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Database: UniProt
Entry: A0A1B6ARD4_9ACTN
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ID   A0A1B6ARD4_9ACTN        Unreviewed;       365 AA.
AC   A0A1B6ARD4;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
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:GAU70005.1};
GN   ORFNames=SSP35_15_01600 {ECO:0000313|EMBL:GAU70005.1};
OS   Streptomyces sp. NBRC 110611.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1621259 {ECO:0000313|EMBL:GAU70005.1, ECO:0000313|Proteomes:UP000094479};
RN   [1] {ECO:0000313|EMBL:GAU70005.1, ECO:0000313|Proteomes:UP000094479}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 110611 {ECO:0000313|EMBL:GAU70005.1,
RC   ECO:0000313|Proteomes:UP000094479};
RA   Igarashi Y., Komaki H., Ichikawa N., Hosoyama A., Fujita N., Panbangred W.;
RT   "Whole genome shotgun sequence of Streptomyces sp. NBRC 110611.";
RL   Submitted (MAR-2015) 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:GAU70005.1}.
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DR   EMBL; BBUY01000015; GAU70005.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B6ARD4; -.
DR   STRING; 1621259.GCA_001590865_05324; -.
DR   UniPathway; UPA00098; UER00359.
DR   Proteomes; UP000094479; 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}; Reference proteome {ECO:0000313|Proteomes:UP000094479};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00456}.
FT   DOMAIN          272..351
FT                   /note="PUA"
FT                   /evidence="ECO:0000259|SMART:SM00359"
FT   BINDING         10
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT   BINDING         48
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT   BINDING         167..168
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
FT   BINDING         209..215
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00456"
SQ   SEQUENCE   365 AA;  38369 MW;  A20AD8932D9B76F1 CRC64;
     MADARRIVVK VGSSSLTTAA GGLDADRVDA LVDVLAKHQD REIVLVSSGA IAAGLAPLGL
     DRRPRDLARQ QAAASVGQGL LVARYTASFA RYGRRVGQVL LTSDDTSRRA HYRNAYRTLD
     QLLAMGAVPI VNENDTVATD EIRFGDNDRL AALVAHLVRA DLLVLLSDVD GLYDGDPSRP
     GTSRIAEVHG PQDLEGVSIG SAGKAGVGTG GMVTKVEAAR IAAAAGIPVV LTSAVHASEA
     LAGGPTGTHF LRTGRRTADR LLWLAHASTP RGALVLDDGA VRAVVERHSS LLPAGIAAVE
     GEFSAGDPVE LRDGTGHPVA RGLVNFDARE IPRLIGRSTR DLARELGPAY EREVVHRDDL
     VLLHH
//
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