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Database: UniProt
Entry: W7WFW1_9BURK
LinkDB: W7WFW1_9BURK
Original site: W7WFW1_9BURK 
ID   W7WFW1_9BURK            Unreviewed;       372 AA.
AC   W7WFW1;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 46.
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:EWS61656.1};
GN   ORFNames=Y694_00586 {ECO:0000313|EMBL:EWS61656.1};
OS   Methylibium sp. T29-B.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Methylibium.
OX   NCBI_TaxID=1437443 {ECO:0000313|EMBL:EWS61656.1, ECO:0000313|Proteomes:UP000019360};
RN   [1] {ECO:0000313|EMBL:EWS61656.1, ECO:0000313|Proteomes:UP000019360}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T29-B {ECO:0000313|EMBL:EWS61656.1,
RC   ECO:0000313|Proteomes:UP000019360};
RA   Gyula P., Szabo Z., Robotka H., Bihari Z.;
RT   "Genome sequencing of the loss-of-function mutant Methylibium sp. T29-B.";
RL   Submitted (DEC-2013) 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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {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:EWS61656.1}.
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DR   EMBL; AZSN01000008; EWS61656.1; -; Genomic_DNA.
DR   RefSeq; WP_036229614.1; NZ_AZSN01000008.1.
DR   AlphaFoldDB; W7WFW1; -.
DR   PATRIC; fig|1437443.4.peg.573; -.
DR   OrthoDB; 9804434at2; -.
DR   UniPathway; UPA00098; UER00359.
DR   Proteomes; UP000019360; 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};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00456}.
FT   DOMAIN          281..364
FT                   /note="PUA"
FT                   /evidence="ECO:0000259|SMART:SM00359"
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"
SQ   SEQUENCE   372 AA;  39408 MW;  67C974268FAA4E16 CRC64;
     MSEVLRGARR IVVKVGSSLV TNEGRGVDAA AIGNWCRQLA SLAGQGREVL MVSSGAIAEG
     MKRLGWNARP KEIHELQAAA AVGQMGLAQM YESKLSEHGI GSAQVLLTHA DLADRERYLN
     ARSTLLTLLS LKVIPVINEN DTVVNDEIKF GDNDTLGALV ANLVDADALV ILTDQPGLYS
     ADPRKDPQAR FIGEAVAGTP ELERMAGGAG SSLGRGGMIT KVLAAKRAAS SGASTVIAWG
     REPDVLLRLA DGEAIGTLLV ARTAKLAARK QWMADHLQMR GTVVIDDGAV AKLRDEGKSL
     LPIGVVEVQG EFVRGDVIAV RSQVGIEIAR GLANYASSEA RLIARKPSSQ IESLLGYSNE
     PEMIHRTNLV LA
//
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