ID A0A437S8D2_9FIRM Unreviewed; 263 AA.
AC A0A437S8D2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
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 ECO:0000313|EMBL:RVU55349.1};
GN ORFNames=EF514_03505 {ECO:0000313|EMBL:RVU55349.1};
OS Anaerosphaera multitolerans.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Anaerosphaera.
OX NCBI_TaxID=2487351 {ECO:0000313|EMBL:RVU55349.1, ECO:0000313|Proteomes:UP000288812};
RN [1] {ECO:0000313|EMBL:RVU55349.1, ECO:0000313|Proteomes:UP000288812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS7-6-2 {ECO:0000313|EMBL:RVU55349.1,
RC ECO:0000313|Proteomes:UP000288812};
RA Rettenmaier R., Liebl W., Zverlov V.;
RT "Genome sequencing and assembly of Anaerosphaera sp. nov., GS7-6-2.";
RL Submitted (NOV-2018) 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}.
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:RVU55349.1}.
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DR EMBL; RLIH01000003; RVU55349.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A437S8D2; -.
DR OrthoDB; 9804434at2; -.
DR UniPathway; UPA00098; UER00359.
DR Proteomes; UP000288812; 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: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; 3.40.1160.10; Acetylglutamate kinase-like; 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 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 PIRSF; PIRSF000729; GK; 1.
DR PRINTS; PR00474; GLU5KINASE.
DR SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR PROSITE; PS00902; GLUTAMATE_5_KINASE; 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 9..239
FT /note="Aspartate/glutamate/uridylate kinase"
FT /evidence="ECO:0000259|Pfam:PF00696"
FT BINDING 14
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 141
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT BINDING 173..174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT BINDING 215..221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
SQ SEQUENCE 263 AA; 28936 MW; EA723DAD003D117F CRC64;
MRKFSNELKT VVVKIGSSSI THENGVINLQ RIDELAWELS NLKNHEINVI LVSSGAIAAG
AKKLNLLSRP RDTVGKQAAS AVGQVALMNT YNRAFHEFGY EAAQILLTKQ IETDLVMREN
ARNTFEKLLN MNVIPVVNEN DTISTFEIEF GDNDTLSAVV SRMVDADLLI LLSDIDGLYD
DDPRQNPKAK LISEVVEISE ELENMAKDSN STVGTGGMTT KINAARLCLE KGIDMVIANS
DDLKNIRKIV EGEEIGTIFK ARA
//