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Database: UniProt
Entry: A0A0G9HG34_9GAMM
LinkDB: A0A0G9HG34_9GAMM
Original site: A0A0G9HG34_9GAMM 
ID   A0A0G9HG34_9GAMM        Unreviewed;       346 AA.
AC   A0A0G9HG34;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Glucokinase {ECO:0000256|HAMAP-Rule:MF_00524};
DE            EC=2.7.1.2 {ECO:0000256|HAMAP-Rule:MF_00524};
DE   AltName: Full=Glucose kinase {ECO:0000256|HAMAP-Rule:MF_00524};
GN   Name=glk {ECO:0000256|HAMAP-Rule:MF_00524};
GN   ORFNames=BJI69_05395 {ECO:0000313|EMBL:APG03404.1}, Y883_04440
GN   {ECO:0000313|EMBL:KLD68114.1};
OS   Luteibacter rhizovicinus DSM 16549.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Luteibacter.
OX   NCBI_TaxID=1440763 {ECO:0000313|EMBL:APG03404.1, ECO:0000313|Proteomes:UP000182987};
RN   [1] {ECO:0000313|EMBL:KLD68114.1, ECO:0000313|Proteomes:UP000035585}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16549 {ECO:0000313|EMBL:KLD68114.1,
RC   ECO:0000313|Proteomes:UP000035585};
RX   PubMed=25481407; DOI=10.1007/s10482-014-0344-8;
RA   Naushad S., Adeolu M., Wong S., Sohail M., Schellhorn H.E., Gupta R.S.;
RT   "A phylogenomic and molecular marker based taxonomic framework for the
RT   order Xanthomonadales: proposal to transfer the families Algiphilaceae and
RT   Solimonadaceae to the order Nevskiales ord. nov. and to create a new family
RT   within the order Xanthomonadales, the family Rhodanobacteraceae fam. nov.,
RT   containing the genus Rhodanobacter and its closest relatives.";
RL   Antonie Van Leeuwenhoek 107:467-485(2015).
RN   [2] {ECO:0000313|EMBL:APG03404.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LJ96 {ECO:0000313|EMBL:APG03404.1};
RX   PubMed=28123952;
RA   Aamot H.U., Hofgaard I.S., Lysoe E.;
RT   "Complete genome sequence of Luteibacter rhizovicinus strain LJ96T,
RT   isolated from the rhizosphere of barley (Hordeum vulgare L.) in Denmark.";
RL   Genom Data 11:104-105(2016).
RN   [3] {ECO:0000313|Proteomes:UP000182987}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LJ96T {ECO:0000313|Proteomes:UP000182987};
RA   Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+);
CC         Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.2;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00524};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00524}.
CC   -!- SIMILARITY: Belongs to the bacterial glucokinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00524, ECO:0000256|RuleBase:RU004046}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00524}.
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DR   EMBL; CP017480; APG03404.1; -; Genomic_DNA.
DR   EMBL; JPLB01000015; KLD68114.1; -; Genomic_DNA.
DR   RefSeq; WP_046966540.1; NZ_JPLB01000015.1.
DR   AlphaFoldDB; A0A0G9HG34; -.
DR   STRING; 1440763.BJI69_05395; -.
DR   KEGG; lrz:BJI69_05395; -.
DR   PATRIC; fig|1440763.5.peg.575; -.
DR   OrthoDB; 9800595at2; -.
DR   Proteomes; UP000035585; Unassembled WGS sequence.
DR   Proteomes; UP000182987; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004340; F:glucokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.420.40; -; 1.
DR   Gene3D; 3.40.367.20; -; 1.
DR   HAMAP; MF_00524; Glucokinase; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR003836; Glucokinase.
DR   NCBIfam; TIGR00749; glk; 1.
DR   PANTHER; PTHR47690; GLUCOKINASE; 1.
DR   PANTHER; PTHR47690:SF1; GLUCOKINASE; 1.
DR   Pfam; PF02685; Glucokinase; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00524};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00524};
KW   Glycolysis {ECO:0000256|HAMAP-Rule:MF_00524};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00524};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00524};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00524}.
SQ   SEQUENCE   346 AA;  36869 MW;  18648A1A1C9B7C94 CRC64;
     MANVSAKAPT LLADLGGTNV RFGIAHPDED QPLIQESVRK YHVKDYASLG DAAKQYFKDA
     GHEAQRAIIA AAGRIDNGET VKVTNNPWAI SAKSLAKELD LEWVHLVNDF AAQSMAVMLM
     TDEKSADGHQ DLVPVGKLGV PKIGAKDEQT FVVVGPGTGL GVGGLLIRGD KVSVLQTEGG
     HAGFAAHSAE DIEILKVLNL RYGRVSNERL ICGQGLVNLY EAICEISGQK PQEGITPEEV
     TKRATDETCP MCGRAVETFA GIFGSVAGDL VLTLGAWDGV YLTGGMTPIL LPWIQKGNFR
     ERFEAKGRFR DSMEQVPTQA IMNPEPGLIG GAALAIVEAG GTPLRR
//
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