ID A0A255H0S5_9ACTN Unreviewed; 379 AA.
AC A0A255H0S5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=CGZ93_12325 {ECO:0000313|EMBL:OYO20986.1};
OS Enemella dayhoffiae.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Enemella.
OX NCBI_TaxID=2016507 {ECO:0000313|EMBL:OYO20986.1, ECO:0000313|Proteomes:UP000216311};
RN [1] {ECO:0000313|EMBL:OYO20986.1, ECO:0000313|Proteomes:UP000216311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML 130396 {ECO:0000313|EMBL:OYO20986.1,
RC ECO:0000313|Proteomes:UP000216311};
RA Bernier A.-M., Bernard K., Domingo M.-C.;
RT "Draft whole genome sequences of clinical Proprionibacteriaceae strains.";
RL Submitted (JUL-2017) 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:OYO20986.1}.
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DR EMBL; NMVQ01000023; OYO20986.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255H0S5; -.
DR OrthoDB; 9804434at2; -.
DR UniPathway; UPA00098; UER00359.
DR Proteomes; UP000216311; 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:UP000216311};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00456}.
FT DOMAIN 281..360
FT /note="PUA"
FT /evidence="ECO:0000259|SMART:SM00359"
FT BINDING 18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT BINDING 177..178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT BINDING 218..224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
SQ SEQUENCE 379 AA; 39824 MW; 6E1919A7F4F8D740 CRC64;
MSDLAADWFG SAPRVVVKVG SSSLTTPQGA IDPDRIQSLV DALAGVRAAG REVVLVSSGA
IAAGISPLGL KRRPRDLATQ QAAASVGQGL LVAHYTRRFL EHGWRVGQVL LTVDDVTRQG
LYRNAYRTLA KLLDFGVIPI VNENDTVATH EIRFGDNDRL AALVAHLVHA DALVLLSDVD
ALHTDHPSRP GARRIPEVAD ATELAGVDIS RTGSAVGTGG MVTKVQAAEI ATSAGIPTLL
TSAANAASAL SGADVGTRFA VTGKRRPTRL LWLQHASYTA GQLHLDAGAV RALVERNASL
LPVGITAVEG EFSAGEPVNL VTPEGAVTAR GLVGFDAADL RRMIGKDSRE LLSALGEDYE
GVAVHRDVLV ILNRHREKS
//
