ID M2ZTH0_9PROT Unreviewed; 370 AA.
AC M2ZTH0;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
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=H261_07166 {ECO:0000313|EMBL:EME70667.1};
OS Paramagnetospirillum caucaseum.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Magnetospirillaceae; Paramagnetospirillum.
OX NCBI_TaxID=1244869 {ECO:0000313|EMBL:EME70667.1, ECO:0000313|Proteomes:UP000011744};
RN [1] {ECO:0000313|EMBL:EME70667.1, ECO:0000313|Proteomes:UP000011744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SO-1 {ECO:0000313|EMBL:EME70667.1,
RC ECO:0000313|Proteomes:UP000011744};
RX PubMed=24723706;
RA Grouzdev D.S., Dziuba M.V., Sukhacheva M.S., Mardanov A.V., Beletskiy A.V.,
RA Kuznetsov B.B., Skryabin K.G.;
RT "Draft Genome Sequence of Magnetospirillum sp. Strain SO-1, a Freshwater
RT Magnetotactic Bacterium Isolated from the Ol'khovka River, Russia.";
RL Genome Announc. 2:e00235-14(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EME70667.1}.
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DR EMBL; AONQ01000014; EME70667.1; -; Genomic_DNA.
DR RefSeq; WP_008615854.1; NZ_AONQ01000014.1.
DR AlphaFoldDB; M2ZTH0; -.
DR STRING; 1244869.H261_07166; -.
DR PATRIC; fig|1244869.3.peg.1447; -.
DR eggNOG; COG0263; Bacteria.
DR OrthoDB; 9804434at2; -.
DR UniPathway; UPA00098; UER00359.
DR Proteomes; UP000011744; 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; 2.
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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00456}.
FT DOMAIN 279..361
FT /note="PUA"
FT /evidence="ECO:0000259|SMART:SM00359"
FT BINDING 13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT BINDING 172..173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT BINDING 214..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
SQ SEQUENCE 370 AA; 39655 MW; 9715B63F03A2C89D CRC64;
MNPLRDAKRL IVKIGSSLLV DDATGQMRRG WLESLAADIA ACTARGQEVI VVSSGAVAVG
RRKLGLVPPL KLEEKQAAAA TGQIRLAHAW QDALAHHAIT VAQVLLTLDD SENRRRYLNA
RSTLETLLRL GAVPVINEND TVATAEIRVG DNDRLAARVA QMVSADALVL FSDIDGLYTA
DPRKDSDARF IPEVRELTPE IEAMAGDPGS AYGSGGMVTK LVAARICLSA GCRMAITRGE
PMHPLKTIED GGRCTWFLPS SEPRTARKQW IFGSMKPAGT LVLDAGAARA LAQGRSLLPA
GITEVNGEFE RGDCVLVKDT EAKVLGRGLV AYSATDARAI MGRKSGEIEA ILGFRGRDEL
IHRDDLVMEG
//
