO:0000313|EMBL:BAI29131.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29131.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29131.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Catalyzes the transfer of a phosphate group to glutamate
CC       to form L-glutamate 5-phosphate. {ECO:0000256|HAMAP-Rule:MF_00456,
CC       ECO:0000256|SAAS:SAAS01129714}.
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:0000256|HAMAP-Rule:MF_00456,
CC         ECO:0000256|SAAS:SAAS01129711};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-
CC       glutamate 5-semialdehyde from L-glutamate: step 1/2.
CC       {ECO:0000256|HAMAP-Rule:MF_00456, ECO:0000256|SAAS:SAAS01129693}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00456,
CC       ECO:0000256|SAAS:SAAS00057525}.
CC   -!- SIMILARITY: Belongs to the glutamate 5-kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00456, ECO:0000256|SAAS:SAAS00559154}.
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DR   EMBL; AP010958; BAI29131.1; -; Genomic_DNA.
DR   RefSeq; WP_001285288.1; NC_013353.1.
DR   SMR; C8U1X3; -.
DR   EnsemblBacteria; BAI29131; BAI29131; ECO103_0257.
DR   KEGG; eoh:ECO103_0257; -.
DR   HOGENOM; HOG000246369; -.
DR   KO; K00931; -.
DR   OMA; THEIRFG; -.
DR   BioCyc; ECOL585395:ECO103_RS01350-MONOMER; -.
DR   UniPathway; UPA00098; UER00359.
DR   Proteomes; UP000000959; 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   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   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;
DR   PRODOM; C8U1X3.
DR   SWISS-2DPAGE; C8U1X3.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00456,
KW   ECO:0000256|SAAS:SAAS00198400};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00456,
KW   ECO:0000256|SAAS:SAAS00198410};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00456,
KW   ECO:0000256|SAAS:SAAS00243864};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00456,
KW   ECO:0000256|SAAS:SAAS00198401, ECO:0000313|EMBL:BAI29131.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00456,
KW   ECO:0000256|SAAS:SAAS00198406};
KW   Proline biosynthesis {ECO:0000256|HAMAP-Rule:MF_00456,
KW   ECO:0000256|SAAS:SAAS00198396};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00456,
KW   ECO:0000256|SAAS:SAAS00198402}.
FT   DOMAIN      275    353       PUA. {ECO:0000259|PROSITE:PS50890}.
FT   NP_BIND     169    170       ATP. {ECO:0000256|HAMAP-Rule:MF_00456}.
FT   NP_BIND     211    217       ATP. {ECO:0000256|HAMAP-Rule:MF_00456}.
FT   BINDING      10     10       ATP. {ECO:0000256|HAMAP-Rule:MF_00456}.
FT   BINDING      50     50       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00456}.
FT   BINDING     137    137       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00456}.
FT   BINDING     149    149       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00456}.
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
//

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