GLK_MAGSA
ID GLK_MAGSA Reviewed; 321 AA.
AC Q2W5F9;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Glucokinase {ECO:0000255|HAMAP-Rule:MF_00524};
DE EC=2.7.1.2 {ECO:0000255|HAMAP-Rule:MF_00524};
DE AltName: Full=Glucose kinase {ECO:0000255|HAMAP-Rule:MF_00524};
GN Name=glk {ECO:0000255|HAMAP-Rule:MF_00524}; OrderedLocusNames=amb2112;
OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=342108;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT "Complete genome sequence of the facultative anaerobic magnetotactic
RT bacterium Magnetospirillum sp. strain AMB-1.";
RL DNA Res. 12:157-166(2005).
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:0000255|HAMAP-Rule:MF_00524};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00524}.
CC -!- SIMILARITY: Belongs to the bacterial glucokinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00524}.
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DR EMBL; AP007255; BAE50916.1; -; Genomic_DNA.
DR RefSeq; WP_011384511.1; NC_007626.1.
DR AlphaFoldDB; Q2W5F9; -.
DR SMR; Q2W5F9; -.
DR STRING; 342108.amb2112; -.
DR EnsemblBacteria; BAE50916; BAE50916; amb2112.
DR KEGG; mag:amb2112; -.
DR HOGENOM; CLU_042582_1_0_5; -.
DR OMA; GIANRFP; -.
DR OrthoDB; 992687at2; -.
DR Proteomes; UP000007058; 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 HAMAP; MF_00524; Glucokinase; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR003836; Glucokinase.
DR Pfam; PF02685; Glucokinase; 1.
DR SUPFAM; SSF53067; SSF53067; 1.
DR TIGRFAMs; TIGR00749; glk; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..321
FT /note="Glucokinase"
FT /id="PRO_0000268776"
FT BINDING 8..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00524"
SQ SEQUENCE 321 AA; 33453 MW; 746C469BC6492DD3 CRC64;
MSQMVLVADI GGTHARFALM GPDGEAVNPV VLRCADYDGP APAIKAYLAE HAGGVAPKGG
AFAVASVIDG DRIELTNSPW RFSIAETRQA VGLQRLEVVN DFTAVALSVR HLKPEHLMSV
GGGMPEAGLP IAVLGPGTGL GVSALIPSAS GEWTALATEG GHVTMAAATE REARILDRLR
TQFDHVSAER VLSGQGLVNL YQAVAALSGH QAVFSTPDVI TKRGLDGSCP VSREAVEVFF
AMMGTVAGNL ALSLGAKGGV FIAGGILPRM AEAFRLSSFR TRFEAHGRFQ PYLAAIPTWL
ITHPLPAFVG LAGLVTDPKN A