PROB1_PSET1
ID PROB1_PSET1 Reviewed; 368 AA.
AC Q3IEY8;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
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}; OrderedLocusNames=PSHAa0279;
OS Pseudoalteromonas translucida (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., Ho C.,
RA Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C., Rouy Z.,
RA Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT "Coping with cold: the genome of the versatile marine Antarctica bacterium
RT Pseudoalteromonas haloplanktis TAC125.";
RL Genome Res. 15:1325-1335(2005).
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}.
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DR EMBL; CR954246; CAI85378.1; -; Genomic_DNA.
DR RefSeq; WP_011326992.1; NC_007481.1.
DR AlphaFoldDB; Q3IEY8; -.
DR SMR; Q3IEY8; -.
DR STRING; 326442.PSHAa0279; -.
DR EnsemblBacteria; CAI85378; CAI85378; PSHAa0279.
DR KEGG; pha:PSHAa0279; -.
DR eggNOG; COG0263; Bacteria.
DR HOGENOM; CLU_025400_2_1_6; -.
DR OMA; INCYEGL; -.
DR OrthoDB; 1480250at2; -.
DR BioCyc; PHAL326442:PSHA_RS01380-MON; -.
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-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; IPR015947; PUA-like_sf.
DR InterPro; IPR036974; PUA_sf.
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;
KW Amino-acid biosynthesis; ATP-binding; Cytoplasm; Kinase;
KW Nucleotide-binding; Proline biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..368
FT /note="Glutamate 5-kinase 1"
FT /id="PRO_0000230055"
FT DOMAIN 274..348
FT /note="PUA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT BINDING 12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT BINDING 167..168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT BINDING 209..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="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
