(data stored in ACNUC7421 zone)

SWISSPROT: PROB_RHOPS

ID   PROB_RHOPS              Reviewed;         376 AA.
AC   Q13DM7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 82.
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=RPD_0574;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of a phosphate group to glutamate
CC       to form L-glutamate 5-phosphate. {ECO:0000255|HAMAP-
CC       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-
CC       glutamate 5-semialdehyde from L-glutamate: step 1/2.
CC       {ECO:0000255|HAMAP-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}.
DR   EMBL; CP000283; ABE37812.1; -; Genomic_DNA.
DR   RefSeq; WP_011500999.1; NC_007958.1.
DR   SMR; Q13DM7; -.
DR   STRING; 316057.RPD_0574; -.
DR   EnsemblBacteria; ABE37812; ABE37812; RPD_0574.
DR   KEGG; rpd:RPD_0574; -.
DR   eggNOG; ENOG4105CGT; Bacteria.
DR   eggNOG; COG0263; LUCA.
DR   HOGENOM; HOG000246368; -.
DR   KO; K00931; -.
DR   OMA; THEIRFG; -.
DR   OrthoDB; 1480250at2; -.
DR   BioCyc; RPAL316057:RPD_RS02950-MONOMER; -.
DR   UniPathway; UPA00098; UER00359.
DR   Proteomes; UP000001818; 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; Q13DM7.
DR   SWISS-2DPAGE; Q13DM7.
KW   Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm;
KW   Kinase; Nucleotide-binding; Proline biosynthesis; Transferase.
FT   CHAIN         1    376       Glutamate 5-kinase.
FT                                /FTId=PRO_1000081100.
FT   DOMAIN      281    358       PUA. {ECO:0000255|HAMAP-Rule:MF_00456}.
FT   NP_BIND     175    176       ATP. {ECO:0000255|HAMAP-Rule:MF_00456}.
FT   BINDING      15     15       ATP. {ECO:0000255|HAMAP-Rule:MF_00456}.
FT   BINDING      56     56       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00456}.
FT   BINDING     143    143       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00456}.
FT   BINDING     155    155       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00456}.
SQ   SEQUENCE   376 AA;  39571 MW;  3D8FDB9FBF41EEA8 CRC64;
     MARPKLHDFR RLVVKVGSSL LIDSGAGEVR ADWLAALAAD IAELHRGGRD VMIVSSGSIA
     LGRSRLKLPR GALKLEESQA AAAVGQIALA RTWSEVLGSH GIGAGQILVT LQDTEERRRY
     LNARSTIAKL LEWRAVPVIN ENDTVATNEI RYGDNDRLAA RVATMASADL LILLSDIDGL
     YTAPPGSNPD AKLIPEVESV TAEIESMAGA AGSELSRGGM RTKIEAAKIA TSAGTHMLIA
     SGKIDHPLKA IAEGGPCTWF LTPANPVTAR KRWIAGSLEP KGTLTIDAGA VSALRAGKSL
     LPAGVIRVDG QFARGDAVIV RGPDTHEIGR GLVAYDADDA DRIKGRSSPD VMMILGISGR
     AEMIHRDDLV VGTAPG
//

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