ID A0A0C3RKX1_9PROT Unreviewed; 335 AA.
AC A0A0C3RKX1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=SQ11_09970 {ECO:0000313|EMBL:KIO48721.1};
OS Nitrosospira sp. NpAV.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosospira.
OX NCBI_TaxID=58133 {ECO:0000313|EMBL:KIO48721.1, ECO:0000313|Proteomes:UP000031969};
RN [1] {ECO:0000313|EMBL:KIO48721.1, ECO:0000313|Proteomes:UP000031969}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NpAV {ECO:0000313|EMBL:KIO48721.1,
RC ECO:0000313|Proteomes:UP000031969};
RA Rice M.C., Lim C.K., Sayavedra-Soto L.A., Norton J.M., Klotz M.G.;
RT "Nitrosospira sp. NpAV genome sequencing.";
RL Submitted (JAN-2015) 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: 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:KIO48721.1}.
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DR EMBL; JXQM01000015; KIO48721.1; -; Genomic_DNA.
DR RefSeq; WP_041514027.1; NZ_JXQM01000015.1.
DR AlphaFoldDB; A0A0C3RKX1; -.
DR OrthoDB; 257751at2; -.
DR Proteomes; UP000031969; Unassembled WGS sequence.
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; PTHR47363; GLUCOKINASE; 1.
DR PANTHER; PTHR47363: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, ECO:0000313|EMBL:KIO48721.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00524};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00524}.
FT BINDING 8..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00524"
SQ SEQUENCE 335 AA; 36443 MW; A9921D51F8E20091 CRC64;
MSQYFISADI GGTKVLLQAA EATEGGMQVR YERRYPSRDY PDFSDILRDF LDRAAMAGAG
GNPASACFAV AGPIMQQRAT LTNLPWVMDS AVIAHEFSIP DVKLINDFKA VALSIEILSA
SDFMSLQAGK LYDKEMGVVL GAGTGMGVAW LIWQDDRYIP LPTEAGHVDF APANELQDHL
LQYLRKKFGH VSVERLLSGP GLTNIFEFLN FHHRNDAPEP VQASLGGDCA ARVADLAFNH
KHPLAVMAMN LFVEIYGAYA GNLALSTLSR GGVYVAGGIA PKIIDKLKEG GFMKAFCDKG
RFSALMSEIP VRVVMNPEAG LLGATREARR MLLEK
//
