(data stored in ACNUC30630 zone)

SWISSPROT: PROB_RHOPT

ID   PROB_RHOPT              Reviewed;         376 AA.
AC   B3Q732;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   11-DEC-2019, entry version 70.
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=Rpal_0158;
OS   Rhodopseudomonas palustris (strain TIE-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=395960;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TIE-1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA   Newman D.K., Roden E., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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}.
DR   EMBL; CP001096; ACE98720.1; -; Genomic_DNA.
DR   RefSeq; WP_012493956.1; NC_011004.1.
DR   SMR; B3Q732; -.
DR   PRIDE; B3Q732; -.
DR   EnsemblBacteria; ACE98720; ACE98720; Rpal_0158.
DR   KEGG; rpt:Rpal_0158; -.
DR   HOGENOM; HOG000246368; -.
DR   KO; K00931; -.
DR   OMA; THEIRFG; -.
DR   OrthoDB; 1480250at2; -.
DR   BioCyc; RPAL395960:RPAL_RS00795-MONOMER; -.
DR   UniPathway; UPA00098; UER00359.
DR   Proteomes; UP000001725; 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; B3Q732.
DR   SWISS-2DPAGE; B3Q732.
KW   Amino-acid biosynthesis; ATP-binding; Cytoplasm; Kinase;
KW   Nucleotide-binding; Proline biosynthesis; Transferase.
FT   CHAIN           1..376
FT                   /note="Glutamate 5-kinase"
FT                   /id="PRO_1000125254"
FT   DOMAIN          281..358
FT                   /note="PUA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT   NP_BIND         175..176
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT   BINDING         15
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT   BINDING         56
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT   BINDING         143
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT   BINDING         155
FT                   /note="Substrate; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
SQ   SEQUENCE   376 AA;  39581 MW;  3F2B6E5AF1AE388A CRC64;
     MASPKLHDFR HIVVKVGSSL LIDSAAGEVR AGWLAALAAD IAELHRGGRD VMVVSSGSIA
     LGRSRLKLPR GPLKLEESQA AAAVGQIELA RTWSEVLGAH GIGAGQILVT FQDTEERRRY
     LNARSTIAKL LEWRAVPVIN ENDTVATTEI RYGDNDRLAA RVATMASADL LILLSDIDGL
     YTAPPGNDPD ATLIPVVEAI TAEIEGMAGA AGSELSRGGM RTKIEAAKIA TSAGTHMLIA
     SGKIDHPLRA IAEGGKCTWF LTPANPVTAR KRWIAGTLEP KGTLTIDAGA VSALRAGKSL
     LPAGVIRVDG QFSRGDAVIV RGPDTHEIGR GLVAYDAEDA EKIKGHSSPD VMMILGITGR
     AEMIHRDDLV VGTAPT
//

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