ID A0A1S2ME71_9BACI Unreviewed; 368 AA.
AC A0A1S2ME71;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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 ORFNames=AWH56_025750 {ECO:0000313|EMBL:QOY36007.1}, AWH56_03260
GN {ECO:0000313|EMBL:OIJ22969.1};
OS Anaerobacillus isosaccharinicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anaerobacillus.
OX NCBI_TaxID=1532552 {ECO:0000313|EMBL:OIJ22969.1, ECO:0000313|Proteomes:UP000180175};
RN [1] {ECO:0000313|EMBL:OIJ22969.1, ECO:0000313|Proteomes:UP000180175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NB2006 {ECO:0000313|EMBL:OIJ22969.1,
RC ECO:0000313|Proteomes:UP000180175};
RA Bassil N.M., Lloyd J.R.;
RT "Draft genome sequences of four alkaliphilic bacteria belonging to the
RT Anaerobacillus genus.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QOY36007.1, ECO:0000313|Proteomes:UP000180175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NB2006 {ECO:0000313|EMBL:QOY36007.1,
RC ECO:0000313|Proteomes:UP000180175};
RX PubMed=28104661;
RA Bassil N.M., Lloyd J.R.;
RT "Draft Genome Sequences of Four Alkaliphilic Bacteria Belonging to the
RT Anaerobacillus Genus.";
RL Genome Announc. 5:e01493-16(2017).
RN [3] {ECO:0000313|EMBL:QOY36007.1, ECO:0000313|Proteomes:UP000180175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NB2006 {ECO:0000313|EMBL:QOY36007.1,
RC ECO:0000313|Proteomes:UP000180175};
RX PubMed=29580368;
RA Bassil N.M., Lloyd J.R.;
RT "Anaerobacillus isosaccharinicus sp. nov., an alkaliphilic bacterium which
RT degrades isosaccharinic acid.";
RL Int. J. Syst. Evol. Microbiol. 69:3666-3671(2019).
RN [4] {ECO:0000313|EMBL:QOY36007.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NB2006 {ECO:0000313|EMBL:QOY36007.1};
RA Bassil N.M., Lloyd J.R.;
RL Submitted (OCT-2020) 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:0000256|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:0000256|HAMAP-Rule:MF_00456};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-glutamate: step 1/2. {ECO:0000256|HAMAP-
CC Rule:MF_00456}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00456}.
CC -!- SIMILARITY: Belongs to the glutamate 5-kinase family.
CC {ECO:0000256|HAMAP-Rule:MF_00456}.
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DR EMBL; LQXD01000010; OIJ22969.1; -; Genomic_DNA.
DR EMBL; CP063356; QOY36007.1; -; Genomic_DNA.
DR RefSeq; WP_071315782.1; NZ_CP063356.1.
DR AlphaFoldDB; A0A1S2ME71; -.
DR KEGG; aia:AWH56_025750; -.
DR OrthoDB; 9804434at2; -.
DR UniPathway; UPA00098; UER00359.
DR Proteomes; UP000180175; Chromosome.
DR Proteomes; UP000180175; Unassembled WGS sequence.
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 CDD; cd21157; PUA_G5K; 1.
DR Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR Gene3D; 2.30.130.10; PUA domain; 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 NCBIfam; TIGR01027; proB; 1.
DR PANTHER; PTHR43654; GLUTAMATE 5-KINASE; 1.
DR PANTHER; PTHR43654:SF1; ISOPENTENYL PHOSPHATE KINASE; 1.
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; Carbamate kinase-like; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR PROSITE; PS00902; GLUTAMATE_5_KINASE; 1.
DR PROSITE; PS50890; PUA; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_00456};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00456};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00456};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00456};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00456};
KW Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650, ECO:0000256|HAMAP-
KW Rule:MF_00456}; Reference proteome {ECO:0000313|Proteomes:UP000180175};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00456}.
FT DOMAIN 277..357
FT /note="PUA"
FT /evidence="ECO:0000259|SMART:SM00359"
FT BINDING 9
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT BINDING 136
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT BINDING 168..169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT BINDING 210..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
SQ SEQUENCE 368 AA; 39518 MW; E17025CBE979C932 CRC64;
MSKQRIVVKI GSSSLTNMKG GLSIEKLTEH ANALAELRRL GHEVILISSG AVAAGFTKLG
YPSRPVTISG KQAAAAVGQG LLMQGYEEAF GHHEIVVAQL LLTRNDFVSQ EQYSNAYAVL
TELLTRGVVP IINENDSTSV EELTFGDNDM LSALVSGLVH ADFLAILTDI NGLYDEDPRK
NPLAKKYHFL PTIHDELLHQ AKDTGSKVGT GGMRSKIEAA KTANSLGVNV FIGTGQGDAK
LVDILLGKGD GTYIGSTTKK VVKNKKQWIA FHSTTTGKIV IDDGAVQALL TKGKSLLPIG
IQEVSGTFKK GDVVEVVSIR GKAIGRGQVN YSSDELLSIK GKESSEAKKT TNCQYDEAIH
RDHWITFS
//
