PROB_MOOTA
ID PROB_MOOTA Reviewed; 378 AA.
AC Q2RKZ7;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=Moth_0562;
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Moorella group; Moorella.
OX NCBI_TaxID=264732;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39073 / JCM 9320;
RX PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT thermoaceticum).";
RL Environ. Microbiol. 10:2550-2573(2008).
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; CP000232; ABC18892.1; -; Genomic_DNA.
DR RefSeq; WP_011392099.1; NC_007644.1.
DR RefSeq; YP_429435.1; NC_007644.1.
DR AlphaFoldDB; Q2RKZ7; -.
DR SMR; Q2RKZ7; -.
DR STRING; 264732.Moth_0562; -.
DR EnsemblBacteria; ABC18892; ABC18892; Moth_0562.
DR KEGG; mta:Moth_0562; -.
DR PATRIC; fig|264732.11.peg.605; -.
DR eggNOG; COG0263; Bacteria.
DR HOGENOM; CLU_025400_2_0_9; -.
DR OMA; TVIHRDN; -.
DR UniPathway; UPA00098; UER00359.
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; -; 2.
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;
KW Amino-acid biosynthesis; ATP-binding; Cytoplasm; Kinase;
KW Nucleotide-binding; Proline biosynthesis; Transferase.
FT CHAIN 1..378
FT /note="Glutamate 5-kinase"
FT /id="PRO_0000230047"
FT DOMAIN 285..363
FT /note="PUA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT BINDING 19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT BINDING 59
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT BINDING 178..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT BINDING 220..226
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
SQ SEQUENCE 378 AA; 40117 MW; 5B28E947BF2A06EE CRC64;
MTERECRLAL SQARRLVIKV GTSTLTHKTG KLNLGRMERL VRELVDQVNA GRQVVLVTSG
AVGAGMGRLG LKEKPRTLPE KQAAAAVGQG LLMHMYEKFF SDYGLLVAQV LLTRADLADR
SRYLNSRHTL AALLRLGVVP IVNENDTVAV EEIRVGDNDT LSALVAGLVD ADILFLLTDT
GGLFTANPVT SDDAVLLPCV TEITPEIEAL AGGAGSTWST GGMATKIQAA RLATSFGIPV
VIASGLQAGQ IEAVLKGEEI GTIFLPREHR AHTRKRWLAY APAVQGQIQV DAGAARAICK
NGKSLLPGGV IAVDGDFDQG AIVSIVDPAG KEIARGMANY PAAAISRIKG RKTGEIGEIL
GYKDYDEIVH RDNLIVLG