ID GLK_NITHX Reviewed; 320 AA.
AC Q1QFN5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 24-JAN-2024, entry version 79.
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=Nham_4371;
OS Nitrobacter hamburgensis (strain DSM 10229 / NCIMB 13809 / X14).
OG Plasmid pNITHX2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Nitrobacter.
OX NCBI_TaxID=323097;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10229 / NCIMB 13809 / X14;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L.,
RA O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T.,
RA Gentry M.E., Bruce D., Richardson P.;
RT "Complete sequence of plasmid 2 of Nitrobacter hamburgensis X14.";
RL Submitted (MAR-2006) 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: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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABE64962.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000321; ABE64962.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q1QFN5; -.
DR SMR; Q1QFN5; -.
DR KEGG; nha:Nham_4371; -.
DR eggNOG; COG0837; Bacteria.
DR HOGENOM; CLU_042582_1_0_5; -.
DR OrthoDB; 9800595at2; -.
DR Proteomes; UP000001953; Plasmid pNITHX2.
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 CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
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; Cytoplasm; Glycolysis; Kinase; Nucleotide-binding; Plasmid;
KW Reference proteome; Transferase.
FT CHAIN 1..320
FT /note="Glucokinase"
FT /id="PRO_0000268779"
FT BINDING 12..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00524"
SQ SEQUENCE 320 AA; 33719 MW; 3963475A2D8C2835 CRC64;
MGKSMTALRV IGDIGGTYAR FAVAERGKYS ELQHLSVSKY AALKDALGEY LAALPRDLRP
TRGALAVAGP VSGDEVKLTN LNWSFSITAL KADLGMSSLV VVNDFAATAM SVPYLPEADC
YPIGPPQSKT SGPVGVIGPG TGLGVSALVP DAGRWILLPG EGGHSTLPPA TQAESLIVEV
LRTHWPHVSA ERALSGAGLV NLYQALCSIE GKRPDPLSPA DVTDRAMRGS DPTCVKAFEV
FCSMLGTVAG DLALTIGATG GIYIAGGILL RFKEAFASSP FRDRFEDKGR FQDYLRRIPT
LLILEESPAL LGLANLPLEP
//
