(data stored in ACNUC7421 zone)

SWISSPROT: PROB1_PSEHT

ID   PROB1_PSEHT             Reviewed;         368 AA.
AC   Q3IEY8;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 80.
DE   RecName: Full=Glutamate 5-kinase 1 {ECO:0000255|HAMAP-Rule:MF_00456};
DE            EC=2.7.2.11 {ECO:0000255|HAMAP-Rule:MF_00456};
DE   AltName: Full=Gamma-glutamyl kinase 1 {ECO:0000255|HAMAP-Rule:MF_00456};
DE            Short=GK 1 {ECO:0000255|HAMAP-Rule:MF_00456};
GN   Name=proB1 {ECO:0000255|HAMAP-Rule:MF_00456};
GN   OrderedLocusNames=PSHAa0279;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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: ATP + L-glutamate = ADP + L-glutamate 5-
CC       phosphate. {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; CR954246; CAI85378.1; -; Genomic_DNA.
DR   RefSeq; WP_011326992.1; NC_007481.1.
DR   ProteinModelPortal; Q3IEY8; -.
DR   SMR; Q3IEY8; -.
DR   STRING; 326442.PSHAa0279; -.
DR   EnsemblBacteria; CAI85378; CAI85378; PSHAa0279.
DR   GeneID; 32567072; -.
DR   KEGG; pha:PSHAa0279; -.
DR   eggNOG; COG0263; LUCA.
DR   HOGENOM; HOG000246368; -.
DR   KO; K00931; -.
DR   OMA; NMINCYE; -.
DR   OrthoDB; POG091H00OF; -.
DR   UniPathway; UPA00098; UER00359.
DR   Proteomes; UP000006843; Chromosome I.
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-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.30.130.10; -; 1.
DR   HAMAP; MF_00456; ProB; 1.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
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_domain.
DR   Pfam; PF00696; AA_kinase; 1.
DR   PIRSF; PIRSF000729; GK; 1.
DR   PRINTS; PR00474; GLU5KINASE.
DR   SUPFAM; SSF53633; SSF53633; 1.
DR   SUPFAM; SSF88697; SSF88697; 1.
DR   TIGRFAMs; TIGR01027; proB; 1.
DR   PROSITE; PS00902; GLUTAMATE_5_KINASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3IEY8.
DR   SWISS-2DPAGE; Q3IEY8.
KW   Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm;
KW   Kinase; Nucleotide-binding; Proline biosynthesis; Reference proteome;
KW   Transferase.
FT   CHAIN         1    368       Glutamate 5-kinase 1.
FT                                /FTId=PRO_0000230055.
FT   DOMAIN      274    348       PUA. {ECO:0000255|HAMAP-Rule:MF_00456}.
FT   NP_BIND     167    168       ATP. {ECO:0000255|HAMAP-Rule:MF_00456}.
FT   NP_BIND     209    215       ATP. {ECO:0000255|HAMAP-Rule:MF_00456}.
FT   BINDING      12     12       ATP. {ECO:0000255|HAMAP-Rule:MF_00456}.
FT   BINDING      52     52       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00456}.
FT   BINDING     135    135       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00456}.
FT   BINDING     147    147       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00456}.
SQ   SEQUENCE   368 AA;  40037 MW;  71D26AC8C04EC235 CRC64;
     MNKLNWRRIV LKVGSALIAP DQDGCRSRYI LTIAQFIVRC RARGIEVILV SSGSVAAGAH
     LFPSDTARSV VMKKAMAAAG QTEMIAMWDR FFDFPSAQLL LTHGDLRDHE RYQSIRETVF
     TLLEHGVLPI INENDAVTTD DLKVGDNDNL SAMVAAAADA DALLIFSDVD GLYDKNPNLH
     DDAILLPEIK SIDDSIYAMA GCATSAVGTG GMKTKIEAAE KATSHGISTY IINGFKEETF
     TRLLAGENPG TIFLPYEKPM QDSVHWMTHT ANEQGEVVVD GSFDKSLEGE TGCIRGDEIM
     AVHGEFAIGD TILVRSEDGT RLAKATANYS SCLLSFIADN EQSEFSEKMQ DSIGPVISEK
     HIALLEKS
//

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