ID A0A3G3GSR2_9BACT Unreviewed; 343 AA.
AC A0A3G3GSR2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Glutamate 5-kinase {ECO:0000313|EMBL:AYQ34485.1};
DE EC=2.7.2.11 {ECO:0000313|EMBL:AYQ34485.1};
GN Name=proB {ECO:0000313|EMBL:AYQ34485.1};
GN ORFNames=DTQ70_21005 {ECO:0000313|EMBL:AYQ34485.1};
OS Runella sp. SP2.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae; Runella.
OX NCBI_TaxID=2268026 {ECO:0000313|EMBL:AYQ34485.1, ECO:0000313|Proteomes:UP000270973};
RN [1] {ECO:0000313|EMBL:AYQ34485.1, ECO:0000313|Proteomes:UP000270973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP2 {ECO:0000313|EMBL:AYQ34485.1,
RC ECO:0000313|Proteomes:UP000270973};
RA Jin H.M.;
RT "Genome sequence of Runella sp. SP1.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP031030; AYQ34485.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G3GSR2; -.
DR KEGG; rup:DTQ70_21005; -.
DR OrthoDB; 9804434at2; -.
DR Proteomes; UP000270973; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004349; F:glutamate 5-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006561; P:proline biosynthetic process; IEA:UniProtKB-KW.
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 InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR001057; Glu/AcGlu_kinase.
DR InterPro; IPR011529; Glu_5kinase.
DR InterPro; IPR005715; Glu_5kinase/COase_Synthase.
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; PS50890; PUA; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AYQ34485.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650};
KW Reference proteome {ECO:0000313|Proteomes:UP000270973};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AYQ34485.1}.
FT DOMAIN 265..341
FT /note="PUA"
FT /evidence="ECO:0000259|SMART:SM00359"
SQ SEQUENCE 343 AA; 37047 MW; 55FF70A38799F8A6 CRC64;
MSKPILVLKF GSAAITKANG ELNQLVMVEI ARQVAQLYTD YHVVIVSSGA VAAGKQYIRS
YAGEITQRKA AAAIGNLLLL NKYAQFFSPY DIPVAQSLCE RGHFANRDQF LQMKDTFQEL
WENGIIPIVN ENDVVSSHEL KFSDNDELAT LIAVGFGADT LMLCTSVGGL LDDKGQVIPR
VSQVNDVFQF VRSDKSSVGL GGMTSKLTFA KLATRMGIRT IIFGMNEPDG ILHAIREETG
TVFAPQDNSL SARNRWLGSG SLVAGRITID DGAAQALQNR KSLLAVGIKN VAGDFEAGEV
VELLNSEGNL VAVAKARESS VVIVQNLRTQ NFEVANANDI VLL
//
